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  • Amino Acid Sequence  (172)
  • American Association for the Advancement of Science (AAAS)  (172)
  • Blackwell Publishing Ltd
  • 2010-2014
  • 1995-1999  (172)
  • 1980-1984
  • 1996  (172)
Collection
Publisher
  • American Association for the Advancement of Science (AAAS)  (172)
  • Blackwell Publishing Ltd
Years
  • 2010-2014
  • 1995-1999  (172)
  • 1980-1984
Year
  • 1
    Publication Date: 1996-11-29
    Description: A 13.1-kilodalton protein, cysteine-rich neurotrophic factor (CRNF), was purified from the mollusk Lymnaea stagnalis by use of a binding assay on the p75 neurotrophin receptor. CRNF bound to p75 with nanomolar affinity but was not similar in sequence to neurotrophins or any other known gene product. CRNF messenger RNA expression was highest in adult foot subepithelial cells; in the central nervous system, expression was regulated by lesion. The factor evoked neurite outgrowth and modulated calcium currents in pedal motor neurons. Thus, CRNF may be involved in target-derived trophic support for motor neurons and could represent the prototype of another family of p75 ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fainzilber, M -- Smit, A B -- Syed, N I -- Wildering, W C -- Hermann -- van der Schors, R C -- Jimenez, C -- Li, K W -- van Minnen, J -- Bulloch, A G -- Ibanez, C F -- Geraerts, W P -- New York, N.Y. -- Science. 1996 Nov 29;274(5292):1540-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Neurobiology, Department of Neuroscience, Karolinska Institute, Berzelius Laboratories Building, Doktorsringen 12A, S-17177 Stockholm, Sweden. michael@cajal.mbb.ki.se〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8929417" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding, Competitive ; Calcium/metabolism ; Hemolymph/chemistry ; Humans ; Lymnaea/*chemistry ; Molecular Sequence Data ; Motor Neurons/ultrastructure ; Nerve Growth Factors/chemistry/genetics/isolation & ; purification/metabolism/*physiology ; Neurites/physiology ; RNA, Messenger/genetics/metabolism ; Receptor, Nerve Growth Factor ; Receptors, Nerve Growth Factor/*metabolism ; Recombinant Proteins/chemistry/isolation & purification/metabolism ; Tumor Cells, Cultured
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  • 2
    Publication Date: 1996-12-13
    Description: The structure of the Staphylococcus aureus alpha-hemolysin pore has been determined to 1.9 A resolution. Contained within the mushroom-shaped homo-oligomeric heptamer is a solvent-filled channel, 100 A in length, that runs along the sevenfold axis and ranges from 14 A to 46 A in diameter. The lytic, transmembrane domain comprises the lower half of a 14-strand antiparallel beta barrel, to which each protomer contributes two beta strands, each 65 A long. The interior of the beta barrel is primarily hydrophilic, and the exterior has a hydrophobic belt 28 A wide. The structure proves the heptameric subunit stoichiometry of the alpha-hemolysin oligomer, shows that a glycine-rich and solvent-exposed region of a water-soluble protein can self-assemble to form a transmembrane pore of defined structure, and provides insight into the principles of membrane interaction and transport activity of beta barrel pore-forming toxins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Song, L -- Hobaugh, M R -- Shustak, C -- Cheley, S -- Bayley, H -- Gouaux, J E -- New York, N.Y. -- Science. 1996 Dec 13;274(5294):1859-66.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Chicago, 920 East 58 Street, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8943190" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Toxins/*chemistry/metabolism ; Cell Membrane/chemistry/metabolism ; Crystallography, X-Ray ; Hemolysin Proteins/*chemistry/metabolism ; Hydrogen Bonding ; Lipid Bilayers/*chemistry ; Membrane Potentials ; Models, Molecular ; Molecular Sequence Data ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Staphylococcus aureus/*chemistry
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  • 3
    Publication Date: 1996-07-19
    Description: Signaling molecules are essential for vertebrate embryonic development. Here, two Xenopus homologs of the Drosophila gene fringe, lunatic Fringe (lFng) and radical Fringe (rFng), were identified and the protein product of lFng further characterized. The messenger RNA of lFng is supplied as a maternal message. Its product is a precursor protein consisting of pre-, pro-, and mature regions. The mature lunatic Fringe protein is secreted extracellularly, and it induced mesodermal tissue formation in animal cap assays. These results indicate that secreted lunatic Fringe can induce mesoderm and reveal that the Fringe proteins are a family of vertebrate signaling molecules.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2080353/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2080353/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, J Y -- Wen, L -- Zhang, W J -- Rao, Y -- R01 CA114197/CA/NCI NIH HHS/ -- R01 CA114197-01A2/CA/NCI NIH HHS/ -- R01 EY014576/EY/NEI NIH HHS/ -- R01 EY014576-03/EY/NEI NIH HHS/ -- R01 GM070967/GM/NIGMS NIH HHS/ -- R01 GM070967-02/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 19;273(5273):355-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Washington University School of Medicine, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662522" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Blastocyst/metabolism ; Cell Line ; Culture Media, Conditioned ; Culture Techniques ; Drosophila Proteins ; Embryo, Nonmammalian/metabolism ; Embryonic Development ; *Embryonic Induction ; *Glycosyltransferases ; Mesoderm/*metabolism ; Molecular Sequence Data ; *N-Acetylglucosaminyltransferases ; Polymerase Chain Reaction ; Protein Processing, Post-Translational ; Proteins/chemistry/genetics/*physiology/secretion ; RNA, Messenger/genetics/metabolism ; *Signal Transduction ; Xenopus/*embryology/genetics ; *Xenopus Proteins
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  • 4
    Publication Date: 1996-11-15
    Description: The initiation of anaphase and exit from mitosis require the activation of a proteolytic system that ubiquitinates and degrades cyclin B. The regulated component of this system is a large ubiquitin ligase complex, termed the anaphase-promoting complex (APC) or cyclosome. Purified Xenopus laevis APC was found to be composed of eight major subunits, at least four of which became phosphorylated in mitosis. In addition to CDC27, CDC16, and CDC23, APC contained a homolog of Aspergillus nidulans BIME, a protein essential for anaphase. Because mutation of bimE can bypass the interphase arrest induced by either nimA mutation or unreplicated DNA, it appears that ubiquitination catalyzed by APC may also negatively regulate entry into mitosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peters, J M -- King, R W -- Hoog, C -- Kirschner, M W -- New York, N.Y. -- Science. 1996 Nov 15;274(5290):1199-201.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8895470" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Anaphase ; Animals ; Aspergillus/chemistry/cytology/metabolism ; Cell Cycle Proteins/*chemistry/metabolism ; Cyclins/metabolism ; Electrophoresis, Polyacrylamide Gel ; Fungal Proteins/analysis/*chemistry/genetics/metabolism ; Ligases/*chemistry/metabolism ; *Mitosis ; Molecular Sequence Data ; Mutation ; Ovum ; Phosphorylation ; Ubiquitin-Protein Ligases ; Xenopus laevis
