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  • Artikel  (115)
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  • American Association for the Advancement of Science (AAAS)  (115)
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  • American Association for the Advancement of Science (AAAS)  (115)
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  • 1
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    Evidence of lactate dehydrogenase-B allozyme effects in the teleost, Fundulus heteroclitus (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-08-23
    Beschreibung: The evolutionary significance of protein polymorphisms has long been debated. Exponents of the balanced theory advocate that selection operates to maintain polymorphisms, whereas the neoclassical school argues that most genetic variation is neutral. Some studies have suggested that protein polymorphisms are not neutral, but their significance has been questioned because one cannot eliminate the possibility that linked loci were responsible for the observed differences. Evidence is presented that an enzymatic phenotype can affect carbon flow through a metabolic pathway. Glucose flux differences between lactate dehydrogenase-B phenotypes of Fundulus heteroclitus were reversed by substituting the Ldh-B gene product of one homozygous genotype with that of another.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DiMichele, L -- Paynter, K T -- Powers, D A -- New York, N.Y. -- Science. 1991 Aug 23;253(5022):898-900.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Wildlife and Fisheries Sciences, Texas A&M University, College Station 77843.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1876847" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Blastocyst/enzymology ; Genotype ; Glucose/metabolism ; Glycolysis ; Isoenzymes ; Killifishes/embryology/*genetics/metabolism ; Kinetics ; L-Lactate Dehydrogenase/*genetics/metabolism ; Lactates/metabolism ; Lactic Acid ; Microinjections ; Phenotype ; Swine
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 2
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    Negative regulation of CD45 protein tyrosine phosphatase activity by ionomycin in T cells (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-09-20
    Beschreibung: CD45 is a leukocyte-specific, transmembrane protein tyrosine phosphatase (PTPase) required for T cell responsiveness. How the activity of PTPases is regulated in vivo is unclear. Treatment of murine thymocytes and a variety of murine T cell lines with the calcium ionophore ionomycin decreased CD45 PTPase activity. Ionomycin treatment also led to a decreased phosphorylation of serine residues in CD45. These results indicate that increased intracellular calcium modulates CD45 PTPase activity, demonstrating regulation of CD45 PTPase activity in vivo, and also implicate serine dephosphorylation as a possible mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ostergaard, H L -- Trowbridge, I S -- CA-17733/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Sep 20;253(5026):1423-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Biology, Salk Institute, San Diego, CA 92186.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1654595" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Antigens, CD/*metabolism ; Antigens, CD45 ; Cell Line ; Histocompatibility Antigens/*metabolism ; Ionomycin/*pharmacology ; Kinetics ; Mice ; Mice, Inbred BALB C ; Phosphoprotein Phosphatases/*metabolism ; Protein Tyrosine Phosphatases ; Spleen/drug effects/enzymology/immunology ; T-Lymphocytes/drug effects/*enzymology/immunology ; Thymus Gland/immunology
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 3
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    An unexpectedly efficient catalytic antibody operating by ping-pong and induced fit mechanisms (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-05-03
    Beschreibung: A transition state analogue was used to produce a mouse antibody that catalyzes transesterification in water. The antibody behaves as a highly efficient catalyst with a covalent intermediate and the characteristic of induced fit. While some features of the catalytic pathway were programmed when the hapten was designed and reflect favorable substrate-antibody interactions, other features are a manifestation of the chemical potential of antibody diversity. The fact that antibodies recapitulate mechanisms and pathways previously thought to be a characteristic of highly evolved enzymes suggests that once an appropriate binding cavity is achieved, reaction pathways commensurate with the intrinsic chemical potential of proteins ensue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wirsching, P -- Ashley, J A -- Benkovic, S J -- Janda, K D -- Lerner, R A -- GM43858-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 3;252(5006):680-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2024120" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Acylation ; Alcohols/metabolism ; Animals ; Antibodies, Monoclonal/immunology/*metabolism ; Antibody Specificity ; Binding Sites, Antibody ; *Catalysis ; Enzymes/metabolism ; Esterification ; Haptens ; Kinetics ; Mice ; Water
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 4
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    Inhibition of Rap1A binding to cytochrome b558 of NADPH oxidase by phosphorylation of Rap1A (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-12-20
    Beschreibung: Rap1A is a low molecular weight guanosine triphosphate (GTP)-binding protein in human neutrophil membranes whose cellular function is unknown. Rap1A was found to form stoichiometric complexes with the cytochrome b558 component of the phagocyte nicotinamide adenine dinucleotide phosphate (NADPH) oxidase system. The (guanosine-5'-O-(3-thiotriphosphate) (GTP-gamma-S)-bound form of Rap1A bound more tightly to cytochrome b558 than did the guanosine diphosphate-bound form. No complex formation was observed between cytochrome b558 and H-Ras-GTP-gamma-S or Rap1A-GTP-gamma-S that had been heat-inactivated, nor between Rap1A-GTP-gamma-S and hydrophobic proteins serving as controls. Complex formation between Rap1A-GTP-gamma-S and cytochrome b558 was inhibited by phosphorylation of Rap1A with cyclic adenosine monophosphate (cAMP)-dependent protein kinase. These observations suggest that Rap1A may participate in the structure or regulation of the NADPH oxidase system and that this function of the Rap1A protein may be altered by phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bokoch, G M -- Quilliam, L A -- Bohl, B P -- Jesaitis, A J -- Quinn, M T -- 5RO126711/PHS HHS/ -- GM39434/GM/NIGMS NIH HHS/ -- GM44428/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1794-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1763330" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Binding Sites ; Chromatography, Gel ; Cytochrome b Group/isolation & purification/*metabolism ; GTP-Binding Proteins/antagonists & inhibitors/isolation & ; purification/*metabolism ; Guanosine 5'-O-(3-Thiotriphosphate)/metabolism ; Humans ; Kinetics ; Macromolecular Substances ; NADH, NADPH Oxidoreductases/*metabolism ; NADPH Oxidase ; Neutrophils/enzymology ; Phosphorylation ; Protein Binding ; Protein Kinase C/metabolism ; Proto-Oncogene Proteins/metabolism ; Recombinant Proteins/antagonists & inhibitors/isolation & purification/metabolism ; rap GTP-Binding Proteins
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 5
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    A phosphorylation site in the Na+ channel required for modulation by protein kinase C (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-11-08
    Beschreibung: Voltage-gated sodium channels are responsible for generation of action potentials in excitable cells. Activation of protein kinase C slows inactivation of sodium channels and reduces peak sodium currents. Phosphorylation of a single residue, serine 1506, that is located in the conserved intracellular loop between domains III and IV and is involved in inactivation of the sodium channel, is required for both modulatory effects. Mutant sodium channels lacking this phosphorylation site have normal functional properties in unstimulated cells but do not respond to activation of protein kinase C. Phosphorylation of this conserved site in sodium channel alpha subunits may regulate electrical activity in a wide range of excitable cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉West, J W -- Numann, R -- Murphy, B J -- Scheuer, T -- Catterall, W A -- GM07270/GM/NIGMS NIH HHS/ -- NS15751/NS/NINDS NIH HHS/ -- NS25704/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):866-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1658937" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Cell Membrane/physiology ; Cells, Cultured ; Membrane Potentials ; Models, Structural ; Molecular Sequence Data ; Phosphorylation ; Protein Conformation ; Protein Kinase C/*metabolism ; Sodium Channels/metabolism/*physiology
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 6
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    Split anergy in a CD8+ T cell: receptor-dependent cytolysis in the absence of interleukin-2 production (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-03-08
    Beschreibung: Engagement of the antigen-specific receptor (TCR) of CD4+ T lymphocytes without a second (costimulatory) signal prevents the subsequent production of interleukin-2 (IL-2) by these cells. Because IL-2 is a key immunoregulatory lymphokine and is also produced by a subset of CD8+ T cells that are able to kill target cells, the effect of engaging the TCR of one such clone in the absence of costimulatory signals was examined. The capacity for TCR-dependent IL-2 production was lost, indicating comparable costimulator-dependent signaling requirements for IL-2 production in CD4+ and CD8+ T cells. However, TCR-mediated cytotoxicity was not impaired, implying that costimulation is required for only certain TCR-dependent effector functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Otten, G R -- Germain, R N -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1228-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lymphocyte Biology Section, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1900952" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Antibodies, Monoclonal/immunology ; Antigen-Presenting Cells/immunology ; Antigens, CD8 ; Antigens, Differentiation, T-Lymphocyte/*immunology ; Female ; Interleukin-2/biosynthesis/*physiology ; Kinetics ; Lymphocyte Activation ; Mice ; Mice, Inbred Strains ; Ovalbumin/immunology ; Rats ; Receptors, Antigen, T-Cell/*immunology ; Spleen/immunology/radiation effects ; T-Lymphocytes/*immunology
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 7
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    The roles of the subunits in the function of the calcium channel (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-09-27
    Beschreibung: Dihydropyridine-sensitive voltage-dependent L-type calcium channels are critical to excitation-secretion and excitation-contraction coupling. The channel molecule is a complex of the main, pore-forming subunit alpha 1 and four additional subunits: alpha 2, delta, beta, and gamma (alpha 2 and delta are encoded by a single messenger RNA). The alpha 1 subunit messenger RNA alone directs expression of functional calcium channels in Xenopus oocytes, and coexpression of the alpha 2/delta and beta subunits enhances the amplitude of the current. The alpha 2, delta, and gamma subunits also have pronounced effects on its macroscopic characteristics, such as kinetics, voltage dependence of activation and inactivation, and enhancement by a dihydropyridine agonist. In some cases, specific modulatory functions can be assigned to individual subunits, whereas in other cases the different subunits appear to act in concert to modulate the properties of the channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Singer, D -- Biel, M -- Lotan, I -- Flockerzi, V -- Hofmann, F -- Dascal, N -- New York, N.Y. -- Science. 1991 Sep 27;253(5027):1553-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Pharmacology, Sackler School of Medicine, Tel Aviv University, Ramat Aviv, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1716787" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): 3-Pyridinecarboxylic acid, ; 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ; ester/pharmacology ; Animals ; Barium/pharmacology ; *Barium Compounds ; Cadmium/pharmacology ; Cadmium Chloride ; Calcium Channels/drug effects/genetics/*physiology ; *Chlorides ; Heart/physiology ; Kinetics ; Macromolecular Substances ; Membrane Potentials/drug effects ; Oocytes/physiology ; RNA, Messenger/genetics ; Xenopus
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 8
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    Transducin activation by rhodopsin without a covalent bond to the 11-cis-retinal chromophore (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-02-01
    Beschreibung: Rhodopsin and the visual pigments are a distinct group within the family of G-protein-linked receptors in that they have a covalently bound ligand, the 11-cis-retinal chromophore, whereas all of the other receptors bind their agonists through noncovalent interactions. The retinal chromophore in rhodopsin is bound by means of a protonated Schiff base linkage to the epsilon-amino group of Lys-296. Two rhodopsin mutants have been constructed, K296G and K296A, in which the covalent linkage to the chromophore is removed. Both mutants form a pigment with an absorption spectrum close to that of the wild type when reconstituted with the Schiff base of an n-alkylamine and 11-cis-retinal. In addition, the pigment formed from K296G and the n-propylamine Schiff base of 11-cis-retinal was found to activate transducin in a light-dependent manner, with 30 to 40% of the specific activity measured for the wild-type protein. It appears that the covalent bond is not essential for binding of the chromophore or for catalytic activation of transducin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhukovsky, E A -- Robinson, P R -- Oprian, D D -- 5T32 GM07596-11/GM/NIGMS NIH HHS/ -- EY07965/EY/NEI NIH HHS/ -- R01 EY007965/EY/NEI NIH HHS/ -- S07 RR07044/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 1;251(4993):558-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate Department of Biochemistry, Brandeis University, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1990431" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Binding Sites ; Guanosine 5'-O-(3-Thiotriphosphate)/metabolism ; Kinetics ; Mutagenesis, Site-Directed ; Protein Binding ; Retinaldehyde/*metabolism ; Rhodopsin/genetics/*metabolism/radiation effects ; Schiff Bases ; Spectrophotometry ; Transducin/*metabolism/radiation effects
    Print ISSN: 0036-8075
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 9
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    Modulation of cardiac sodium channels by cAMP receptors on the myocyte surface (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-09-13
    Beschreibung: The phosphorylation of the cardiac sodium channel by adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase A leads to its inactivation. It was shown that extracellular cAMP can also modulate the sodium channel of rat, guinea pig, and frog ventricular myocytes in a rapid (less than 50 milliseconds), reversible, and dose-dependent manner. The decrease in the sodium current was accompanied by a 10- to 15-millivolt shift in the steady-state availability of the sodium channel toward more negative potentials and was inhibited by guanosine-5'-O-(2-thiodiphosphate) or pertussis toxin, suggesting that the extracellular modulation of the sodium channel by cAMP is mediated by a membrane-delimited mechanism that includes a pertussis toxin-sensitive G protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sorbera, L A -- Morad, M -- HL16152/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 Sep 13;253(5025):1286-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Pennsylvania, Philadelphia 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1653970" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Cyclic AMP/*pharmacology ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Guanosine Diphosphate/analogs & derivatives/pharmacology ; Guinea Pigs ; Heart/drug effects/*physiology ; Isoproterenol/pharmacology ; Kinetics ; Membrane Potentials/drug effects ; Pertussis Toxin ; Rana pipiens ; Rats ; Receptors, Cyclic AMP/drug effects/*physiology ; Sodium Channels/drug effects/*physiology ; Thionucleotides/pharmacology ; Virulence Factors, Bordetella/pharmacology
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 10
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    Cloning and expression of a cocaine-sensitive rat dopamine transporter (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-10-25
    Beschreibung: The action of dopamine and other monoamine neurotransmitters at synapses is terminated predominantly by high-affinity reuptake into presynaptic terminals by specific sodium-dependent neurotransmitter transport proteins. A complementary DNA encoding a rat dopamine transporter has been isolated that exhibits high sequence similarity with the previously cloned norepinephrine and gamma-aminobutyric acid transporters. Transient expression of the complementary DNA in HeLa cells confirms the cocaine sensitivity of this transporter.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kilty, J E -- Lorang, D -- Amara, S G -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):578-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Yale University, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948035" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/drug effects/*genetics/metabolism ; Cloning, Molecular ; Cocaine/*pharmacology ; Dopamine/*metabolism ; Dopamine Plasma Membrane Transport Proteins ; Gene Expression ; HeLa Cells ; Humans ; Kinetics ; *Membrane Glycoproteins ; *Membrane Transport Proteins ; Molecular Sequence Data ; *Nerve Tissue Proteins ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction/methods ; Rats ; Sequence Homology, Nucleic Acid ; Transfection
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 11
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    Visualizing the higher order folding of a catalytic RNA molecule (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-01-25
    Beschreibung: The higher order folding process of the catalytic RNA derived from the self-splicing intron of Tetrahymena thermophila was monitored with the use of Fe(II)-EDTA-induced free radical chemistry. The overall tertiary structure of the RNA molecule forms cooperatively with the uptake of at least three magnesium ions. Local folding transitions display different metal ion dependencies, suggesting that the RNA tertiary structure assembles through a specific folding intermediate before the catalytic core is formed. Enzymatic activity, assayed with an RNA substrate that is complementary to the catalytic RNA active site, coincides with the cooperative structural transition. The higher order RNA foldings produced by Mg(II), Ca(II), and Sr(II) are similar; however, only the Mg(II)-stabilized RNA is catalytically active. Thus, these results directly demonstrate that divalent metal ions participate in general folding of the ribozyme tertiary structure, and further indicate a more specific involvement of Mg(II) in catalysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Celander, D W -- Cech, T R -- New York, N.Y. -- Science. 1991 Jan 25;251(4992):401-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309-0215.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1989074" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Base Sequence ; Calcium/metabolism ; Densitometry ; Kinetics ; Magnesium/metabolism ; Magnesium Chloride/pharmacology ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA, Catalytic/*chemistry/drug effects/metabolism ; Strontium/metabolism ; Tetrahymena
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 12
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    In vitro and in vivo consequences of VLA-2 expression on rhabdomyosarcoma cells (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-03-29
    Beschreibung: Cloned integrin alpha 2 subunit complementary DNA was expressed on human rhabdomyosarcoma (RD) cells to give a functional VLA-2 (alpha 2 beta 1) adhesion receptor. The VLA-2-positive RDA2 cells not only showed increased adhesion to collagen and laminin in vitro, but also formed substantially more metastatic tumor colonies in nude mice after either intravenous or subcutaneous injection. These results show that a specific adhesion receptor (VLA-2) can markedly enhance both experimental and spontaneous metastasis. In contrast to the metastasis results, there was no difference in either the in vitro growth rate or apparent in vivo tumorigenicity of RD and RDA2 cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, B M -- Matsuura, N -- Takada, Y -- Zetter, B R -- Hemler, M E -- CA 37393/CA/NCI NIH HHS/ -- GM 38903/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 29;251(5001):1600-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2011740" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; *Cell Adhesion ; Cell Line ; Collagen ; Fibronectins ; Humans ; Kinetics ; Laminin ; Lung Neoplasms/pathology/secondary ; Mice ; Mice, Nude ; Neoplasm Metastasis ; Neoplasm Transplantation ; Receptors, Very Late Antigen/genetics/*physiology ; Rhabdomyosarcoma/*pathology ; Transplantation, Heterologous
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 13
