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  • Artikel  (213)
  • Mutation  (121)
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  • 1
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-12-10
    Beschreibung: The function and regulation of DNA methylation in eukaryotes remain unclear. Genes affecting methylation were identified in the fungus Neurospora crassa. A mutation in one gene, dim-2, resulted in the loss of all detectable DNA methylation. Abnormal segregation of the methylation defects in crosses led to the discovery that the methylation mutants frequently generate strains with extra chromosomes or chromosomal parts. Starvation for S-adenosylmethionine, the presumed methyl group donor for DNA methylation, also produced aneuploidy. These results suggest that DNA methylation plays a role in the normal control of chromosome behavior.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Foss, H M -- Roberts, C J -- Claeys, K M -- Selker, E U -- GM-35690/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 10;262(5140):1737-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology, University of Oregon, Eugene 97403.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7505062" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): 5-Methylcytosine ; Aneuploidy ; Azacitidine/pharmacology ; Blotting, Southern ; Chromosomes, Fungal/*metabolism ; Crosses, Genetic ; Cytosine/*analogs & derivatives/analysis ; DNA, Fungal/chemistry/*metabolism ; Genes, Fungal ; Genetic Complementation Test ; Methionine/metabolism ; Methylation ; Mutation ; Neurospora crassa/*genetics/growth & development ; Phenotype ; S-Adenosylmethionine/metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 2
    Publikationsdatum: 1993-07-23
    Beschreibung: Transcription initiation factor TFIIB recruits RNA polymerase II to the promoter subsequent to interaction with a preformed TFIID-promoter complex. The domains of TFIIB required for binding to the TFIID-promoter complex and for transcription initiation have been determined. The carboxyl-terminal two-thirds of TFIIB, which contains two direct repeats and two basic residue repeats, is sufficient for interaction with the TFIID-promoter complex. An extra 84-residue amino-terminal region, with no obvious known structural motifs, is required for basal transcription activity. Basic residues within the second basic repeat of TFIIB are necessary for stable interaction with the TFIID-promoter complex, whereas the basic character of the first basic repeat is not. Functional roles of other potential structural motifs are discussed in light of the present study.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamashita, S -- Hisatake, K -- Kokubo, T -- Doi, K -- Roeder, R G -- Horikoshi, M -- Nakatani, Y -- AI27397/AI/NIAID NIH HHS/ -- CA42567/CA/NCI NIH HHS/ -- GM45258/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jul 23;261(5120):463-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institute of Neurological Diseases and Stroke, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8332911" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Binding Sites ; DNA-Binding Proteins/*metabolism ; Drosophila ; Molecular Sequence Data ; Mutation ; *Promoter Regions, Genetic ; Protein Binding ; Transcription Factor TFIIB ; Transcription Factor TFIID ; Transcription Factors/*chemistry/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 3
    Publikationsdatum: 1993-12-17
    Beschreibung: In Saccharomyces cerevisiae, the HMR-E silencer blocks site-specific interactions between proteins and their recognition sequences in the vicinity of the silencer. Silencer function is correlated with the firing of an origin of replication at HMR-E. An essential gene with a role in transcriptional silencing was identified by means of a screen for mutations affecting expression of HMR. This gene, known as ORC2, was shown to encode a component of the origin recognition complex that binds yeast origins of replication. A temperature-sensitive mutation in ORC2 disrupted silencing in cells grown at the permissive temperature. At the restrictive temperature, the orc2-1 mutation caused cell cycle arrest at a point in the cell cycle indicative of blocks in DNA replication. The orc2-1 mutation also resulted in the enhanced mitotic loss of a plasmid, suggestive of a defect in replication. These results provide strong evidence for an in vivo role of ORC in both chromosomal replication and silencing, and provide a link between the mechanism of silencing and DNA replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Foss, M -- McNally, F J -- Laurenson, P -- Rine, J -- GM31105/GM/NIGMS NIH HHS/ -- P30ES01896-12/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 17;262(5141):1838-44.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266071" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Alleles ; Amino Acid Sequence ; Cell Cycle ; Cloning, Molecular ; *DNA Replication ; DNA, Fungal/genetics/metabolism ; *DNA-Binding Proteins ; Fungal Proteins/chemistry/*genetics/metabolism ; *Gene Expression Regulation, Fungal ; *Genes, Fungal ; Molecular Sequence Data ; Mutation ; Origin Recognition Complex ; Phenotype ; Plasmids ; *Replicon ; Repressor Proteins/chemistry/*genetics/metabolism ; Saccharomyces cerevisiae/cytology/*genetics/metabolism ; Saccharomyces cerevisiae Proteins ; Transcription, Genetic
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 4
    Publikationsdatum: 1993-08-27
    Beschreibung: The gene encoding alpha 6(IV) collagen, COL4A6, was identified on the human X chromosome in a head-to-head arrangement and within 452 base pairs of the alpha 5(IV) collagen gene, COL4A5. In earlier studies, intragenic deletions of COL4A5 were detected in a subset of patients with Alport syndrome (AS), a hereditary defect of basement membranes. In some families, AS cosegregates with diffuse leiomyomatosis (DL), a benign smooth muscle tumor diathesis. Here it is shown that patients with AS-DL harbor deletions that disrupt both COL4A5 and COL4A6. Thus, type IV collagen may regulate smooth muscle differentiation and morphogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, J -- Mochizuki, T -- Smeets, H -- Antignac, C -- Laurila, P -- de Paepe, A -- Tryggvason, K -- Reeders, S T -- New York, N.Y. -- Science. 1993 Aug 27;261(5125):1167-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06536-0812.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8356449" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Base Sequence ; Cell Differentiation ; Collagen/chemistry/*genetics ; Exons ; Female ; Fetus/metabolism ; *Gene Deletion ; Genetic Linkage ; Humans ; Leiomyoma/*genetics ; Male ; Molecular Sequence Data ; Morphogenesis ; Muscle, Smooth/cytology ; Mutation ; Nephritis, Hereditary/*genetics ; RNA, Messenger/genetics/metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 5
    Publikationsdatum: 1993-04-02
    Beschreibung: The human BTF2 basic transcription factor (also called TFIIH), which is similar to the delta factor in rat and factor b in yeast, is required for class II gene transcription. A strand displacement assay was used to show that highly purified preparation of BTF2 had an adenosine triphosphate-dependent DNA helicase activity, in addition to the previously characterized carboxyl-terminal domain kinase activity. Amino acid sequence analysis of the tryptic digest generated from the 89-kilodalton subunit of BTF2 indicated that this polypeptide corresponded to the ERCC-3 gene product, a presumed helicase implicated in the human DNA excision repair disorders xeroderma pigmentosum and Cockayne's syndrome. These findings suggest that transcription and nucleotide excision repair may share common factors and hence may be considered to be functionally related.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schaeffer, L -- Roy, R -- Humbert, S -- Moncollin, V -- Vermeulen, W -- Hoeijmakers, J H -- Chambon, P -- Egly, J M -- New York, N.Y. -- Science. 1993 Apr 2;260(5104):58-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉UPR 6520 (CNRS), Unite 184 (INSERM), Faculte de Medecine, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8465201" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenosine Triphosphate/pharmacology ; Binding Sites ; Cockayne Syndrome/enzymology/genetics ; DNA/metabolism ; DNA Helicases/metabolism ; *DNA Repair ; Humans ; Immunoblotting ; Peptide Fragments ; Promoter Regions, Genetic ; Protein Kinases/metabolism ; RNA Polymerase II/metabolism ; Recombinant Proteins/metabolism ; Sequence Analysis ; Transcription Factor TFIIH ; Transcription Factors/*metabolism ; *Transcription Factors, TFII ; Transcription, Genetic ; Trypsin/metabolism ; Xeroderma Pigmentosum/enzymology/genetics
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 6
    Publikationsdatum: 1993-09-10
    Beschreibung: Recent progress in regioselective and enantioselective epoxidations catalyzed by metalloporphyrins is discussed here, with an explanation of the biomimetic antecedents of this area and its relevance to synthetic applications. Classification of the catalysts that have been studied allows useful conclusions to be drawn about the development of this field. In particular, both the most promising biomimetic and practical catalysts have arisen from systems that can be systematically modified by convenient synthetic methodology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Collman, J P -- Zhang, X -- Lee, V J -- Uffelman, E S -- Brauman, J I -- 5R37-GM 17880/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 10;261(5127):1404-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8367724" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Alkenes/chemistry ; Binding Sites ; Catalysis ; Epoxy Compounds/chemistry/*metabolism ; Ethylenediamines/chemistry ; Hydroxylation ; Ligands ; Metalloporphyrins/chemistry/*metabolism ; Molecular Structure ; Oxidation-Reduction ; Stereoisomerism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 7
    Publikationsdatum: 1993-08-27
    Beschreibung: The Escherichia coli Ada protein repairs methylphosphotriesters in DNA by direct, irreversible methyl transfer to one of its own cysteines. Upon methyl transfer, Ada acquires the ability to bind specific DNA sequences and thereby to induce genes that confer resistance to methylating agents. The amino-terminal domain of Ada, which comprises the methylphosphotriester repair and sequence-specific DNA binding elements, contains a tightly bound zinc ion. Analysis of the zinc binding site by cadmium-113 nuclear magnetic resonance and site-directed mutagenesis revealed that zinc participates in the autocatalytic activation of the active site cysteine and may also function as a conformational switch.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Myers, L C -- Terranova, M P -- Ferentz, A E -- Wagner, G -- Verdine, G L -- New York, N.Y. -- Science. 1993 Aug 27;261(5125):1164-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program for Higher Degrees in Biophysics, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8395079" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Bacterial Proteins/chemistry/genetics/*metabolism ; Binding Sites ; Cadmium ; Cysteine/metabolism ; DNA/*metabolism ; *DNA Repair ; *Escherichia coli Proteins ; Isotopes ; Magnetic Resonance Spectroscopy ; Methylation ; Mutagenesis, Site-Directed ; O(6)-Methylguanine-DNA Methyltransferase ; Protons ; Transcription Factors ; Zinc/chemistry/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 8
    Publikationsdatum: 1993-08-06
    Beschreibung: The structure of the bifunctional, pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase was determined to 2.1-angstrom resolution. Model building suggests that a single cleavage site catalyzes both decarboxylation and transamination by maximizing stereoelectronic advantages and providing electrostatic and general base catalysis. The enzyme contains two binding sites for alkali metal ions. One is located near the active site and accounts for the dependence of activity on potassium ions. The other is located at the carboxyl terminus of an alpha helix. These sites help show how proteins can specifically bind alkali metals and how these ions can exert functional effects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Toney, M D -- Hohenester, E -- Cowan, S W -- Jansonius, J N -- GM13854/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Aug 6;261(5122):756-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Biology, University of Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8342040" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amination ; Amino Acid Sequence ; Binding Sites ; Carboxy-Lyases/*chemistry/metabolism ; Catalysis ; Computer Graphics ; Decarboxylation ; Metals, Alkali/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Secondary ; X-Ray Diffraction
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-12-10
    Beschreibung: Transmission of an external signal from receptors to downstream targets is often mediated by a conserved set of protein kinases that act in sequence (a kinase cascade). In haploid strains of Saccharomyces cerevisiae, a signal initiated by peptide pheromones is transmitted through this kinase cascade to a transcription factor STE12, which is required for the expression of many mating-specific genes. Here it was shown that in diploids some of the same kinases and STE12 are required for filamentous growth, but the pheromone receptors and guanosine triphosphate-binding protein are not required for filament formation. Thus, a similar kinase cascade is activated by different signals in haploids and diploids and mediates different developmental outcomes in the two cell types.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, H -- Styles, C A -- Fink, G R -- GM 35010/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 10;262(5140):1741-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Cambridge 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8259520" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Fungal Proteins/*metabolism ; GTP-Binding Proteins/metabolism ; Genes, Fungal ; Mutation ; Peptides/*metabolism/pharmacology ; Phenotype ; Protein Kinases/*metabolism ; Receptors, Mating Factor ; Receptors, Peptide/metabolism ; Saccharomyces cerevisiae/genetics/*growth & development/metabolism ; *Saccharomyces cerevisiae Proteins ; *Signal Transduction ; Transcription Factors/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 10
    Publikationsdatum: 1993-10-01
    Beschreibung: Technological advances have made possible the development of high-resolution genetic linkage maps for the mouse. These maps in turn offer exciting prospects for understanding mammalian genome evolution through comparative mapping, for developing mouse models of human disease, and for identifying the function of all genes in the organism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Copeland, N G -- Jenkins, N A -- Gilbert, D J -- Eppig, J T -- Maltais, L J -- Miller, J C -- Dietrich, W F -- Weaver, A -- Lincoln, S E -- Steen, R G -- HG00198/HG/NHGRI NIH HHS/ -- N01-CO-74101/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Oct 1;262(5130):57-66.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉ABL-Basic Research Program, 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/8211130" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Biological Evolution ; *Chromosome Mapping ; Cloning, Molecular ; Crosses, Genetic ; Female ; Genetic Markers ; *Genome ; Human Genome Project ; Humans ; Male ; Mice/*genetics ; Multigene Family ; Muridae/*genetics ; Mutation ; Neoplasms/genetics
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 11
    Publikationsdatum: 1993-11-05
    Beschreibung: B7 delivers a costimulatory signal through CD28, resulting in interleukin-2 secretion and T cell proliferation. Blockade of this pathway results in T cell anergy. The in vivo role of B7 was evaluated with B7-deficient mice. These mice had a 70 percent decrease in costimulation of the response to alloantigen. Despite lacking B7 expression, activated B cells from these mice bound CTLA-4 and GL1 monoclonal antibody, demonstrating that alternative CTLA-4 ligand or ligands exist. These receptors are functionally important because the residual allogenic mixed lymphocyte responses were blocked by CTLA4Ig. Characterization of these CTLA-4 ligands should lead to strategies for manipulating the immune response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freeman, G J -- Borriello, F -- Hodes, R J -- Reiser, H -- Hathcock, K S -- Laszlo, G -- McKnight, A J -- Kim, J -- Du, L -- Lombard, D B -- CA 40216/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 5;262(5135):907-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Hematologic Malignancies, Dana-Farber Cancer Institute, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7694362" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Abatacept ; Animals ; Antigens, CD ; Antigens, CD80/genetics/*immunology/metabolism ; Antigens, Differentiation/immunology/*metabolism ; B-Lymphocytes/*immunology ; Base Sequence ; CTLA-4 Antigen ; Cell Line ; *Immunoconjugates ; Interleukin-2/secretion ; Isoantigens/immunology ; Lymphocyte Activation ; Lymphocyte Culture Test, Mixed ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Mice, Knockout ; Molecular Sequence Data ; Mutation ; T-Lymphocytes/*immunology ; Transfection
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 12
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-09-10
    Beschreibung: An iterative in vitro selection procedure was used to isolate a new class of catalytic RNAs (ribozymes) from a large pool of random-sequence RNA molecules. These ribozymes ligate two RNA molecules that are aligned on a template by catalyzing the attack of a 3'-hydroxyl on an adjacent 5'-triphosphate--a reaction similar to that employed by the familiar protein enzymes that synthesize RNA. The corresponding uncatalyzed reaction also yields a 3',5'-phosphodiester bond. In vitro evolution of the population of new ribozymes led to improvement of the average ligation activity and the emergence of ribozymes with reaction rates 7 million times faster than the uncatalyzed reaction rate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bartel, D P -- Szostak, J W -- New York, N.Y. -- Science. 1993 Sep 10;261(5127):1411-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Massachusetts General Hospital, Boston 02114.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7690155" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Base Sequence ; Biological Evolution ; Catalysis ; Kinetics ; Magnesium/metabolism ; Molecular Sequence Data ; Mutation ; Oligoribonucleotides/metabolism ; RNA/*metabolism ; RNA Ligase (ATP)/chemistry/isolation & purification/metabolism ; RNA, Catalytic/chemistry/*isolation & purification/metabolism ; Temperature ; Templates, Genetic
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 13
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-02-12