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  • 5
    Publication Date: 1996-05-10
    Description: Transcription factors of the NFAT family are thought to play a major role in regulating the expression of cytokine genes and other inducible genes during the immune response. The role of NFAT1 was investigated by targeted disruption of the NFAT1 gene. Unexpectedly, cells from NFAT1 -/- mice showed increased primary responses to Leishmania major and mounted increased secondary responses to ovalbumin in vitro. In an in vivo model of allergic inflammation, the accumulation of eosinophils and levels of serum immunoglobulin E were increased in NFAT1 -/- mice. These results suggest that NFAT1 exerts a negative regulatory influence on the immune response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xanthoudakis, S -- Viola, J P -- Shaw, K T -- Luo, C -- Wallace, J D -- Bozza, P T -- Luk, D C -- Curran, T -- Rao, A -- CA42471/CA/NCI NIH HHS/ -- GM46227/GM/NIGMS NIH HHS/ -- P30 CA21765/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 May 10;272(5263):892-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Neurogenetics Program, Department of CNS Research, Hoffmann-LaRoche, Nutley, NJ 07110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8629027" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Protozoan/immunology ; Cell Line ; Cytokines/biosynthesis ; DNA-Binding Proteins/genetics/*physiology ; Eosinophils/immunology ; Gene Targeting ; Hypersensitivity/*immunology ; *Immunity ; Immunoglobulin E/biosynthesis ; Immunologic Memory ; Leishmania major/immunology ; *Lymphocyte Activation ; Mice ; Molecular Sequence Data ; NFATC Transcription Factors ; *Nuclear Proteins ; Ovalbumin/immunology ; T-Lymphocytes/immunology ; Transcription Factors/genetics/*physiology
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  • 6
    Publication Date: 1996-03-08
    Description: Friedreich's ataxia (FRDA) is an autosomal recessive, degenerative disease that involves the central and peripheral nervous systems and the heart. A gene, X25, was identified in the critical region for the FRDA locus on chromosome 9q13. This gene encodes a 210-amino acid protein, frataxin, that has homologs in distant species such as Caenorhabditis elegans and yeast. A few FRDA patients were found to have point mutations in X25, but the majority were homozygous for an unstable GAA trinucleotide expansion in the first X25 intron.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Campuzano, V -- Montermini, L -- Molto, M D -- Pianese, L -- Cossee, M -- Cavalcanti, F -- Monros, E -- Rodius, F -- Duclos, F -- Monticelli, A -- Zara, F -- Canizares, J -- Koutnikova, H -- Bidichandani, S I -- Gellera, C -- Brice, A -- Trouillas, P -- De Michele, G -- Filla, A -- De Frutos, R -- Palau, F -- Patel, P I -- Di Donato, S -- Mandel, J L -- Cocozza, S -- Koenig, M -- Pandolfo, M -- 722/Telethon/Italy -- NS34192/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1996 Mar 8;271(5254):1423-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department de Genetica, University of Valencia, Spain.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596916" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Base Sequence ; Chromosomes, Human, Pair 9/*genetics ; DNA Primers ; Female ; Friedreich Ataxia/*genetics ; Genes, Recessive ; Heterozygote ; Humans ; *Introns ; *Iron-Binding Proteins ; Male ; Molecular Sequence Data ; Pedigree ; Point Mutation ; Polymerase Chain Reaction ; Proteins/chemistry/*genetics ; Sequence Alignment ; *Trinucleotide Repeats
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  • 7
    Publication Date: 1996-08-16
    Description: A signaling pathway has been elucidated whereby growth factors activate the transcription factor cyclic adenosine monophosphate response element-binding protein (CREB), a critical regulator of immediate early gene transcription. Growth factor-stimulated CREB phosphorylation at serine-133 is mediated by the RAS-mitogen-activated protein kinase (MAPK) pathway. MAPK activates CREB kinase, which in turn phosphorylates and activates CREB. Purification, sequencing, and biochemical characterization of CREB kinase revealed that it is identical to a member of the pp90(RSK) family, RSK2. RSK2 was shown to mediate growth factor induction of CREB serine-133 phosphorylation both in vitro and in vivo. These findings identify a cellular function for RSK2 and define a mechanism whereby growth factor signals mediated by RAS and MAPK are transmitted to the nucleus to activate gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xing, J -- Ginty, D D -- Greenberg, M E -- CA43855/CA/NCI NIH HHS/ -- NS34814-01/NS/NINDS NIH HHS/ -- P30-HD18655/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 16;273(5277):959-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Biological and Biomedical Sciences, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8688081" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Line ; Cell Nucleus/metabolism ; Cyclic AMP Response Element-Binding Protein/*metabolism ; Epidermal Growth Factor/pharmacology ; *Gene Expression Regulation ; Growth Substances/*pharmacology ; Humans ; Molecular Sequence Data ; Nerve Growth Factors/pharmacology ; PC12 Cells ; Phosphorylation ; Protein-Serine-Threonine Kinases/*metabolism ; Rats ; Ribosomal Protein S6 Kinases ; *Signal Transduction ; Tetradecanoylphorbol Acetate/pharmacology ; Transcriptional Activation ; Transfection ; Tumor Cells, Cultured ; ras Proteins/metabolism
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-02-23
    Description: The pleiotropic biological activities of interleukin-1 (IL-1) are mediated by its type I receptor (IL-1RI). When the ligand binds, IL-1RI initiates a signaling cascade that results in the activation of the transcription regulator nuclear factor kappa B (NF-kappa B). A protein kinase designated IRAK (IL-1 receptor-associated kinase) was purified, and its complementary DNA was molecularly cloned. When human embryonic kidney cells (cell line 293) over-expressing IL-1RI or HeLa cells were exposed to IL-1, IRAK rapidly associated with the IL-1RI complex and was phosphorylated. The primary amino acid sequence of IRAK shares similarity with that of Pelle, a protein kinase that is essential for the activation of a NF-kappa B homolog in Drosophila.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cao, Z -- Henzel, W J -- Gao, X -- New York, N.Y. -- Science. 1996 Feb 23;271(5252):1128-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Department, Tularik, Incorporated, South San Francisco, CA 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599092" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cloning, Molecular ; DNA, Complementary/genetics ; Drosophila ; *Drosophila Proteins ; HeLa Cells ; Humans ; Interleukin-1/*metabolism/pharmacology ; Interleukin-1 Receptor-Associated Kinases ; Molecular Sequence Data ; Phosphorylation ; Protein Kinases/chemistry/genetics/isolation & purification/*metabolism ; Protein-Serine-Threonine Kinases/chemistry ; Receptors, Interleukin-1/*metabolism ; Transfection