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    Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-07-26
    Beschreibung: The structure of a 20-amino acid peptide inhibitor bound to the catalytic subunit of cyclic AMP-dependent protein kinase, and its interactions with the enzyme, are described. The x-ray crystal structure of the complex is the basis of the analysis. The peptide inhibitor, derived from a naturally occurring heat-stable protein kinase inhibitor, contains an amphipathic helix that is followed by a turn and an extended conformation. The extended region occupies the cleft between the two lobes of the enzyme and contains a five-residue consensus recognition sequence common to all substrates and peptide inhibitors of the catalytic subunit. The helical portion of the peptide binds to a hydrophobic groove and conveys high affinity binding. Loops from both domains converge at the active site and contribute to a network of conserved residues at the sites of magnesium adenosine triphosphate binding and catalysis. Amino acids associated with peptide recognition, nonconserved, extend over a large surface area.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Knighton, D R -- Zheng, J H -- Ten Eyck, L F -- Xuong, N H -- Taylor, S S -- Sowadski, J M -- RR01644/RR/NCRR NIH HHS/ -- T32CA09523/CA/NCI NIH HHS/ -- T32DK07233/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 26;253(5018):414-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, San Diego, La Jolla 92093-0654.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1862343" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Carrier Proteins/*chemistry/metabolism ; Computer Simulation ; Enzyme Inhibitors/*chemistry ; *Intracellular Signaling Peptides and Proteins ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Kinases/*chemistry/metabolism ; X-Ray Diffraction
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 14
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    Protein kinase activity closely associated with a reconstituted calcium-activated potassium channel (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-08-02
    Beschreibung: Modulation of the activity of potassium and other ion channels is an essential feature of nervous system function. The open probability of a large conductance Ca(2+)-activated K+ channel from rat brain, incorporated into planar lipid bilayers, is increased by the addition of adenosine triphosphate (ATP) to the cytoplasmic side of the channel. This modulation takes place without the addition of protein kinase, requires Mg2+, and is mimicked by an ATP analog that serves as a substrate for protein kinases but not by a nonhydrolyzable ATP analog. Addition of protein phosphatase 1 reverses the modulation by MgATP. Thus, there may be an endogenous protein kinase activity firmly associated with this K+ channel. Some ion channels may exist in a complex that contains regulatory protein kinases and phosphatases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chung, S K -- Reinhart, P H -- Martin, B L -- Brautigan, D -- Levitan, I B -- DK31374/DK/NIDDK NIH HHS/ -- NS17910/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 2;253(5019):560-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate Department of Biochemistry, Brandeis University, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1857986" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenosine Triphosphate/pharmacology ; Animals ; Brain/*physiology ; Calcium/*pharmacology ; Kinetics ; Lipid Bilayers ; Potassium Channels/drug effects/metabolism/*physiology ; Protein Kinases/*metabolism ; Rats
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 15
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    A heparin-binding growth factor secreted by macrophage-like cells that is related to EGF (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-02-22
    Beschreibung: Macrophage-like U-937 cells secrete a 22-kilodalton heparin-binding growth factor that is mitogenic for BALB-3T3 fibroblasts and smooth muscle cells, but not endothelial cells. The amino acid sequence predicted from complementary DNA clones indicates that the mitogen is a new member of the epidermal growth factor (EGF) family. This heparin-binding EGF-like growth factor (HB-EGF) binds to EGF receptors on A-431 epidermoid carcinoma cells and smooth muscle cells, but is a far more potent mitogen for smooth muscle cells than is EGF. HB-EGF is also expressed in cultured human macrophages and may be involved in macrophage-mediated cellular proliferation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Higashiyama, S -- Abraham, J A -- Miller, J -- Fiddes, J C -- Klagsbrun, M -- CA37392/CA/NCI NIH HHS/ -- CA45548/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 22;251(4996):936-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Surgical Research, Children's Hospital, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1840698" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Cell Division/drug effects ; Cell Line ; Chromatography, Affinity ; Chromatography, High Pressure Liquid ; DNA Replication/drug effects ; Epidermal Growth Factor/genetics/isolation & ; purification/*metabolism/pharmacology ; Growth Substances/*metabolism ; Heparin/*metabolism ; Humans ; Kinetics ; Macrophages/*metabolism ; Molecular Sequence Data ; Protein Binding ; Receptor, Epidermal Growth Factor/metabolism ; Sequence Homology, Nucleic Acid
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 16
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    Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-08-23
    Beschreibung: The three-dimensional structure of acetylcholinesterase from Torpedo californica electric organ has been determined by x-ray analysis to 2.8 angstrom resolution. The form crystallized is the glycolipid-anchored homodimer that was purified subsequent to solubilization with a bacterial phosphatidylinositol-specific phospholipase C. The enzyme monomer is an alpha/beta protein that contains 537 amino acids. It consists of a 12-stranded mixed beta sheet surrounded by 14 alpha helices and bears a striking resemblance to several hydrolase structures including dienelactone hydrolase, serine carboxypeptidase-II, three neutral lipases, and haloalkane dehalogenase. The active site is unusual because it contains Glu, not Asp, in the Ser-His-acid catalytic triad and because the relation of the triad to the rest of the protein approximates a mirror image of that seen in the serine proteases. Furthermore, the active site lies near the bottom of a deep and narrow gorge that reaches halfway into the protein. Modeling of acetylcholine binding to the enzyme suggests that the quaternary ammonium ion is bound not to a negatively charged "anionic" site, but rather to some of the 14 aromatic residues that line the gorge.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sussman, J L -- Harel, M -- Frolow, F -- Oefner, C -- Goldman, A -- Toker, L -- Silman, I -- New York, N.Y. -- Science. 1991 Aug 23;253(5022):872-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Chemistry, Weizmann Institute of Science, Rehovot, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1678899" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Acetylcholine/*metabolism ; Acetylcholinesterase/*chemistry/metabolism ; Amino Acid Sequence ; Animals ; Binding Sites ; Cell Membrane/enzymology ; Chemistry, Physical ; Crystallization ; Electric Organ/*enzymology ; Glutamates ; Glutamic Acid ; Macromolecular Substances ; Molecular Sequence Data ; Molecular Structure ; Phosphatidylinositols/metabolism ; Physicochemical Phenomena ; Protein Conformation ; Sequence Homology, Nucleic Acid ; *Torpedo ; X-Ray Diffraction
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 17
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    Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-12-09
    Beschreibung: The three-dimensional structure of an active, disulfide cross-linked dimer of the ligand-binding domain of the Salmonella typhimurium aspartate receptor and that of an aspartate complex have been determined by x-ray crystallographic methods at 2.4 and 2.0 angstrom (A) resolution, respectively. A single subunit is a four-alpha-helix bundle with two long amino-terminal and carboxyl-terminal helices and two shorter helices that form a cylinder 20 A in diameter and more than 70 A long. The two subunits in the disulfide-bonded dimer are related by a crystallographic twofold axis in the apo structure, but by a noncrystallographic twofold axis in the aspartate complex structure. The latter structure reveals that the ligand binding site is located more than 60 A from the presumed membrane surface and is at the interface of the two subunits. Aspartate binds between two alpha helices from one subunit and one alpha helix from the other in a highly charged pocket formed by three arginines. The comparison of the apo and aspartate complex structures shows only small structural changes in the individual subunits, except for one loop region that is disordered, but the subunits appear to change orientation relative to each other. The structures of the two forms of this protein provide a step toward understanding the mechanisms of transmembrane signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milburn, M V -- Prive, G G -- Milligan, D L -- Scott, W G -- Yeh, J -- Jancarik, J -- Koshland, D E Jr -- Kim, S H -- AI 30725/AI/NIAID NIH HHS/ -- DK09765/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1342-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1660187" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Aspartic Acid/metabolism ; Binding Sites ; Disulfides/analysis ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; *Receptors, Amino Acid ; Receptors, Cell Surface/*chemistry/metabolism ; Salmonella typhimurium/metabolism ; X-Ray Diffraction
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 18
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    Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-03-22
    Beschreibung: Defensins (molecular weight 3500 to 4000) act in the mammalian immune response by permeabilizing the plasma membranes of a broad spectrum of target organisms, including bacteria, fungi, and enveloped viruses. The high-resolution crystal structure of defensin HNP-3 (1.9 angstrom resolution, R factor 0.19) reveals a dimeric beta sheet that has an architecture very different from other lytic peptides. The dimeric assembly suggests mechanisms by which defensins might bind to and permeabilize the lipid bilayer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hill, C P -- Yee, J -- Selsted, M E -- Eisenberg, D -- New York, N.Y. -- Science. 1991 Mar 22;251(5000):1481-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Eisenberg, Molecular Biology Institute, Los Angeles, CA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2006422" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Blood Proteins/chemistry/*ultrastructure ; Cell Membrane Permeability ; Crystallography ; Defensins ; Guinea Pigs ; Humans ; Macromolecular Substances ; Membrane Proteins/chemistry/ultrastructure ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Protein Conformation ; Rabbits ; Rats ; Structure-Activity Relationship ; X-Ray Diffraction ; *alpha-Defensins
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 19
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    Similarity of protein G and ubiquitin (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-10-25
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kraulis, P J -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):581-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1658931" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Binding Sites, Antibody ; Immunoglobulin G ; Models, Molecular ; Molecular Sequence Data ; Nerve Tissue Proteins/*chemistry/genetics/immunology ; Protein Conformation ; Sequence Homology, Nucleic Acid ; Ubiquitins/*chemistry/genetics
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 20
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    A neuron-silicon junction: a Retzius cell of the leech on an insulated-gate field-effect transistor (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-05-31
    Beschreibung: An identified neuron of the leech, a Retzius cell, has been attached to the open gate of a p-channel field-effect transistor. Action potentials, spontaneous or stimulated, modulate directly the source-drain current in silicon. The electronic signals match the shape of the action potential. The average voltage on the gate was up to 25 percent of the intracellular voltage change. Occasionally weak signals that resemble the first derivative of the action potential were observed. The junctions can be described by a model that includes capacitive coupling of the plasma membrane and the gate oxide and that accounts for variable resistance of the seal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fromherz, P -- Offenhausser, A -- Vetter, T -- Weis, J -- New York, N.Y. -- Science. 1991 May 31;252(5010):1290-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Abteilung Biophysik der Universitat Ulm, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925540" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Action Potentials ; Animals ; Electric Conductivity ; Electrophysiology ; Kinetics ; Leeches/*physiology ; Microscopy, Electron, Scanning ; Neurons/*physiology/ultrastructure ; *Silicon ; Transistors, Electronic
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 21
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    Modulation of the time course of fast EPSCs and glutamate channel kinetics by aniracetam (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-10-11
    Beschreibung: It is generally accepted that glutamate serves as the neurotransmitter at most excitatory synapses in the mammalian central nervous system (CNS). Synaptic release of glutamate may trigger a fast and a slow excitatory postsynaptic current (EPSC). The slow EPSC is mediated by N-methyl-D-aspartate (NMDA) receptor channels, whereas the fast EPSC is mediated by non-NMDA receptor channels. The nootropic agent aniracetam selectively and reversibly slows the desensitization kinetics of non-NMDA channels and lengthens their single-channel open times. Antiracetam also modulates the kinetics of the fast EPSC in a manner that mirrors its action on the kinetics of the non-NMDA channels. These results support the hypothesis that the properties of the non-NMDA glutamate channels rather than the rate of neurotransmitter clearance are the primary determinants of the kinetics of the fast EPSC in the mammalian CNS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tang, C M -- Shi, Q Y -- Katchman, A -- Lynch, G -- NS28158/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 11;254(5029):288-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, University of Pennsylvania, Philadelphia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1681589" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Action Potentials/*drug effects ; Animals ; Glutamates/*physiology ; Glutamic Acid ; Kinetics ; Pyrrolidinones/*pharmacology ; Rats ; Receptors, Glutamate ; Receptors, N-Methyl-D-Aspartate/drug effects ; Receptors, Neurotransmitter/drug effects ; Synapses/*drug effects
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 22
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    Pulmonary surfactant protein B (SP-B): structure-function relationships (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-10-25
    Beschreibung: SP-B is a protein in pulmonary surfactant that is, in greatest part, responsible for resistance to surface tension and prevention of collapse of pulmonary alveoli. Peptides of 21 residues, synthesized following the sequence of SP-B or resembling the hydrophobic and hydrophilic domains of SP-B (such as RLLLLRLLLLRLLLLRLLLLR, R, Arg, and L, Leu), enhanced the abilities of phospholipids to reduce surface tension both in vitro and in vivo. Intermittent positively charged residues were essential for this activity. The SP-B-like peptides were found by tryptophan fluorescence to partition within the phospholipid layer in contact with both polar head groups and acyl side chains. These data, together with findings that the SP-B-related peptides increase inter- and intramolecular order of the phospholipid layer, suggest that SP-B resists surface tension by increasing lateral stability of the phospholipid layer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cochrane, C G -- Revak, S D -- GM-37696/GM/NIGMS NIH HHS/ -- HL-23584/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):566-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948032" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Kinetics ; Molecular Sequence Data ; Peptides/*chemical synthesis/chemistry ; Phospholipids/metabolism ; Proteolipids/chemistry/*metabolism ; Pulmonary Surfactants/chemistry/*metabolism ; Structure-Activity Relationship ; Surface Tension
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 23
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    Specific DNA binding by c-Myb: evidence for a double helix-turn-helix-related motif (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-09-06
    Beschreibung: The c-Myb protein is a sequence-specific DNA binding protein that activates transcription in hematopoietic cells. Three imperfect repeats (R1, R2, and R3) that contain regularly spaced tryptophan residues form the DNA binding domain of c-Myb. A fragment of c-Myb that contained the R2 and R3 regions bound specifically to a DNA sequence recognized by c-Myb plus ten additional base pairs at the 3' end of the element. The R2R3 fragment was predicted to contain two consecutive helix-turn-helix (HTH) motifs with unconventional turns. Mutagenesis of amino acids in R2R3 at positions that correspond to DNA-contacting amino acids in other HTH-containing proteins abolished specific DNA binding without affecting nonspecific DNA interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gabrielsen, O S -- Sentenac, A -- Fromageot, P -- New York, N.Y. -- Science. 1991 Sep 6;253(5024):1140-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire d'Ingenierie des Proteines, Centre d'Etudes de Saclay, Gif-sur-Yvette, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1887237" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Chickens ; DNA/*metabolism ; DNA-Binding Proteins/*metabolism ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oligonucleotide Probes ; Oncogenes ; Polymerase Chain Reaction ; Protein Conformation ; Proto-Oncogene Proteins/genetics/*metabolism ; Proto-Oncogene Proteins c-myb ; Recombinant Proteins/metabolism ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; Transcription Factors/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 24
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    Ca(2+)-induced Ca2+ release in sea urchin egg homogenates: modulation by cyclic ADP-ribose (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-09-06
    Beschreibung: Calcium-induced calcium release (CICR) may function widely in calcium-mediated cell signaling, but has been most thoroughly characterized in muscle cells. In a homogenate of sea urchin eggs, which display transients in the intracellular free calcium concentration ([Ca2+]i) during fertilization and anaphase, addition of Ca2+ triggered CICR. Ca2+ release was also induced by the CICR modulators ryanodine and caffeine. Responses to both Ca2+ and CICR modulators (but not Ca2+ release mediated by inositol 1,4,5-trisphosphate) were inhibited by procaine and ruthenium red, inhibitors of CICR. Intact eggs also displayed transients of [Ca2+]i when microinjected with ryanodine. Cyclic ADP-ribose, a metabolite with potent Ca(2+)-releasing properties, appears to act by way of the CICR mechanism and may thus be an endogenous modulator of CICR. A CICR mechanism is present in these nonmuscle cells as is assumed in various models of intracellular Ca2+ wave propagation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Galione, A -- Lee, H C -- Busa, W B -- HD17484/HD/NICHD NIH HHS/ -- HD22879/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1991 Sep 6;253(5024):1143-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Johns Hopkins University, Baltimore, MD 21218.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1909457" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenosine Diphosphate Ribose/*pharmacology ; Adenosine Triphosphate/metabolism ; Animals ; Calcium/*metabolism/pharmacology ; Cyclic ADP-Ribose ; Egtazic Acid/pharmacology ; Kinetics ; Ovum/drug effects/*physiology ; Sea Urchins ; Spectrometry, Fluorescence ; Time Factors
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 25
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    Engineered metal-binding proteins: purification to protein folding (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-06-28
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arnold, F H -- Haymore, B L -- New York, N.Y. -- Science. 1991 Jun 28;252(5014):1796-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1648261" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Binding Sites ; Carrier Proteins/*chemical synthesis/chemistry/isolation & purification ; Cytochrome c Group/chemistry ; Histidine ; Ligands ; Metals/*metabolism ; Models, Molecular ; Protein Conformation ; *Protein Engineering
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 26
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    A component of calcium-activated potassium channels encoded by the Drosophila slo locus (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-08-02