    Beschreibung: Pyruvate oxidase from Lactobacillus plantarum is a tetrameric enzyme that decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. Structure determination at 2.1 angstroms showed that the cofactors thiamine pyrophosphate (TPP) and flavin adenine dinucleotide (FAD) are bound at the carboxyl termini of six-stranded parallel beta sheets. The pyrophosphate moiety of TPP is bound to a metal ion and to a beta alpha alpha beta unit corresponding to an established sequence fingerprint. The spatial arrangement of TPP and FAD suggests that the oxidation of the oxyethyl intermediate does not occur by hydride displacement but rather by a two-step transfer of two electrons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Muller, Y A -- Schulz, G E -- New York, N.Y. -- Science. 1993 Feb 12;259(5097):965-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Organische Chemie und Biochemie, Albert-Ludwigs-Universitat, Freiburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8438155" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Binding Sites ; Chemistry, Physical ; Crystallization ; Flavin-Adenine Dinucleotide/metabolism/*pharmacology ; Lactobacillus/*enzymology ; Macromolecular Substances ; Molecular Sequence Data ; Molecular Structure ; Physicochemical Phenomena ; Protein Structure, Secondary ; Pyruvate Oxidase/*chemistry/metabolism ; Thiamine Pyrophosphate/metabolism/*pharmacology ; X-Ray Diffraction
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 14
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-08-13
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freedman, D -- New York, N.Y. -- Science. 1993 Aug 13;261(5123):844-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8346437" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; *Artificial Intelligence ; Base Sequence ; Collagen/chemistry/genetics/physiology ; DNA/chemistry/genetics ; Humans ; Molecular Sequence Data ; Mutation ; *Protein Structure, Secondary ; *Protein Structure, Tertiary ; *Sequence Analysis, DNA ; Software
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 15
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-12-03
    Beschreibung: Studies in vivo and in vitro have shown that the packaging of DNA into chromatin can affect gene expression. Here, binding of the yeast transcriptional activator GAL4 to DNA in chromatin has been investigated in vivo with a yeast episome. A positioned nucleosome that is present in cells grown in glucose and contains a single GAL4 binding site is disrupted by GAL4 binding in galactose. GAL4 can also bind to DNA in chromatin when the carboxyl-terminal activation domain of GAL4 is either masked by GAL80 or is absent. These results show that a transcription factor can bind to its site in vivo in what would appear to be a repressive chromatin structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morse, R H -- New York, N.Y. -- Science. 1993 Dec 3;262(5139):1563-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular and Developmental 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/8248805" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Base Sequence ; Binding Sites ; DNA-Binding Proteins/*metabolism ; Fungal Proteins/*metabolism ; Galactose/metabolism ; Glucose/metabolism ; Molecular Sequence Data ; Nucleosomes/*metabolism ; Plasmids ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/*metabolism ; *Saccharomyces cerevisiae Proteins ; Transcription Factors/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 16
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-07-30
    Beschreibung: Anopheles gambiae, the primary vector of human malaria in Africa, is responsible for approximately a million deaths per year, mostly of children. Despite its significance in disease transmission, this mosquito has not been studied extensively by genetic or molecular techniques. To facilitate studies on this vector, a genetic map has been developed that covers the X chromosome at an average resolution of 2 centimorgans. This map has been integrated with the chromosome banding pattern and used to localize a recessive, sex-linked mutation (white eye) to within 1 centimorgan of flanking markers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zheng, L -- Collins, F H -- Kumar, V -- Kafatos, F C -- New York, N.Y. -- Science. 1993 Jul 30;261(5121):605-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Developmental Biology, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8342025" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Alleles ; Animals ; Anopheles/*genetics ; Base Sequence ; Chromosome Banding ; *Chromosome Mapping ; Crosses, Genetic ; DNA, Satellite/genetics ; Female ; *Genes, Insect ; Genes, Recessive ; Genetic Markers ; Insect Vectors/*genetics ; Malaria/transmission ; Male ; Molecular Sequence Data ; Mutation ; Recombination, Genetic ; *X Chromosome
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 17
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-02-19
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Funder, J W -- New York, N.Y. -- Science. 1993 Feb 19;259(5098):1132-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Baker Medical Research Institute, Prahran, Victoria, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8382375" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Base Sequence ; Binding Sites ; DNA/*metabolism ; DNA-Binding Proteins/*metabolism ; Gene Expression Regulation ; Glucocorticoids/*physiology ; Mineralocorticoids/*physiology ; Models, Biological ; Molecular Sequence Data ; Receptors, Glucocorticoid/*metabolism ; Receptors, Mineralocorticoid ; Receptors, Steroid/*metabolism ; *Transcription, Genetic
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 18
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-04-16
    Beschreibung: Klenow fragment of Escherichia coli DNA polymerase I, which was cocrystallized with duplex DNA, positioned 11 base pairs of DNA in a groove that lies at right angles to the cleft that contains the polymerase active site and is adjacent to the 3' to 5' exonuclease domain. When the fragment bound DNA, a region previously referred to as the "disordered domain" became more ordered and moved along with two helices toward the 3' to 5' exonuclease domain to form the binding groove. A single-stranded, 3' extension of three nucleotides bound to the 3' to 5' exonuclease active site. Although this cocrystal structure appears to be an editing complex, it suggests that the primer strand approaches the catalytic site of the polymerase from the direction of the 3' to 5' exonuclease domain and that the duplex DNA product may bend to enter the cleft that contains the polymerase catalytic site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beese, L S -- Derbyshire, V -- Steitz, T A -- GM28550/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Apr 16;260(5106):352-5.〈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/8469987" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Base Sequence ; Binding Sites ; Crystallization ; DNA/chemistry/*metabolism ; DNA Polymerase I/*chemistry/metabolism ; DNA Replication ; DNA, Single-Stranded/chemistry/metabolism ; Escherichia coli/*enzymology ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Templates, Genetic
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 19
    Publikationsdatum: 1993-11-26
    Beschreibung: A DNA sequence rich in (A+T), located upstream of the -10, -35 region of the Escherichia coli ribosomal RNA promoter rrnB P1 and called the UP element, stimulates transcription by a factor of 30 in vivo, as well as in vitro in the absence of protein factors other than RNA polymerase (RNAP). When fused to other promoters, such as lacUV5, the UP element also stimulates transcription, indicating that it is a separate promoter module. Mutations in the carboxyl-terminal region of the alpha subunit of RNAP prevent stimulation of these promoters by the UP element although the mutant enzymes are effective in transcribing the "core" promoters (those lacking the UP element). Protection of UP element DNA by the mutant RNAPs is severely reduced in footprinting experiments, suggesting that the selective decrease in transcription might result from defective interactions between alpha and the UP element. Purified alpha binds specifically to the UP element, confirming that alpha acts directly in promoter recognition. Transcription of three other promoters was also reduced by the COOH-terminal alpha mutations. These results suggest that UP elements comprise a third promoter recognition region (in addition to the -10, -35 recognition hexamers, which interact with the sigma subunit) and may account for the presence of (A+T)-rich DNA upstream of many prokaryotic promoters. Since the same alpha mutations also block activation by some transcription factors, mechanisms of promoter stimulation by upstream DNA elements and positive control by certain transcription factors may be related.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ross, W -- Gosink, K K -- Salomon, J -- Igarashi, K -- Zou, C -- Ishihama, A -- Severinov, K -- Gourse, R L -- AI90035/AI/NIAID NIH HHS/ -- GM49242/GM/NIGMS NIH HHS/ -- R01 GM37048/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 26;262(5138):1407-13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Bacteriology, University of Wisconsin-Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8248780" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Base Sequence ; Binding Sites ; Carrier Proteins/metabolism ; DNA, Bacterial/*metabolism ; DNA-Binding Proteins/metabolism ; DNA-Directed RNA Polymerases/*metabolism ; Escherichia coli/enzymology/*genetics ; *Escherichia coli Proteins ; Integration Host Factors ; Molecular Sequence Data ; *Promoter Regions, Genetic ; Transcription Factors/metabolism ; Transcription, Genetic ; *rRNA Operon
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 20
    Publikationsdatum: 1993-05-28
    Beschreibung: A gene discovered by positional cloning has been identified as the von Hippel-Lindau (VHL) disease tumor suppressor gene. A restriction fragment encompassing the gene showed rearrangements in 28 of 221 VHL kindreds. Eighteen of these rearrangements were due to deletions in the candidate gene, including three large nonoverlapping deletions. Intragenic mutations were detected in cell lines derived from VHL patients and from sporadic renal cell carcinomas. The VHL gene is evolutionarily conserved and encodes two widely expressed transcripts of approximately 6 and 6.5 kilobases. The partial sequence of the inferred gene product shows no homology to other proteins, except for an acidic repeat domain found in the procyclic surface membrane glycoprotein of Trypanosoma brucei.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Latif, F -- Tory, K -- Gnarra, J -- Yao, M -- Duh, F M -- Orcutt, M L -- Stackhouse, T -- Kuzmin, I -- Modi, W -- Geil, L -- New York, N.Y. -- Science. 1993 May 28;260(5112):1317-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Immunobiology, National Cancer Institute-Frederick Cancer Research and Development Center (NCI-FCRDC), Frederick, MD 21702-1201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8493574" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Base Sequence ; Carcinoma, Renal Cell/genetics ; Chromosomes, Human, Pair 3 ; Cloning, Molecular ; Gene Deletion ; *Genes, Tumor Suppressor ; Humans ; Kidney Neoplasms/genetics ; Membrane Glycoproteins/chemistry/*genetics ; Molecular Sequence Data ; Mutation ; Open Reading Frames ; Pedigree ; Polymorphism, Genetic ; Tumor Cells, Cultured ; von Hippel-Lindau Disease/*genetics
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 21
    Publikationsdatum: 1993-01-29
    Beschreibung: The phosphocarrier protein IIIGlc is an integral component of the bacterial phosphotransferase (PTS) system. Unphosphorylated IIIGlc inhibits non-PTS carbohydrate transport systems by binding to diverse target proteins. The crystal structure at 2.6 A resolution of one of the targets, glycerol kinase (GK), in complex with unphosphorylated IIIGlc, glycerol, and adenosine diphosphate was determined. GK contains a region that is topologically identical to the adenosine triphosphate binding domains of hexokinase, the 70-kD heat shock cognate, and actin. IIIGlc binds far from the catalytic site of GK, indicating that long-range conformational changes mediate the inhibition of GK by IIIGlc. GK and IIIGlc are bound by hydrophobic and electrostatic interactions, with only one hydrogen bond involving an uncharged group. The phosphorylation site of IIIGlc, His90, is buried in a hydrophobic environment formed by the active site region of IIIGlc and a 3(10) helix of GK, suggesting that phosphorylation prevents IIIGlc binding to GK by directly disrupting protein-protein interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hurley, J H -- Faber, H R -- Worthylake, D -- Meadow, N D -- Roseman, S -- Pettigrew, D W -- Remington, S J -- 5-R37 GM38759/GM/NIGMS NIH HHS/ -- GM 42618-01A1/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jan 29;259(5095):673-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology, University of Oregon, Eugene 97403.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8430315" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenosine Diphosphate/metabolism ; Amino Acid Sequence ; Binding Sites ; Escherichia coli/*enzymology ; Escherichia coli Proteins ; Glycerol Kinase/*chemistry/*metabolism ; Hydrogen Bonding ; Models, Molecular ; Models, Structural ; Phosphoenolpyruvate Sugar Phosphotransferase System/*chemistry/*metabolism ; *Protein Structure, Secondary
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 22
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-06-04
    Beschreibung: Pectate lyases are secreted by pathogens and initiate soft-rot diseases in plants by cleaving polygalacturonate, a major component of the plant cell wall. The three-dimensional structure of pectate lyase C from Erwinia chrysanthemi has been solved and refined to a resolution of 2.2 angstroms. The enzyme folds into a unique motif of parallel beta strands coiled into a large helix. Within the core, the amino acids form linear stacks and include a novel asparagine ladder. The sequence similarities that pectate lyases share with pectin lyases, pollen and style proteins, and tubulins suggest that the parallel beta helix motif may occur in a broad spectrum of proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoder, M D -- Keen, N T -- Jurnak, F -- New York, N.Y. -- Science. 1993 Jun 4;260(5113):1503-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of California, Riverside 92521.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8502994" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Binding Sites ; Calcium ; Crystallography ; Isoenzymes/*chemistry ; Models, Molecular ; Molecular Sequence Data ; Pectobacterium chrysanthemi/enzymology ; Polysaccharide-Lyases/*chemistry ; Protein Structure, Secondary ; *Protein Structure, Tertiary
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 23
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-06-18
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1993 Jun 18;260(5115):1722-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8511575" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): *Aggression ; Female ; *Genes, Recessive ; Genetic Diseases, Inborn ; Humans ; Male ; Monoamine Oxidase/deficiency/*genetics ; Mutation ; Pedigree ; *X Chromosome
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 24
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-10-01
    Beschreibung: Several proteins are involved in the early steps of the spliceosome assembly pathway. Protein-protein interactions have been identified between two Saccharomyces cerevisiae yeast splicing factors, PRP9 and SPP91. Here it is demonstrated that protein-protein interactions occur between SPP91 and PRP11. The combination of the prp9-1 mutant and a truncated prp11 mutant exhibits a synthetic lethal phenotype, suggestive of a common biochemical defect. The PRP9 and PRP11 proteins do not interact directly, but the PRP9 and PRP11 molecules can simultaneously bind SPP91 to form a three-molecule complex. Structurally and functionally related proteins are found in mammalian cells and are associated in a single biochemical fraction. This strongly suggests that the PRP9-SPP91-PRP11 complex is a key element of the splicing machinery.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Legrain, P -- Chapon, C -- New York, N.Y. -- Science. 1993 Oct 1;262(5130):108-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departement de Biologie Moleculaire, Institut Pasteur, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211114" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Fungal Proteins/genetics/*metabolism ; Genes, Fungal ; Genes, Reporter ; Mutation ; Phenotype ; *RNA Splicing ; RNA-Binding Proteins ; Recombinant Fusion Proteins/biosynthesis ; Saccharomyces cerevisiae/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Spliceosomes/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 25
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-06-18
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lehn, J M -- New York, N.Y. -- Science. 1993 Jun 18;260(5115):1762-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉College de France, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8511582" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Binding Sites ; Chemical Phenomena ; *Chemistry ; *Macromolecular Substances
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 26
    Publikationsdatum: 1993-05-07
    Beschreibung: A predisposition to colorectal cancer is shown to be linked to markers on chromosome 2 in some families. Molecular features of "familial" cancers were compared with those of sporadic colon cancers. Neither the familial nor sporadic cancers showed loss of heterozygosity for chromosome 2 markers, and the incidence of mutations in KRAS, P53, and APC was similar in the two groups of tumors. Most of the familial cancers, however, had widespread alterations in short repeated DNA sequences, suggesting that numerous replication errors had occurred during tumor development. Thirteen percent of sporadic cancers had identical abnormalities and these cancers shared biologic properties with the familial cases. These data suggest a mechanism for familial tumorigenesis different from that mediated by classic tumor suppressor genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aaltonen, L A -- Peltomaki, P -- Leach, F S -- Sistonen, P -- Pylkkanen, L -- Mecklin, J P -- Jarvinen, H -- Powell, S M -- Jen, J -- Hamilton, S R -- CA 35494/CA/NCI NIH HHS/ -- CA 47527/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 May 7;260(5109):812-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Genetics, University of Helsinki, Finland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8484121" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Chromosome Mapping ; *Chromosomes, Human, Pair 2 ; Colonic Neoplasms/*genetics ; Colorectal Neoplasms/*genetics ; DNA, Satellite/genetics ; Female ; Genetic Markers ; Humans ; Lod Score ; Male ; Mutation ; Pedigree ; Polymorphism, Genetic ; Rectal Neoplasms/genetics ; Repetitive Sequences, Nucleic Acid
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 27
    Publikationsdatum: 1993-09-17