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-10-18
    Description: In mice, susceptibility to Leishmania major is associated with the early expansion of T helper 2 cells (TH2) cells, but nothing is known of the specificity of these cells. A previously identified antigen, Leishmania homolog of receptors for activated C kinase (LACK), was found to be the focus of this initial response. Mice made tolerant to LACK by the transgenic expression of the antigen in the thymus exhibited both a diminished TH2 response and a healing phenotype. Thus, T cells that are activated early and are reactive to a single antigen play a pivotal role in directing the immune response to the entire parasite.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Julia, V -- Rassoulzadegan, M -- Glaichenhaus, N -- New York, N.Y. -- Science. 1996 Oct 18;274(5286):421-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CNRS, Institut de Pharmacologie Moleculaire et Cellulaire, 660 Route des Lucioles, 06560 Valbonne, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8832890" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Protozoan/*immunology ; Crosses, Genetic ; Female ; Immune Tolerance ; Immunity, Innate ; Immunization ; Interleukin-4/secretion ; Interleukin-5/secretion ; Leishmania major/*immunology ; Leishmaniasis, Cutaneous/*immunology ; Lymphocyte Activation ; Male ; Mice ; Mice, Inbred BALB C ; Mice, Transgenic ; Molecular Sequence Data ; Phenotype ; Protozoan Proteins/*immunology ; Th1 Cells/immunology ; Th2 Cells/*immunology
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  • 10
    Publication Date: 1996-06-21
    Description: ZPR1 is a zinc finger protein that binds to the cytoplasmic tyrosine kinase domain of the epidermal growth factor receptor (EGFR). Deletion analysis demonstrated that this binding interaction is mediated by the zinc fingers of ZPR1 and subdomains X and XI of the EGFR tyrosine kinase. Treatment of mammalian cells with EGF caused decreased binding of ZPR1 to the EGFR and the accumulation of ZPR1 in the nucleus. The effect of EGF to regulate ZPR1 binding is dependent on tyrosine phosphorylation of the EGFR. ZPR1 therefore represents a prototype for a class of molecule that binds to the EGFR and is released from the receptor after activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Galcheva-Gargova, Z -- Konstantinov, K N -- Wu, I H -- Klier, F G -- Barrett, T -- Davis, R J -- R01-CA58396/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 21;272(5269):1797-802.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650580" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry/*metabolism/secretion ; Cell Line ; Cell Nucleus/metabolism ; Cloning, Molecular ; Cytoplasm/metabolism ; Epidermal Growth Factor/pharmacology ; Humans ; Immunoblotting ; Male ; Mice ; Molecular Sequence Data ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein Structure, Secondary ; RNA, Messenger/genetics/metabolism ; Receptor, Epidermal Growth Factor/chemistry/*metabolism ; Testis/metabolism ; Type C Phospholipases/metabolism ; Vanadates/pharmacology ; *Zinc Fingers ; src Homology Domains
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  • 11
    Publication Date: 1996-05-31
    Description: Unesterified sterol modulates the function of eukaryotic membranes. In human cells, sterol is esterified to a storage form by acyl-coenzyme A (CoA): cholesterol acyl transferase (ACAT). Here, two genes are identified, ARE1 and ARE2, that encode ACAT-related enzymes in yeast. The yeast enzymes are 49 percent identical to each other and exhibit 23 percent identity to human ACAT. Deletion of ARE2 reduced sterol ester levels to approximately 25 percent of normal levels, whereas disruption of ARE1 did not affect sterol ester biosynthesis. Deletion of both genes resulted in a viable cell with undetectable esterified sterol. Measurements of [14C]acetate incorporation into saponified lipids indicated down-regulation of sterol biosynthesis in the are1 are2 mutant cells. With the use of a consensus sequence to the yeast and human genes, an additional number of the ACAT gene family was identified in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, H -- Bard, M -- Bruner, D A -- Gleeson, A -- Deckelbaum, R J -- Aljinovic, G -- Pohl, T M -- Rothstein, R -- Sturley, S L -- GM 50237/GM/NIGMS NIH HHS/ -- HG00861/HG/NHGRI NIH HHS/ -- R01 AI38598/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 May 31;272(5266):1353-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Human Nutrition, Columbia University College of Physicians and Surgeons, New York, 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650549" target="_blank"〉PubMed〈/a〉
    Keywords: Acetates/metabolism ; Acyltransferases/chemistry/*genetics/metabolism ; Amino Acid Sequence ; Base Sequence ; Cell Membrane/metabolism ; Cholesterol Esters/metabolism ; Cyclin-Dependent Kinase 8 ; *Cyclin-Dependent Kinases ; DNA, Complementary/genetics ; Ergosterol/metabolism ; Esterification ; *Genes, Fungal ; Homeostasis ; Humans ; Molecular Sequence Data ; Mutation ; Oleic Acid ; Oleic Acids/metabolism ; Saccharomyces cerevisiae/*genetics/metabolism ; Saccharomyces cerevisiae Proteins ; Sterol O-Acyltransferase/*genetics/metabolism ; Sterols/*metabolism ; Transformation, Genetic
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  • 12
    Publication Date: 1996-03-15
    Description: Iron must cross biological membranes to reach essential intracellular enzymes. Two proteins in the plasma membrane of yeast--a multicopper oxidase, encoded by the FET3 gene, and a permease, encoded by the FTR1 gene--were shown to mediate high-affinity iron uptake. FET3 expression was required for FTR1 protein to be transported to the plasma membrane. FTR1 expression was required for apo-FET3 protein to be loaded with copper and thus acquire oxidase activity. FTR1 protein also played a direct role in iron transport. Mutations in a conserved sequence motif of FTR1 specifically blocked iron transport.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stearman, R -- Yuan, D S -- Yamaguchi-Iwai, Y -- Klausner, R D -- Dancis, A -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1552-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institutes of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599111" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Biological Transport ; Carrier Proteins/chemistry/*genetics/*metabolism ; Cell Membrane/metabolism ; *Ceruloplasmin ; Copper/metabolism/pharmacology ; Endoplasmic Reticulum/metabolism ; Ferric Compounds/metabolism ; Ferritins/chemistry/metabolism ; Ferrous Compounds/metabolism ; Genes, Fungal ; Golgi Apparatus/metabolism ; Iron/*metabolism ; Membrane Transport Proteins/chemistry/*genetics/*metabolism ; Models, Biological ; Molecular Sequence Data ; Multienzyme Complexes/*metabolism ; Mutation ; Open Reading Frames ; Oxidation-Reduction ; Oxidoreductases/*metabolism ; Saccharomyces cerevisiae/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Transformation, Genetic
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  • 13
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-11-29