    Beschreibung: Calcium-activated potassium channels mediate many biologically important functions in electrically excitable cells. Despite recent progress in the molecular analysis of voltage-activated K+ channels, Ca(2+)-activated K+ channels have not been similarly characterized. The Drosophila slowpoke (slo) locus, mutations of which specifically abolish a Ca(2+)-activated K+ current in muscles and neurons, provides an opportunity for molecular characterization of these channels. Genomic and complementary DNA clones from the slo locus were isolated and sequenced. The polypeptide predicted by slo is similar to voltage-activated K+ channel polypeptides in discrete domains known to be essential for function. Thus, these results indicate that slo encodes a structural component of Ca(2+)-activated K+ channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Atkinson, N S -- Robertson, G A -- Ganetzky, B -- NS15390/NS/NINDS NIH HHS/ -- T32 GM07131/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 2;253(5019):551-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genetics, University of Wisconsin, Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1857984" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Calcium/pharmacology ; Chromosome Aberrations ; Chromosome Deletion ; Cloning, Molecular ; DNA/genetics/isolation & purification ; Drosophila/*genetics/physiology ; Exons ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Phenotype ; Potassium Channels/drug effects/*genetics/physiology ; Protein Conformation ; Sequence Homology, Nucleic Acid ; Transcription, Genetic ; Translocation, Genetic
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 27
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    Requirement of GTP hydrolysis for dissociation of the signal recognition particle from its receptor (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-05-24
    Beschreibung: The signal recognition particle (SRP) directs signal sequence specific targeting of ribosomes to the rough endoplasmic reticulum. Displacement of the SRP from the signal sequence of a nascent polypeptide is a guanosine triphosphate (GTP)-dependent reaction mediated by the membrane-bound SRP receptor. A nonhydrolyzable GTP analog can replace GTP in the signal sequence displacement reaction, but the SRP then fails to dissociate from the membrane. Complexes of the SRP with its receptor containing the nonhydrolyzable analog are incompetent for subsequent rounds of protein translocation. Thus, vectorial targeting of ribosomes to the endoplasmic reticulum is controlled by a GTP hydrolysis cycle that regulates the affinity between the SRP, signal sequences, and the SRP receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Connolly, T -- Rapiejko, P J -- Gilmore, R -- GM 35687/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 24;252(5009):1171-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester 01655.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1851576" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Centrifugation, Density Gradient ; Endoplasmic Reticulum/metabolism ; GTP-Binding Proteins/genetics/metabolism ; Guanosine Triphosphate/*metabolism ; Guanylyl Imidodiphosphate/pharmacology ; Hydrolysis ; Kinetics ; Macromolecular Substances ; Protein Binding ; Protein Biosynthesis ; Receptors, Cell Surface/isolation & purification/*metabolism ; *Receptors, Cytoplasmic and Nuclear ; *Receptors, Peptide ; Ribonucleoproteins/genetics/isolation & purification/*metabolism ; Ribosomes/metabolism ; Signal Recognition Particle ; Transcription, Genetic ; Vesicular stomatitis Indiana virus/genetics/metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 28
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    First protein kinase structure (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-07-26
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, M -- New York, N.Y. -- Science. 1991 Jul 26;253(5018):383.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1862341" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Carrier Proteins/chemistry/metabolism ; Enzyme Inhibitors/chemistry ; *Intracellular Signaling Peptides and Proteins ; Models, Molecular ; Protein Conformation ; Protein Kinases/*chemistry/metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 29
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    The N-end rule in bacteria (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-11-29
    Beschreibung: The N-end rule relates the in vivo half-life of a protein to the identity of its amino-terminal residue. Distinct versions of the N-end rule operate in all eukaryotes examined. It is shown that the bacterium Escherichia coli also has the N-end rule pathway. Amino-terminal arginine, lysine, leucine, phenylalanine, tyrosine, and tryptophan confer 2-minute half-lives on a test protein; the other amino-terminal residues confer greater than 10-hour half-lives on the same protein. Amino-terminal arginine and lysine are secondary destabilizing residues in E. coli because their activity depends on their conjugation to the primary destabilizing residues leucine or phenylalanine by leucine, phenylalanine-transfer RNA-protein transferase. The adenosine triphosphate-dependent protease Clp (Ti) is required for the degradation of N-end rule substrates in E. coli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tobias, J W -- Shrader, T E -- Rocap, G -- Varshavsky, A -- DK39520/DK/NIDDK NIH HHS/ -- GM31530/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1374-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1962196" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Bacteria/*metabolism ; Bacterial Proteins/*metabolism ; Escherichia coli/enzymology/metabolism ; Half-Life ; Kinetics ; Molecular Sequence Data ; Rabbits ; Reticulocytes/metabolism ; Saccharomyces cerevisiae/enzymology/metabolism ; Structure-Activity Relationship ; beta-Galactosidase/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 30
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    Stimulation of protein tyrosine phosphorylation by NMDA receptor activation (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-08-23
    Beschreibung: The N-methyl-D-aspartate (NMDA) receptor, a subtype of glutamate receptors, plays a key role in synaptic plasticity in the nervous system. After NMDA receptor activation, calcium entry into the postsynaptic neuron is a critical initial event. However, the subsequent mechanisms by which the NMDA receptor signal is processed are incompletely understood. Stimulation of cultured rat hippocampal cells with glutamate resulted in the rapid and transient tyrosine phosphorylation of a 39-kilodalton protein (p39). Tyrosine phosphorylation of p39 was triggered by the NMDA receptor and required an influx of Ca2+ from the extracellular medium. Because p39 was found to be highly related or identical to the microtubule-associated protein 2 kinase, the NMDA receptor signal may be processed by a sequential activation of protein kinases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bading, H -- Greenberg, M E -- CA 43855/CA/NCI NIH HHS/ -- NS 28829/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 23;253(5022):912-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1715095" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): 2-Amino-5-phosphonovalerate/pharmacology ; Animals ; Calcium/metabolism ; Calcium-Calmodulin-Dependent Protein Kinases ; Cells, Cultured ; Glutamates/pharmacology ; Glutamic Acid ; Hippocampus/drug effects/metabolism ; Immunoblotting ; Kinetics ; Phosphoproteins/*metabolism ; Phosphorylation ; Phosphotyrosine ; Protein Kinases/metabolism ; Rats ; Receptors, N-Methyl-D-Aspartate/*metabolism ; Tyrosine/*analogs & derivatives/metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 31
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    Critical structural elements of the VP16 transcriptional activation domain (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-01-04
    Beschreibung: Virion protein 16 (VP16) of herpes simplex virus type 1 contains an acidic transcriptional activation domain. Missense mutations within this domain have provided insights into the structural elements critical for its function. Net negative charge contributed to, but was not sufficient for, transcriptional activation by VP16. A putative amphipathic alpha helix did not appear to be an important structural component of the activation domain. A phenylalanine residue at position 442 was exquisitely sensitive to mutation. Transcriptional activators of several classes contain hydrophobic amino acids arranged in patterns resembling that of VP16. Therefore, the mechanism of transcriptional activation by VP16 and other proteins may involve both ionic and specific hydrophobic interactions with target molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cress, W D -- Triezenberg, S J -- AI 27323/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1991 Jan 4;251(4989):87-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Michigan State University, East Lansing 48824-1319.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1846049" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; *Immediate-Early Proteins ; Molecular Sequence Data ; Mutation ; Protein Conformation ; *Simplexvirus ; Structure-Activity Relationship ; Transcription Factors/*chemistry/genetics/pharmacology ; Transcription, Genetic/*drug effects ; Transfection ; Viral Proteins/*genetics ; Virion
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 32
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    Membrane-mediated assembly of filamentous bacteriophage Pf1 coat protein (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-05-31
    Beschreibung: Filamentous bacteriophage Pf1 assembles by a membrane-mediated process during which the viral DNA is secreted through the membrane while being encapsulated by the major coat protein. Neutron diffraction studies showed that in the virus most of the coat protein consists of two alpha-helical segments arranged end-to-end with an intervening mobile surface loop. Nuclear magnetic resonance studies of the coat protein in the membrane-bound form have shown that the secondary structure is essentially identical to that in the intact virus. A comparison indicates that during membrane-mediated viral assembly, while the secondary structure of the coat protein is largely conserved, its tertiary structure changes substantially.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nambudripad, R -- Stark, W -- Opella, S J -- Makowski, L -- New York, N.Y. -- Science. 1991 May 31;252(5010):1305-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, Boston University, MA 02215.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925543" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Bacteriophages/chemistry ; Capsid/*chemistry/metabolism ; *Capsid Proteins ; Cell Membrane/*metabolism ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Structure ; Neutrons ; Protein Conformation
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 33
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    Dynamic tracking of cardiac vulnerability by complex demodulation of the T wave (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-04-19
    Beschreibung: A link is found between T wave alternans and vulnerability to ventricular fibrillation, and a new approach is provided for quantification of susceptibility to malignant arrhythmias. Complex demodulation reveals that alternation of the electrocardiogram is concentrated during the first half of the T wave, coinciding with the vulnerable period of the cardiac cycle. During myocardial ischemia and reperfusion, there are marked increases in the degree of T wave alternans that parallel the established time course of changes in vulnerability. The influence of the sympathetic nervous system in arrhythmogenesis is also accurately detected. Ultimately, complex demodulation of the electrocardiogram could provide a technique for identification and management of individuals at risk for sudden cardiac death.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nearing, B D -- Huang, A H -- Verrier, R L -- HL-33567/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 Apr 19;252(5004):437-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Georgetown University School of Medicine, Washington, DC 20007.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2017682" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Constriction ; Coronary Vessels ; Dogs ; Electric Stimulation ; *Electrocardiography ; Electrophysiology ; Female ; Heart Conduction System/*physiopathology ; Kinetics ; Male ; Mathematics ; Reperfusion ; Ventricular Fibrillation/*physiopathology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 34
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    Regulation of phospholipase C-gamma 1 by profilin and tyrosine phosphorylation (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-03-08
    Beschreibung: Epidermal growth factor and platelet-derived growth factor can stimulate the production of the second messenger inositol trisphosphate in responsive cells, but the biochemical pathway for these signaling events has been uncertain because the reactions have not been reconstituted with purified molecules in vitro. A reconstitution is described that requires not only the growth factor, its receptor with tyrosine kinase activity, and the soluble phospholipase C-gamma 1, but also the small soluble actin-binding protein profilin. Profilin binds to the substrate phosphatidylinositol 4,5-bisphosphate and inhibits its hydrolysis by unphosphorylated phospholipase C-gamma 1. Phosphorylation of phospholipase C-gamma 1 by the epidermal growth factor receptor tyrosine kinase overcomes the inhibitory effect of profilin and results in an effective activation of phospholipase C-gamma 1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldschmidt-Clermont, P J -- Kim, J W -- Machesky, L M -- Rhee, S G -- Pollard, T D -- GM-26338/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1231-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Anatomy, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1848725" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Contractile Proteins/metabolism ; Epidermal Growth Factor/*metabolism ; Inositol Phosphates/metabolism ; Isoenzymes/*metabolism ; Kinetics ; Microfilament Proteins/*metabolism ; Phosphatidylinositol 4,5-Diphosphate ; Phosphatidylinositols/metabolism ; Phosphorylation ; Profilins ; Protein-Tyrosine Kinases/*metabolism ; Receptor, Epidermal Growth Factor/*metabolism ; Signal Transduction ; Type C Phospholipases/*metabolism ; Tyrosine
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 35
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    Cloning of complementary DNA encoding a functional human interleukin-8 receptor (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-09-13
    Beschreibung: Interleukin-8 (IL-8) is an inflammatory cytokine that activates neutrophil chemotaxis, degranulation, and the respiratory burst. Neutrophils express receptors for IL-8 that are coupled to guanine nucleotide-binding proteins (G proteins); binding of IL-8 to its receptor induces the mobilization of intracellular calcium stores. A cDNA clone from HL-60 neutrophils, designated p2, has now been isolated that encodes a human IL-8 receptor. When p2 is expressed in oocytes from Xenopus laevis, the oocytes bind 125I-labeled IL-8 specifically and respond to IL-8 by mobilizing calcium stores with an EC50 of 20 nM. This IL-8 receptor has 77% amino acid identity with a second human neutrophil receptor isotype that binds IL-8 with higher affinity. It also exhibits 69% amino acid identity with a protein reported to be an N-formyl peptide receptor from rabbit neutrophils, but less than 30% identity with all other known G protein-coupled receptors, including the human N-formyl peptide receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murphy, P M -- Tiffany, H L -- New York, N.Y. -- Science. 1991 Sep 13;253(5025):1280-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Host Defenses, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1891716" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Binding, Competitive ; Cloning, Molecular/methods ; DNA/genetics ; Gene Library ; Humans ; Interleukin-8/*metabolism/pharmacology ; Kinetics ; Molecular Sequence Data ; Neutrophils/immunology ; Oocytes/drug effects/physiology ; Protein Biosynthesis ; Rabbits ; Receptors, Immunologic/drug effects/*genetics/physiology ; Receptors, Interleukin-8A ; Recombinant Proteins/metabolism ; Sequence Homology, Nucleic Acid ; Signal Transduction ; Transcription, Genetic ; Xenopus
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 36
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    Molecular basis of gating charge immobilization in Shaker potassium channels (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-11-01
    Beschreibung: Voltage-dependent ion channels respond to changes in the membrane potential by means of charged voltage sensors intrinsic to the channel protein. Changes in transmembrane potential cause movement of these charged residues, which results in conformational changes in the channel. Movements of the charged sensors can be detected as currents known as gating currents. Measurement of the gating currents of the Drosophila Shaker potassium channel indicates that the charge on the voltage sensor of the channels is progressively immobilized by prolonged depolarizations. The charge is not immobilized in a mutant of the channel that lacks inactivation. These results show that the region of the molecule responsible for inactivation interacts, directly or indirectly, with the voltage sensor to prevent the return of the charge to its original position. The gating transitions between closed states of the channel appear not to be independent, suggesting that the channel subunits interact during activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bezanilla, F -- Perozo, E -- Papazian, D M -- Stefani, E -- GM30376/GM/NIGMS NIH HHS/ -- GM43459/GM/NIGMS NIH HHS/ -- HL37044/HL/NHLBI NIH HHS/ -- R01 GM043459/GM/NIGMS NIH HHS/ -- R01 GM043459-09/GM/NIGMS NIH HHS/ -- R01 GM043459-10/GM/NIGMS NIH HHS/ -- R01 GM043459-11/GM/NIGMS NIH HHS/ -- R01 GM043459-12/GM/NIGMS NIH HHS/ -- R01 GM043459-13/GM/NIGMS NIH HHS/ -- R01 GM043459-14/GM/NIGMS NIH HHS/ -- R01 GM043459-15/GM/NIGMS NIH HHS/ -- R01 GM043459-15S1/GM/NIGMS NIH HHS/ -- R01 GM043459-16/GM/NIGMS NIH HHS/ -- R01 GM043459-17/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Nov 1;254(5032):679-83.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, UCLA School of Medicine 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948047" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Drosophila/physiology ; *Ion Channel Gating/drug effects ; Kinetics ; Mutagenesis, Site-Directed ; Oocytes/drug effects/physiology ; Potassium Channels/drug effects/genetics/*physiology ; Tetraethylammonium ; Tetraethylammonium Compounds/pharmacology ; Xenopus
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 37
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    Transmission between pairs of hippocampal slice neurons: quantal levels, oscillations, and LTP (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-05-03
    Beschreibung: Long-term potentiation (LTP) of synaptic transmission after coincident pre- and postsynaptic activity is considered a cellular model of changes underlying learning and memory. In intact tissue, LTP has been observed only between populations of neurons, making analysis of mechanisms difficult. Transmission between individual pre- and postsynaptic hippocampal cells was studied, suggesting quantal amplitude distributions with little variability in quantal size. LTP between such pairs is manifested by large, persistent, and synapse-specific potentiation with a shift in amplitude distribution that suggests presynaptic changes. Oscillations in amplitude of transmission, apparently of presynaptic origin, are common and can be triggered by LTP.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Malinow, R -- New York, N.Y. -- Science. 1991 May 3;252(5006):722-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Physiology, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1850871" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Electric Conductivity ; Electrophysiology ; Hippocampus/*cytology ; Kinetics ; Membrane Potentials ; Neurons/*physiology ; Rats ; Statistics as Topic ; Synapses/*physiology ; Synaptic Transmission/*physiology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 38
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    Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-06-28
    Beschreibung: Human apolipoprotein E, a blood plasma protein, mediates the transport and uptake of cholesterol and lipid by way of its high affinity interaction with different cellular receptors, including the low-density lipoprotein (LDL) receptor. The three-dimensional structure of the LDL receptor-binding domain of apoE has been determined at 2.5 angstrom resolution by x-ray crystallography. The protein forms an unusually elongated (65 angstroms) four-helix bundle, with the helices apparently stabilized by a tightly packed hydrophobic core that includes leucine zipper-type interactions and by numerous salt bridges on the mostly charged surface. Basic amino acids important for LDL receptor binding are clustered into a surface patch on one long helix. This structure provides the basis for understanding the behavior of naturally occurring mutants that can lead to atherosclerosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, C -- Wardell, M R -- Weisgraber, K H -- Mahley, R W -- Agard, D A -- HL-41633/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 Jun 28;252(5014):1817-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, San Francisco 94143-0448.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2063194" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Apolipoproteins E/*chemistry/genetics/metabolism ; Binding Sites ; Computer Graphics ; Humans ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Receptors, LDL/*metabolism ; X-Ray Diffraction