    Beschreibung: Staphylococcal nuclease is an enzyme with enormous catalytic power, accelerating phosphodiester bond hydrolysis by a factor of 10(16) over the spontaneous rate. The mechanistic basis for this rate acceleration was investigated by substitution of the active site residues Glu43, Arg35, and Arg87 with unnatural amino acid analogs. Two Glu43 mutants, one containing the nitro analog of glutamate and the other containing homoglutamate, retained high catalytic activity at pH 9.9, but were less active than the wild-type enzyme at lower pH values. The x-ray crystal structure of the homoglutamate mutant revealed that the carboxylate side chain of this residue occupies a position and orientation similar to that of Glu43 in the wild-type enzyme. The increase in steric bulk is accommodated by a backbone shift and altered torsion angles. The nitro and the homoglutamate mutants display similar pH versus rate profiles, which differ from that of the wild-type enzyme. Taken together, these studies suggest that Glu43 may not act as a general base, as previously thought, but may play a more complex structural role during catalysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Judice, J K -- Gamble, T R -- Murphy, E C -- de Vos, A M -- Schultz, P G -- GM 14012-02S1/GM/NIGMS NIH HHS/ -- R01 GM49220/GM/NIGMS NIH HHS/ -- T32GM-08388/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 17;261(5128):1578-81.〈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/8103944" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): 2-Aminoadipic Acid/chemistry ; Amino Acids/chemistry ; Aminobutyrates/chemistry ; Arginine/*chemistry ; Binding Sites ; Catalysis ; Glutamates/*chemistry ; Glutamic Acid ; Homocysteine/analogs & derivatives/chemistry ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Kinetics ; Micrococcal Nuclease/chemistry/genetics/*metabolism ; Mutation ; Plasmids ; X-Ray Diffraction
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 28
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-12-17
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Newlon, C S -- New York, N.Y. -- Science. 1993 Dec 17;262(5141):1830-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, University of Medicine and Dentistry-New Jersey Medical School, Newark 07103.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266070" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Base Sequence ; *DNA Replication ; DNA, Fungal/genetics/metabolism ; DNA-Binding Proteins/chemistry/*genetics ; Fungal Proteins/chemistry/*genetics/metabolism ; *Gene Expression Regulation, Fungal ; Genes, Fungal ; Molecular Sequence Data ; Mutation ; Origin Recognition Complex ; *Replicon ; Repressor Proteins/*genetics/metabolism ; Saccharomyces cerevisiae/*genetics ; Transcription, Genetic
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 29
    Publikationsdatum: 1993-09-10
    Beschreibung: Expression of either the CD4 or CD8 glycoproteins discriminates two functionally distinct lineages of T lymphocytes. A null mutation in the gene encoding CD4 impairs the development of the helper cell lineage that is normally defined by CD4 expression. Infection of CD4-null mice with Leishmania has revealed a population of functional helper T cells that develops despite the absence of CD4. These CD8- alpha beta T cell receptor+ T cells are major histocompatibility complex class II-restricted and produce interferon-gamma when challenged with parasite antigens. These results indicate that T lymphocyte lineage commitment and peripheral function need not depend on the function of CD4.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Locksley, R M -- Reiner, S L -- Hatam, F -- Littman, D R -- Killeen, N -- AI30663/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 10;261(5127):1448-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Francisco 94143-0654.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8367726" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Antigens, CD4/genetics/*immunology ; Antigens, CD8/immunology ; Antigens, Protozoan/immunology ; B-Lymphocytes/immunology ; Base Sequence ; CD4-CD8 Ratio ; Histocompatibility Antigens Class II/immunology ; Hypersensitivity, Delayed ; Interferon-gamma/biosynthesis/immunology ; Leishmania tropica/*immunology ; Leishmaniasis, Cutaneous/*immunology ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Mutation ; Oligodeoxyribonucleotides ; Receptors, Antigen, T-Cell, alpha-beta/immunology ; T-Lymphocytes/immunology ; T-Lymphocytes, Helper-Inducer/*immunology
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  • 30
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-08-06
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, J -- New York, N.Y. -- Science. 1993 Aug 6;261(5122):678.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7688140" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Antiviral Agents/*pharmacology ; Didanosine/pharmacology ; HIV/*drug effects/enzymology/genetics ; Mutation ; Nevirapine ; Pyridines/pharmacology ; *Reverse Transcriptase Inhibitors ; Virus Replication/drug effects ; Zidovudine/pharmacology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 31
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-06-11
    Beschreibung: The guanosine triphosphate (GTP)-binding protein Ras functions in regulating growth and differentiation; however, little is known about the protein interactions that bring about its biological activity. Wild-type Ras or mutant forms of Ras were covalently attached to an insoluble matrix and then used to examine the interaction of signaling proteins with Ras. Forms of Ras activated either by mutation (Gly12Val) or by binding of the GTP analog, guanylyl-imidodiphosphate (GMP-PNP) interacted specifically with Raf-1 whereas an effector domain mutant, Ile36Ala, failed to interact with Raf-1. Mitogen-activated protein kinase (MAP kinase) activity was only associated with activated forms of Ras. The specific interaction of activated Ras with active MAP kinase kinase (MAPKK) was confirmed by direct assays. Thus the forming of complexes containing MAPKK activity and Raf-1 protein are dependent upon the activity of Ras.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moodie, S A -- Willumsen, B M -- Weber, M J -- Wolfman, A -- CA 39076/CA/NCI NIH HHS/ -- CA 40042/CA/NCI NIH HHS/ -- GM 41220/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1993 Jun 11;260(5114):1658-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Cleveland Clinic Foundation, OH 44106.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8503013" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Brain/metabolism ; Guanosine Triphosphate/*metabolism ; Guanylyl Imidodiphosphate/metabolism ; In Vitro Techniques ; Mitogen-Activated Protein Kinase 1 ; Mitogen-Activated Protein Kinase Kinases ; Mutation ; Phosphorylation ; Protein Binding ; Protein Kinases/*metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Protein-Tyrosine Kinases/metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-raf ; Proto-Oncogene Proteins p21(ras)/*metabolism ; Rats ; Signal Transduction/physiology
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    Standort Signatur Erwartet Verfügbarkeit
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  • 32
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-05-14
    Beschreibung: Antigen receptor genes are assembled by site-specific DNA rearrangement. The recombination activator genes RAG-1 and RAG-2 are essential for this process, termed V(D)J rearrangement. The activity and stability of the RAG-2 protein have now been shown to be regulated by phosphorylation. In fibroblasts RAG-2 was phosphorylated predominantly at two serine residues, one of which affected RAG-2 activity in vivo. The threonine at residue 490 was phosphorylated by p34cdc2 kinase in vitro; phosphorylation at this site in vivo was associated with rapid degradation of RAG-2. Instability was transferred to chimeric proteins by a 90-residue portion of RAG-2. Mutation of the p34cdc2 phosphorylation site of the tumor suppressor protein p53 conferred a similar phenotype, suggesting that this association between phosphorylation and degradation is a general mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, W C -- Desiderio, S -- CA16519/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 May 14;260(5110):953-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Genetics, 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/8493533" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): 3T3 Cells ; Amino Acid Sequence ; Animals ; CDC2 Protein Kinase/metabolism ; Cell Line ; *DNA-Binding Proteins ; *Gene Rearrangement ; Humans ; Mice ; Molecular Sequence Data ; Mutation ; Nuclear Proteins ; Phosphorylation ; Proteins/chemistry/genetics/*metabolism ; Receptors, Antigen/*genetics ; Recombinant Fusion Proteins/metabolism ; Transfection ; Tumor Suppressor Protein p53/genetics
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 33
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-11-26
    Beschreibung: Protein phosphatases play important roles in the regulation of cell growth and metabolism, yet little is known about their enzymatic mechanism. By extrapolation from data on inhibitors of other types of hydrolases, an inhibitor of prostatic acid phosphatase was designed that is likely to function as a mechanism-based phosphotyrosine phosphatase inactivator. This molecule, 4-(fluoromethyl)phenyl phosphate, represents a useful paradigm for the design of potent and specific phosphatase inhibitors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Myers, J K -- Widlanski, T S -- R01 GM47918-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 26;262(5138):1451-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Indiana University, Bloomington 47405.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8248785" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Acid Phosphatase/*antagonists & inhibitors/metabolism ; Alkylation ; Binding Sites ; Drug Design ; Humans ; Hydrolysis ; Kinetics ; Male ; Organophosphorus Compounds/metabolism/*pharmacology ; Prostate/*enzymology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 34
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-09-03
    Beschreibung: Annexins are a family of calcium- and phospholipid-binding proteins implicated in mediating membrane-related processes such as secretion, signal transduction, and ion channel activity. The crystal structure of rat annexin V was solved to 1.9 angstrom resolution by multiple isomorphous replacement. Unlike previously solved annexin V structures, all four domains bound calcium in this structure. Calcium binding in the third domain induced a large relocation of the calcium-binding loop regions, exposing the single tryptophan residue to the solvent. These alterations in annexin V suggest a role for domain 3 in calcium-triggered interaction with phospholipid membranes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Concha, N O -- Head, J F -- Kaetzel, M A -- Dedman, J R -- Seaton, B A -- R01-DK-41740/DK/NIDDK NIH HHS/ -- R01-NS-20357/NS/NINDS NIH HHS/ -- R29-GM-44554/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 3;261(5126):1321-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, Boston University School of Medicine, MA 02118.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8362244" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Annexin A5/*chemistry/metabolism ; Binding Sites ; Calcium/*metabolism ; Computer Graphics ; Crystallization ; Humans ; Hydrogen Bonding ; Molecular Sequence Data ; Protein Conformation ; Rats ; Sequence Alignment ; Tryptophan/chemistry ; X-Ray Diffraction
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 35
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-11-19
    Beschreibung: Humanized antibodies are highly efficient as immunotherapeutic reagents and have many advantages over rodent antibodies. A mouse strain was generated by gene targeting to replace the mouse kappa light chain constant (C) region gene with the human C kappa gene. Mice homozygous for the replacement mutation (C kappa R) produced normal concentrations of serum antibodies, most of which carry chimeric kappa light chains, and mounted normal immune responses to hapten-protein conjugates. This technology provides a feasible option for the generation of high-affinity humanized antibodies by means of the powerful somatic hypermutation-selection mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zou, Y R -- Gu, H -- Rajewsky, K -- New York, N.Y. -- Science. 1993 Nov 19;262(5137):1271-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genetics, University of Cologne, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235658" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; B-Lymphocytes/*immunology ; Base Sequence ; Gene Rearrangement ; *Genes, Immunoglobulin ; Humans ; Immunoglobulin Constant Regions/*biosynthesis/genetics ; Immunoglobulin Isotypes/biosynthesis ; Immunoglobulin kappa-Chains/*biosynthesis/genetics ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; Mutation ; Polymerase Chain Reaction ; Recombinant Fusion Proteins/biosynthesis ; Stem Cells ; Transfection
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 36
    Publikationsdatum: 1993-07-02
    Beschreibung: The enhancer for the immunoglobulin mu heavy chain gene (IgH) activates a heterologous gene at the pre-B cell stage of B lymphocyte differentiation. A lymphoid-specific element, microB, is necessary for enhancer function in pre-B cells. A microB binding protein is encoded by the PU.1/Spi-1 proto-oncogene. Another sequence element, microA, was identified in the mu enhancer that binds the product of the ets-1 proto-oncogene. The microA motif was required for microB-dependent enhancer activity, which suggests that a minimal B cell-specific enhancer is composed of both the PU.1 and Ets-1 binding sites. Co-expression of both PU.1 and Ets-1 in nonlymphoid cells trans-activated reporter plasmids that contained the minimal mu enhancer. These results implicate two members of the Ets family in the activation of IgH gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nelsen, B -- Tian, G -- Erman, B -- Gregoire, J -- Maki, R -- Graves, B -- Sen, R -- 1K04GM00563/GM/NIGMS NIH HHS/ -- GM38663/GM/NIGMS NIH HHS/ -- GM38925/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jul 2;261(5117):82-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rosenstiel Research Center, Brandeis University, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8316859" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; B-Lymphocytes/cytology/*metabolism ; Base Sequence ; Binding Sites ; Cell Differentiation ; Cell Line ; DNA-Binding Proteins/*genetics/metabolism ; *Enhancer Elements, Genetic ; Female ; Genes, Immunoglobulin ; Humans ; Immunoglobulin mu-Chains/*genetics ; Molecular Sequence Data ; Mutation ; Proto-Oncogene Protein c-ets-1 ; Proto-Oncogene Proteins/*genetics/metabolism ; Proto-Oncogene Proteins c-ets ; Retroviridae Proteins, Oncogenic ; Transcription Factors/*genetics/metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 37
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-12-17
    Beschreibung: The genes encoding two of the subunits of the Saccharomyces cerevisiae origin recognition complex (ORC) have been isolated. Characterization of a temperature-sensitive mutation in the gene encoding the 72-kD subunit of ORC (ORC2) indicates that this protein complex functions early in the DNA replication process. Moreover, ORC derived from orc2ts cells is defective for DNA binding. Others have shown a defect in orc2ts cells in transcriptional silencing at the silent mating-type loci. Consistent with this finding, ORC specifically binds to each of the four mating-type silencers identified in yeast. These findings support the hypothesis that ORC acts as an initiator protein at yeast origins of DNA replication and suggest that ORC also functions in the determination of transcriptional domains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bell, S P -- Kobayashi, R -- Stillman, B -- AI20460/AI/NIAID NIH HHS/ -- CA13106/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 17;262(5141):1844-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, NY 11724.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266072" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; *DNA Replication ; DNA, Fungal/biosynthesis ; *DNA-Binding Proteins ; Fungal Proteins/chemistry/*genetics/metabolism ; *Gene Expression Regulation, Fungal ; Genes, Fungal ; Genes, Mating Type, Fungal ; Molecular Sequence Data ; Mutation ; Origin Recognition Complex ; *Replicon ; Repressor Proteins/chemistry/*genetics/metabolism ; S Phase ; Saccharomyces cerevisiae/cytology/*genetics/metabolism ; Saccharomyces cerevisiae Proteins ; Temperature ; Transcription, Genetic
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 38
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-06-04
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schroeder, R -- Streicher, B -- Wank, H -- New York, N.Y. -- Science. 1993 Jun 4;260(5113):1443-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Microbiology and Genetics, Vienna Biocenter, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8502988" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Aminoglycosides ; Anti-Bacterial Agents/metabolism/*pharmacology ; Anticodon/genetics ; Binding Sites ; Codon/genetics ; Introns/genetics ; Models, Genetic ; RNA Splicing/*drug effects ; RNA, Catalytic/drug effects ; RNA, Ribosomal/*drug effects/genetics/metabolism ; RNA, Ribosomal, 16S/drug effects
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 39
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-11-19
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Losick, R -- Shapiro, L -- New York, N.Y. -- Science. 1993 Nov 19;262(5137):1227-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biological Laboratories, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235653" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Bacteria/genetics/growth & development/*ultrastructure ; Bacterial Proteins/genetics/*metabolism ; Flagella/metabolism/*ultrastructure ; *Gene Expression Regulation, Bacterial ; Genes, Bacterial ; *Morphogenesis ; Mutation ; Sigma Factor/genetics/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 40
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-04-02