    Description: The proteins encoded by the myc proto-oncogene family are involved in cell proliferation, apoptosis, differentiation, and neoplasia. Myc acts through dimerization with Max to bind DNA and activate transcription. Homologs of the myc and max genes were cloned from the fruit fly Drosophila melanogaster and their protein products (dMyc and dMax) were shown to heterodimerize, recognize the same DNA sequence as their vertebrate homologs, and activate transcription. The dMyc protein is likely encoded by the Drosophila gene diminutive (dm), a mutation in which results in small body size and female sterility caused by degeneration of the ovaries. These findings indicate a potential role for Myc in germ cell development and set the stage for genetic analysis of Myc and Max.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gallant, P -- Shiio, Y -- Cheng, P F -- Parkhurst, S M -- Eisenman, R N -- R01CA47138/CA/NCI NIH HHS/ -- R01GM47852/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 29;274(5292):1523-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Basic Sciences, Fred Hutchinson Cancer Research Center, 1124 Columbia Street, Seattle WA 98104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8929412" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; Basic-Leucine Zipper Transcription Factors ; Cloning, Molecular ; DNA Transposable Elements ; DNA, Complementary ; DNA-Binding Proteins/chemistry/genetics/metabolism ; Dimerization ; *Drosophila Proteins ; Drosophila melanogaster/chemistry/*genetics/growth & development/metabolism ; Female ; Gene Expression Regulation, Developmental ; Genes, Insect ; Genes, myc ; *Helix-Loop-Helix Motifs ; Humans ; Molecular Sequence Data ; Oligonucleotide Probes/metabolism ; Ovary/metabolism ; Proto-Oncogene Proteins c-myc/chemistry/genetics/metabolism ; RNA, Messenger/genetics/metabolism ; Transcription Factors/chemistry/genetics/*metabolism ; Transcription, Genetic
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  • 14
    Publication Date: 1996-07-12
    Description: The three-dimensional structure of the amino-terminal core domain (residues 1 through 151) of the human immunodeficiency virus-type 1 (HIV-1) capsid protein has been solved by multidimensional heteronuclear magnetic resonance spectroscopy. The structure is unlike those of previously characterized viral coat proteins and is composed of seven alpha helices, two beta hairpins, and an exposed partially ordered loop. The domain is shaped like an arrowhead, with the beta hairpins and loop exposed at the trailing edge and the carboxyl-terminal helix projecting from the tip. The proline residue Pro1 forms a salt bridge with a conserved, buried aspartate residue (Asp51), which suggests that the amino terminus of the protein rearranges upon proteolytic maturation. The binding site for cyclophilin A, a cellular rotamase that is packaged into the HIV-1 virion, is located on the exposed loop and encompasses the essential proline residue Pro90. In the free monomeric domain, Pro90 adopts kinetically trapped cis and trans conformations, raising the possibility that cyclophilin A catalyzes interconversion of the cis- and trans-Pro90 loop structures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gitti, R K -- Lee, B M -- Walker, J -- Summers, M F -- Yoo, S -- Sundquist, W I -- AI30917/AI/NIAID NIH HHS/ -- CA 42014/CA/NCI NIH HHS/ -- GM 42561/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 12;273(5272):231-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Chemistry and Biochemistry, University of Maryland Baltimore County, Baltimore, MD 21228, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662505" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Isomerases/metabolism ; Amino Acid Sequence ; Aspartic Acid/chemistry ; Binding Sites ; Capsid/*chemistry/metabolism ; Carrier Proteins/metabolism ; HIV Core Protein p24/*chemistry/metabolism ; HIV-1/*chemistry ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Peptidylprolyl Isomerase ; Proline/chemistry ; Protein Conformation ; Protein Processing, Post-Translational ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Virion/chemistry
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  • 15
    Publication Date: 1996-05-10
    Description: Cells deprived of serum mitogens will either undergo immediate cell cycle arrest or complete mitosis and arrest in the next cell cycle. The transition from mitogen dependence to mitogen independence occurs in the mid-to late G1 phase of the cell cycle and is called the restriction point. Murine Balb/c-3T3 fibroblasts deprived of serum mitogens accumulated the cyclin-dependent kinase (CDK) inhibitor p27Kip1. This was correlated with inactivation of essential G1 cyclin-CDK complexes and with cell cycle arrest in G1. The ability of specific mitogens to allow transit through the restriction point paralleled their ability to down-regulate p27, and antisense inhibition of p27 expression prevented cell cycle arrest in response to mitogen depletion. Therefore, p27 is an essential component of the pathway that connects mitogenic signals to the cell cycle at the restriction point.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coats, S -- Flanagan, W M -- Nourse, J -- Roberts, J M -- New York, N.Y. -- Science. 1996 May 10;272(5263):877-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA 98104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8629023" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Amino Acid Sequence ; Animals ; Base Sequence ; *Cell Cycle Proteins ; Culture Media ; Cyclin-Dependent Kinase Inhibitor p27 ; Cyclin-Dependent Kinases/*antagonists & inhibitors/metabolism ; Cyclins/metabolism ; Down-Regulation ; Enzyme Inhibitors/*metabolism ; Epidermal Growth Factor/pharmacology ; *G1 Phase ; Gene Expression/drug effects ; Insulin-Like Growth Factor I/pharmacology ; Mice ; Microtubule-Associated Proteins/biosynthesis/genetics/*metabolism ; Mitogens/pharmacology ; Molecular Sequence Data ; Oligonucleotides, Antisense/pharmacology ; Platelet-Derived Growth Factor/pharmacology ; Proto-Oncogene Proteins c-sis ; *Tumor Suppressor Proteins
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  • 16
    Publication Date: 1996-11-22
    Description: The Caenorhabditis elegans dauer larva is specialized for dispersal without growth and is formed under conditions of overcrowding and limited food. The daf-7 gene, required for transducing environmental cues that support continuous development with plentiful food, encodes a transforming growth factor-beta (TGF-beta) superfamily member. A daf-7 reporter construct is expressed in the ASI chemosensory neurons. Dauer-inducing pheromone inhibits daf-7 expression and promotes dauer formation, whereas food reactivates daf-7 expression and promotes recovery from the dauer state. When the food/pheromone ratio is high, the level of daf-7 mRNA peaks during the L1 larval stage, when commitment to non-dauer development is made.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ren, P -- Lim, C S -- Johnsen, R -- Albert, P S -- Pilgrim, D -- Riddle, D L -- HD11239/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 22;274(5291):1389-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Program and Division of Biological Sciences, 311 Tucker Hall, University of Missouri, Columbia, MO 65211, USA. riddle@biosci.mbp.missouri.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8910282" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Caenorhabditis elegans/genetics/*growth & development/metabolism ; *Caenorhabditis elegans Proteins ; Genes, Helminth ; Genes, Reporter ; Green Fluorescent Proteins ; Helminth Proteins/chemistry/genetics/*physiology ; Humans ; Larva/growth & development/metabolism ; Ligands ; Luminescent Proteins/genetics ; Molecular Sequence Data ; Mutation ; Neurons, Afferent/*metabolism ; Phenotype ; Pheromones/pharmacology ; Temperature ; Transforming Growth Factor beta/chemistry/genetics/*physiology ; Transgenes