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 39
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    Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-11-08
    Beschreibung: The three-dimensional structure of the lactose complex of the Erythrina corallodendron lectin (EcorL), a dimer of N-glycosylated subunits, was determined crystallographically and refined at 2.0 angstrom resolution to an R value of 0.19. The tertiary structure of the subunit is similar to that of other legume lectins, but interference by the bulky N-linked heptasaccharide, which is exceptionally well ordered in the crystal, forces the EcorL dimer into a drastically different quaternary structure. Only the galactose moiety of the lactose ligand resides within the combining site. The galactose moiety is oriented differently from ligands in the mannose-glucose specific legume lectins and is held by hydrophobic interactions with Ala88, Tyr106, Phe131, and Ala218 and by seven hydrogen bonds, four of which are to the conserved Asp89, Asn133, and NH of Gly107. The specificity of legume lectins toward the different C-4 epimers appears to be associated with extensive variations in the outline of the variable parts of the binding sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shaanan, B -- Lis, H -- Sharon, N -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):862-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948067" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Carbohydrate Conformation ; Carbohydrate Sequence ; Computer Simulation ; Erythrina ; Glycosylation ; Hydrogen Bonding ; Lectins/*chemistry ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Oligosaccharides ; Plant Lectins ; Plants, Medicinal ; Protein Conformation ; X-Ray Diffraction
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 40
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    Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-05-31
    Beschreibung: The crystal structure of a murine adenosine deaminase complexed with 6-hydroxyl-1,6-dihydropurine ribonucleoside, a nearly ideal transition-state analog, has been determined and refined at 2.4 angstrom resolution. The structure is folded as an eight-stranded parallel alpha/beta barrel with a deep pocket at the beta-barrel COOH-terminal end wherein the inhibitor and a zinc are bound and completely sequestered. The presence of the zinc cofactor and the precise structure of the bound analog were not previously known. The 6R isomer of the analog is very tightly held in place by the coordination of the 6-hydroxyl to the zinc and the formation of nine hydrogen bonds. On the basis of the structure of the complex a stereoselective addition-elimination or SN2 mechanism of the enzyme is proposed with the zinc atom and the Glu and Asp residues playing key roles. A molecular explanation of a hereditary disease caused by several point mutations of an enzyme is also presented.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, D K -- Rudolph, F B -- Quiocho, F A -- CA14030/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 31;252(5010):1278-84.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925539" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenosine Deaminase/*chemistry/deficiency/metabolism ; Amino Acid Sequence ; Animals ; Binding Sites ; Catalysis ; Crystallization ; Immunologic Deficiency Syndromes/*enzymology/genetics ; Mice ; Models, Molecular ; Molecular Structure ; Mutation ; Protein Conformation ; Purine Nucleosides/chemistry/*metabolism ; Ribonucleosides/chemistry/*metabolism ; Zinc/metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 41
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    The trk proto-oncogene product: a signal transducing receptor for nerve growth factor (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-04-26
    Beschreibung: The trk proto-oncogene encodes a 140-kilodalton, membrane-spanning protein tyrosine kinase (p140prototrk) that is expressed only in neural tissues. Nerve growth factor (NGF) stimulates phosphorylation of p140prototrk in neural cell lines and in embryonic dorsal root ganglia. Affinity cross-linking and equilibrium binding experiments with 125I-labeled NGF indicate that p140prototrk binds NGF specifically in cultured cells with a dissociation constant of 10(-9) molar. The identification of p140prototrk as an NGF receptor indicates that this protein participates in the primary signal transduction mechanism of NGF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaplan, D R -- Hempstead, B L -- Martin-Zanca, D -- Chao, M V -- Parada, L F -- N01-CO-74101/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Apr 26;252(5005):554-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Eukaryotic Signal Transduction Group, National Cancer Institute-Frederick Cancer Research and Development Center, MD 21702.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1850549" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Cell Line ; Cell Membrane/physiology ; Cross-Linking Reagents ; Embryo, Mammalian ; Ganglia, Spinal/*metabolism ; Humans ; Kinetics ; Mice ; Nerve Growth Factors/metabolism/*physiology ; Neuroblastoma ; Protein-Tyrosine Kinases/*metabolism ; Proto-Oncogene Proteins/*metabolism ; *Proto-Oncogenes ; Receptor, trkA ; Receptors, Cell Surface/metabolism/*physiology ; Receptors, Nerve Growth Factor ; *Signal Transduction
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 42
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    Refined structure of charybdotoxin: common motifs in scorpion toxins and insect defensins (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-12-06
    Beschreibung: Conflicting three-dimensional structures of charybdotoxin (Chtx), a blocker of K+ channels, have been previously reported. A high-resolution model depicting the tertiary structure of Chtx has been obtained by DIANA and X-PLOR calculations from new proton nuclear magnetic resonance (NMR) data. The protein possesses a small triple-stranded antiparallel beta sheet linked to a short helix by two disulfides and to an extended fragment by one disulfide, respectively. This motif also exists in all known structures of scorpion toxins, irrespective of their size, sequence, and function. Strikingly, antibacterial insect defensins also adopt this folding pattern.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bontems, F -- Roumestand, C -- Gilquin, B -- Menez, A -- Toma, F -- New York, N.Y. -- Science. 1991 Dec 6;254(5037):1521-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departement d'Ingenierie et d'Etudes des Proteines, Gif sur Yvette, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1720574" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Blood Proteins/*ultrastructure ; Charybdotoxin ; Defensins ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; Neurotoxins/*chemistry ; Potassium Channels/drug effects ; Protein Conformation ; Scorpion Venoms/*chemistry ; Scorpions ; Sequence Alignment
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 43
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    NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-05-31
    Beschreibung: Filamentous bacteriophage coat protein undergoes a remarkable structural transition during the viral assembly process as it is transferred from the membrane environment of the cell, where it spans the phospholipid bilayer, to the newly extruded virus particles. Nuclear magnetic resonance (NMR) studies show the membrane-bound form of the 46-residue Pf1 coat protein to be surprisingly complex with five distinct regions. The secondary structure consists of a long hydrophobic helix (residues 19 to 42) that spans the bilayer and a short amphipathic helix (residues 6 to 13) parallel to the plane of the bilayer. The NH2-terminus (residues 1 to 5), the COOH-terminus (residues 43 to 46), and residues 14 to 18 connecting the two helices are mobile. By comparing the structure and dynamics of the membrane-bound coat protein with that of the viral form as determined by NMR and neutron diffraction, essential features of assembly process can be identified.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shon, K J -- Kim, Y -- Colnago, L A -- Opella, S J -- AI20770-06/AI/NIAID NIH HHS/ -- GM34343-06/GM/NIGMS NIH HHS/ -- RR-02301/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1991 May 31;252(5010):1303-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Pennsylvania, Philadelphia 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925542" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Capsid/*chemistry/metabolism ; *Capsid Proteins ; Cell Membrane/metabolism ; Lipid Bilayers/metabolism ; *Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Structure ; Protein Conformation
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 44
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    OPC-21268, an orally effective, nonpeptide vasopressin V1 receptor antagonist (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-04-26
    Beschreibung: An orally effective, nonpeptide, vasopressin V1 receptor antagonist, OPC-21268, has been identified. This compound selectively antagonized binding to the V1 subtype of the vasopressin receptor in a competitive manner. In vivo, the compound acted as a specific antagonist of arginine vasopressin (AVP)-induced vasoconstriction. After oral administration in conscious rats, the compound also antagonized pressor responses to AVP. OPC-21268 can be used to study the physiological role of AVP and may be therapeutically useful in the treatment of hypertension and congestive heart failure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamamura, Y -- Ogawa, H -- Chihara, T -- Kondo, K -- Onogawa, T -- Nakamura, S -- Mori, T -- Tominaga, M -- Yabuuchi, Y -- New York, N.Y. -- Science. 1991 Apr 26;252(5005):572-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Second Tokushima Institute of New Drug Research, Otsuka Pharmaceutical Co., Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1850553" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Administration, Oral ; Angiotensin II/pharmacology ; Animals ; Arginine Vasopressin/antagonists & inhibitors/metabolism/*pharmacology ; Binding, Competitive ; Blood Pressure/*drug effects ; Cell Membrane/metabolism ; Kidney/metabolism ; Kinetics ; Liver/metabolism ; Norepinephrine/pharmacology ; Piperidines/administration & dosage/*pharmacology ; Quinolones/administration & dosage/*pharmacology ; Rats ; Receptors, Angiotensin/*drug effects/metabolism ; Receptors, Vasopressin ; Time Factors
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 45
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    Mutations affecting internal TEA blockade identify the probable pore-forming region of a K+ channel (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-02-22
    Beschreibung: The active site of voltage-activated potassium channels is a transmembrane aqueous pore that permits ions to permeate the cell membrane in a rapid yet highly selective manner. A useful probe for the pore of potassium-selective channels is the organic ion tetraethylammonium (TEA), which binds with millimolar affinity to the intracellular opening of the pore and blocks potassium current. In the potassium channel encoded by the Drosophila Shaker gene, an amino acid residue that specifically affects the affinity for intracellular TEA has now been identified by site-directed mutagenesis. This residue is in the middle of a conserved stretch of 18 amino acids that separates two locations that are both near the external opening of the pore. These findings suggest that this conserved region is intimately involved in the formation of the ion conduction pore of voltage-activated potassium channels. Further, a stretch of only eight amino acid residues must traverse 80 percent of the transmembrane electric potential difference.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yellen, G -- Jurman, M E -- Abramson, T -- MacKinnon, R -- GM4399/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 22;251(4996):939-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2000494" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Binding Sites ; Drosophila/genetics ; Genes ; Membrane Potentials ; Models, Structural ; Molecular Sequence Data ; *Mutagenesis, Site-Directed ; Potassium Channels/drug effects/genetics/*physiology ; Protein Conformation ; Tetraethylammonium ; Tetraethylammonium Compounds/*pharmacology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 46
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    Subunit communication in the anthranilate synthase complex from Salmonella typhimurium (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-06-28
    Beschreibung: The anthranilate synthase-phosphoribosyl transferase complex of the tryptophan biosynthetic pathway in Salmonella typhimurium is an allosteric, heterotetrameric (TrpE2-TrpD2) enzyme whose multiple activities are negatively feedback-regulated by L-tryptophan. A hybrid complex containing one catalytically active, feedback-insensitive and one catalytically inactive, feedback-sensitive mutant TrpE subunit was assembled in vitro and used to investigate communication between regulatory and catalytic sites located on different subunits. The properties of the hybrid complex demonstrate that the binding of a single inhibitor molecule to one TrpE subunit is sufficient for the propagation of a conformational change that affects the active site of the companion subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Caligiuri, M G -- Bauerle, R -- GM07082/GM/NIGMS NIH HHS/ -- GM35889/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Jun 28;252(5014):1845-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of Virginia, Charlottesville 22901.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2063197" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Anthranilate Phosphoribosyltransferase/isolation & purification/*metabolism ; Anthranilate Synthase/isolation & purification/*metabolism ; Chromatography, Affinity ; Chromatography, Gel ; Feedback ; Kinetics ; Multienzyme Complexes/isolation & purification/*metabolism ; Salmonella typhimurium/*enzymology ; Tryptophan/biosynthesis/pharmacology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 47
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    Structurally homologous ligand binding of integrin Mac-1 and viral glycoprotein C receptors (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-11-22
    Beschreibung: Three spatially distant surface loops were found to mediate the interaction of the coagulation protein factor X with the leukocyte integrin Mac-1. This interacting region, which by computational modeling defines a three-dimensional macromotif in the catalytic domain, was also recognized by glycoprotein C (gC), a factor X receptor expressed on herpes simplex virus (HSV)-infected endothelial cells. Peptidyl mimicry of each loop inhibited factor X binding to Mac-1 and gC, blocked monocyte generation of thrombin, and prevented monocyte adhesion to HSV-infected endothelium. These data link the ligand recognition of Mac-1 to established mechanisms of receptor-mediated vascular injury.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Altieri, D C -- Etingin, O R -- Fair, D S -- Brunck, T K -- Geltosky, J E -- Hajjar, D P -- Edgington, T S -- HL 46408/HL/NHLBI NIH HHS/ -- P01 HL 16411/HL/NHLBI NIH HHS/ -- R01 HL 43773/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Nov 22;254(5035):1200-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1957171" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Binding, Competitive ; Cell Line ; Factor X/*metabolism/ultrastructure ; Humans ; In Vitro Techniques ; Ligands ; Macrophage-1 Antigen/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Peptides/chemistry/metabolism ; Protein Conformation ; Viral Envelope Proteins/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 48
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    Mechanism for regulating cell surface distribution of Na+,K(+)-ATPase in polarized epithelial cells (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-11-08
    Beschreibung: Restriction of sodium, potassium adenosine triphosphatase (Na+,K(+)-ATPase) to either the apical or basal-lateral membrane domain of polarized epithelial cells is fundamental to vectorial ion and solute transport in many tissues and organs. A restricted membrane distribution of Na+,K(+)-ATPase in Madin-Darby canine kidney (MDCK) epithelial cells was found experimentally to be generated by preferential retention of active enzyme in the basal-lateral membrane domain and selective inactivation and loss from the apical membrane domain, rather than by vectorial targeting of newly synthesized protein from the Golgi complex to the basal-lateral membrane domain. These results show how different distributions of the same subunits of Na+,K(+)-ATPase may be generated in normal polarized epithelial and in disease states.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hammerton, R W -- Krzeminski, K A -- Mays, R W -- Ryan, T A -- Wollner, D A -- Nelson, W J -- GM 35527/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):847-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Physiology, Stanford University School of Medicine, CA 94305-5426.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1658934" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Binding Sites ; Cell Communication ; Cell Line ; Cell Membrane/*enzymology/physiology ; *Cell Polarity ; Dogs ; Epithelium/enzymology/physiology ; Kinetics ; Ouabain/metabolism ; Sodium-Potassium-Exchanging ATPase/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 49
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    Regulation of Ras-GAP and the neurofibromatosis-1 gene product by eicosanoids (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-04-26
    Beschreibung: Ras-GAP (GTPase activating protein) is a regulatory protein that stimulates the intrinsic guanosine triphosphatase (GTPase) activity of the proto-oncogene product p21ras. A domain of the neurofibromatosis gene product (NF1) that has sequence similarity to the catalytic domain of Ras-GAP and to yeast IRA gene products also has a specific stimulatory activity toward p21ras GTPase. Arachidonic acid and phosphatidic acid inactivate GAP, but no agents have been identified that stimulate GAP and thereby switch p21ras off. With the use of recombinant Ha-c-Ras and Ras-GAP, NF1, and GAP catalytic domains, it was found that prostaglandins PGF2 alpha and PGA2 stimulated Ras-GAP and that prostacyclin PGI2 inhibited Ras-GAP. The stimulatory effect of PGF2 alpha was saturable and structure-specific and competed with the inhibitory effect of arachidonic acid. Arachidonic acid also inhibited the catalytic activity of NF1, but prostaglandins were not stimulatory. These results suggest a mechanism for the allosteric control of Ras function through the modulation of arachidonate metabolism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Han, J W -- McCormick, F -- Macara, I G -- CA 38888/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Apr 26;252(5005):576-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics, University of Rochester Medical Center, NY 14642.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1902323" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Arachidonic Acid ; Arachidonic Acids/pharmacology ; Dinoprost/pharmacology ; GTP Phosphohydrolases/metabolism ; GTPase-Activating Proteins ; Gene Expression Regulation/drug effects ; Genes, ras/*drug effects ; Guanosine Triphosphate/metabolism ; Humans ; Kinetics ; Neurofibromatosis 1/genetics ; Neurofibromin 1 ; Prostaglandins/*pharmacology ; Proteins/*genetics ; Proto-Oncogene Proteins p21(ras)/metabolism ; Recombinant Proteins/metabolism ; ras GTPase-Activating Proteins
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 50
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    Kinetic characterization of ribonuclease-resistant 2'-modified hammerhead ribozymes (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-07-19
    Beschreibung: The incorporation of 2'-fluoro- and 2'-aminonucleotides into a hammerhead ribozyme was accomplished by automated chemical synthesis. The presence of 2'-fluorouridines, 2'-fluorocytidines, or 2'-aminouridines did not appreciably decrease catalytic efficiency. Incorporation of 2'-aminocytidines decreased ribozyme activity approximately by a factor of 20. The replacement of all adenosines with 2'-fluoroadenosines abolished catalysis in the presence of MgCl2 within the limits of detection, but some activity was retained in the presence of MnCl2. This effect on catalysis was localized to a specific group of adenines within the conserved single-stranded region of the ribozyme. The decrease in catalytic efficiency was caused by a decrease in the rate constant; the Michaelis constant was unaltered. The 2'-fluoro and 2'-amino modifications conferred resistance toward ribonuclease degradation. Ribozymes containing 2'-fluoro- or 2'-aminonucleotides at all uridine and cytidine positions were stabilized against degradation in rabbit serum by a factor of at least 10(3) compared to unmodified ribozyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pieken, W A -- Olsen, D B -- Benseler, F -- Aurup, H -- Eckstein, F -- New York, N.Y. -- Science. 1991 Jul 19;253(5017):314-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Experimentelle Medizin, Abteilung Chemie, Gottingen, Federal Republic of Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1857967" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Base Sequence ; *Chlorides ; Kinetics ; Magnesium Chloride/pharmacology ; Manganese/pharmacology ; *Manganese Compounds ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA, Catalytic/chemical synthesis/*metabolism ; Ribonucleases/*metabolism ; Ribonucleotides ; Substrate Specificity