    Beschreibung: Lesions in the transcribed strand block transcription and are repaired more rapidly than lesions in the nontranscribed (coding) strand which do not block RNA polymerase (RNAP). It has been shown previously that in Escherichia coli the mfd (mutation frequency decline) gene is necessary for strand-specific repair. The mfd gene was cloned and sequenced and the Mfd protein was purified and used to reconstitute strand-specific repair in a completely defined system. The mfd gene encodes a protein of 130 kilodaltons and contains the so-called "helicase motifs," a leucine zipper motif, and regions of sequence similarity to UvrB and RecG proteins. The Mfd protein was shown to (i) displace RNAP stalled at a lesion in an adenosine triphosphate-dependent reaction, (ii) bind to the damage recognition subunit (UvrA) of the excision nuclease, and (iii) stimulate the repair of the transcribed strand only when transcription is taking place. Thus, Mfd appears to target the transcribed strand for repair by recognizing a stalled RNAP and actively recruiting the repair enzyme to the transcription blocking lesion as it dissociates the stalled RNAP.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Selby, C P -- Sancar, A -- New York, N.Y. -- Science. 1993 Apr 2;260(5104):53-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of North Carolina School of Medicine, Chapel Hill 27599.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8465200" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Bacterial Proteins/chemistry/*genetics/metabolism ; Base Sequence ; Binding Sites ; Cloning, Molecular ; *DNA Helicases ; DNA Repair/*genetics ; DNA, Bacterial/metabolism ; DNA-Directed RNA Polymerases/metabolism ; Endodeoxyribonucleases/metabolism ; Escherichia coli/*genetics ; *Escherichia coli Proteins ; Leucine Zippers ; Molecular Sequence Data ; Multienzyme Complexes/chemistry/genetics ; Mutation/genetics ; Transcription Factors/chemistry/*genetics/metabolism ; *Transcription, Genetic
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 41
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-12-17
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nowak, R -- New York, N.Y. -- Science. 1993 Dec 17;262(5141):1818.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266068" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Female ; Genetic Linkage ; Humans ; Mice ; Mutation ; Receptors, Interleukin/chemistry/genetics/metabolism ; Receptors, Interleukin-2/*chemistry/genetics/metabolism ; Receptors, Interleukin-4 ; Receptors, Interleukin-7 ; Receptors, Mitogen/*chemistry/genetics/metabolism ; Severe Combined Immunodeficiency/genetics/*immunology ; X Chromosome
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 42
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-08-06
    Beschreibung: Metalloenzymes effect a variety of important chemical transformations, often involving small molecule substrates or products such as molecular oxygen, hydrogen, nitrogen, and water. A diverse array of ions or metal clusters is observed at the active-site cores, but living systems use basic recurring structures that have been modified or tuned for specific purposes. Inorganic chemists are actively involved in the elucidation of the structure, spectroscopy, and mechanism of action of these biological catalysts, in part through a synthetic modeling approach involving biomimetic studies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karlin, K D -- GM28962/GM/NIGMS NIH HHS/ -- GM45971/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Aug 6;261(5122):701-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Johns Hopkins University, Baltimore, MD 21218.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7688141" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Oxidoreductases/chemistry/metabolism ; Binding Sites ; Electron Transport ; Enzymes/*chemistry/metabolism ; Hydrolysis ; Iron-Sulfur Proteins/chemistry/metabolism ; Metalloproteins/*chemistry/metabolism ; *Models, Chemical ; Models, Molecular ; Nitric Oxide/metabolism ; Nitric Oxide Synthase ; Oxidation-Reduction ; Peptides/metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 43
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-12-24
    Beschreibung: The mitochondrial inner membrane protease is required for the maturation of mitochondrial proteins that are delivered to the intermembrane space. In the yeast Saccharomyces cerevisiae, this protease is now shown to be a complex that contains two catalytic subunits, Imp2p and the previously identified Imp1p. Primary structure similarity indicates that Imp1p and Imp2p are related to each other and to the family of eubacterial and eukaryotic signal peptidases. Imp1p and Imp2p have separate, nonoverlapping substrate specificities. In addition to its catalyzing the cleavage of intermembrane space sorting signals, Imp2p is required for the stable and functional expression of Imp1p. Thus, inner membrane protease, and by analogy eukaryotic multisubunit signal peptidases, may have acquired multiple catalytic subunits by gene duplication to broaden their range of substrate specificity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nunnari, J -- Fox, T D -- Walter, P -- New York, N.Y. -- Science. 1993 Dec 24;262(5142):1997-2004.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California Medical School, San Francisco 94143-0448.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266095" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Biological Transport/physiology ; Catalysis ; Endopeptidases/chemistry/*metabolism ; Fungal Proteins/metabolism ; *Membrane Proteins ; Mitochondria/*enzymology ; Mitochondrial Proteins ; Molecular Sequence Data ; Mutation ; Protein Precursors/*metabolism ; Saccharomyces cerevisiae/enzymology ; *Saccharomyces cerevisiae Proteins ; Sequence Homology, Amino Acid ; *Serine Endopeptidases ; Substrate Specificity
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  • 44
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-12-24
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Culotta, E -- Koshland, D E Jr -- New York, N.Y. -- Science. 1993 Dec 24;262(5142):1958-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7903477" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Alzheimer Disease/metabolism ; Bunyaviridae Infections/microbiology ; Climate ; Electric Conductivity ; Genes, p53/*physiology ; Hantavirus/isolation & purification ; Humans ; Mutation ; Myosins/physiology ; Neoplasms/*genetics ; Ozone ; Paclitaxel/supply & distribution ; Research ; Signal Transduction/physiology ; Tuberculosis/prevention & control ; Tumor Suppressor Protein p53/genetics/*physiology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 45
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-02-12
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kassavetis, G A -- Geiduschek, E P -- New York, N.Y. -- Science. 1993 Feb 12;259(5097):944-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California San Diego, La Jolla 92093-0634.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7679800" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Binding Sites ; Dna ; DNA Polymerase II/metabolism ; DNA-Directed RNA Polymerases/*metabolism ; Escherichia coli/enzymology ; Humans ; Hydrolysis ; RNA/biosynthesis/*metabolism ; Templates, Genetic ; Transcription Factors/metabolism/pharmacology ; *Transcription Factors, TFII ; Transcription, Genetic
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 46
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-12-03
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Birge, R B -- Hanafusa, H -- New York, N.Y. -- Science. 1993 Dec 3;262(5139):1522-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Oncology, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7504323" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Binding Sites ; Molecular Sequence Data ; Phosphotyrosine ; Proto-Oncogene Proteins pp60(c-src)/*chemistry ; Receptor Protein-Tyrosine Kinases/*metabolism ; Sequence Homology, Amino Acid ; Signal Transduction/physiology ; Structure-Activity Relationship ; Tyrosine/analogs & derivatives/metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 47
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-08-27
    Beschreibung: In adult animals, template-independent (or N) nucleotides are frequently added during the rearrangement of variable (V), diversity (D), and joining (J) segments of lymphocyte receptor genes, greatly enhancing junctional diversity. Receptor genes from adult mice carrying a mutation in the terminal deoxynucleotidyl transferase (TdT) gene have few N nucleotides, providing proof that this enzyme is essential for creating diversity. Unlike those from normal adults, receptor genes from adult mutant mice show extensive evidence of homology-directed recombination, suggesting that TdT blocks this process. Thus, switch-on of the TdT gene during the first week after birth provokes an even greater expansion of lymphocyte receptor diversity than had previously been thought.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gilfillan, S -- Dierich, A -- Lemeur, M -- Benoist, C -- Mathis, D -- New York, N.Y. -- Science. 1993 Aug 27;261(5125):1175-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Genetique Moleculaire des Eucaryotes du CNRS, Institut de Chimie Biologique, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8356452" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Base Sequence ; DNA Nucleotidylexotransferase/genetics/*metabolism ; Gene Rearrangement, B-Lymphocyte ; Gene Rearrangement, T-Lymphocyte ; *Genes, Immunoglobulin ; Immunoglobulin Joining Region/genetics ; Immunoglobulin Variable Region/genetics ; Lymphocytes/*immunology ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Mutation ; Nucleotides/*metabolism ; Receptors, Antigen, T-Cell/*genetics ; Recombination, Genetic
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 48
    Publikationsdatum: 1993-07-30
    Beschreibung: T cell receptor stimulation without costimulation is insufficient for the induction of an optimal immune response. It is thought that engagement of the CD28 molecule with its ligand B7 provides an essential costimulatory signal without which full activation of T cells cannot occur. A mouse strain with a defective CD28 gene was established. Development of T and B cells in the CD28-deficient mice appeared normal. However, T lymphocytes derived from CD28-/- mutant mice had impaired responses to lectins. Lectin stimulation did not trigger interleukin-2 (IL-2) production, IL-2 receptor alpha expression was significantly decreased, and exogenous IL-2 only partially rescued the CD28 defect. Basal immunoglobulin (Ig) concentrations in CD28-deficient mice were about one-fifth of those found in wild-type controls, with low titers of IgG1 and IgG2b but an increase in IgG2a. In addition, activity of T helper cells in CD28-/- mice was reduced and immunoglobulin class switching was diminished after infection with vesicular stomatitis virus. However, cytotoxic T cells could still be induced and the mice showed delayed-type hypersensitivity after infection with lymphocytic choriomeningitis virus. Thus, CD28 is not required for all T cell responses in vivo, suggesting that alternative costimulatory pathways may exist.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shahinian, A -- Pfeffer, K -- Lee, K P -- Kundig, T M -- Kishihara, K -- Wakeham, A -- Kawai, K -- Ohashi, P S -- Thompson, C B -- Mak, T W -- New York, N.Y. -- Science. 1993 Jul 30;261(5121):609-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Biophysics and Immunology, University of Toronto, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7688139" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Antibodies, Viral/blood ; Antigens, CD/genetics/*immunology ; Antigens, CD28 ; Antigens, CD80 ; Antigens, Differentiation, T-Lymphocyte/genetics/*immunology ; Antigens, Surface/immunology ; B-Lymphocytes/immunology ; Concanavalin A/pharmacology ; Immunoglobulins/blood ; Interleukin-2/biosynthesis/pharmacology ; *Lymphocyte Activation ; Lymphocytic Choriomeningitis/immunology ; Mice ; Mice, Inbred C57BL ; Mice, Inbred DBA ; Mice, Mutant Strains ; Mutation ; Receptors, Interleukin-2/metabolism ; T-Lymphocytes/*immunology ; T-Lymphocytes, Cytotoxic/immunology ; T-Lymphocytes, Helper-Inducer/immunology ; Vesicular stomatitis Indiana virus/immunology ; Virus Diseases/immunology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 49
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-03-26
    Beschreibung: The RAD51 protein functions in the processes of DNA repair and in mitotic and meiotic genetic recombination in the yeast Saccharomyces cerevisiae. The protein has adenosine triphosphate-dependent DNA binding activities similar to those of the Escherichia coli RecA protein, and the two proteins have 30 percent sequence homology. RAD51 polymerized on double-stranded DNA to form a helical filament nearly identical in low-resolution, three-dimensional structure to that formed by RecA. Like RecA, RAD51 also appears to force DNA into a conformation of approximately a 5.1-angstrom rise per base pair and 18.6 base pairs per turn. As in other protein families, its structural conservation appears to be stronger than its sequence conservation. Both the structure of the protein polymer formed by RecA and the DNA conformation induced by RecA appear to be general properties of a class of recombination proteins found in prokaryotes as well as eukaryotes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ogawa, T -- Yu, X -- Shinohara, A -- Egelman, E H -- GM35269/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Mar 26;259(5103):1896-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Osaka University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8456314" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenosine Triphosphate/pharmacology ; Binding Sites ; DNA/chemistry/metabolism ; DNA Repair ; DNA, Single-Stranded/chemistry/metabolism ; DNA-Binding Proteins/*chemistry/metabolism ; Fourier Analysis ; Fungal Proteins/*chemistry/metabolism ; Meiosis ; Mitosis ; Molecular Structure ; Nucleic Acid Conformation ; Protein Structure, Secondary ; Rad51 Recombinase ; Rec A Recombinases/*chemistry/metabolism ; Recombinant Proteins/chemistry/metabolism ; Saccharomyces cerevisiae/*chemistry ; Saccharomyces cerevisiae Proteins
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 50
    Publikationsdatum: 1993-03-19
    Beschreibung: Interferon-gamma (IFN-gamma) is a pleiotrophic cytokine with immunomodulatory effects on a variety of immune cells. Mice with a targeted disruption of the IFN-gamma gene were generated. These mice developed normally and were healthy in the absence of pathogens. However, mice deficient in IFN-gamma had impaired production of macrophage antimicrobial products and reduced expression of macrophage major histocompatibility complex class II antigens. IFN-gamma-deficient mice were killed by a sublethal dose of the intracellular pathogen Mycobacterium bovis. Splenocytes exhibited uncontrolled proliferation in response to mitogen and alloantigen. After a mixed lymphocyte reaction, T cell cytolytic activity was enhanced against allogeneic target cells. Resting splenic natural killer cell activity was reduced in IFN-gamma-deficient mice. Thus, IFN-gamma is essential for the function of several cell types of the murine immune system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dalton, D K -- Pitts-Meek, S -- Keshav, S -- Figari, I S -- Bradley, A -- Stewart, T A -- New York, N.Y. -- Science. 1993 Mar 19;259(5102):1739-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genentech Inc., South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8456300" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Cell Division ; Cytotoxicity, Immunologic ; Histocompatibility Antigens Class II/immunology ; *Immunity ; Interferon-gamma/*genetics/physiology ; Isoantigens/immunology ; Killer Cells, Natural/immunology ; Lymphocyte Culture Test, Mixed ; Macrophages/immunology ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Mutation ; Mycobacterium bovis ; Nitric Oxide/metabolism ; Spleen/cytology/immunology ; T-Lymphocytes/immunology ; Transfection ; Tuberculosis/immunology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 51
    Publikationsdatum: 1993-10-15
    Beschreibung: Unlike most serine proteases of the chymotrypsin family, tissue-type plasminogen activator (tPA) is secreted from cells as an active, single-chain enzyme with a catalytic efficiency only slightly lower than that of the proteolytically cleaved form. A zymogenic mutant of tPA has been engineered that displays a reduction in catalytic efficiency by a factor of 141 in the single-chain form while retaining full activity in the cleaved form. The residues introduced in the mutant, serine 292 and histidine 305, are proposed to form a hydrogen-bonded network with aspartate 477, similar to the aspartate 194-histidine 40-serine 32 network found to stabilize the zymogen chymotrypsinogen.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Madison, E L -- Kobe, A -- Gething, M J -- Sambrook, J F -- Goldsmith, E J -- New York, N.Y. -- Science. 1993 Oct 15;262(5132):419-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211162" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Aspartic Acid/chemistry ; Base Sequence ; Catalysis ; Chymotrypsin/chemistry/metabolism ; Enzyme Precursors/chemistry/*metabolism ; Histidine/chemistry ; Hydrogen Bonding ; Kinetics ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutation ; Plasminogen/metabolism ; Plasminogen Activator Inhibitor 1/metabolism ; Serine/chemistry ; Tissue Plasminogen Activator/chemistry/genetics/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 52
    Publikationsdatum: 1993-08-20
    Beschreibung: Single-site mutants in the Cu,Zn superoxide dismutase (SOD) gene (SOD1) occur in patients with the fatal neurodegenerative disorder familial amyotrophic lateral sclerosis (FALS). Complete screening of the SOD1 coding region revealed that the mutation Ala4 to Val in exon 1 was the most frequent one; mutations were identified in exons 2, 4, and 5 but not in the active site region formed by exon 3. The 2.4 A crystal structure of human SOD, along with two other SOD structures, established that all 12 observed FALS mutant sites alter conserved interactions critical to the beta-barrel fold and dimer contact, rather than catalysis. Red cells from heterozygotes had less than 50 percent normal SOD activity, consistent with a structurally defective SOD dimer. Thus, defective SOD is linked to motor neuron death and carries implications for understanding and possible treatment of FALS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Deng, H X -- Hentati, A -- Tainer, J A -- Iqbal, Z -- Cayabyab, A -- Hung, W Y -- Getzoff, E D -- Hu, P -- Herzfeldt, B -- Roos, R P -- New York, N.Y. -- Science. 1993 Aug 20;261(5124):1047-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Northwestern University Medical School, Chicago, IL 60611.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8351519" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Amyotrophic Lateral Sclerosis/enzymology/*genetics ; Base Sequence ; Binding Sites ; Erythrocytes/enzymology ; Exons ; Free Radicals/metabolism ; Humans ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Folding ; Protein Structure, Tertiary ; Superoxide Dismutase/blood/chemistry/*genetics/metabolism ; X-Ray Diffraction
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 53
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-10-22