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  • 17
    Publication Date: 1996-10-04
    Description: Afg3p and Rca1p are adenosine triphosphate (ATP)-dependent metalloproteases in yeast mitochondria. Cells lacking both proteins exhibit defects in respiration-dependent growth, degradation of mitochondrially synthesized proteins, and assembly of inner-membrane complexes. Defects in growth and protein assembly, but not in degradation, were suppressed by overproduction of yeast mitochondrial Lon, an ATP-dependent serine protease. Suppression by Lon was enhanced by inactivation of the proteolytic site and was prevented by mutation of the ATP-binding site. It is suggested that the mitochondrial proteases Lon, Afg3p, and Rca1p can also serve a chaperone-like function in the assembly of mitochondrial protein complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rep, M -- van Dijl, J M -- Suda, K -- Schatz, G -- Grivell, L A -- Suzuki, C K -- New York, N.Y. -- Science. 1996 Oct 4;274(5284):103-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Cell Biology, University of Amsterdam, Kruislaan 318, 1098 SM Amsterdam, The Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8810243" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Dependent Proteases ; Adenosine Triphosphatases/metabolism ; Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Base Sequence ; Binding Sites ; Electron Transport Complex IV/metabolism ; Fungal Proteins/*metabolism ; Heat-Shock Proteins/genetics/*metabolism ; Membrane Proteins/*metabolism ; *Metalloendopeptidases ; Mitochondria/*metabolism ; Mitochondrial Proteins ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Proton-Translocating ATPases/metabolism ; Saccharomyces cerevisiae/genetics/growth & development/*metabolism ; *Saccharomyces cerevisiae Proteins ; Serine Endopeptidases/genetics/*metabolism
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  • 18
    Publication Date: 1996-10-25
    Description: A cytosolic yeast karyopherin, Kap104p, was isolated and shown to function in the nuclear import of a specific class of proteins. The protein bound directly to repeat-containing nucleoporins and to a cytosolic pool of two nuclear messenger RNA (mRNA) binding proteins, Nab2p and Nab4p. Depletion of Kap104p resulted in a rapid shift of Nab2p from the nucleus to the cytoplasm without affecting the localization of other nuclear proteins tested. This finding suggests that the major function of Kap104p lies in returning mRNA binding proteins to the nucleus after mRNA export.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aitchison, J D -- Blobel, G -- Rout, M P -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):624-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA. blobel@rockvax.rockefeller.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8849456" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Biological Transport ; Carrier Proteins/chemistry/isolation & purification/*metabolism ; Cell Nucleus/*metabolism ; Cytosol/chemistry/metabolism ; Fungal Proteins/*metabolism ; *Karyopherins ; Membrane Proteins/metabolism ; Molecular Sequence Data ; Mutation ; Nuclear Envelope/metabolism ; *Nuclear Pore Complex Proteins ; Nuclear Proteins/*metabolism ; *Nucleocytoplasmic Transport Proteins ; RNA, Messenger/genetics/metabolism ; RNA-Binding Proteins/*metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/*metabolism ; *Saccharomyces cerevisiae Proteins ; Temperature ; beta Karyopherins
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  • 19
    Publication Date: 1996-02-02
    Description: Rho, a Ras-like small guanosine triphosphatase, has been implicated in cytoskeletal responses to extracellular signals such as lysophosphatidic acid (LPA) to form stress fibers and focal contacts. The form of RhoA bound to guanosine triphosphate directly bound to and activated a serine-threonine kinase, protein kinase N (PKN). Activated RhoA formed a complex with PKN and activated it in COS-7 cells. PKN was phosphorylated in Swiss 3T3 cells stimulated with LPA, and this phosphorylation was blocked by treatment of cells with botulinum C3 exoenzyme. Activation of Rho may be linked directly to a serine-threonine kinase pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Amano, M -- Mukai, H -- Ono, Y -- Chihara, K -- Matsui, T -- Hamajima, Y -- Okawa, K -- Iwamatsu, A -- Kaibuchi, K -- New York, N.Y. -- Science. 1996 Feb 2;271(5249):648-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Signal Transduction, Nara Institute of Science and Technology, Ikoma, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8571127" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; ADP Ribose Transferases/pharmacology ; Amino Acid Sequence ; Animals ; *Botulinum Toxins ; Cell Line ; Chromatography, Affinity ; Enzyme Activation ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/*metabolism ; Guanosine Triphosphate/metabolism ; Lysophospholipids/pharmacology ; Mice ; Molecular Sequence Data ; Phosphorylation ; Protein Kinase C/*metabolism ; Recombinant Fusion Proteins/metabolism ; rhoA GTP-Binding Protein
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  • 20
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-09-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thiel, B L -- Viney, C -- New York, N.Y. -- Science. 1996 Sep 13;273(5281):1480-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8801632" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Crystallization ; *Fibroins ; Magnetic Resonance Spectroscopy ; Microscopy, Electron ; Molecular Sequence Data ; Peptides/chemistry ; *Protein Structure, Secondary ; Proteins/*chemistry
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  • 21
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-06-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rosch, P -- Willbold, D -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1672.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biopolymers, University of Bayreuth, Germany. paul.rosch@uni-bayreuth.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658146" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Gene Products, tat/*chemistry ; Homeodomain Proteins/*chemistry ; Infectious Anemia Virus, Equine/*chemistry ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; Protein Structure, Secondary ; Sequence Homology, Amino Acid
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  • 22
    Publication Date: 1996-08-30