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 51
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    Structural basis for the activation of glycogen phosphorylase b by adenosine monophosphate (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-11-29
    Beschreibung: The three-dimensional structure of the activated state of glycogen phosphorylase (GP) as induced by adenosine monophosphate (AMP) has been determined from crystals of pyridoxalpyrophosphoryl-GP. The same quaternary changes relative to the inactive conformation as those induced by phosphorylation are induced by AMP, although the two regulatory signals function through different local structural mechanisms. Moreover, previous descriptions of the phosphorylase active state have been extended by demonstrating that, on activation, the amino- and carboxyl-terminal domains of GP rotate apart by 5 degrees, thereby increasing access of substrates to the catalytic site. The structure also reveals previously unobserved interactions with the nucleotide that accounts for the specificity of the nucleotide binding site for AMP in preference to inosine monophosphate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sprang, S R -- Withers, S G -- Goldsmith, E J -- Fletterick, R J -- Madsen, N B -- R01 DK26081/DK/NIDDK NIH HHS/ -- R01 DK31507/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1367-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas 75235-9050.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1962195" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenosine Monophosphate/*pharmacology ; Amino Acid Sequence ; Binding Sites ; Enzyme Activation ; Macromolecular Substances ; Models, Molecular ; Phosphorylase b/chemistry/*metabolism ; Protein Conformation ; Pyridoxal Phosphate/analogs & derivatives/metabolism ; X-Ray Diffraction
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 52
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    Self-assembled organic monolayers: model systems for studying adsorption of proteins at surfaces (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-05-24
    Beschreibung: Self-assembled monolayers (SAMs) of omega-functionalized long-chain alkanethiolates on gold films are excellent model systems with which to study the interactions of proteins with organic surfaces. Monolayers containing mixtures of hydrophobic (methyl-terminated) and hydrophilic [hydroxyl-, maltose-, and hexa(ethylene glycol)-terminated] alkanethiols can be tailored to select specific degrees of adsorption: the amount of protein adsorbed varies monotonically with the composition of the monolayer. The hexa(ethylene glycol)-terminated SAMs are the most effective in resisting protein adsorption. The ability to create interfaces with similar structures and well-defined compositions should make it possible to test hypotheses concerning protein adsorption.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Prime, K L -- Whitesides, G M -- New York, N.Y. -- Science. 1991 May 24;252(5009):1164-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2031186" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adsorption ; Alkanes ; Fibrinogen/chemistry ; Kinetics ; *Models, Chemical ; Proteins/*chemistry ; Pyruvate Kinase/chemistry ; Ribonucleases/chemistry ; Surface Properties
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  • 53
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    Identity elements for specific aminoacylation of yeast tRNA(Asp) by cognate aspartyl-tRNA synthetase (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-06-21
    Beschreibung: The nucleotides crucial for the specific aminoacylation of yeast tRNA(Asp) by its cognate synthetase have been identified. Steady-state aminoacylation kinetics of unmodified tRNA transcripts indicate that G34, U35, C36, and G73 are important determinants of tRNA(Asp) identity. Mutations at these positions result in a large decrease (19- to 530-fold) of the kinetic specificity constant (ratio of the catalytic rate constant kcat and the Michaelis constant Km) for aspartylation relative to wild-type tRNA(Asp). Mutation to G10-C25 within the D-stem reduced kcat/Km eightfold. This fifth mutation probably indirectly affects the presentation of the highly conserved G10 nucleotide to the synthetase. A yeast tRNA(Phe) was converted into an efficient substrate for aspartyl-tRNA synthetase through introduction of the five identity elements. The identity nucleotides are located in regions of tight interaction between tRNA and synthetase as shown in the crystal structure of the complex and suggest sites of base-specific contacts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Putz, J -- Puglisi, J D -- Florentz, C -- Giege, R -- New York, N.Y. -- Science. 1991 Jun 21;252(5013):1696-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Biochimie, Institut de Biologie Moleculaire et Cellulaire du CNRS, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2047878" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Aspartate-tRNA Ligase/*metabolism ; Base Sequence ; Computer Graphics ; DNA Mutational Analysis ; Fungal Proteins/metabolism ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; RNA, Fungal/metabolism ; RNA, Transfer, Amino Acyl/metabolism ; RNA, Transfer, Asp/*metabolism ; Saccharomyces cerevisiae/*enzymology ; Structure-Activity Relationship ; Substrate Specificity ; *Transfer RNA Aminoacylation
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 54
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    1990: annus mirabilis of potassium channels (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-05-24
    Beschreibung: Voltage-gated potassium channels make up a large molecular family of integral membrane proteins that are fundamentally involved in the generation of bioelectric signals such as nerve impulses. These proteins span the cell membrane, forming potassium-selective pores that are rapidly switched open or closed by changes in membrane voltage. After the cloning of the first potassium channel over 3 years ago, recombinant DNA manipulation of potassium channel genes is now leading to a molecular understanding of potassium channel behavior. During the past year, functional domains responsible for channel gating and potassium selectivity have been identified, and detailed structural pictures underlying these functions are beginning to emerge.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, C -- New York, N.Y. -- Science. 1991 May 24;252(5009):1092-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Graduate Department of Biochemistry, Brandeis University, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2031183" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Action Potentials ; Amino Acid Sequence ; Animals ; Ion Channel Gating ; Models, Structural ; Molecular Sequence Data ; Potassium Channels/genetics/*physiology ; Protein Conformation
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 55
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    Activation of a small GTP-binding protein by nucleoside diphosphate kinase (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-11-08
    Beschreibung: Genes that encode nucleoside diphosphate kinases (NDKs) have been implicated as regulators of mammalian tumor metastasis and development in Drosophila melanogaster. However, the cellular pathways through which NDKs function are not known. One potential mechanism of regulation is phosphorylation of guanosine diphosphate (GDP) bound to regulatory guanosine triphosphate (GTP) binding proteins. NDK-catalyzed phosphorylation of bound GDP was investigated for the adenosine diphosphate ribosylation factor (ARF), a 21-kilodalton GTP-binding protein that functions in the protein secretion pathway. Bovine liver NDK, recombinant human NDK, and the protein product of the mouse gene nm23-1, which suppresses the metastatic potential of certain tumor cells, used ARF-GDP as a substrate, thereby allowing rapid and efficient production of activated ARF (ARF-GTP) in the absence of nucleotide exchange. These data are consistent with the proposed function of NDK as an activator of a small GTP-binding protein and provide a mechanism of activation for a regulatory GTP-binding protein that is independent of nucleotide exchange.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Randazzo, P A -- Northup, J K -- Kahn, R A -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):850-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biological Chemistry, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1658935" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Cattle ; Cholera Toxin/pharmacology ; Drosophila melanogaster/metabolism ; GTP-Binding Proteins/*metabolism ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Humans ; Kinetics ; Liver/enzymology ; Nucleoside-Diphosphate Kinase/*metabolism ; Phosphorylation ; Recombinant Proteins/metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 56
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    The energy landscapes and motions of proteins (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-12-13
    Beschreibung: Recent experiments, advances in theory, and analogies to other complex systems such as glasses and spin glasses yield insight into protein dynamics. The basis of the understanding is the observation that the energy landscape is complex: Proteins can assume a large number of nearly isoenergetic conformations (conformational substates). The concepts that emerge from studies of the conformational substates and the motions between them permit a quantitative discussion of one simple reaction, the binding of small ligands such as carbon monoxide to myoglobin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Frauenfelder, H -- Sligar, S G -- Wolynes, P G -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1598-603.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Advanced Study, University of Illinois, Champaign, Urbana 61801.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1749933" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Carbon Monoxide/chemistry ; Chemistry, Physical ; Motion ; Myoglobin/*chemistry ; Physicochemical Phenomena ; Protein Conformation ; Structure-Activity Relationship ; Temperature ; Thermodynamics
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 57
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    Intrasubunit signal transduction by the aspartate chemoreceptor (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-12-23
    Beschreibung: Receptors that transmit signals across cell membranes are typically composed of multiple subunits. To test whether subunit interactions are required for transmembrane signaling by the bacterial aspartate receptor, dimers were constructed with (i) two full-length subunits, (ii) one full-length subunit and one subunit lacking the cytoplasmic domain, or (iii) one full-length subunit and one subunit lacking both the cytoplasmic and the transmembrane domains. Methylation of the cytoplasmic domain of all three receptor constructs was stimulated by the binding of aspartate. These findings demonstrate that transmembrane signaling does not require interactions between cytoplasmic or transmembrane domains of adjacent subunits and suggest that signaling occurs via conformational changes transduced through a single subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milligan, D L -- Koshland, D E Jr -- DK 09765/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1651-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1661030" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Aspartic Acid/*physiology ; DNA Mutational Analysis ; Ligands ; Macromolecular Substances ; Methylation ; Protein Conformation ; *Receptors, Amino Acid ; Receptors, Cell Surface/*chemistry ; Recombinant Proteins ; Salmonella typhimurium ; Signal Transduction ; Structure-Activity Relationship
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 58
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    Cloning of a serotonin transporter affected by antidepressants (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-10-25
    Beschreibung: A complementary DNA clone for a serotonin (5HT) transporter has been isolated from rat basophilic leukemia cells. The complementary DNA sequence predicts a 653-amino acid protein with 12 to 13 putative transmembrane domains. The 5HT transporter has significant homology to the gamma-aminobutyric acid, dopamine, and norepinephrine transporters. Uptake by CV-1 cells expressing the transporter complementary DNA resembles 5HT uptake by platelets and brain synaptosomes; it is sensitive to antidepressants, amphetamine derivatives, and cocaine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, B J -- Mezey, E -- Brownstein, M J -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):579-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cell Biology, National Institute of Mental Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948036" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Antidepressive Agents/*pharmacology ; Base Sequence ; Carrier Proteins/drug effects/*genetics/metabolism ; Cell Line ; Cloning, Molecular ; Kinetics ; Leukemia, Basophilic, Acute ; Molecular Sequence Data ; Oligonucleotide Probes ; Rats ; Serotonin/*metabolism ; Transfection
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 59
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    A bacterial system for investigating transport effects of cystic fibrosis--associated mutations (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-10-04
    Beschreibung: LIV-I, a high-affinity system that transports neutral, branched-chain amino acids into Escherichia coli, has two components, LivG and LivF, that are homologous to the cystic fibrosis (CF) transmembrane conductance regulator (CFTR). CF-associated mutations of human CFTR were introduced into corresponding regions of LivG, and their effects on leucine transport could be grouped into three classes. Mutations were found that (i) abolished LIV-I--directed transport, (ii) retained about a quarter of wild-type activity at the Michaelis-Menten constant (KM), and (iii) had minimal activity at the KM. A mutation equivalent to a benign polymorphism had no effect on transport. The correlation of these mutational phenotypes in LivG and CFTR suggests that the LIV-I prokaryotic transporter is functionally similar to the CF protein and that this similarity can be exploited to clarify the properties of the nucleotide-binding fold in this superfamily of proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibson, A L -- Wagner, L M -- Collins, F S -- Oxender, D L -- New York, N.Y. -- Science. 1991 Oct 4;254(5028):109-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, University of Michigan, Ann Arbor 48109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1718037" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): ATP-Binding Cassette Transporters ; Amino Acid Sequence ; Bacterial Proteins/*genetics ; Biological Transport, Active ; Cloning, Molecular ; Cystic Fibrosis/*genetics ; Cystic Fibrosis Transmembrane Conductance Regulator ; DNA Mutational Analysis ; Escherichia coli/genetics ; *Escherichia coli Proteins ; Humans ; Kinetics ; Leucine/metabolism ; Membrane Proteins/*genetics ; *Membrane Transport Proteins ; Molecular Sequence Data ; Protein Binding ; Restriction Mapping ; Sequence Alignment ; Structure-Activity Relationship
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 60
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    New 3-D protein structures revealed. The shape of cholera (1991)
    American Association for the Advancement of Science (AAAS)
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    Publikationsdatum: 1991-07-26
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbons, A -- New York, N.Y. -- Science. 1991 Jul 26;253(5018):382-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1862340" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Cholera Toxin/*chemistry ; Macromolecular Substances ; Models, Molecular ; Protein Conformation
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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    Induction by NGF of meiotic maturation of Xenopus oocytes expressing the trk proto-oncogene product (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-04-26
    Beschreibung: The effect of nerve growth factor (NGF) was assessed in Xenopus oocytes expressing the human trk proto-oncogene product, p140prototrk. Oocytes injected with trk messenger RNA expressed polypeptides recognized by antibodies to the trk gene product. Exposure of these oocytes to nanomolar amounts of NGF resulted in specific surface binding of 125I-labeled NGF, tyrosine phosphorylation of p140prototrk, and meiotic maturation, as determined by germinal vesicle breakdown and maturation promoting factor (p34cdc2) kinase activation. Thus the trk proto-oncogene product can act as a receptor for NGF in a functionally productive manner.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nebreda, A R -- Martin-Zanca, D -- Kaplan, D R -- Parada, L F -- Santos, E -- New York, N.Y. -- Science. 1991 Apr 26;252(5005):558-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1850550" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Enzyme Activation ; Female ; Humans ; In Vitro Techniques ; Kinetics ; Meiosis/*drug effects ; Microinjections ; Nerve Growth Factors/metabolism/*pharmacology ; Oocytes/cytology/drug effects/*physiology ; Progesterone/pharmacology ; Protein-Tyrosine Kinases/genetics ; Proto-Oncogene Proteins/*genetics/metabolism ; *Proto-Oncogenes ; RNA, Messenger/administration & dosage/genetics ; Receptor, trkA ; Receptors, Cell Surface/drug effects/metabolism ; Receptors, Nerve Growth Factor ; Xenopus laevis
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 62
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    Structure and functional expression of a human interleukin-8 receptor (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-09-13
    Beschreibung: Interleukin-8 (IL-8) is a member of a family of pro-inflammatory cytokines. Although the best characterized activities of IL-8 include the chemoattraction and activation of neutrophils, other members of this family have a wide range of specific actions including the chemotaxis and activation of monocytes, the selective chemotaxis of memory T cells, the inhibition of hematopoietic stem cell proliferation, and the induction of neutrophil infiltration in vivo. A complementary DNA encoding the IL-8 receptor from human neutrophils has now been isolated. The amino acid sequence shows that the receptor is a member of the superfamily of receptors that couple to guanine nucleotide binding proteins (G proteins). The sequence is 29% identical to that of receptors for the other neutrophil chemoattractants, fMet-Leu-Phe and C5a. Mammalian cells transfected with the IL-8 receptor cDNA clone bind IL-8 with high affinity and respond specifically to IL-8 by transiently mobilizing calcium. The IL-8 receptor may be part of a subfamily of related G protein-coupled receptors that transduce signals for the IL-8 family of pro-inflammatory cytokines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holmes, W E -- Lee, J -- Kuang, W J -- Rice, G C -- Wood, W I -- New York, N.Y. -- Science. 1991 Sep 13;253(5025):1278-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Genentech, Inc., South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1840701" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Cell Line ; Cloning, Molecular ; DNA Probes ; Humans ; Interleukin-8/*metabolism ; Kinetics ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Plasmids ; RNA, Messenger/genetics ; Receptors, Immunologic/*genetics/metabolism ; Receptors, Interleukin-8A ; Recombinant Proteins/metabolism ; Sequence Homology, Nucleic Acid ; Transfection
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 63
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    Enhanced motility in NIH 3T3 fibroblasts that overexpress gelsolin (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-03-08
    Beschreibung: Increasing the content of the actin-binding protein gelsolin in cultured mouse fibroblasts by up to 125 percent by gene transfection proportionally enhanced the rate at which the cells migrated through porous filters toward a gradient of serum and closed a wound made on a confluent monolayer of cells in a tissue culture dish. These results provide direct evidence that gelsolin, which promotes both actin assembly and disassembly in vitro, is an important element in fibroblast locomotion and demonstrate that the manipulation of intracellular machinery can increase cell motility.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cunningham, C C -- Stossel, T P -- Kwiatkowski, D J -- AI28465/AI/NIAID NIH HHS/ -- HL07680/HL/NHLBI NIH HHS/ -- HL19429/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1233-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hematology-Oncology Unit, Massachusetts General Hospital, Boston 02129.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1848726" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Calcium-Binding Proteins/genetics/*physiology ; Cell Line ; *Chemotaxis ; Fibroblasts/physiology ; Gelsolin ; Gene Expression ; Humans ; Kinetics ; Mice ; Microfilament Proteins/genetics/*physiology ; RNA Splicing ; RNA, Messenger/genetics ; Transfection