    Beschreibung: Many bacterial signaling pathways involve a two-component design. In these pathways, a sensor kinase, when activated by a signal, phosphorylates its own histidine, which then serves as a phosphoryl donor to an aspartate in a response regulator protein. The Sln1 protein of the yeast Saccharomyces cerevisiae has sequence similarities to both the histidine kinase and the response regulator proteins of bacteria. A missense mutation in SLN1 is lethal in the absence but not in the presence of the N-end rule pathway, a ubiquitin-dependent proteolytic system. The finding of SLN1 demonstrates that a mode of signal transduction similar to the bacterial two-component design operates in eukaryotes as well.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ota, I M -- Varshavsky, A -- New York, N.Y. -- Science. 1993 Oct 22;262(5133):566-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211183" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Bacterial Proteins/chemistry/genetics/metabolism ; Base Sequence ; Fungal Proteins/chemistry/*genetics/metabolism ; Genes, Fungal ; Intracellular Signaling Peptides and Proteins ; *Ligases ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Protein Kinases/chemistry/*genetics/metabolism ; Saccharomyces cerevisiae/*genetics/growth & development/metabolism ; *Saccharomyces cerevisiae Proteins ; Sequence Alignment ; *Signal Transduction ; *Ubiquitin-Protein Ligases
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 54
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-12-17
    Beschreibung: Most members of the guanosine triphosphatase (GTPase) superfamily hydrolyze guanosine triphosphate (GTP) quite slowly unless stimulated by a GTPase activating protein or GAP. The alpha subunits (G alpha) of the heterotrimeric G proteins hydrolyze GTP much more rapidly and contain an approximately 120-residue insert not found in other GTPases. Interactions between a G alpha insert domain and a G alpha GTP-binding core domain, both expressed as recombinant proteins, show that the insert acts biochemically as a GAP. The results suggest a general mechanism for GAP-dependent hydrolysis of GTP by other GTPases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Markby, D W -- Onrust, R -- Bourne, H R -- 5F32-GM13918/GM/NIGMS NIH HHS/ -- CA54427/CA/NCI NIH HHS/ -- GM27800/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 17;262(5141):1895-901.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmcology, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266082" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenylyl Cyclases/metabolism ; Amino Acid Sequence ; Animals ; Cell Line ; Colforsin/pharmacology ; Cyclic AMP/metabolism ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/chemistry/*metabolism ; Guanosine 5'-O-(3-Thiotriphosphate)/metabolism/pharmacology ; Guanosine Triphosphate/*metabolism ; Hydrolysis ; Kinetics ; Molecular Sequence Data ; Mutation ; Protein Conformation
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 55
    Publikationsdatum: 1993-07-30
    Beschreibung: Mutations in the unc-17 gene of the nematode Caenorhabditis elegans produce deficits in neuromuscular function. This gene was cloned and complementary DNAs were sequenced. On the basis of sequence similarity to mammalian vesicular transporters of biogenic amines and of localization to synaptic vesicles of cholinergic neurons in C. elegans, unc-17 likely encodes the vesicular transporter of acetylcholine. Mutations that eliminated all unc-17 gene function were lethal, suggesting that the acetylcholine transporter is essential. Molecular analysis of unc-17 mutations will allow the correlation of specific parts of the gene (and the protein) with observed functional defects. The mutants will also be useful for the isolation of extragenic suppressors, which could identify genes encoding proteins that interact with UNC-17.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alfonso, A -- Grundahl, K -- Duerr, J S -- Han, H P -- Rand, J B -- R01 GM038679/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jul 30;261(5121):617-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Molecular and Cell Biology, Oklahoma Medical Research Foundation, Oklahoma City 73104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8342028" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Acetylcholine/*metabolism ; Alleles ; Amino Acid Sequence ; Animals ; Caenorhabditis elegans/chemistry/cytology/*genetics ; *Caenorhabditis elegans Proteins ; Carrier Proteins/analysis/chemistry/*genetics ; Cloning, Molecular ; *Genes, Helminth ; Helminth Proteins/analysis/chemistry/*genetics ; *Membrane Transport Proteins ; Molecular Sequence Data ; Mutation ; Neurons/*chemistry ; Parasympathetic Nervous System/chemistry ; Phenotype ; Sequence Alignment ; Synaptic Vesicles/*chemistry ; Vesicular Acetylcholine Transport Proteins ; *Vesicular Transport Proteins
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 56
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-12-10
    Beschreibung: Disulfide bonds are rarely found in cytoplasmic proteins. Mutations were selected for in Escherichia coli that allow disulfide bond formation in the cytoplasm. In the presence of these mutations, export-defective versions of alkaline phosphatase and mouse urokinase were able to fold into their enzymatically active conformations in the cytoplasm because their disulfide bonds were formed. The mutations were mapped to the gene for thioredoxin reductase and diminish or eliminate the activity of this enzyme. Thioredoxin itself was found to be unnecessary for this disulfide bond formation. Thioredoxin reductase, but not thioredoxin, is thus implicated in keeping cysteines reduced in cytoplasmic proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Derman, A I -- Prinz, W A -- Belin, D -- Beckwith, J -- New York, N.Y. -- Science. 1993 Dec 10;262(5140):1744-7.〈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/8259521" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Alkaline Phosphatase/*chemistry/metabolism ; Cysteine/metabolism ; Cytoplasm/*enzymology ; Disulfides/metabolism ; Escherichia coli/*enzymology/genetics/growth & development ; *Genes, Bacterial ; Mutation ; Oxidation-Reduction ; Protein Folding ; Protein Sorting Signals ; Recombinant Proteins/chemistry/metabolism ; Thioredoxin-Disulfide Reductase/genetics/*metabolism ; Urokinase-Type Plasminogen Activator/*chemistry/metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 57
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-12-17
    Beschreibung: Myosin II, which converts the energy of adenosine triphosphate hydrolysis into the movement of actin filaments, is a hexamer of two heavy chains, two essential light chains, and two regulatory light chains (RLCs). Dictyostelium myosin II is known to be regulated in vitro by phosphorylation of the RLC. Cells in which the wild-type myosin II heavy chain was replaced with a recombinant form that lacks the binding site for RLC carried out cytokinesis and almost normal development, processes known to be dependent on functional myosin II. Characterization of the purified recombinant protein suggests that a complex of RLC and the RLC binding site of the heavy chain plays an inhibitory role for adenosine triphosphatase activity and a structural role for the movement of myosin along actin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Uyeda, T Q -- Spudich, J A -- GM46551/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 17;262(5141):1867-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Stanford University School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266074" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Actins/metabolism ; Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Ca(2+) Mg(2+)-ATPase/metabolism ; Calcium-Transporting ATPases/metabolism ; Cell Division ; Dictyostelium/cytology/genetics/*metabolism ; Genes, Fungal ; Molecular Sequence Data ; Myosin-Light-Chain Kinase/metabolism ; Myosins/chemistry/genetics/*metabolism ; Phosphorylation ; Recombinant Proteins/chemistry/metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 58
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-12-17
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alper, J -- New York, N.Y. -- Science. 1993 Dec 17;262(5141):1817.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266067" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Binding Sites ; Epithelium/microbiology ; Gastric Mucosa/*microbiology ; Helicobacter Infections/microbiology ; Helicobacter pylori/*metabolism ; Humans ; Lewis Blood-Group System/*metabolism ; Sialic Acids/*metabolism ; Stomach Neoplasms/microbiology ; Stomach Ulcer/microbiology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 59
    Publikationsdatum: 1993-09-17
    Beschreibung: Plants are continually subjected to ultraviolet-B (UV-B) irradiation (290 to 320 nanometers) as a component of sunlight, which induces a variety of types of damage to the plant DNA. Repair of the two major DNA photoproducts was analyzed in wild-type Arabidopsis thaliana and in a mutant derivative whose growth was sensitive to UV-B radiation. In wild-type seedlings, repair of cyclobutane pyrimidine dimers occurred more slowly in the dark than in the light; repair of this photoproduct was not affected in the mutant. Repair, in the dark, of pyrimidine-pyrimidinone(6-4) dimers was defective in the UV-sensitive mutant.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Britt, A B -- Chen, J J -- Wykoff, D -- Mitchell, D -- New York, N.Y. -- Science. 1993 Sep 17;261(5128):1571-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Botany, University of California at Davis 95616.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8372351" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Arabidopsis/*genetics/growth & development/radiation effects ; *DNA Repair ; Darkness ; Light ; Mutation ; Pyrimidine Dimers/*metabolism ; *Ultraviolet Rays
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    Standort Signatur Erwartet Verfügbarkeit
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  • 60
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-09-24
    Beschreibung: Zinc finger proteins, of the type first discovered in transcription factor IIIA (TFIIIA), are one of the largest and most important families of DNA-binding proteins. The crystal structure of a complex containing the five Zn fingers from the human GLI oncogene and a high-affinity DNA binding site has been determined at 2.6 A resolution. Finger one does not contact the DNA. Fingers two through five bind in the major groove and wrap around the DNA, but lack the simple, strictly periodic arrangement observed in the Zif268 complex. Fingers four and five of GLI make extensive base contacts in a conserved nine base-pair region, and this section of the DNA has a conformation intermediate between B-DNA and A-DNA. Analyzing the GLI complex and comparing it with Zif268 offers new perspectives on Zn finger-DNA recognition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pavletich, N P -- Pabo, C O -- GM-31471/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 24;261(5129):1701-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8378770" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Base Sequence ; Binding Sites ; Computer Graphics ; DNA/*chemistry/metabolism ; DNA-Binding Proteins/chemistry/metabolism ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oncogene Proteins/*chemistry/genetics/metabolism ; Oncogenes ; Protein Conformation ; Trans-Activators ; Transcription Factors/*chemistry/genetics/metabolism ; X-Ray Diffraction ; *Zinc Fingers
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 61
    Publikationsdatum: 1993-06-25
    Beschreibung: Arrestins have been implicated in the regulation of many G protein-coupled receptor signaling cascades. Mutations in two Drosophila photoreceptor-specific arrestin genes, arrestin 1 and arrestin 2, were generated. Analysis of the light response in these mutants shows that the Arr1 and Arr2 proteins are mediators of rhodopsin inactivation and are essential for the termination of the phototransduction cascade in vivo. The saturation of arrestin function by an excess of activated rhodopsin is responsible for a continuously activated state of the photoreceptors known as the prolonged depolarized afterpotential. In the absence of arrestins, photoreceptors undergo light-dependent retinal degeneration as a result of the continued activity of the phototransduction cascade. These results demonstrate the fundamental requirement for members of the arrestin protein family in the regulation of G protein-coupled receptors and signaling cascades in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dolph, P J -- Ranganathan, R -- Colley, N J -- Hardy, R W -- Socolich, M -- Zuker, C S -- R01 EY008768/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1993 Jun 25;260(5116):1910-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, La Jolla, CA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8316831" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; *Arrestins ; Drosophila ; Drosophila Proteins ; Eye Proteins/genetics/*physiology ; Female ; GTP-Binding Proteins/*metabolism ; Genes, Insect ; Kinetics ; Male ; Molecular Sequence Data ; Mutation ; Phosphoproteins/genetics/*physiology ; Photic Stimulation ; Photoreceptor Cells/cytology/*physiology ; Rhodopsin/analogs & derivatives/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 62
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-05-14
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brugge, J S -- New York, N.Y. -- Science. 1993 May 14;260(5110):918-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉ARIAD Pharmaceuticals, Inc., Cambridge, MA 02139-4234.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8388123" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Binding Sites ; *Drug Design ; Growth Substances/metabolism ; Humans ; Peptides/chemistry/*metabolism/therapeutic use ; Proteins/*metabolism ; Receptors, Cell Surface/metabolism ; *Signal Transduction
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 63
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-06-25
    Beschreibung: Three DNA hypomethylation mutants of the flowering plant Arabidopsis thaliana were isolated by screening mutagenized populations for plants containing centromeric repetitive DNA arrays susceptible to digestion by a restriction endonuclease that was sensitive to methylated cytosines. The mutations are recessive, and at least two are alleles of a single locus, designated DDM1 (for decrease in DNA methylation). Amounts of 5-methylcytosine were reduced over 70 percent in ddm1 mutants. Despite this reduction in DNA methylation levels, ddm1 mutants developed normally and exhibited no striking morphological phenotypes. However, the ddm1 mutations are associated with a segregation distortion phenotype. The ddm1 mutations were used to demonstrate that de novo DNA methylation in vivo is slow.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vongs, A -- Kakutani, T -- Martienssen, R A -- Richards, E J -- New York, N.Y. -- Science. 1993 Jun 25;260(5116):1926-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, NY 11724.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8316832" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): 5-Methylcytosine ; Arabidopsis/*genetics/growth & development ; Centromere ; Crosses, Genetic ; Cytosine/analogs & derivatives/analysis ; DNA/chemistry/*metabolism ; DNA, Ribosomal/chemistry/metabolism ; *Genes, Plant ; *Genes, Recessive ; Methylation ; Mutation ; Phenotype
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 64
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-08-20
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1993 Aug 20;261(5124):986.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8351523" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amyotrophic Lateral Sclerosis/enzymology/*genetics ; Binding Sites ; Free Radicals/metabolism ; Genes ; Humans ; Point Mutation ; Protein Folding ; Protein Structure, Tertiary ; Superoxide Dismutase/chemistry/*genetics/metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 65
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-11-26
    Beschreibung: Coiled-coil sequences in proteins consist of heptad repeats containing two characteristic hydrophobic positions. The role of these buried hydrophobic residues in determining the structures of coiled coils was investigated by studying mutants of the GCN4 leucine zipper. When sets of buried residues were altered, two-, three-, and four-helix structures were formed. The x-ray crystal structure of the tetramer revealed a parallel, four-stranded coiled coil. In the tetramer conformation, the local packing geometry of the two hydrophobic positions in the heptad repeat is reversed relative to that in the dimer. These studies demonstrate that conserved, buried residues in the GCN4 leucine zipper direct dimer formation. In contrast to proposals that the pattern of hydrophobic and polar amino acids in a protein sequence is sufficient to determine three-dimensional structure, the shapes of buried side chains in coiled coils are essential determinants of the global fold.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harbury, P B -- Zhang, T -- Kim, P S -- Alber, T -- GM44162/GM/NIGMS NIH HHS/ -- GM48958/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 26;262(5138):1401-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8248779" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Crystallography, X-Ray ; *DNA-Binding Proteins ; Fungal Proteins/*chemistry/genetics ; Hydrogen Bonding ; *Leucine Zippers ; Molecular Sequence Data ; Mutation ; Protein Conformation ; Protein Kinases/*chemistry/genetics ; Protein Structure, Secondary ; *Saccharomyces cerevisiae Proteins
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 66
    facet.materialart.
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-04-23
    Beschreibung: Ribozymes derived from the self-splicing pre-ribosomal RNA of Tetrahymena act as sequence-specific endonucleases. The reaction involves binding an RNA or DNA substrate by base pairing to the internal guide sequence (IGS) to form helix P1. Site-specific photo-crosslinking localized the 5' end of the IGS in helix P1 to the vicinity of conserved bases between helices P4 and P5, supporting a major feature of the Michel-Westhof three-dimensional structure model. The crosslinked ribozyme retained catalytic activity. When not base-paired, the IGS was still specifically crosslinked, but the major site was 37 A distant from the reactive site in the experimentally supported three-dimensional model. The data indicate that a substantial induced-fit conformational change accompanies P1 formation, and they provide a physical basis for understanding the transport of oligonucleotides to the catalytic core of the ribozyme. The ability of RNA to orchestrate large-scale conformational changes may help explain why the ribosome and the spliceosome are RNA-based machines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, J F -- Downs, W D -- Cech, T R -- New York, N.Y. -- Science. 1993 Apr 23;260(5107):504-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7682726" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Base Composition ; Base Sequence ; Binding Sites ; Catalysis ; DNA/chemistry/metabolism ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligoribonucleotides/chemistry/metabolism ; RNA/chemistry/*metabolism ; RNA, Catalytic/chemistry/*metabolism ; RNA, Guide/chemistry/*metabolism ; RNA, Protozoan/chemistry/metabolism ; Tetrahymena/enzymology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 67
    facet.materialart.