    Description: During neurogenesis in Drosophila both neurons and nonneuronal cells are produced from a population of initially equivalent cells. The kuzbanian (kuz) gene described here is essential for the partitioning of neural and nonneuronal cells during development of both the central and peripheral nervous systems in Drosophila. Mosaic analyses indicated that kuz is required for cells to receive signals inhibiting the neural fate. These analyses further revealed that the development of a neuron requires a kuz-mediated positive signal from neighboring cells. The kuz gene encodes a metalloprotease-disintegrin protein with a highly conserved bovine homolog, raising the possibility that kuz homologs may act in similar processes during mammalian neurogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rooke, J -- Pan, D -- Xu, T -- Rubin, G M -- New York, N.Y. -- Science. 1996 Aug 30;273(5279):1227-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, CT 06536, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703057" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cloning, Molecular ; Disintegrins/chemistry/genetics/*physiology ; Drosophila/cytology/embryology/*genetics/physiology ; *Drosophila Proteins ; *Genes, Insect ; Metalloendopeptidases/chemistry/genetics/*physiology ; Molecular Sequence Data ; Mosaicism ; Mutation ; Nervous System/embryology ; Neurons/*cytology ; Photoreceptor Cells, Invertebrate/cytology/embryology
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  • 23
    Publication Date: 1996-05-17
    Description: The adenomatous polyposis coli gene (APC) is mutated in familial adenomatous polyposis and in sporadic colorectal tumors, and its product binds to the adherens junction protein beta-catenin. Overexpression of APC blocks cell cycle progression. The APC-beta-catenin complex was shown to bind to DLG, the human homolog of the Drosophila discs large tumor suppressor protein. This interaction required the carboxyl-terminal region of APC and the DLG homology repeat region of DLG. APC colocalized with DLG at the lateral cytoplasm in rat colon epithelial cells and at the synapse in cultured hippocampal neurons. These results suggest that the APC-DLG complex may participate in regulation of both cell cycle progression and neuronal function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matsumine, A -- Ogai, A -- Senda, T -- Okumura, N -- Satoh, K -- Baeg, G H -- Kawahara, T -- Kobayashi, S -- Okada, M -- Toyoshima, K -- Akiyama, T -- New York, N.Y. -- Science. 1996 May 17;272(5264):1020-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Oncogene Research, Institute for Microbial Diseases, Osaka University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638125" target="_blank"〉PubMed〈/a〉
    Keywords: Adenomatous Polyposis Coli Protein ; Amino Acid Sequence ; Animals ; Cell Cycle ; Cells, Cultured ; Colon/chemistry/cytology ; Cytoskeletal Proteins/analysis/chemistry/*metabolism ; Drosophila ; *Drosophila Proteins ; Epithelial Cells ; Epithelium/chemistry ; Fluorescent Antibody Technique ; Hippocampus/chemistry/cytology ; Humans ; Insect Hormones/analysis/chemistry/*metabolism ; Mice ; Molecular Sequence Data ; Neurons/chemistry/cytology ; Protein Binding ; Recombinant Fusion Proteins/metabolism ; Synapses/chemistry ; *Trans-Activators ; *Tumor Suppressor Proteins ; beta Catenin
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  • 24
    Publication Date: 1996-04-05
    Description: Spiders produce a variety of silks that range from Lycra-like elastic fibers to Kevlar-like superfibers. A gene family from the spider Araneus diadematus was found to encode silk-forming proteins (fibroins) with different proportions of amorphous glycine-rich domains and crystal domains built from poly(alanine) and poly(glycine-alanine) repeat motifs. Spiders produce silks of different composition by gland-specific expression of this gene family, which allows for a range of mechanical properties according to the crystal-forming potential of the constituent fibroins. These principles of fiber property control may be important in the development of genetically engineered structural proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guerette, P A -- Ginzinger, D G -- Weber, B H -- Gosline, J M -- New York, N.Y. -- Science. 1996 Apr 5;272(5258):112-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of British Columbia, Vancouver, British Columbia, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8600519" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/analysis ; Animals ; Base Sequence ; Blotting, Northern ; Crystallization ; DNA, Complementary/genetics ; Exocrine Glands/*metabolism ; Fibroins/*chemistry/genetics ; Gene Expression Regulation ; Gene Library ; *Insect Proteins ; Molecular Sequence Data ; Peptides/analysis ; Proline/analysis ; Protein Structure, Secondary ; Proteins/chemistry/genetics ; *Silk ; Spiders/*chemistry/genetics
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  • 25
    Publication Date: 1996-04-05
    Description: The rotavirus nonstructural glycoprotein NSP4 is an intracellular receptor that mediates the acquisition of a transient membrane envelope as subviral particles bud into the endoplasmic reticulum. NSP4 also causes an increase in intracellular calcium in insect cells. Purified NSP4 or a peptide corresponding to NSP4 residues 114 to 135 induced diarrhea in young (6 to 10 days old) CD1 mice. This disease response was age-dependent, dose-dependent, and specific. Electrophysiologic data from intestinal mucosa showed that the NSP4 114-135 peptide potentiates chloride secretion by a calcium-dependent signaling pathway. Diarrhea is induced when NSP4, acting as a viral enterotoxin, triggers a signal transduction pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ball, J M -- Tian, P -- Zeng, C Q -- Morris, A P -- Estes, M K -- DK 30144/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1996 Apr 5;272(5258):101-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Virology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8600515" target="_blank"〉PubMed〈/a〉
    Keywords: *Aging ; Amino Acid Sequence ; Animals ; Calcium/metabolism ; Carbachol/pharmacology ; Chlorides/metabolism ; Colforsin/pharmacology ; Diarrhea/*etiology/prevention & control/virology ; Enterotoxins/*toxicity ; Glycoproteins/immunology/*toxicity ; Immune Sera/administration & dosage ; Immunization ; In Vitro Techniques ; Intestinal Mucosa/drug effects/secretion ; Mice ; Molecular Sequence Data ; Peptide Fragments/toxicity ; Receptors, Virus ; Rotavirus/*pathogenicity ; Rotavirus Infections/prevention & control/*virology ; Signal Transduction ; Toxins, Biological ; Viral Nonstructural Proteins/immunology/*toxicity
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  • 26
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-01-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1996 Jan 26;271(5248):448.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8560255" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Archaea/classification ; Bacteria/classification ; Cyanobacteria ; Enzymes/*chemistry ; *Eukaryotic Cells/classification/enzymology ; *Evolution, Molecular ; Fossils ; Phylogeny ; *Prokaryotic Cells/classification/enzymology
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  • 27
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-06-21