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 64
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    Recognition of a cell-surface oligosaccharide of pathogenic Salmonella by an antibody Fab fragment (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-07-26
    Beschreibung: The 2.05 angstrom (A) resolution crystal structure of a dodecasaccharide-Fab complex revealed an unusual carbohydrate recognition site, defined by aromatic amino acids and a structured water molecule, rather than the carboxylic acid and amide side chains and a structured water molecule, rather than the carboxylic acid and amide side chains that are features of transport and other carbohydrate binding proteins. A trisaccharide epitope of a branched bacterial lipopolysaccharide fills this hydrophobic pocket (8 A deep by 7 A wide) in an entropy-assisted association (association constant = 2.05 x 10(5) liters per mole, enthalpy = -20.5 +/- 1.7 kilojoules per mole, and temperature times entropy = +10.0 +/- 2.9 kilojoules per mole). The requirement for the complementarity of van der Waals surfaces and the requirements of saccharide-saccharide and protein-saccharide hydrogen-bonding networks determine the antigen conformation adopted in the bound state.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cygler, M -- Rose, D R -- Bundle, D R -- New York, N.Y. -- Science. 1991 Jul 26;253(5018):442-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biotechnology Research Institute, National Research Council of Canada, Montreal, Quebec.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1713710" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; *Antigen-Antibody Complex ; Carbohydrate Conformation ; Carbohydrate Sequence ; Epitopes/chemistry ; Humans ; Immunoglobulin Fab Fragments/chemistry/*immunology ; Immunoglobulin G/classification/*immunology ; Lipopolysaccharides/chemistry/*immunology ; Models, Molecular ; Molecular Sequence Data ; Oligosaccharides/chemistry/*immunology ; Protein Conformation ; Salmonella/*immunology/pathogenicity
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 65
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    Carbamate formation and the neurotoxicity of L-alpha amino acids (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-03-29
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nunn, P B -- Davis, A J -- O'Brien, P -- New York, N.Y. -- Science. 1991 Mar 29;251(5001):1619-20.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1859531" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acids/chemistry/*toxicity ; Animals ; *Carbamates ; Cysteine/chemistry ; Humans ; Kinetics ; Molecular Conformation ; N-Methylaspartate/chemistry ; *Neurotoxins
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 66
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    A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-08-09
    Beschreibung: The high-resolution three-dimensional structure of a single immunoglobulin binding domain (B1, which comprises 56 residues including the NH2-terminal Met) of protein G from group G Streptococcus has been determined in solution by nuclear magnetic resonance spectroscopy on the basis of 1058 experimental restraints. The average atomic root-mean-square distribution about the mean coordinate positions is 0.27 angstrom (A) for the backbone atoms, 0.65 A for all atoms, and 0.39 A for atoms excluding disordered surface side chains. The structure has no disulfide bridges and is composed of a four-stranded beta sheet, on top of which lies a long helix. The central two strands (beta 1 and beta 4), comprising the NH2- and COOH-termini, are parallel, and the outer two strands (beta 2 and beta 3) are connected by the helix in a +3x crossover. This novel topology (-1, +3x, -1), coupled with an extensive hydrogen-bonding network and a tightly packed and buried hydrophobic core, is probably responsible for the extreme thermal stability of this small domain (reversible melting at 87 degrees C).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gronenborn, A M -- Filpula, D R -- Essig, N Z -- Achari, A -- Whitlow, M -- Wingfield, P T -- Clore, G M -- New York, N.Y. -- Science. 1991 Aug 9;253(5020):657-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1871600" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Bacterial Proteins/*chemistry/immunology ; Binding Sites ; Calorimetry ; Hydrogen Bonding ; *Immunoglobulin G ; Magnetic Resonance Spectroscopy/methods ; Models, Molecular ; Protein Conformation
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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    Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-12-13
    Beschreibung: Calcium-dependent (C-type) animal lectins participate in many cell surface recognition events mediated by protein-carbohydrate interactions. The C-type lectin family includes cell adhesion molecules, endocytic receptors, and extracellular matrix proteins. Mammalian mannose-binding proteins are C-type lectins that function in antibody-independent host defense against pathogens. The crystal structure of the carbohydrate-recognition domain of a rat mannose-binding protein, determined as the holmium-substituted complex by multiwavelength anomalous dispersion (MAD) phasing, reveals an unusual fold consisting of two distinct regions, one of which contains extensive nonregular secondary structure stabilized by two holmium ions. The structure explains the conservation of 32 residues in all C-type carbohydrate-recognition domains, suggesting that the fold seen here is common to these domains. The strong anomalous scattering observed at the Ho LIII edge demonstrates that traditional heavy atom complexes will be generally amenable to the MAD phasing method.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weis, W I -- Kahn, R -- Fourme, R -- Drickamer, K -- Hendrickson, W A -- GM34102/GM/NIGMS NIH HHS/ -- GM42628/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1608-15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1721241" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Acute-Phase Proteins/*chemistry ; Amino Acid Sequence ; Animals ; Calcium/metabolism ; Calcium-Binding Proteins/*chemistry ; Carrier Proteins/*chemistry ; Collagen/chemistry ; Crystallography ; Holmium ; Hydrogen Bonding ; Lanthanum ; Lectins/*chemistry ; Ligands ; Mannose-Binding Lectins ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Protein Conformation ; Rats ; Recombinant Proteins/chemistry ; Sequence Alignment ; X-Ray Diffraction/methods
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 68
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    Molecular architecture and electrostatic properties of a bacterial porin (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-12-13
    Beschreibung: The integral membrane protein porin from Rhodobacter capsulatus consists of three tightly associated 16-stranded beta barrels that give rise to three distinct diffusion channels for small solutes through the outer membrane. The x-ray structure of this porin has revealed details of its shape, the residue distributions within the pore and at the membrane-facing surface, and the location of calcium sites. The electrostatic potential has been calculated and related to function. Moreover, potential calculations were found to predict the Ca2+ sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weiss, M S -- Abele, U -- Weckesser, J -- Welte, W -- Schiltz, E -- Schulz, G E -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1627-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Organische Chemie und Biochemie, Freiburg, Federal Republic of Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1721242" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Bacterial Outer Membrane Proteins/*chemistry ; Calcium/metabolism ; Calcium-Binding Proteins/metabolism ; Computer Graphics ; Crystallography ; Ion Channels/*chemistry ; Ions ; Macromolecular Substances ; Models, Molecular ; Molecular Structure ; Porins ; Protein Conformation ; Rhodobacter capsulatus/*chemistry ; X-Ray Diffraction
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 69
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    Control of embryonic motoneuron survival in vivo by ciliary neurotrophic factor (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-03-29
    Beschreibung: During development of the nervous system, neurons in many regions are overproduced by proliferation, after which the excess cells are eliminated by cell death. The survival of only a proportion of neurons during normal development is thought to be regulated by the limited availability of neurotrophic agents. One such putative trophic agent is ciliary neurotrophic factor (CNTF), a polypeptide that promotes the survival of ciliary, sensory, and sympathetic neurons in vitro. In contrast to the results of in vitro studies, however, the daily treatment of chick embryos in vivo with purified human recombinant CNTF failed to rescue any of these cell populations from cell death, whereas CNTF did promote the in vivo survival of spinal motoneurons. Thus, CNTF may not act as a neurotrophic agent in vivo for those embryonic neurons (especially ciliary neurons) on which it acts in vitro. Rather, CNTF may be required for in vivo survival of motoneurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oppenheim, R W -- Prevette, D -- Yin, Q W -- Collins, F -- MacDonald, J -- NS 20402/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 29;251(5001):1616-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology and Anatomy, Bowman Gray School of Medicine, Wake Forest University, Winston-Salem, NC 27103.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2011743" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Cell Survival/drug effects ; Cells, Cultured ; Chick Embryo ; Ciliary Neurotrophic Factor ; Kinetics ; Motor Neurons/*cytology/drug effects ; Nerve Growth Factors/*pharmacology ; Nerve Tissue Proteins/*pharmacology ; Recombinant Proteins/pharmacology ; Spinal Cord/cytology/embryology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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    A corticosteroid receptor in neuronal membranes (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-06-28
    Beschreibung: Steroids may rapidly alter neuronal function and behavior through poorly characterized, direct actions on neuronal membranes. The membrane-bound receptors mediating these behavioral responses have not been identified. [3H]Corticosterone labels a population of specific, high-affinity recognition sites (dissociation constant = 0.51 nanomolar) in synaptic membranes from an amphibian brain. These binding sites were localized by receptor autoradiography in the neuropil, outside the regions of perikarya. The affinities of corticoids for this [3H]corticosterone binding site were linearly related to their potencies in rapidly suppressing male reproductive behavior. Thus, it appears that brain membranes contain a corticosteroid receptor that could participate in the regulation of behavior.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Orchinik, M -- Murray, T F -- Moore, F L -- New York, N.Y. -- Science. 1991 Jun 28;252(5014):1848-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, Oregon State University, Corvallis 97331.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2063198" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amphibians ; Animals ; Autoradiography ; Binding, Competitive ; Brain/*metabolism ; Cell Fractionation ; Cell Membrane ; Corticosterone/*metabolism/pharmacology ; Kinetics ; Male ; Neurons/*metabolism ; Receptors, Glucocorticoid/*metabolism ; Sexual Behavior, Animal/drug effects ; Synaptosomes/metabolism ; Tritium
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 71
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    Novel fold and putative receptor binding site of granulocyte-macrophage colony-stimulating factor (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-12-20
    Beschreibung: Granulocyte-macrophage colony-stimulating factor (GM-CSF) stimulates the development of and the cytotoxic activity of white blood cells. Recombinant human GM-CSF has proven useful in the treatment of blood disorders. The structure of GM-CSF, which was determined at 2.4 angstrom resolution by x-ray crystallography, has a novel fold combining a two-stranded antiparallel beta sheet with an open bundle of four alpha helices. Residues implicated in receptor recognition, which are distant in the primary sequence, are on adjacent alpha helices in the folded protein. A working model for the receptor binding site is presented.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Diederichs, K -- Boone, T -- Karplus, P A -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1779-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, NY 14853.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1837174" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Binding Sites ; Granulocyte-Macrophage Colony-Stimulating Factor/*chemistry/metabolism ; Humans ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Receptors, Granulocyte-Macrophage Colony-Stimulating Factor/*chemistry/metabolism ; X-Ray Diffraction
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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    Mediation of the attachment or fusion step in vesicular transport by the GTP-binding Ypt1 protein (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-06-14
    Beschreibung: The function of the guanosine triphosphate (GTP)-binding protein Ypt1 in regulating vesicular traffic was studied in a cell-free system that reconstitutes transport from the endoplasmic reticulum to the Golgi. Blocking the Ypt1 protein activity resulted in accumulation of vesicles that act as an intermediate passing between the two compartments. The Ypt1 protein was found on the outer side of these vesicles. The transport process is completed by fusion of these vesicles with the acceptor compartment, and Ypt1 protein activity was needed for this step. Thus, a specific GTP-binding protein is required for either attachment or fusion (or both) of secretory vesicles with the acceptor compartment during protein secretion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Segev, N -- New York, N.Y. -- Science. 1991 Jun 14;252(5012):1553-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacological and Physiological Sciences, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1904626" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Cell-Free System ; Endoplasmic Reticulum/metabolism ; Fungal Proteins/*metabolism ; GTP-Binding Proteins/*metabolism ; Glycosylation ; Golgi Apparatus/metabolism ; Kinetics ; Microsomes/metabolism ; Peptides/genetics ; Protein Precursors/metabolism ; Protein Processing, Post-Translational ; Proteins/*metabolism ; Saccharomyces cerevisiae/*metabolism ; *Saccharomyces cerevisiae Proteins ; Trypsin/pharmacology ; *rab GTP-Binding Proteins
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 73
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    X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-10-25
    Beschreibung: The x-ray crystal structure of a peptide corresponding to the leucine zipper of the yeast transcriptional activator GCN4 has been determined at 1.8 angstrom resolution. The peptide forms a parallel, two-stranded coiled coil of alpha helices packed as in the "knobs-into-holes" model proposed by Crick in 1953. Contacts between the helices include ion pairs and an extensive hydrophobic interface that contains a distinctive hydrogen bond. The conserved leucines, like the residues in the alternate hydrophobic repeat, make side-to-side interactions (as in a handshake) in every other layer of the dimer interface. The crystal structure of the GCN4 leucine zipper suggests a key role for the leucine repeat, but also shows how other features of the coiled coil contribute to dimer formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Shea, E K -- Klemm, J D -- Kim, P S -- Alber, T -- GM 44162/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):539-44.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948029" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Computer Simulation ; DNA-Binding Proteins/*chemistry ; Fungal Proteins/*chemistry ; Hydrogen Bonding ; *Leucine Zippers ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; *Protein Kinases ; *Saccharomyces cerevisiae Proteins ; Transcription Factors/*chemistry ; X-Ray Diffraction
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 74
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    An analog of myristic acid with selective toxicity for African trypanosomes (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-06-28
    Beschreibung: Trypanosoma brucei, the protozoan parasite responsible for African sleeping sickness, evades the host immune response through the process of antigenic variation. The variant antigen, known as the variant surface glycoprotein (VSG), is anchored to the cell surface by a glycosyl phosphatidylinositol (GPI) structure that contains myristate (n-tetradecanoate) as its only fatty acid component. The utilization of heteroatom-containing analogs of myristate was studied both in a cell-free system and in vivo. Results indicated that the specificity of fatty acid incorporation depends on chain length rather than on hydrophobicity. One analog, 10-(propoxy)decanoic acid, was highly toxic to trypanosomes in culture although it is nontoxic to mammalian cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doering, T L -- Raper, J -- Buxbaum, L U -- Adams, S P -- Gordon, J I -- Hart, G W -- Englund, P T -- 5T32GM07309/GM/NIGMS NIH HHS/ -- AI21334/AI/NIAID NIH HHS/ -- AI27179/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1991 Jun 28;252(5014):1851-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, Johns Hopkins Medical School, Baltimore, MD 21210.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1829548" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Acyl Coenzyme A/metabolism ; Animals ; Cell-Free System ; Glycolipids/metabolism ; Glycosylphosphatidylinositols ; Kinetics ; Mice ; Myristic Acid ; Myristic Acids/*metabolism/*pharmacology ; Phosphatidylinositols/metabolism ; Structure-Activity Relationship ; Trypanosoma brucei brucei/*drug effects/metabolism/ultrastructure
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 75
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    Three-dimensional structure of recombinant human interferon-gamma (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-05-03
    Beschreibung: The x-ray crystal structure of recombinant human interferon-gamma has been determined with the use of multiple-isomorphous-replacement techniques. Interferon-gamma, which is dimeric in solution, crystallizes with two dimers related by a noncrystallographic twofold axis in the asymmetric unit. The protein is primarily alpha helical, with six helices in each subunit that comprise approximately 62 percent of the structure; there is no beta sheet. The dimeric structure of human interferon-gamma is stabilized by the intertwining of helices across the subunit interface with multiple intersubunit interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ealick, S E -- Cook, W J -- Vijay-Kumar, S -- Carson, M -- Nagabhushan, T L -- Trotta, P P -- Bugg, C E -- CA-13148/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 3;252(5006):698-702.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Alabama, Birmingham 35294.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1902591" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Crystallization ; Glycosylation ; Humans ; Interferon-gamma/*chemistry ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Recombinant Proteins ; Sequence Homology, Nucleic Acid ; X-Ray Diffraction
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 76
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    Recoverin: a calcium sensitive activator of retinal rod guanylate cyclase (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-02-22
    Beschreibung: Vertebrate retinal photoreceptors recover from photoexcitation-induced hydrolysis of guanosine 3', 5'-monophosphate (cyclic GMP) by resynthesizing cyclic GMP, which reopens cation channels that have been closed by light. Activation of guanylate cyclase by light-induced depletion of cytosolic calcium is a key event in this recovery process. This cyclase has now been shown to be regulated by a 23-kilodalton calcium binding protein. The protein is present in both rod and cone photoreceptors and was named recoverin because it promotes recovery of the dark state. The amino acid sequence of recoverin exhibits three potential calcium binding sites (EF hands). That recoverin binds calcium was confirmed with calcium-45 and by observing calcium-induced changes in its tryptophan fluorescence. Recoverin activated guanylate cyclase when free calcium was lowered from 450 to 40 nM, an effect that was blocked by an antibody to recoverin. Thus, guanylate cyclase in retinal rods is stimulated during recovery by the calcium-free form of recoverin. A comparison of recoverin with other calcium binding proteins reveals that it may represent, along with the protein visinin, a family of proteins that are regulated by submicromolar calcium concentrations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dizhoor, A M -- Ray, S -- Kumar, S -- Niemi, G -- Spencer, M -- Brolley, D -- Walsh, K A -- Philipov, P P -- Hurley, J B -- Stryer, L -- EY02005/EY/NEI NIH HHS/ -- EY06641/EY/NEI NIH HHS/ -- GM15731/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 22;251(4996):915-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1672047" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Calcium/*pharmacology ; Calcium-Binding Proteins/genetics/isolation & purification/*metabolism ; Cattle ; Enzyme Activation ; *Eye Proteins ; Guanylate Cyclase/*metabolism ; Hippocalcin ; Kinetics ; *Lipoproteins ; Molecular Sequence Data ; Molecular Weight ; *Nerve Tissue Proteins ; Organ Specificity ; Photoreceptor Cells/*metabolism ; Recoverin ; Retina/cytology ; Rod Cell Outer Segment/*metabolism ; Sequence Homology, Nucleic Acid