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-05-07
    Beschreibung: RNA recombination has been described for a number of viruses in the plant and animal kingdoms, but the mechanisms of selection of recombination sites are poorly understood. The nonrandom recombination between two subviral RNAs associated with turnip crinkle virus was used to study the requirement for specific sequences and structures in the generation of recombinant molecules. Single-base mutations that disrupted either the stem or the loop of one of the two computer-predicted stem-loop structures eliminated detectable recombinant molecules. However, recombinants were detected if compensatory mutations were generated that re-formed a stable hairpin structure. These results provide evidence for the necessity of specific structures in the formation of recombinant molecules in this system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cascone, P J -- Haydar, T F -- Simon, A E -- New York, N.Y. -- Science. 1993 May 7;260(5109):801-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Molecular and Cellular Biology, University of Massachusetts, Amherst 01003.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8484119" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Base Sequence ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; Plant Viruses/*genetics/physiology ; Plants/microbiology ; RNA Viruses/*genetics/physiology ; RNA, Viral/chemistry/*genetics ; *Recombination, Genetic
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 68
    Publikationsdatum: 1993-09-17
    Beschreibung: The CD8 alpha cytoplasmic domain associates with p56lck, a nonreceptor protein-tyrosine kinase. The biological relevance of CD8 alpha-Lck association in T cell development was tested with transgenic mice generated to express a CD8 alpha molecule with two amino acid substitutions in its cytoplasmic domain, which abolishes the association of CD8 alpha with Lck. The CD8 alpha mutant was analyzed in a CD8-/- background and in the context of the transgenic 2C T cell receptor. The development and function of CD8+ T cells in these mice were apparently normal. Thus, CD8 alpha-Lck association is not necessary for positive selection, negative selection, or CD8-dependent cytotoxic function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, I T -- Limmer, A -- Louie, M C -- Bullock, E D -- Fung-Leung, W P -- Mak, T W -- Loh, D Y -- AI 155322-13/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 17;261(5128):1581-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Medicine, Genetics, and Molecular Microbiology, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8372352" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Antigens, CD4/metabolism ; Antigens, CD8/immunology/*metabolism ; *Cytotoxicity, Immunologic ; Female ; Genes, MHC Class I ; Lymphocyte Culture Test, Mixed ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck) ; Male ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C3H ; Mice, Inbred C57BL ; Mice, Transgenic ; Mutation ; Phosphorylation ; Protein-Tyrosine Kinases/*metabolism ; Receptors, Antigen, T-Cell ; T-Lymphocytes, Cytotoxic/*immunology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 69
    Publikationsdatum: 1993-07-16
    Beschreibung: Mice that bear the X-linked immunodeficiency (xid) mutation have a B lymphocyte-specific defect resulting in an inability to make antibody responses to polysaccharide antigens. A backcross of 1114 progeny revealed the colocalization of xid with Bruton's agammaglobulinemia tyrosine kinase (btk) gene, which is implicated in the human immune deficiency, X-linked agammaglobulinemia. Mice that carry xid have a missense mutation that alters a highly conserved arginine near the amino-terminus of the btk protein, Btk. Because this region of Btk lies outside any obvious kinase domain, the xid mutation may define another aspect of tyrosine kinase function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thomas, J D -- Sideras, P -- Smith, C I -- Vorechovsky, I -- Chapman, V -- Paul, W E -- GM33160/GM/NIGMS NIH HHS/ -- HG00277/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1993 Jul 16;261(5119):355-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Immunology, 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/8332900" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Agammaglobulinemia/enzymology/*genetics/immunology ; Amino Acid Sequence ; Animals ; B-Lymphocytes/enzymology/immunology ; Base Sequence ; Chromosome Mapping ; Crosses, Genetic ; Female ; *Genes ; Genetic Linkage ; Immunologic Deficiency Syndromes/enzymology/*genetics/immunology ; Male ; Mice ; Mice, Inbred CBA ; Mice, Mutant Strains ; Molecular Sequence Data ; Muridae ; Mutation ; Protein-Tyrosine Kinases/chemistry/*genetics/metabolism ; *X Chromosome
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 70
    Publikationsdatum: 1993-03-26
    Beschreibung: Heparin or heparin-like heparan sulfate proteoglycans are obligatory for activity of the heparin-binding fibroblast growth factor (FGF) family. Heparin interacts independently of FGF ligand with a specific sequence (K18K) in one of the immunoglobulin-like loops in the extracellular domain of the FGF receptor tyrosine kinase transmembrane glycoprotein. A synthetic peptide corresponding to K18K inhibited heparin and heparin-dependent FGF binding to the receptor. K18K and an antibody to K18K were antagonists of FGF-stimulated cell growth. Point mutations of lysine residues in the K18K sequence abrogated both heparin- and ligand-binding activities of the receptor kinase. The results indicate that the FGF receptor is a ternary complex of heparan sulfate proteoglycan, tyrosine kinase transmembrane glycoprotein, and ligand.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kan, M -- Wang, F -- Xu, J -- Crabb, J W -- Hou, J -- McKeehan, W L -- New York, N.Y. -- Science. 1993 Mar 26;259(5103):1918-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉W. Alton Jones Cell Science Center, Inc. Lake Placid, NY 12946.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8456318" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Antibodies, Monoclonal ; Binding Sites ; Fibroblast Growth Factors/metabolism ; Heparan Sulfate Proteoglycans ; Heparin/*metabolism ; Heparitin Sulfate/metabolism ; Humans ; Immunohistochemistry ; Lysine/metabolism ; Metalloendopeptidases/metabolism ; Molecular Sequence Data ; Mutagenesis ; Peptide Fragments/isolation & purification/metabolism ; Protein-Tyrosine Kinases/chemistry/genetics/*metabolism ; Proteoglycans/metabolism ; Receptors, Fibroblast Growth Factor/chemistry/genetics/*metabolism ; Recombinant Proteins/metabolism ; Sodium Chloride/pharmacology ; Trypsin/metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 71
    Publikationsdatum: 1993-08-13
    Beschreibung: The zeta subunit of the T cell antigen receptor complex is required for targeting nascent receptor complexes to the cell surface and for receptor-mediated signal transduction. To examine the significance of the zeta subunit in T cell development, mice deficient for zeta expression were generated by gene targeting. These zeta-/- mice had few CD4+CD8+ thymocytes, and the generation of CD4+ and CD8+ single positive T cells was impaired but not completely abrogated. Peripheral T cells were present but were unusual in that they expressed small amounts of CD5 and few T cell receptors. Thus, zeta chain expression influences thymocyte differentiation but is not absolutely required for the generation of single positive T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Love, P E -- Shores, E W -- Johnson, M D -- Tremblay, M L -- Lee, E J -- Grinberg, A -- Huang, S P -- Singer, A -- Westphal, H -- New York, N.Y. -- Science. 1993 Aug 13;261(5123):918-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Mammalian Genes and Development, National Institute of Child Health and Human Development, National Institutes of Health (NIH), Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7688481" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Antigens, CD/analysis ; Antigens, CD3/analysis ; Antigens, CD4/analysis ; Antigens, CD5 ; Antigens, CD8/analysis ; Cell Differentiation ; Membrane Proteins/genetics/*physiology ; Mice ; Mutation ; RNA, Messenger/genetics/metabolism ; Receptors, Antigen, T-Cell/genetics/*physiology ; Receptors, Antigen, T-Cell, alpha-beta/analysis ; T-Lymphocyte Subsets/*cytology/immunology ; Thymus Gland/cytology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 72
    Publikationsdatum: 1993-10-15
    Beschreibung: Electrophysiology and structural studies were performed on an annexin V variant containing a mutation of glutamic acid-95 to serine in the center of the pore region. The mutation resulted in a lower single channel conductance for calcium and a strongly increased conductance for sodium and potassium, indicating that glutamic acid-95 is a crucial constituent of the ion selectivity filter. There were only minor differences in the crystal structures of mutant and wild-type annexin V around the mutation site; however, the mutant showed structural differences elsewhere, including the presence of a calcium binding site in domain III unrelated to the mutation. Analysis of the membrane-bound form of annexin V by electron microscopy revealed no differences between the wild type and mutant.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berendes, R -- Voges, D -- Demange, P -- Huber, R -- Burger, A -- New York, N.Y. -- Science. 1993 Oct 15;262(5132):427-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Biochemie, Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7692599" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Annexin A5/*chemistry/genetics/metabolism ; Binding Sites ; Calcium/metabolism ; Computer Graphics ; Crystallography, X-Ray ; Electric Conductivity ; Glutamates/chemistry ; Glutamic Acid ; Humans ; Ion Channels/*metabolism ; Microscopy, Electron ; Mutagenesis, Site-Directed ; Potassium/metabolism ; Protein Structure, Secondary ; Serine/chemistry ; Sodium/metabolism ; Structure-Activity Relationship
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  • 73
    Publikationsdatum: 1993-10-22
    Beschreibung: The large subunit of the human pre-messenger RNA splicing factor U2 small nuclear ribonucleoprotein auxiliary factor (hU2AF65) is required for spliceosome assembly in vitro. A complementary DNA clone encoding the large subunit of Drosophila U2AF (dU2AF50) has been isolated. The dU2AF50 protein is closely related to its mammalian counterpart and contains three carboxyl-terminal ribonucleoprotein consensus sequence RNA binding domains and an amino-terminal arginine- and serine-rich (R/S) domain. Recombinant dU2AF50 protein complements mammalian splicing extracts depleted of U2AF activity. Germline transformation of Drosophila with the dU2AF50 complementary DNA rescues a lethal mutation, establishing that the dU2AF50 gene is essential for viability. R/S domains have been found in numerous metazoan splicing factors, but their function is unknown. The mutation in Drosophila U2AF will allow in vivo analysis of a conserved R/S domain-containing general splicing factor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kanaar, R -- Roche, S E -- Beall, E L -- Green, M R -- Rio, D C -- R01-HD28063/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1993 Oct 22;262(5133):569-73.〈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/7692602" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Base Sequence ; Conserved Sequence ; DNA, Complementary ; Drosophila melanogaster/*genetics/growth & development ; Female ; Gene Transfer Techniques ; Genes, Insect ; Genes, Lethal ; In Situ Hybridization ; Male ; Molecular Sequence Data ; Mutation ; *Nuclear Proteins ; RNA/metabolism ; RNA Precursors/*metabolism ; *RNA Splicing ; Recombinant Proteins/metabolism ; Ribonucleoproteins/chemistry/*genetics/metabolism ; Sequence Alignment
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  • 74
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-01-15
    Beschreibung: Rab geranylgeranyl transferase (GG transferase) is a two-component enzyme that attaches 20-carbon isoprenoid groups to cysteine residues in Rab proteins, a family of guanosine triphosphate-binding proteins that regulate vesicular traffic. The mutant gene in human choroideremia, an X-linked form of retinal degeneration, encodes a protein that resembles component A of rat Rab GG transferase. Lymphoblasts from choroideremia subjects showed a marked deficiency in the activity of component A, but not component B, of Rab GG transferase. The deficiency was more pronounced when the substrate was Rab3A, a synaptic vesicle protein, than it was when the substrate was Rab1A, a protein of the endoplasmic reticulum. The data imply the existence of multiple component A proteins, one of which is missing in choroideremia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seabra, M C -- Brown, M S -- Goldstein, J L -- HL 20948/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1993 Jan 15;259(5093):377-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8380507" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adult ; *Alkyl and Aryl Transferases ; Cell Line, Transformed ; Cells, Cultured ; Choroid/chemistry ; Choroideremia/*genetics ; Female ; GTP-Binding Proteins/analysis/*metabolism ; Gene Expression Regulation, Enzymologic ; Humans ; Lymphocyte Activation ; Male ; Middle Aged ; Mutation ; Nerve Tissue Proteins/analysis/*metabolism ; Photoreceptor Cells/chemistry ; Pigment Epithelium of Eye/chemistry ; Protein Prenylation ; Retina/chemistry ; Substrate Specificity ; Transferases/*deficiency/genetics ; rab1 GTP-Binding Proteins ; rab3 GTP-Binding Proteins
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 75
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-12-24
    Beschreibung: Two models describing the interaction between U6 small nuclear RNA (snRNA) and the 5' splice site of introns have been proposed on the basis of cross-linking experiments. Here it is shown that a conserved sequence present in U6 snRNA forms base pairs with conserved nucleotides at the 5' splice junction and that this interaction is involved in 5' splice site choice. These results demonstrate a specific function for U6 snRNA in splicing and suggest that U6 snRNA has a proofreading role during splice site selection. A model is presented in which this new interaction, in concert with previously described interactions between U6 snRNA, U2 snRNA, and the pre-messenger RNA, would position the branch point near the 5' splice site for the catalysis of the first splicing step.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kandels-Lewis, S -- Seraphin, B -- New York, N.Y. -- Science. 1993 Dec 24;262(5142):2035-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology, Laboratory, Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266100" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Base Sequence ; Binding Sites/genetics ; Conserved Sequence/physiology ; Genes, Reporter ; Introns/genetics ; Models, Genetic ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; RNA Splicing/genetics/*physiology ; RNA, Small Nuclear/genetics/*physiology ; Saccharomyces cerevisiae/genetics ; beta-Galactosidase/genetics
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 76
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-01-22
    Beschreibung: The bZIP motif is characterized by a leucine zipper domain that mediates dimerization and a basic domain that contacts DNA. A series of transition metal dimerization domains were used to alter systematically the relative orientation of basic domain peptides. Both the affinity and the specificity of the peptide-DNA interaction depend on domain orientation. These results indicate that the precise configuration linking the domains is important; dimerization is not always sufficient for DNA binding. This approach to studying the effect of orientation on protein function complements mutagenesis and could be used in many systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cuenoud, B -- Schepartz, A -- New York, N.Y. -- Science. 1993 Jan 22;259(5094):510-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Yale University, New Haven, CT 06511-8118.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8424173" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Base Sequence ; Binding Sites ; Circular Dichroism ; Cyclic AMP Response Element-Binding Protein/chemistry/metabolism ; DNA/*metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Fungal Proteins/chemistry/*metabolism ; *Leucine Zippers ; Macromolecular Substances ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Protein Kinases/chemistry/*metabolism ; Protein Structure, Secondary ; Proto-Oncogene Proteins c-jun/chemistry/metabolism ; *Saccharomyces cerevisiae Proteins ; Substrate Specificity
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 77
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-04-16
    Beschreibung: A mobile endogenous transposable element, Tag1, has been identified in the plant Arabidopsis thaliana. Tag1 was found in the nitrate transporter gene, CHL1, of a chlorate-resistant mutant present in a population of plants containing an active maize Ac transposon. Tag1 excises from the chl1 gene producing chlorate-sensitive revertants with Tag1 or Tag1-related elements at different loci. Tag1 and related elements are present in the Landsberg but not Columbia or Wassilewskija ecotypes of Arabidopsis. Thus, Tag1 provides a tool for the insertional mutagenesis of plant genes essential for biological processes of agronomic importance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tsay, Y F -- Frank, M J -- Page, T -- Dean, C -- Crawford, N M -- 5T32CA09345-12/CA/NCI NIH HHS/ -- GM 40672/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Apr 16;260(5106):342-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, San Diego, La Jolla 92093-0116.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8385803" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Arabidopsis/drug effects/*genetics/metabolism ; Base Sequence ; Chlorates/pharmacology ; Cloning, Molecular ; DNA/chemistry/genetics ; *DNA Transposable Elements ; Drug Resistance ; *Genes, Plant ; Molecular Sequence Data ; Mutation ; Nitrates/metabolism ; Plants, Genetically Modified
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 78
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-06-11