    Description: The human beta T cell receptor (TCR) locus, comprising a complex family of genes, has been sequenced. The locus contains two types of coding elements--TCR elements (65 variable gene segments and two clusters of diversity, joining, and constant segments) and eight trypsinogen genes --that constitute 4.6 percent of the DNA. Genome-wide interspersed repeats and locus-specific repeats span 30 and 47 percent, respectively, of the 685-kilobase sequence. A comparison of the germline variable elements with their approximately 300 complementary DNA counterparts reveals marked differential patterns of variable gene expression, the importance of exonuclease activity in generating TCR diversity, and the predominant tendency for only functional variable elements to be present in complementary DNA libraries.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rowen, L -- Koop, B F -- Hood, L -- New York, N.Y. -- Science. 1996 Jun 21;272(5269):1755-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biotechnology, University of Washington, Seattle 98195-7730, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650574" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Biological Evolution ; Chromosomes, Human, Pair 7 ; Chromosomes, Human, Pair 9 ; DNA, Complementary/genetics ; Exons ; Genetic Variation ; Humans ; Introns ; Molecular Sequence Data ; *Multigene Family ; Polymorphism, Genetic ; Promoter Regions, Genetic ; Pseudogenes ; RNA Splicing ; Receptors, Antigen, T-Cell, alpha-beta/*genetics ; Repetitive Sequences, Nucleic Acid ; Translocation, Genetic ; Trypsinogen/genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 28
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-03-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bork, P -- New York, N.Y. -- Science. 1996 Mar 8;271(5254):1431-2; author reply 1434-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596918" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing ; Amino Acid Sequence ; Animals ; DNA, Complementary ; Female ; Frameshifting, Ribosomal ; Humans ; Male ; Molecular Sequence Data ; Protein Sorting Signals/chemistry ; Protein-Tyrosine Kinases/*chemistry/genetics ; Proto-Oncogene Proteins/*chemistry/genetics ; Receptor Protein-Tyrosine Kinases/*chemistry/genetics ; Sequence Alignment ; Sperm-Ovum Interactions ; Spermatozoa/*chemistry
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 29
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-10-11
    Description: In Saccharomyces cerevisiae, MAD2 is required for mitotic arrest if the spindle assembly is perturbed. The human homolog of MAD2 was isolated and shown to be a necessary component of the mitotic checkpoint in HeLa cells by antibody electroporation experiments. Human, or Homo sapiens, MAD2 (hsMAD2) was localized at the kinetochore after chromosome condensation but was no longer observed at the kinetochore in metaphase, suggesting that MAD2 might monitor the completeness of the spindle-kinetochore attachment. Finally, T47D, a human breast tumor cell line that is sensitive to taxol and nocodazole, had reduced MAD2 expression and failed to arrest in mitosis after nocodazole treatment. Thus, defects in the mitotic checkpoint may contribute to the sensitivity of certain tumors to mitotic spindle inhibitors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Y -- Benezra, R -- P30-CA-08748/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Oct 11;274(5285):246-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Genetics Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8824189" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anaphase ; *Calcium-Binding Proteins ; Carrier Proteins/chemistry/*genetics/*metabolism ; Cell Cycle Proteins ; Electroporation ; HeLa Cells ; Humans ; Interphase ; Kinetochores/*metabolism ; Mad2 Proteins ; Metaphase ; *Mitosis ; Molecular Sequence Data ; Nocodazole/pharmacology ; Paclitaxel/pharmacology ; Repressor Proteins ; Spindle Apparatus/drug effects/*metabolism ; Tumor Cells, Cultured
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  • 30
    Publication Date: 1996-02-02
    Description: The Rho guanosine 5'-triphosphatase (GTPase) cycles between the active guanosine triphosphate (GTP)-bound form and the inactive guanosine diphosphate-bound form and regulates cell adhesion and cytokinesis, but how it exerts these actions is unknown. The yeast two-hybrid system was used to clone a complementary DNA for a protein (designated Rhophilin) that specifically bound to GTP-Rho. The Rho-binding domain of this protein has 40 percent identity with a putative regulatory domain of a protein kinase, PKN. PKN itself bound to GTP-Rho and was activated by this binding both in vitro and in vivo. This study indicates that a serine-threonine protein kinase is a Rho effector and presents an amino acid sequence motif for binding to GTP-Rho that may be shared by a family of Rho target proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Watanabe, G -- Saito, Y -- Madaule, P -- Ishizaki, T -- Fujisawa, K -- Morii, N -- Mukai, H -- Ono, Y -- Kakizuka, A -- Narumiya, S -- New York, N.Y. -- Science. 1996 Feb 2;271(5249):645-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Kyoto University Faculty of Medicine, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8571126" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Cell Line ; Cloning, Molecular ; Enzyme Activation ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/chemistry/*metabolism ; Guanosine Triphosphate/metabolism ; Humans ; Membrane Proteins/*metabolism ; Mice ; Molecular Sequence Data ; Phosphorylation ; Protein Kinase C/chemistry/*metabolism ; *Protein-Serine-Threonine Kinases ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Signal Transduction ; ras Proteins ; *rho GTP-Binding Proteins ; rhoA GTP-Binding Protein ; rhoB GTP-Binding Protein
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  • 31
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-10-25
    Description: Human leukocyte antigen (HLA)-DM is a critical participant in antigen presentation that catalyzes the release of class II-associated invariant chain-derived peptides (CLIP) from newly synthesized class II histocompatibility molecules, freeing the peptide-binding site for acquisition of antigenic peptides. The mechanism for the selective release of CLIP but not other peptides is unknown. DM was found to enhance the rate of peptide dissociation to an extent directly proportional to the intrinsic rate of peptide dissociation from HLA-DR, regardless of peptide sequence. Thus, CLIP is rapidly released in the presence of DM, because its intrinsic rate of dissociation is relatively high. In antigen presentation, DM has the potential to markedly enhance the rate of peptide exchange, favoring the presentation of peptides with slower intrinsic rates of dissociation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weber, D A -- Evavold, B D -- Jensen, P E -- AI30554/AI/NIAID NIH HHS/ -- AI33614/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):618-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology and Laboratory Medicine, Emory University School of Medicine, Atlanta, GA 30322, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8849454" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigen Presentation ; Antigens, Differentiation, B-Lymphocyte/*metabolism ; Binding Sites ; HLA-D Antigens/*metabolism ; HLA-DR Antigens/immunology/*metabolism ; Histocompatibility Antigens Class II/*metabolism ; Humans ; Kinetics ; Molecular Sequence Data ; Peptides/immunology/*metabolism ; Recombinant Fusion Proteins/metabolism