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 77
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    Atomic structure of ferredoxin-NADP+ reductase: prototype for a structurally novel flavoenzyme family (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-01-04
    Beschreibung: The three-dimensional structure of spinach ferredoxin-NADP+ reductase (NADP+, nicotinamide adenine dinucleotide phosphate) has been determined by x-ray diffraction at 2.6 angstroms (A) resolution and initially refined to an R factor of 0.226 at 2.2 A resolution. The model includes the flavin-adenine dinucleotide (FAD) prosthetic group and the protein chain from residue 19 through the carboxyl terminus at residue 314 and is composed of two domains. The FAD binding domain (residues 19 to 161) has an antiparallel beta barrel core and a single alpha helix for binding the pyrophosphate of FAD. The NADP binding domain (residues 162 to 314) has a central five-strand parallel beta sheet and six surrounding helices. Binding of the competitive inhibitor 2'-phospho-AMP (AMP, adenosine monophosphate) places the NADP binding site at the carboxyl-terminal edge of the sheet in a manner similar to the nucleotide binding of the dehydrogenase family. The structures reveal the key residues that function in cofactor binding and the catalytic center. With these key residues as a guide, conclusive evidence is presented that the ferredoxin reductase structure is a prototype for the nicotinamide dinucleotide and FAD binding domains of the enzymes NADPH-cytochrome P450 reductase, NADPH-sulfite reductase, NADH-cytochrome b5 reductase, and NADH-nitrate reductase. Thus this structure provides a structural framework for the NADH- or NADPH-dependent flavoenzyme parts of five distinct enzymes involved in photosynthesis, in the assimilation of inorganic nitrogen and sulfur, in fatty-acid oxidation, in the reduction of methemoglobin, and in the metabolism of many pesticides, drugs, and carcinogens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karplus, P A -- Daniels, M J -- Herriott, J R -- New York, N.Y. -- Science. 1991 Jan 4;251(4989):60-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, NY 14853.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1986412" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenosine Diphosphate/metabolism ; Amino Acid Sequence ; Binding Sites ; Crystallization ; Ferredoxin-NADP Reductase/*chemistry ; Ferredoxins/metabolism ; Flavin-Adenine Dinucleotide/metabolism ; Hydrogen Bonding ; Molecular Sequence Data ; Molecular Structure ; NADP/metabolism ; Nucleotides/metabolism ; Plants/enzymology ; Protein Conformation ; Sequence Homology, Nucleic Acid ; X-Ray Diffraction
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 78
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    Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-08-30
    Beschreibung: The 3 angstrom resolution crystal structure of the Escherichia coli catabolite gene activator protein (CAP) complexed with a 30-base pair DNA sequence shows that the DNA is bent by 90 degrees. This bend results almost entirely from two 40 degrees kinks that occur between TG/CA base pairs at positions 5 and 6 on each side of the dyad axis of the complex. DNA sequence discrimination by CAP derives both from sequence-dependent distortion of the DNA helix and from direct hydrogen-bonding interactions between three protein side chains and the exposed edges of three base pairs in the major groove of the DNA. The structure of this transcription factor--DNA complex provides insights into possible mechanisms of transcription activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schultz, S C -- Shields, G C -- Steitz, T A -- GM-22778/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 30;253(5023):1001-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1653449" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Base Sequence ; Binding Sites ; Cyclic AMP Receptor Protein/*chemistry/metabolism ; DNA, Bacterial/*chemistry/metabolism ; DNA-Directed RNA Polymerases/metabolism ; Escherichia coli/metabolism ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Protein Binding ; Protein Conformation ; X-Ray Diffraction/methods
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 79
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    Protein electron transfer rates set by the bridging secondary and tertiary structure (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-05-31
    Beschreibung: The rate of long-distance electron transfer in proteins rapidly decreases with distance, which is indicative of an electron tunneling process. Calculations predict that the distance dependence of electron transfer in native proteins is controlled by the protein's structural motif. The helix and sheet content of a protein and the tertiary arrangement of these secondary structural units define the distance dependence of electronic coupling in that protein. The calculations use a tunneling pathway model applied previously with success to ruthenated proteins. The analysis ranks the average distance decay constant for electronic coupling in electron transfer proteins and identifies the amino acids that are coupled to the charge localization site more strongly or weakly than average for their distance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beratan, D N -- Betts, J N -- Onuchic, J N -- New York, N.Y. -- Science. 1991 May 31;252(5010):1285-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Beratan, Jet Propulsion Laboratory, California Institute of Technology, Pasadena 91109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1656523" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acids/chemistry ; Azurin/chemistry/metabolism ; *Bacterial Proteins ; Chemistry, Physical ; Cytochrome c Group/chemistry/metabolism ; Cytochromes b5/chemistry/metabolism ; *Electron Transport ; Iron-Sulfur Proteins/chemistry/metabolism ; Mathematics ; Models, Molecular ; Myoglobin/chemistry/metabolism ; *Photosynthetic Reaction Center Complex Proteins ; Physicochemical Phenomena ; Protein Conformation ; Proteins/*chemistry/metabolism ; Structure-Activity Relationship
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 80
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    Alteration of four identified K+ currents in Drosophila muscle by mutations in eag (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-06-14
    Beschreibung: Voltage-clamp analysis of Drosophila larval muscle revealed that ether a go-go (eag) mutations affected all identified potassium currents, including those specifically eliminated by mutations in the Shaker or slowpoke gene. Together with DNA sequence analysis, the results suggest that the eag locus encodes a subunit common to different potassium channels. Thus, combinatorial assembly of polypeptides from different genes may contribute to potassium channel diversity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhong, Y -- Wu, C F -- New York, N.Y. -- Science. 1991 Jun 14;252(5012):1562-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of Iowa, Iowa City 52242.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2047864" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): 4-Aminopyridine/pharmacology ; Animals ; Calcium/pharmacology ; Chromosome Mapping ; Drosophila/*genetics/physiology ; Electric Stimulation ; Kinetics ; Larva ; Membrane Potentials/drug effects ; Muscles/*physiology ; *Mutation ; Potassium Channels/drug effects/genetics/*physiology ; Quinidine/pharmacology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 81
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    Three-dimensional structures of acidic and basic fibroblast growth factors (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-01-04
    Beschreibung: Members of the fibroblast growth factor (FGF) family of proteins stimulate the proliferation and differentiation of a variety of cell types through receptor-mediated pathways. The three-dimensional structures of two members of this family, bovine acidic FGF and human basic FGF, have been crystallographically determined. These structures contain 12 antiparallel beta strands organized into a folding pattern with approximate threefold internal symmetry. Topologically equivalent folds have been previously observed for soybean trypsin inhibitor and interleukins-1 beta and -1 alpha. The locations of sequences implicated in receptor and heparin binding by FGF are presented. These sites include beta-sheet strand 10, which is adjacent to the site of an extended sequence insertion in several oncogene proteins of the FGF family, and which shows sequence conservation among the FGF family and interleukin-1 beta.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhu, X -- Komiya, H -- Chirino, A -- Faham, S -- Fox, G M -- Arakawa, T -- Hsu, B T -- Rees, D C -- New York, N.Y. -- Science. 1991 Jan 4;251(4989):90-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1702556" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Cattle ; Chemistry, Physical ; Crystallization ; Fibroblast Growth Factor 1/*chemistry/metabolism ; Fibroblast Growth Factor 2/*chemistry/metabolism ; Heparin/metabolism ; Humans ; Interleukin-1/chemistry ; Molecular Sequence Data ; Molecular Structure ; Physicochemical Phenomena ; Protein Conformation ; Recombinant Proteins/chemistry ; Sequence Homology, Nucleic Acid ; X-Ray Diffraction
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 82
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    Reverse transcriptase encoded by a human transposable element (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-12-30
    Beschreibung: L1 elements are highly repeated mammalian DNA sequences whose structure suggests dispersal by retrotransposition. A consensus L1 element encodes a protein with sequence similarity to known reverse transcriptases. The second open reading frame from the human L1 element L1.2A was expressed as a fusion protein targeted to Ty1 virus-like particles in Saccharomyces cerevisiae and shown to have reverse transcriptase activity. This activity was eliminated by a missense mutation in the highly conserved amino acid motif Y/F-X-D-D. Thus, L1 represents a potential source of the reverse transcriptase activity necessary for dispersion of the many classes of mammalian retroelements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mathias, S L -- Scott, A F -- Kazazian, H H Jr -- Boeke, J D -- Gabriel, A -- AI00803/AI/NIAID NIH HHS/ -- CA16519/CA/NCI NIH HHS/ -- GM28931/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1808-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1722352" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Base Sequence ; Cloning, Molecular ; *DNA Transposable Elements ; Epitopes/analysis ; Humans ; Immunoblotting ; Kinetics ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Open Reading Frames ; Plasmids ; Polyribonucleotides ; RNA-Directed DNA Polymerase/*genetics/isolation & purification/metabolism ; Recombinant Fusion Proteins/isolation & purification/metabolism ; Saccharomyces cerevisiae/genetics ; Templates, Genetic
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 83
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    A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-01-25
    Beschreibung: An in vitro assay for the interaction of SecB, a molecular chaperone from Escherichia coli, with polypeptide ligands was established based on the ability of SecB to block the refolding of denatured maltose-binding protein. Competition experiments show that SecB binds selectively to nonnative proteins with high affinity and without specificity for a particular sequence of amino acids. It is proposed that selectivity in binding is due to a kinetic partitioning of polypeptides between folding and association with SecB.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hardy, S J -- Randall, L L -- New York, N.Y. -- Science. 1991 Jan 25;251(4992):439-43.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, Washington State University, Pullman 99164-4660.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1989077" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): *ATP-Binding Cassette Transporters ; Amino Acid Sequence ; Bacterial Proteins/*metabolism ; Binding, Competitive ; Carrier Proteins/*metabolism ; *Escherichia coli ; *Escherichia coli Proteins ; Kinetics ; Ligands ; Maltose/metabolism ; Maltose-Binding Proteins ; *Monosaccharide Transport Proteins ; Protein Conformation
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 84
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    Identification of a competitive HGF antagonist encoded by an alternative transcript (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-11-29
    Beschreibung: We identified a naturally occurring hepatocyte growth factor (HGF) variant, whose predicted sequence extends only through the second kringle domain of this plasminogen-related molecule. This smaller molecule, derived from an alternative HGF transcript, lacked mitogenic activity but specifically inhibited HGF-induced mitogenesis. Cross-linking studies demonstrated that the truncated molecule competes with HGF for binding to the HGF receptor, which has been identified as the c-met protooncogene product. Thus, the same gene encodes both a growth factor and its direct antagonist.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, A M -- Rubin, J S -- Bottaro, D P -- Hirschfield, D W -- Chedid, M -- Aaronson, S A -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1382-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1720571" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Base Sequence ; Blotting, Northern ; Cell Line ; Culture Media ; DNA/genetics ; DNA Replication/drug effects ; Epidermal Growth Factor/pharmacology ; Growth Substances/*genetics/isolation & purification/pharmacology ; Hepatocyte Growth Factor ; Humans ; Kinetics ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Plasmids ; Poly A/genetics/isolation & purification ; Polymerase Chain Reaction/methods ; RNA/genetics/isolation & purification ; RNA, Messenger ; Thymidine/metabolism ; *Transcription, Genetic ; Transfection
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 85
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    Quantitation of hepatic glycogenolysis and gluconeogenesis in fasting humans with 13C NMR (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-10-25
    Beschreibung: The rate of net hepatic glycogenolysis was assessed in humans by serially measuring hepatic glycogen concentration at 3- to 12-hour intervals during a 68-hour fast with 13C nuclear magnetic resonance spectroscopy. The net rate of gluconeogenesis was calculated by subtracting the rate of net hepatic glycogenolysis from the rate of glucose production in the whole body measured with tritiated glucose. Gluconeogenesis accounted for 64 +/- 5% (mean +/- standard error of the mean) of total glucose production during the first 22 hours of fasting. In the subsequent 14-hour and 18-hour periods of the fast, gluconeogenesis accounted for 82 +/- 5% and 96 +/- 1% of total glucose production, respectively. These data show that gluconeogenesis accounts for a substantial fraction of total glucose production even during the first 22 hours of a fast in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rothman, D L -- Magnusson, I -- Katz, L D -- Shulman, R G -- Shulman, G I -- DK-34576/DK/NIDDK NIH HHS/ -- DK-40936/DK/NIDDK NIH HHS/ -- MO1-RR-00125-26/RR/NCRR NIH HHS/ -- R01 DK040936/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):573-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, Yale University School of Medicine, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948033" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adult ; Blood Glucose/metabolism ; Carbon Isotopes ; Fasting ; Female ; Glucagon/blood ; *Gluconeogenesis ; Humans ; Hydrocortisone/blood ; Insulin/blood ; Kinetics ; Liver/*metabolism ; Liver Glycogen/*metabolism ; Magnetic Resonance Spectroscopy/methods ; Male ; Nitrogen/*urine
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 86
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    Dimerization of human growth hormone by zinc (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-08-02
    Beschreibung: Size-exclusion chromatography and sedimentation equilbrium studies demonstrated that zinc ion (Zn2+) induced the dimerization of human growth hormone (hGH). Scatchard analysis of 65Zn2+ binding to hGH showed that two Zn2+ ions associate per dimer of hGH in a cooperative fashion. Cobalt (II) can substitute for Zn2+ in the hormone dimer and gives a visible spectrum characteristic of cobalt coordinated in a tetrahedral fashion by oxygen- and nitrogen-containing ligands. Replacement of potential Zn2+ ligands (His18, His21, and Glu174) in hGH with alanine weakened both Zn2+ binding and hGH dimer formation. The Zn(2+)-hGH dimer was more stable than monomeric hGH to denaturation in guanidine-HCl. Formation of a Zn(2+)-hGH dimeric complex may be important for storage of hGH in secretory granules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cunningham, B C -- Mulkerrin, M G -- Wells, J A -- New York, N.Y. -- Science. 1991 Aug 2;253(5019):545-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Protein Engineering, Genentech, South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1907025" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Binding Sites ; Chromatography, Gel ; Edetic Acid/pharmacology ; Growth Hormone/*metabolism ; Humans ; Kinetics ; Macromolecular Substances ; Models, Molecular ; Protein Binding ; Protein Conformation ; Protein Denaturation ; Spectrophotometry ; Zinc/metabolism/*pharmacology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 87
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    Dimers direct development (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-03-08
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1176-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1848724" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; DNA-Binding Proteins/*metabolism ; Drosophila ; Mammals ; Models, Structural ; Muscle Proteins/genetics ; MyoD Protein ; Protein Conformation
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 88
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    Identification and characterization of zinc binding sites in protein kinase C (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-12-20
    Beschreibung: Metal ion coordination in the regulatory domain of protein kinase C (PKC) is suggested by the conservation of six cysteines and two histidines in two homologous regions found therein. By monitoring x-ray fluorescence from a purified sample of rat PKC beta I overexpressed in insect cells, direct evidence has been obtained that PKC beta I tightly binds four zinc ions (Zn2+) per molecule. Extended x-ray absorption fine structure (EXAFS) data are best fit by an average Zn2+ coordination of one nitrogen and three sulfur atoms. Of the plausible Zn2+ coordination models, only those featuring nonbridged Zn2+ sites accommodate the EXAFS data and all of the conserved potential ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hubbard, S R -- Bishop, W R -- Kirschmeier, P -- George, S J -- Cramer, S P -- Hendrickson, W A -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1776-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, New York, NY.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1763327" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Absorptiometry, Photon/methods ; Amino Acid Sequence ; Animals ; Binding Sites ; Humans ; Macromolecular Substances ; Molecular Sequence Data ; Protein Conformation ; Protein Kinase C/chemistry/genetics/*metabolism ; Recombinant Proteins/chemistry/metabolism ; Sequence Homology, Nucleic Acid ; Zinc/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 89
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    Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-04-05
    Beschreibung: The crystal structure of the ribonuclease (RNase) H domain of HIV-1 reverse transcriptase (RT) has been determined at a resolution of 2.4 A and refined to a crystallographic R factor of 0.20. The protein folds into a five-stranded mixed beta sheet flanked by an asymmetric distribution of four alpha helices. Two divalent metal cations bind in the active site surrounded by a cluster of four conserved acidic amino acid residues. The overall structure is similar in most respects to the RNase H from Escherichia coli. Structural features characteristic of the retroviral protein suggest how it may interface with the DNA polymerase domain of p66 in the mature RT heterodimer. These features also offer insights into why the isolated RNase H domain is catalytically inactive but when combined in vitro with the isolated p51 domain of RT RNase H activity can be reconstituted. Surprisingly, the peptide bond cleaved by HIV-1 protease near the polymerase-RNase H junction of p66 is completely inaccessible to solvent in the structure reported here. This suggests that the homodimeric p66-p66 precursor of mature RT is asymmetric with one of the two RNase H domains at least partially unfolded.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davies, J F 2nd -- Hostomska, Z -- Hostomsky, Z -- Jordan, S R -- Matthews, D A -- GM 39599/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Apr 5;252(5002):88-95.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Agouron Pharmaceuticals, Inc., La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1707186" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Binding Sites ; Computer Graphics ; Crystallography ; Endoribonucleases/chemistry/*ultrastructure ; Escherichia coli/enzymology ; HIV-1/*enzymology ; Manganese/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; RNA-Directed DNA Polymerase/chemistry/*ultrastructure ; Ribonuclease H ; Structure-Activity Relationship ; X-Ray Diffraction