    Beschreibung: The propensity of an amino acid to form an alpha helix in a protein was determined by multiple amino substitutions at positions 44 and 131 in T4 lysozyme. These positions are solvent-exposed sites within the alpha helices that comprise, respectively, residues 39 to 50 and 126 to 134. Except for two acidic substitutions that may be involved in salt bridges, the changes in stability at the two sites agree well. The stability values also agree with those observed for corresponding amino acid substitutions in some model peptides. Thus, helix propensity values derived from model peptides can be applicable to proteins. Among the 20 naturally occurring amino acids, proline, glycine, and alanine each have a structurally unique feature that helps to explain their low or high helix propensities. For the remaining 17 amino acids, it appears that the side chain hydrophobic surface buried against the side of the helix contributes substantially to alpha helix propensity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blaber, M -- Zhang, X J -- Matthews, B W -- GM 21967/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jun 11;260(5114):1637-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology, Howard Hughes Medical Institute, University of Oregon, Eugene 97403.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8503008" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acids/*chemistry ; Bacteriophage T4/enzymology ; Enzyme Stability ; Models, Molecular ; Muramidase/chemistry ; Mutation ; *Protein Structure, Secondary ; Thermodynamics
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    Standort Signatur Erwartet Verfügbarkeit
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  • 79
    Publikationsdatum: 1993-07-23
    Beschreibung: The three-dimensional solution structure of a complex between the DNA binding domain of the chicken erythroid transcription factor GATA-1 and its cognate DNA site has been determined with multidimensional heteronuclear magnetic resonance spectroscopy. The DNA binding domain consists of a core which contains a zinc coordinated by four cysteines and a carboxyl-terminal tail. The core is composed of two irregular antiparallel beta sheets and an alpha helix, followed by a long loop that leads into the carboxyl-terminal tail. The amino-terminal part of the core, including the helix, is similar in structure, although not in sequence, to the amino-terminal zinc module of the glucocorticoid receptor DNA binding domain. In the other regions, the structures of these two DNA binding domains are entirely different. The DNA target site in contact with the protein spans eight base pairs. The helix and the loop connecting the two antiparallel beta sheets interact with the major groove of the DNA. The carboxyl-terminal tail, which is an essential determinant of specific binding, wraps around into the minor groove. The complex resembles a hand holding a rope with the palm and fingers representing the protein core and the thumb, the carboxyl-terminal tail. The specific interactions between GATA-1 and DNA in the major groove are mainly hydrophobic in nature, which accounts for the preponderance of thymines in the target site. A large number of interactions are observed with the phosphate backbone.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Omichinski, J G -- Clore, G M -- Schaad, O -- Felsenfeld, G -- Trainor, C -- Appella, E -- Stahl, S J -- Gronenborn, A M -- New York, N.Y. -- Science. 1993 Jul 23;261(5120):438-46.〈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/8332909" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Chickens ; DNA-Binding Proteins/*chemistry ; Erythroid-Specific DNA-Binding Factors ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Tertiary ; Transcription Factors/*chemistry ; Zinc Fingers
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  • 80
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-12-24
    Beschreibung: Five small nuclear RNAs (U1, U2, U4, U5, and U6) participate in precursor messenger RNA (pre-mRNA) splicing. To probe their interactions within the active center of the mammalian spliceosome, substrates containing a single photoactivatable 4-thiouridine residue adjacent to either splice site were synthesized, and crosslinks were induced during the course of in vitro splicing. An invariant loop sequence in U5 small nuclear RNA contacts exon 1 before and after the first step of splicing because a crosslink between U5 and the last residue of exon 1 appeared in the pre-mRNA and then in the cutoff exon 1 intermediate. Both of these crosslinked species could undergo subsequent splicing, indicating that the crosslinks reflect a functional interaction that is maintained through both reaction steps. The same U5 loop aligns the two exons for ligation since the first residue of exon 2 also became crosslinked to U5 in the lariat intermediate. An invariant sequence in U6 RNA became crosslinked to the conserved second position of the intron within both the lariat intermediate and the lariat intron product. On the basis of these results, several conformational arrangements of small nuclear RNAs within the spliceosomal active center can be distinguished, and additional mechanistic parallels between the spliceosome and self-splicing introns can be drawn.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sontheimer, E J -- Steitz, J A -- GM26514/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 24;262(5142):1989-96.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, Boyer Center for Molecular Medicine, New Haven, CT 06536-0812.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266094" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenoviridae/genetics ; Base Sequence ; Binding Sites ; Catalysis ; Exons/genetics ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA Precursors/metabolism ; RNA Splicing/*physiology ; RNA, Small Nuclear/*physiology ; RNA, Viral/physiology ; Spliceosomes/*physiology ; Thiouridine
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  • 81
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-05-07
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1993 May 7;260(5109):751-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8484115" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): *Chromosomes, Human, Pair 2 ; Colonic Neoplasms/*genetics ; Colorectal Neoplasms/*genetics ; DNA, Satellite/*genetics ; Disease Susceptibility ; Female ; *Genes ; Genetic Markers ; Humans ; Male ; Mutation
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 82
    Publikationsdatum: 1993-05-28
    Beschreibung: The retinoblastoma gene product (Rb) is a nuclear phosphoprotein that regulates cell cycle progression. Elf-1 is a lymphoid-specific Ets transcription factor that regulates inducible gene expression during T cell activation. In this report, it is demonstrated that Elf-1 contains a sequence motif that is highly related to the Rb binding sites of several viral oncoproteins and binds to the pocket region of Rb both in vitro and in vivo. Elf-1 binds exclusively to the underphosphorylated form of Rb and fails to bind to Rb mutants derived from patients with retinoblastoma. Co-immunoprecipitation experiments demonstrated an association between Elf-1 and Rb in resting normal human T cells. After T cell activation, the phosphorylation of Rb results in the release of Elf-1, which is correlated temporally with the activation of Elf-1-mediated transcription. Overexpression of a phosphorylation-defective form of Rb inhibited Elf-1-dependent transcription during T cell activation. These results demonstrate that Rb interacts specifically with a lineage-restricted Ets transcription factor. This regulated interaction may be important for the coordination of lineage-specific effector functions such as lymphokine production with cell cycle progression in activated T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, C Y -- Petryniak, B -- Thompson, C B -- Kaelin, W G -- Leiden, J M -- R01 AI29673-01/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1993 May 28;260(5112):1330-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8493578" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Cell Cycle ; Cell Line ; DNA-Binding Proteins/chemistry/*metabolism ; Eye Neoplasms/genetics ; Humans ; Lymphocyte Activation ; Molecular Sequence Data ; Mutation ; Oligodeoxyribonucleotides ; Phosphorylation ; Recombinant Fusion Proteins/metabolism ; Retinoblastoma/genetics ; Retinoblastoma Protein/*metabolism ; T-Lymphocytes/immunology/*metabolism ; Transcription Factors/chemistry/*metabolism ; Transcription, Genetic
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 83
    Publikationsdatum: 1993-02-19
    Beschreibung: Ligand-gated ion channels gated by glutamate constitute the major excitatory neurotransmitter system in the mammalian brain. The functional modulation of GluR6, a kainate-activated glutamate receptor, by adenosine 3',5'-monophosphate-dependent protein kinase A (PKA) was examined with receptors expressed in human embryonic kidney cells. Kainate-evoked currents underwent a rapid desensitization that was blocked by lectins. Kainate currents were potentiated by intracellular perfusion of PKA, and this potentiation was blocked by co-application of an inhibitory peptide. Site-directed mutagenesis was used to identify the site or sites of phosphorylation on GluR6. Although mutagenesis of two serine residues, Ser684 and Ser666, was required for complete abolition of the PKA-induced potentiation, Ser684 may be the preferred site of phosphorylation in native GluR6 receptor complexes. These results indicate that glutamate receptor function can be directly modulated by protein phosphorylation and suggest that a dynamic regulation of excitatory receptors could be associated with some forms of learning and memory in the mammalian brain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, L Y -- Taverna, F A -- Huang, X P -- MacDonald, J F -- Hampson, D R -- New York, N.Y. -- Science. 1993 Feb 19;259(5098):1173-5.〈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/8382377" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Base Sequence ; Binding Sites ; Brain/*physiology ; Cells, Cultured ; Concanavalin A/pharmacology ; Evoked Potentials/drug effects ; Humans ; Kainic Acid/*pharmacology ; Kidney ; Kinetics ; Membrane Potentials/drug effects ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oligodeoxyribonucleotides ; Protein Kinases/*metabolism ; Receptors, Glutamate/drug effects/genetics/*physiology ; Receptors, Kainic Acid ; Serine ; Wheat Germ Agglutinins/pharmacology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 84
    Publikationsdatum: 1993-01-08
    Beschreibung: The human and Drosophila heat shock transcription factors (HSFs) are multi-zipper proteins with high-affinity binding to DNA that is regulated by heat shock-induced trimerization. Formation of HSF trimers is dependent on hydrophobic heptad repeats located in the amino-terminal region of the protein. Two subregions at the carboxyl-terminal end of human HSF1 were identified that maintain the monomeric form of the protein under normal conditions. One of these contains a leucine zipper motif that is conserved between vertebrate and insect HSFs. These results suggest that the carboxyl-terminal zipper may suppress formation of trimers by the amino-terminal HSF zipper elements by means of intramolecular coiled-coil interactions that are sensitive to heat shock.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rabindran, S K -- Haroun, R I -- Clos, J -- Wisniewski, J -- Wu, C -- New York, N.Y. -- Science. 1993 Jan 8;259(5092):230-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8421783" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Binding Sites ; Cell Line ; DNA/metabolism ; Drosophila/chemistry ; Heat-Shock Proteins/*chemistry/genetics/metabolism ; Hot Temperature ; Humans ; *Leucine Zippers ; Macromolecular Substances ; Molecular Sequence Data ; Mutagenesis ; Structure-Activity Relationship ; Transfection
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 85
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-08-06
    Beschreibung: Regions of Escherichia coli ribonuclease P (RNase P) RNA in proximity to a bound transfer RNA (tRNA) substrate were mapped by photoaffinity. A photoaffinity cross-linking reagent was introduced at specific sites in the interior of the native tRNA structure by modification of the 5' ends of circularly permuted tRNAs (cptRNAs). The polymerase chain reaction was used for the production of cptRNA templates. After the amplification of a segment of a tandemly duplicated tRNA gene, the cptRNA gene was transcribed in vitro to produce cptRNA. Modified cptRNAs were cross-linked to RNase P RNA, and the conjugation sites in RNase P RNA were determined by primer extension. These sites occur in phylogenetically conserved structures and sequences and identify regions of the ribozyme that form part of the tRNA binding site. The use of circularly permuted molecules to position specific modifications is applicable to the study of many inter- and intramolecular interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nolan, J M -- Burke, D H -- Pace, N R -- GM34527/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Aug 6;261(5122):762-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Indiana University, Bloomington 47405.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7688143" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Affinity Labels ; Base Sequence ; Binding Sites ; Endoribonucleases/*chemistry/metabolism ; Escherichia coli/enzymology/genetics ; *Escherichia coli Proteins ; Molecular Sequence Data ; Nucleic Acid Conformation ; Polymerase Chain Reaction ; RNA/chemistry/metabolism ; RNA, Bacterial/*chemistry/genetics/metabolism ; RNA, Catalytic/*chemistry/metabolism ; RNA, Transfer/*chemistry/genetics/metabolism ; Ribonuclease P
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  • 86
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-02-12
    Beschreibung: To investigate the mechanism of interaction of the toxin colicin E1 with membranes, three cysteine substitution mutants and the wild type of the channel-forming fragment were spin labeled at the unique thiol. Time-resolved interaction of these labeled proteins with phospholipid vesicles was investigated with stopped-flow electron paramagnetic resonance spectroscopy. The fragment interacts with neutral bilayers at low pH, indicating that the interaction is hydrophobic rather than electrostatic. The interaction occurs in at least two distinct steps: (i) rapid adsorption to the surface; and (ii) slow, rate-limiting insertion of the hydrophobic central helices into the membrane interior.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shin, Y K -- Levinthal, C -- Levinthal, F -- Hubbell, W L -- EY05216/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1993 Feb 12;259(5097):960-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Jules Stein Eye Institute, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8382373" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adsorption ; Binding Sites ; Cell Membrane/*metabolism ; Colicins/chemistry/genetics/*metabolism ; Cysteine/genetics ; Electron Spin Resonance Spectroscopy ; Hydrogen-Ion Concentration ; Kinetics ; Lipid Bilayers/metabolism ; *Mutagenesis ; Peptide Fragments/metabolism ; Protein Structure, Secondary ; *Spin Labels
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 87
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-10-15
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tsou, C L -- New York, N.Y. -- Science. 1993 Oct 15;262(5132):380-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211158" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Binding Sites ; Creatine Kinase/chemistry/metabolism ; Enzyme Inhibitors ; Enzymes/chemistry/*metabolism ; Glyceraldehyde-3-Phosphate Dehydrogenases/chemistry/metabolism ; Guanidine ; Guanidines/pharmacology ; Papain/chemistry/metabolism ; Protein Conformation ; Protein Denaturation ; Protein Folding ; Ribonuclease, Pancreatic/chemistry/metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 88
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-03-05
    Beschreibung: A molecular docking computer program (DOCK) was used to screen the Fine Chemical Directory, a database of commercially available compounds, for molecules that are complementary to thymidylate synthase (TS), a chemotherapeutic target. Besides retrieving the substrate and several known inhibitors, DOCK proposed putative inhibitors previously unknown to bind to the enzyme. Three of these compounds inhibited Lactobacillus casei TS at submillimolar concentrations. One of these inhibitors, sulisobenzone, crystallized with TS in two configurations that differed from the DOCK-favored geometry: a counterion was bound in the substrate site, which resulted in a 6 to 9 angstrom displacement of the inhibitor. The structure of the complexes suggested another binding region in the active site that could be exploited. This region was probed with molecules sterically similar to sulisobenzone, which led to the identification of a family of phenolphthalein analogs that inhibit TS in the 1 to 30 micromolar range. These inhibitors do not resemble the substrates of the enzyme. A crystal structure of phenolphthalein with TS shows that it binds in the target site in a configuration that resembles the one suggested by DOCK.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shoichet, B K -- Stroud, R M -- Santi, D V -- Kuntz, I D -- Perry, K M -- GM24485/GM/NIGMS NIH HHS/ -- GM31497/GM/NIGMS NIH HHS/ -- GM39553/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1993 Mar 5;259(5100):1445-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmaceutical Chemistry, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8451640" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Benzophenones/chemistry/*pharmacology ; Binding Sites ; *Computers ; Databases, Factual ; Lactobacillus casei/enzymology ; Models, Molecular ; Molecular Conformation ; Molecular Structure ; Phenolphthaleins/chemistry/*pharmacology ; Protein Structure, Secondary ; Thymidylate Synthase/*antagonists & inhibitors/chemistry ; X-Ray Diffraction
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 89
    Publikationsdatum: 1993-10-15
    Beschreibung: The cell cycle regulatory protein CksHs2 binds to the catalytic subunit of the cyclin-dependent kinases (Cdk's) and is essential for their biological function. The crystal structure of the protein was determined at 2.1 A resolution. The CksHs2 structure is an unexpected hexamer formed by the symmetric assembly of three interlocked dimers into an unusual 12-stranded beta barrel fold that may represent a prototype for this class of protein structures. Sequence-conserved regions form the unusual beta strand exchange between the subunits of the dimer, and the metal and anion binding sites associated with the hexamer assembly. The two other sequence-conserved regions line a 12 A diameter tunnel through the beta barrel and form the six exposed, charged helix pairs. Six kinase subunits can be modeled to bind the assembled hexamer without collision, and therefore this CksHs2 hexamer may participate in cell cycle control by acting as the hub for Cdk multimerization in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parge, H E -- Arvai, A S -- Murtari, D J -- Reed, S I -- Tainer, J A -- New York, N.Y. -- Science. 1993 Oct 15;262(5132):387-95.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Department of Molecular 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/8211159" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Binding Sites ; CDC2-CDC28 Kinases ; Carrier Proteins/*chemistry/physiology ; *Cell Cycle ; *Cell Cycle Proteins ; Computer Graphics ; Conserved Sequence ; Crystallography, X-Ray ; Humans ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Protein Folding ; Protein Kinases/metabolism ; Protein Structure, Secondary ; Sequence Alignment