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 90
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    Regulation of kainate receptors by cAMP-dependent protein kinase and phosphatases (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-09-06
    Beschreibung: In the mammalian central nervous system, receptors for excitatory amino acid neurotransmitters such as the alpha-amino-3-hydroxy-5-methyl-4- isoxazolepropionic acid (AMPA)-kainate receptor mediate a large fraction of excitatory transmission. Currents induced by activation of the AMPA-kainate receptor were potentiated by agents that specifically stimulate adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase A (PKA) activity or were supported by intracellular application of the catalytic subunit of PKA by itself or in combination with cAMP. Furthermore, depression of these currents by a competitive inhibitor of PKA indicates that AMPA-kainate receptors are regulated by endogenous PKA. Endogenous protein phosphatases also regulate these receptors because an inhibitor of cellular phosphates enhanced kainate currents. Modulation of PKA and phosphatases may regulate the function of these receptors and thus contribute to synaptic plasticity in hippocampal neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, L Y -- Salter, M W -- MacDonald, J F -- New York, N.Y. -- Science. 1991 Sep 6;253(5024):1132-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1653455" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Cells, Cultured ; Cyclic AMP/pharmacology/physiology ; Ethers, Cyclic/*pharmacology ; Fetus ; Hippocampus/*physiology ; Homeostasis ; Kainic Acid/*metabolism ; Kinetics ; Macromolecular Substances ; Membrane Potentials/drug effects ; Mice ; N-Methylaspartate/pharmacology ; Neurons/drug effects/*physiology ; Okadaic Acid ; Phosphoprotein Phosphatases/*metabolism ; Protein Kinase Inhibitors ; Protein Kinases/*metabolism ; Receptors, Kainic Acid ; Receptors, Neurotransmitter/drug effects/*physiology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 91
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    Solution structures of beta peptide and its constituent fragments: relation to amyloid deposition (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-07-12
    Beschreibung: The secondary structures in solution of the synthetic, naturally occurring, amyloid beta peptides, residues 1 to 42 [beta (1-42)] and beta (1-39), and related fragments, beta (1-28) and beta (29-42), have been studied by circular dichroism and two-dimensional nuclear magnetic resonance spectroscopy. In patients with Alzheimer's disease, extracellular amyloid plaque core is primarily composed of beta (1-42), whereas cerebrovascular amyloid contains the more soluble beta (1-39). In aqueous trifluoroethanol solution, the beta (1-28), beta (1-39), and beta (1-42) peptides adopt monomeric alpha-helical structures at both low and high pH, whereas at intermediate pH (4 to 7) an oligomeric beta structure (the probable structure in plaques) predominates. Thus, beta peptide is not by itself an insoluble protein (as originally thought), and localized or normal age-related alterations of pH may be necessary for the self-assembly and deposition of beta peptide. The hydrophobic carboxyl-terminal segment, beta(29-42), exists exclusively as an oligomeric beta sheet in solution, regardless of differences in solvent, pH, or temperature, suggesting that this segment directs the folding of the complete beta (1-42) peptide to produce the beta-pleated sheet found in amyloid plaques.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barrow, C J -- Zagorski, M G -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):179-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Suntory Institute for Bioorganic Research, Osaka, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1853202" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Alzheimer Disease/*pathology ; Amino Acid Sequence ; Amyloid beta-Peptides/*chemistry ; Circular Dichroism ; Humans ; In Vitro Techniques ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; Peptides/chemistry ; Protein Conformation
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 92
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    Regulation of phagocytosis and [Ca2+]i flux by distinct regions of an Fc receptor (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-12-20
    Beschreibung: The binding of multivalent immunoglobulin G complexes to Fc receptors (Fc gamma Rs) on macrophages activates multiple immune functions. A murine macrophage cell line, but not a fibroblast cell line, that was transfected with human Fc gamma RIIA mediated phagocytosis and an intracellular Ca2+ concentration ([Ca2+]i) flux upon cross-linking of human Fc gamma RIIA. Transfected macrophages that expressed a truncated receptor lacking 17 carboxy-terminal amino acids phagocytosed small antibody complexes. However, only wild-type transfectants phagocytosed labeled erythrocytes and fluxed [Ca2+]i. Thus, the cytoplasmic domain of human Fc gamma RIIA contains distinct functional regions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Odin, J A -- Edberg, J C -- Painter, C J -- Kimberly, R P -- Unkeless, J C -- AI 24322/AI/NIAID NIH HHS/ -- AI 24671/AI/NIAID NIH HHS/ -- AR 33062/AR/NIAMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1785-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Mount Sinai Medical Center, New York, NY 10029.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1837175" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Antibodies, Monoclonal ; Antigens, Differentiation/genetics/*physiology ; CHO Cells ; Calcium/*metabolism ; Cell Line ; Cloning, Molecular ; Cricetinae ; Homeostasis ; Humans ; Immunoglobulin G/metabolism ; Kinetics ; Macrophages ; Mice ; *Phagocytosis ; Receptors, Fc/genetics/*physiology ; Receptors, IgG ; Recombinant Proteins/metabolism ; *Transfection
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 93
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    A distinct potassium channel polypeptide encoded by the Drosophila eag locus (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-06-14
    Beschreibung: Many of the signaling properties of neurons and other electrically excitable cells are determined by a diverse family of potassium channels. A number of genes that encode potassium channel polypeptides have been cloned from various organisms on the basis of their sequence similarity to the Drosophila Shaker (Sh) locus. As an alternative strategy, a molecular analysis of other Drosophila genes that were defined by mutations that perturb potassium channel function was undertaken. Sequence analysis of complementary DNA from the ether a go-go (eag) locus revealed that it encodes a structural component of potassium channels that is related to but is distinct from all identified potassium channel polypeptides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Warmke, J -- Drysdale, R -- Ganetzky, B -- NS15390/NS/NINDS NIH HHS/ -- T32GM07131/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Jun 14;252(5012):1560-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Cambridge, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1840699" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Base Sequence ; Chromosome Mapping ; DNA/genetics ; Drosophila/*genetics ; Molecular Sequence Data ; Potassium Channels/*genetics ; Protein Conformation ; Sequence Homology, Nucleic Acid
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 94
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    Enhancement of the glutamate response by cAMP-dependent protein kinase in hippocampal neurons (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-09-06
    Beschreibung: Receptor channels activated by glutamate, an excitatory neurotransmitter in the mammalian brain, are involved in processes such as long-term potentiation and excitotoxicity. Studies of glutamate receptor channels expressed in cultured hippocampal pyramidal neurons reveal that these channels are subject to neuromodulatory regulation through the adenylate cyclase cascade. The whole-cell current response to glutamate and kainate [a non-NMDA (N-methyl-D-aspartate) receptor agonist] was enhanced by forskolin, an activator of adenylate cyclase. Single-channel analysis revealed that an adenosine 3',5'-monophosphate-dependent protein kinase (PKA) increases the opening frequency and the mean open time of the non-NMDA-type glutamate receptor channels. Analysis of synaptic events indicated that forskolin, acting through PKA, increased the amplitude and decay time of spontaneous excitatory postsynaptic currents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Greengard, P -- Jen, J -- Nairn, A C -- Stevens, C F -- New York, N.Y. -- Science. 1991 Sep 6;253(5024):1135-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular and Cellular Neuroscience, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1716001" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenosine Triphosphate/pharmacology ; Animals ; Animals, Newborn ; Cells, Cultured ; Colforsin/pharmacology ; Electric Conductivity/drug effects ; Glutamates/metabolism/*pharmacology ; Hippocampus/*physiology ; Ion Channel Gating/drug effects ; Ion Channels/drug effects/*physiology ; Kainic Acid/*pharmacology ; Kinetics ; Membrane Potentials/drug effects ; N-Methylaspartate/*pharmacology ; Neurons/drug effects/*physiology ; Protein Kinases/*metabolism ; Rats ; Receptors, Glutamate ; Receptors, Neurotransmitter/drug effects/*physiology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 95
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    Reexamination of the folding of BPTI: predominance of native intermediates (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-09-20
    Beschreibung: Bovine pancreatic trypsin inhibitor (BPTI) continues to be the only protein for which a detailed pathway of folding has been described. Previous studies led to the conclusion that nonnative states are well populated in the oxidative folding of BPTI. This conclusion has broadly influenced efforts to understand protein folding. The population of intermediates present during the folding of BPTI has been reexamined by modern separation techniques. It was found that all well-populated folding intermediates contain only native disulfide bonds. These data emphasize the importance of native protein structure for understanding protein folding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weissman, J S -- Kim, P S -- GM 41307/GM/NIGMS NIH HHS/ -- RR 05927/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1991 Sep 20;253(5026):1386-93.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1716783" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Aprotinin/*chemistry ; Chromatography, High Pressure Liquid ; Disulfides/analysis ; Indicators and Reagents ; Models, Structural ; Molecular Sequence Data ; Peptide Fragments/isolation & purification ; Protein Conformation
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 96
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    Mechanism of assembly of the tyrosyl radical-dinuclear iron cluster cofactor of ribonucleotide reductase (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-07-29
    Beschreibung: Incubation of the apoB2 subunit of Escherichia coli ribonucleotide reductase with Fe2+ and O2 produces native B2, which contains the tyrosyl radical-dinuclear iron cluster cofactor required for nucleotide reduction. The chemical mechanism of this reconstitution reaction was investigated by stopped-flow absorption spectroscopy and by rapid freeze-quench EPR (electron paramagnetic resonance) spectroscopy. Two novel intermediates have been detected in the reaction. The first exhibits a broad absorption band centered at 565 nanometers. Based on known model chemistry, this intermediate is proposed to be a mu-peroxodiferric complex. The second intermediate exhibits a broad absorption band centered at 360 nanometers and a sharp, isotropic EPR signal with g = 2.00. When the reaction is carried out with 57Fe2+, this EPR signal is broadened, demonstrating that the intermediate is an iron-coupled radical. Variation of the ratio of Fe2+ to B2 in the reaction and comparison of the rates of formation and decay of the intermediates to the rate of formation of the tyrosyl radical (.Y122) suggest that both intermediates can generate .Y122. This conclusion is supported by the fact that both intermediates exhibit an increased lifetime in a mutant B2 subunit (B2-Y122F) lacking the oxidizable Y122. Based on these kinetic and spectroscopic data, a mechanism for the reaction is proposed. Unlike reactions catalyzed by heme-iron peroxidases, oxygenases, and model complexes, the reconstitution reaction appears not to involve high-valent iron intermediates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bollinger, J M Jr -- Edmondson, D E -- Huynh, B H -- Filley, J -- Norton, J R -- Stubbe, J -- GM29433/GM/NIGMS NIH HHS/ -- GM29595/GM/NIGMS NIH HHS/ -- GM32187/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 19;253(5017):292-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1650033" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Binding Sites ; Electron Spin Resonance Spectroscopy ; Escherichia coli/enzymology ; Iron/*metabolism ; Kinetics ; Macromolecular Substances ; Models, Theoretical ; Oxygen/*metabolism ; Ribonucleotide Reductases/*metabolism ; Spectrophotometry, Ultraviolet ; Time Factors ; Tyrosine/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 97
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    Glycosylphosphatidylinositol: a candidate system for interleukin-2 signal transduction (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-01-04
    Beschreibung: The mechanism of interleukin-2 (IL-2) signal transduction was analyzed by use of an inducible B lymphoma. Like normal antigen-activated B lymphocytes, the lymphoma cells respond to IL-2 by proliferating and differentiating into antibody-secreting cells; both responses are blocked by a second interleukin, IL-4. Analyses of the signaling pathway showed that IL-2 stimulated the rapid hydrolysis of an inositol-containing glycolipid to yield two possible second messengers, a myristylated diacylglycerol and an inositol phosphate-glycan. The myristylated diacylglycerol response exhibited the same IL-2 dose dependence as the growth and differentiative responses, and the generation of both hydrolysis products was inhibited by IL-4. These correlations implicate the glycosyl-phosphatidylinositol system in the intracellular relay of the IL-2 signal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eardley, D D -- Koshland, M E -- A107079/PHS HHS/ -- New York, N.Y. -- Science. 1991 Jan 4;251(4989):78-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of California, Santa Barbara 93106.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1824727" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Arachidonic Acid ; Arachidonic Acids/metabolism ; B-Lymphocytes/*immunology ; Cell Division ; Diglycerides/metabolism ; Glucosamine/metabolism ; Glycolipids/*physiology ; Glycosylphosphatidylinositols ; Inositol/metabolism ; Interleukin-2/*pharmacology ; Interleukin-4/pharmacology ; Kinetics ; Lymphoma, B-Cell/immunology/metabolism/pathology ; Myristic Acid ; Myristic Acids/metabolism ; Phosphatidylinositols/*physiology ; Polysaccharides/metabolism ; *Signal Transduction ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 98
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    Cloning and expression of a cocaine-sensitive dopamine transporter complementary DNA (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-10-25
    Beschreibung: A rat dopamine (DA) transporter complementary DNA has been isolated with combined complementary DNA homology and expression approaches. The DA transporter is a 619-amino acid protein with 12 hydrophobic putative membrane-spanning domains and homology to the norepinephrine and gamma-aminobutyric acid transporters. The expressed complementary DNA confers transport of [3H]DA in Xenopus oocytes and in COS cells. Binding of the cocaine analog [3H]CFT ([3H]2 beta-carbomethoxy-3 beta-(4-fluorophenyl)tropane) to transfected COS cell membranes yields a pharmacological profile similar to that in striatal membranes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shimada, S -- Kitayama, S -- Lin, C L -- Patel, A -- Nanthakumar, E -- Gregor, P -- Kuhar, M -- Uhl, G -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):576-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Neurobiology, National Institute on Drug Abuse, Baltimore, MD 21224.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948034" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/drug effects/*genetics/metabolism ; Cell Line ; Cell Membrane/metabolism ; Cloning, Molecular ; Cocaine/analogs & derivatives/metabolism/*pharmacology ; Dopamine/*metabolism ; Dopamine Plasma Membrane Transport Proteins ; Female ; Kinetics ; *Membrane Glycoproteins ; *Membrane Transport Proteins ; Models, Structural ; Molecular Sequence Data ; *Nerve Tissue Proteins ; Oligodeoxyribonucleotides ; Oocytes/physiology ; Plasmids ; Polymerase Chain Reaction ; Protein Conformation ; RNA, Messenger/genetics ; Rats ; Transcription, Genetic ; Transfection ; Xenopus
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 99
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    Modulation of the affinity of integrin alpha IIb beta 3 (GPIIb-IIIa) by the cytoplasmic domain of alpha IIb (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-11-08
    Beschreibung: Intracellular signaling alters integrin adhesive functions in inflammation, immune responses, hemostasis, thrombosis, and retinal development. By truncating the cytoplasmic domain of alpha IIb, the affinity of integrin alpha IIb beta 3 for ligand was increased. Reconstitution with the cytoplasmic domain from integrin alpha 5 did not reverse the increased affinity. Thus, the cytoplasmic domain of the alpha subunit of GPIIb-IIIa controls ligand binding affinity, which suggests mechanisms for inside-out transmembrane signaling through integrins. These findings imply the existence of hitherto unappreciated hereditary and acquired thrombotic disorders in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Toole, T E -- Mandelman, D -- Forsyth, J -- Shattil, S J -- Plow, E F -- Ginsberg, M H -- HL 39150/HL/NHLBI NIH HHS/ -- HL16411/HL/NHLBI NIH HHS/ -- HL28235/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):845-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Committee on Vascular Biology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948065" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; CHO Cells ; Cell Aggregation ; Cricetinae ; Cytoplasm/metabolism ; Fibrinogen/metabolism ; Kinetics ; Macromolecular Substances ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Platelet Membrane Glycoproteins/genetics/*physiology ; Transfection
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 100
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    Molecular self-assembly and nanochemistry: a chemical strategy for the synthesis of nanostructures (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-11-29
    Beschreibung: Molecular self-assembly is the spontaneous association of molecules under equilibrium conditions into stable, structurally well-defined aggregates joined by noncovalent bonds. Molecular self-assembly is ubiquitous in biological systems and underlies the formation of a wide variety of complex biological structures. Understanding self-assembly and the associated noncovalent interactions that connect complementary interacting molecular surfaces in biological aggregates is a central concern in structural biochemistry. Self-assembly is also emerging as a new strategy in chemical synthesis, with the potential of generating nonbiological structures with dimensions of 1 to 10(2) nanometers (with molecular weights of 10(4) to 10(10) daltons). Structures in the upper part of this range of sizes are presently inaccessible through chemical synthesis, and the ability to prepare them would open a route to structures comparable in size (and perhaps complementary in function) to those that can be prepared by microlithography and other techniques of microfabrication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Whitesides, G M -- Mathias, J P -- Seto, C T -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1312-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1962191" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Biotechnology/methods ; DNA/chemical synthesis/*chemistry ; Models, Chemical ; Models, Molecular ; Protein Conformation ; Proteins/chemical synthesis/*chemistry ; Thermodynamics ; Triazines/chemical synthesis/chemistry
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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