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  • 90
    Publikationsdatum: 1993-09-24
    Beschreibung: Interferons induce transcriptional activation through tyrosine phosphorylation of the latent, cytoplasmic transcription factor interferon-stimulated gene factor-3 (ISGF-3). Growth factors and cytokines were found to use a similar pathway: The 91-kilodalton subunit of ISGF-3 was activated and tyrosine phosphorylated in response to epidermal growth factor (EGF), platelet-derived growth factor, and colony stimulating factor-1. The tyrosine phosphorylated factor acquired DNA binding activity and accumulated in nuclei. Activation required the major sites for autophosphorylation on the EGF receptor that bind Src homology region 2 domain-containing proteins implicated in Ras activation. However, activation of this factor was independent of the normal functioning of Ras.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Silvennoinen, O -- Schindler, C -- Schlessinger, J -- Levy, D E -- AI-28900/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 24;261(5129):1736-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, New York University School of Medicine, New York, 10016.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8378775" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): 3T3 Cells ; Animals ; Base Sequence ; Cell Line ; DNA-Binding Proteins/*metabolism ; Epidermal Growth Factor/pharmacology ; Genes, ras ; Growth Substances/*pharmacology ; Humans ; Interferon-Stimulated Gene Factor 3 ; Interferon-Stimulated Gene Factor 3, gamma Subunit ; Macrophage Colony-Stimulating Factor/pharmacology ; Mice ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Platelet-Derived Growth Factor/pharmacology ; Receptor, Epidermal Growth Factor/metabolism ; STAT1 Transcription Factor ; *Signal Transduction ; *Trans-Activators ; Transcription Factors/*metabolism ; Tyrosine/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 91
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-12-24
    Beschreibung: The key cell-cycle regulator Cdc2 belongs to a family of cyclin-dependent kinases in higher eukaryotes. Dominant-negative mutations were used to address the requirement for kinases of this family in progression through the human cell cycle. A dominant-negative Cdc2 mutant arrested cells at the G2 to M phase transition, whereas mutants of the cyclin-dependent kinases Cdk2 and Cdk3 caused a G1 block. The mutant phenotypes were specifically rescued by the corresponding wild-type kinases. These data reveal that Cdk3, in addition to Cdc2 and Cdk2, executes a distinct and essential function in the mammalian cell cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉van den Heuvel, S -- Harlow, E -- New York, N.Y. -- Science. 1993 Dec 24;262(5142):2050-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Massachusetts General Hospital Cancer Center, Charlestown 02129.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266103" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; CDC2 Protein Kinase/physiology ; *CDC2-CDC28 Kinases ; Cell Cycle/*physiology ; Cyclin-Dependent Kinase 2 ; *Cyclin-Dependent Kinases ; Cyclins/*physiology ; Genetic Vectors ; Humans ; Molecular Sequence Data ; Mutation ; Plasmids ; Protein Kinases/genetics/*physiology ; *Protein-Serine-Threonine Kinases ; Tumor Cells, Cultured
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  • 92
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-01-15
    Beschreibung: A transfer RNA (tRNA) binding protein present in HeLa cell nuclear extracts was purified and identified as the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Studies with mutant tRNAs indicated that GAPDH recognizes both sequence and structural features in the RNA. GAPDH discriminated between wild-type tRNA and two tRNA mutants that are defective in nuclear export, which suggests that the protein may participate in RNA export. The cofactor nicotinamide adenine dinucleotide disrupted complex formation between tRNA and GAPDH and thus may share a common binding site with the RNA. Indirect immunofluorescence experiments showed that GAPDH is present in the nucleus as well as in the cytoplasm.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Singh, R -- Green, M R -- GM35490/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jan 15;259(5093):365-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Molecular Medicine, University of Massachusetts Medical Center, Worcester 01605.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8420004" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Base Sequence ; Binding Sites ; Binding, Competitive ; Cell Nucleus/enzymology ; Cytoplasm/enzymology ; Escherichia coli/genetics ; Glyceraldehyde-3-Phosphate Dehydrogenases/chemistry/immunology/*metabolism ; HeLa Cells ; Humans ; Molecular Sequence Data ; Mutagenesis ; RNA, Transfer, Met/chemistry/*metabolism ; RNA, Transfer, Ser/metabolism ; RNA, Transfer, Tyr/metabolism ; Saccharomyces cerevisiae/genetics ; Transcription, Genetic
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 93
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-10-29
    Beschreibung: The gamma delta resolvase protein is one of a large family of transposon-encoded site-specific recombinases. It performs recombination in a DNA-protein complex that contains 12 resolvase protomers and two copies of the 120-base pair DNA substrate, res (each with three binding sites for a resolvase dimer). A derivative of resolvase with altered DNA binding specificity was used to show that the role of resolvase at site I, which contains the crossover point, differs from its role at the other two binding sites. The resolvase dimers that initially bind to site I are the only ones that require the residue Ser10, essential for catalysis of DNA breakage. In addition, these site I-bound dimers do not use a specific interaction between dimers that is required elsewhere in the complex for synapsis of the res sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grindley, N D -- New York, N.Y. -- Science. 1993 Oct 29;262(5134):738-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, Bass Center for Molecular and Structural Biology, New Haven, CT 06511.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235593" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Base Sequence ; Binding Sites ; Biopolymers ; Catalysis ; DNA-Binding Proteins/*chemistry ; Molecular Sequence Data ; Mutation ; Nucleoproteins/chemistry ; Nucleotidyltransferases/*chemistry ; Synaptosomes/*chemistry ; Transposases
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  • 94
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-06-04
    Beschreibung: Aminoglycoside inhibitors of translation have been shown previously to inhibit in vitro self-splicing by group I introns. Chemical probing of the phage T4-derived sunY intron shows that neomycin, streptomycin, and related antibiotics protected the N-7 position of G96, a universally conserved guanine in the binding site for the guanosine cofactor in the splicing reaction. The antibiotics also disrupted structural contacts that have been proposed to bring the 5' cleavage site of the intron into proximity to the catalytic core. In contrast, the strictly competitive inhibitors deoxyguanosine and arginine protected only the N-7 position of G96. Parallels between these results and previously observed protection of 16S ribosomal RNA by aminoglycosides raise the possibility that group I intron splicing and transfer RNA selection by ribosomes involve similar RNA structural motifs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉von Ahsen, U -- Noller, H F -- GM17129/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jun 4;260(5113):1500-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sinsheimer Laboratories, University of California, Santa Cruz 95064.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8502993" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Aminoglycosides ; Animals ; Anti-Bacterial Agents/metabolism/*pharmacology ; Base Sequence ; Binding Sites ; Introns/genetics ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation/drug effects ; RNA Splicing/drug effects ; RNA, Catalytic/chemistry/*drug effects/metabolism ; Tetrahymena/genetics
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 95
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-10-15
    Beschreibung: The Tax protein of human T cell leukemia virus type-1 (HTLV-I) transcriptionally activates the HTLV-I promoter. This activation requires binding sites for activating transcription factor (ATF) proteins, a family of cellular proteins that contain basic region-leucine zipper (bZIP) DNA binding domains. Data are presented showing that Tax increases the in vitro DNA binding activity of multiple ATF proteins. Tax also stimulated DNA binding by other bZIP proteins, but did not affect DNA binding proteins that lack a bZIP domain. The increase in DNA binding occurred because Tax promotes dimerization of the bZIP domain in the absence of DNA, and the elevated concentration of the bZIP homodimer then facilitates the DNA binding reaction. These results help explain how Tax activates viral transcription and transforms cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wagner, S -- Green, M R -- New York, N.Y. -- Science. 1993 Oct 15;262(5132):395-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Molecular Medicine, University of Massachusetts Medical Center, Worcester 01605.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211160" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Activating Transcription Factor 1 ; Activating Transcription Factor 2 ; Base Sequence ; Basic-Leucine Zipper Transcription Factors ; Binding Sites ; Cell Line ; Cell Transformation, Viral ; Cyclic AMP Response Element-Binding Protein/metabolism ; DNA/*metabolism ; DNA-Binding Proteins ; G-Box Binding Factors ; Gene Products, tax/*metabolism ; Leucine Zippers ; Molecular Sequence Data ; Oligodeoxyribonucleotides/*metabolism ; Plant Proteins ; Polymers ; Recombinant Fusion Proteins/metabolism ; Transcription Factors/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 96
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-08-13
    Beschreibung: The peptide alpha 4 is a designed four-helix bundle that contains a highly simplified hydrophobic core composed exclusively of leucine residues; its tertiary structure is therefore largely dictated by hydrophobic forces. This small protein adopts a structure with properties intermediate between those of the native and molten globule states of proteins: it is compact, globular, and has very stable helices, but its apolar side chains are mobile and not as well packed as in many natural proteins. To induce a more native-like state, two Zn(2+)-binding sites were introduced into the protein, thereby replacing some of the non-specific hydrophobic interactions with more geometrically restrictive metal-ligand interactions. In the metal-bound state, this protein has properties that approach those of native proteins. Thus, hydrophobic interactions alone are sufficient to drive polypeptide chain folding nearly to completion, but specific interactions are required for a unique structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Handel, T M -- Williams, S A -- DeGrado, W F -- New York, N.Y. -- Science. 1993 Aug 13;261(5123):879-85.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Du Pont Merck Pharmaceutical Company, Wilmington, DE 19880-0328.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8346440" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Anilino Naphthalenesulfonates/metabolism ; Binding Sites ; Histidine/chemistry/metabolism ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Proteins/chemical synthesis/*chemistry/metabolism ; Thermodynamics ; Zinc/*chemistry
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 97
    Publikationsdatum: 1993-11-12
    Beschreibung: Calmodulin is a highly conserved regulatory protein found in all eukaryotic organisms which mediates a variety of calcium ion-dependent signalling pathways. In the Drosophila retina, calmodulin was concentrated in the photoreceptor cell microvillar structure, the rhabdomere, and was found in lower amounts in the sub-rhabdomeral cytoplasm. This calmodulin localization was dependent on the NINAC (neither inactivation nor afterpotential C) unconventional myosins. Mutant flies lacking the rhabdomere-specific p174 NINAC protein did not concentrate calmodulin in the rhabdomere, whereas flies lacking the sub-rhabdomeral p132 isoform had no detectable cytoplasmic calmodulin. Furthermore, a defect in vision resulted when calmodulin was not concentrated in the rhabdomeres, suggesting a role for calmodulin in the regulation of fly phototransduction. A general function of unconventional myosins may be to control the subcellular distribution of calmodulin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Porter, J A -- Yu, M -- Doberstein, S K -- Pollard, T D -- Montell, C -- EY08117/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 12;262(5136):1038-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, 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/8235618" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Calcium/metabolism ; Calmodulin/*metabolism ; Drosophila ; *Drosophila Proteins ; Electroretinography ; Eye Proteins/*metabolism ; Mutation ; *Myosin Heavy Chains ; Myosins/*metabolism ; Nerve Degeneration ; Photoreceptor Cells, Invertebrate/*metabolism ; Retina/metabolism
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    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 98
    Publikationsdatum: 1993-04-30
    Beschreibung: A congenic, non-obese diabetic (NOD) mouse strain that contains a segment of chromosome 3 from the diabetes-resistant mouse strain B6.PL-Thy-1a was less susceptible to diabetes than NOD mice. A fully penetrant immunological defect also mapped to this segment, which encodes the high-affinity Fc receptor for immunoglobulin G (IgG), Fc gamma RI. The NOD Fcgr1 allele, which results in a deletion of the cytoplasmic tail, caused a 73 percent reduction in the turnover of cell surface receptor-antibody complexes. The development of congenic strains and the characterization of Mendelian traits that are specific to the disease phenotype demonstrate the feasibility of dissecting the pathophysiology of complex, non-Mendelian diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Prins, J B -- Todd, J A -- Rodrigues, N R -- Ghosh, S -- Hogarth, P M -- Wicker, L S -- Gaffney, E -- Podolin, P L -- Fischer, P A -- Sirotina, A -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1993 Apr 30;260(5108):695-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nuffield Department of Surgery, University of Oxford, John Radcliffe Hospital, Headington, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8480181" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Autoimmune Diseases/*genetics ; Base Sequence ; Crosses, Genetic ; Diabetes Mellitus, Type 1/*genetics ; Endocytosis ; Female ; Gene Deletion ; *Genetic Linkage ; Genetic Markers ; Immunoglobulin G/metabolism ; Male ; Mice ; Mice, Inbred NOD ; Molecular Sequence Data ; Mutation ; Phenotype ; Receptors, IgG/*genetics/metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 99
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-09-17
    Beschreibung: In budding yeast genes that encode G1 cyclins and proteins involved in DNA synthesis are transcriptionally activated in late G1. A transcription factor, called SBF, is composed of Swi4 and Swi6 proteins and activates transcription of G1 cyclin genes. A different, but related, complex called MBF binds to MCB elements (Mlu I cell cycle box) found in the promoter of most DNA synthesis genes. MBF contains Swi6 and a 120-kilodalton protein (p120). MBF was purified and the gene encoding p120 (termed MBP1) was cloned. A deletion of MBP1 was not lethal but led to deregulated expression of DNA synthesis genes, indicating a direct regulatory role for MBF in MCB-driven transcription. Mbp1 is related to Swi4. Strains deleted for both MBP1 and SWI4 were inviable, demonstrating that transcriptional activation by MBF and SBF has an important role in the transition from G1 to S phase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koch, C -- Moll, T -- Neuberg, M -- Ahorn, H -- Nasmyth, K -- New York, N.Y. -- Science. 1993 Sep 17;261(5128):1551-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Pathology, Vienna, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8372350" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Base Sequence ; CDC28 Protein Kinase, S cerevisiae/genetics/metabolism ; Cloning, Molecular ; Cyclins/genetics ; DNA, Fungal/biosynthesis ; DNA-Binding Proteins ; Fungal Proteins/chemistry/*genetics/metabolism ; *G1 Phase ; Gene Expression Regulation, Fungal ; Genes, Fungal ; Molecular Sequence Data ; Mutation ; Promoter Regions, Genetic ; *S Phase ; Saccharomyces cerevisiae/cytology/*genetics ; *Saccharomyces cerevisiae Proteins ; Sequence Alignment ; Transcription Factors/chemistry/*genetics/metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 100
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1993-04-30
    Beschreibung: Intermediate filaments are abundant cytoskeletal components whose specific cellular functions are poorly understood. The Saccharomyces cerevisiae protein MDM1 displays structure and solubility properties that are similar to those of intermediate filament proteins of animal cells. Yeast cells that have a mutant form of MDM1 exhibit temperature-sensitive growth and defective transfer of nuclei and mitochondria to daughter cells during incubation at the nonpermissive temperature of 37 degrees C. The purified, wild-type MDM1 protein readily forms 10-nanometer-wide filaments at either 4 degrees C or 37 degrees C. In contrast, the purified, mutant protein forms filaments at 4 degrees C but fails to form such structures at 37 degrees C. These results suggest that intermediate filament proteins are universal components of eukaryotic cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McConnell, S J -- Yaffe, M P -- New York, N.Y. -- Science. 1993 Apr 30;260(5108):687-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, San Diego, La Jolla 92093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8480179" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): *Cell Cycle Proteins ; Cell Division ; Cell Nucleus/metabolism ; Fungal Proteins/genetics/*metabolism ; Genes, Fungal ; Intermediate Filament Proteins ; Intermediate Filaments/*metabolism/ultrastructure ; Microscopy, Electron ; Mitochondria/metabolism ; Mutation ; Saccharomyces cerevisiae/genetics/*metabolism/ultrastructure ; *Saccharomyces cerevisiae Proteins ; Temperature
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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