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  • 32
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-05-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, N -- New York, N.Y. -- Science. 1996 May 17;272(5264):946.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638136" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Computer Communication Networks ; Databases, Factual/*economics ; European Union ; Financing, Government ; Proteins/*chemistry ; Switzerland
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  • 33
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-11-01
    Description: The neurotransmitter functions of nitric oxide are dependent on dynamic regulation of its biosynthetic enzyme, neuronal nitric oxide synthase (nNOS). By means of a yeast two-hybrid screen, a 10-kilodalton protein was identified that physically interacts with and inhibits the activity of nNOS. This inhibitor, designated PIN, appears to be one of the most conserved proteins in nature, showing 92 percent amino acid identity with the nematode and rat homologs. Binding of PIN destabilizes the nNOS dimer, a conformation necessary for activity. These results suggest that PIN may regulate numerous biological processes through its effects on nitric oxide synthase activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jaffrey, S R -- Snyder, S H -- DA00074/DA/NIDA NIH HHS/ -- GM-07309/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 1;274(5288):774-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8864115" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry/genetics/*metabolism/pharmacology ; Cell Line ; Cyclic GMP/metabolism ; Dimerization ; *Drosophila Proteins ; Dyneins ; Enzyme Inhibitors/chemistry/*metabolism/pharmacology ; Humans ; Molecular Sequence Data ; Molecular Weight ; Neurons/enzymology ; Nitric Oxide Synthase/*antagonists & inhibitors/metabolism ; Rats ; Recombinant Fusion Proteins/metabolism/pharmacology ; Saccharomyces cerevisiae ; Transfection
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  • 34
    Publication Date: 1996-01-05
    Description: The molecular origin of the exceptional mechanical properties of spider silk is unclear. This paper presents solid-state 2H nuclear magnetic resonance data from unoriented, oriented, and supercontracted fibers, indicating that the crystalline fraction of dragline silk consists of two types of alanine-rich regions, one that is highly oriented and one that is poorly oriented and less densely packed. A new model for the molecular-level structure of individual silk molecules and their arrangement in the fibers is proposed. These data suggest that it will be necessary to control the secondary structure of individual polymer molecules in order to obtain optimum properties in bio-inspired polymers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Simmons, A H -- Michal, C A -- Jelinski, L W -- New York, N.Y. -- Science. 1996 Jan 5;271(5245):84-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Advanced Technology in Biotechnology, Cornell University, Ithaca, NY 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539605" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine/analysis ; Algorithms ; Amino Acid Sequence ; Animals ; Crystallization ; Crystallography, X-Ray ; *Fibroins ; Glycine/analysis ; *Insect Proteins ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Peptides/analysis ; Protein Conformation ; Protein Structure, Secondary ; Proteins/*chemistry ; Silk ; Spiders/*chemistry
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  • 35
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-06-14
    Description: Mitogen-activated protein kinase (MAPK) cascades, termed MAPK modules, channel extracellular signals into specific cellular responses. Chimeric molecules were constructed between p38 and p44 MAPKs, which transduce stress and growth factor signals, respectively. A discrete region of 40 residues located in the amono-terminal p38MAPK lobe directed the specificity of response to extracellular signals, whereas the p44MAPK chimera, expressed in vivo, redirected stress signals into early mitogenic responses, demonstrating the functional independence of these domains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brunet, A -- Pouyssegur, J -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1652-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre de Biochemie-CNRS, UMR134, Parc Valrose, Faculte des Sciences, Nice, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658140" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Anisomycin/pharmacology ; Binding Sites ; Calcium-Calmodulin-Dependent Protein Kinases/genetics/*metabolism ; Cell Division ; Cell Line ; Cricetinae ; Cricetulus ; Enzyme Activation ; Gene Expression Regulation ; Genes, fos ; Growth Substances/metabolism ; Mice ; Mitogen-Activated Protein Kinase 3 ; *Mitogen-Activated Protein Kinases ; Molecular Sequence Data ; Phosphorylation/drug effects ; Protein Kinases/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Recombinant Fusion Proteins/genetics/metabolism ; Ribosomal Protein S6 Kinases ; Signal Transduction ; Sorbitol/pharmacology ; Substrate Specificity ; p38 Mitogen-Activated Protein Kinases
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  • 36
    Publication Date: 1996-12-20
    Description: The human Kv1.5 potassium channel (hKv1.5) contains proline-rich sequences identical to those that bind to Src homology 3 (SH3) domains. Direct association of the Src tyrosine kinase with cloned hKv1.5 and native hKv1.5 in human myocardium was observed. This interaction was mediated by the proline-rich motif of hKv1.5 and the SH3 domain of Src. Furthermore, hKv1.5 was tyrosine phosphorylated, and the channel current was suppressed, in cells coexpressing v-Src. These results provide direct biochemical evidence for a signaling complex composed of a potassium channel and a protein tyrosine kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holmes, T C -- Fadool, D A -- Ren, R -- Levitan, I B -- F32 NS009952/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1996 Dec 20;274(5295):2089-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Volen Center for Complex Systems, Brandeis University, Waltham, MA 02254, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8953041" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Line ; Cloning, Molecular ; Humans ; Kv1.5 Potassium Channel ; Molecular Sequence Data ; Myocardium/chemistry ; Oncogene Protein pp60(v-src)/metabolism ; Patch-Clamp Techniques ; Phosphorylation ; Phosphotyrosine/metabolism ; Potassium Channels/chemistry/*metabolism ; *Potassium Channels, Voltage-Gated ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Transfection ; src Homology Domains/*physiology ; src-Family Kinases/chemistry/*metabolism
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  • 37
    Publication Date: 1996-02-23
    Description: Transmembrane signaling by bacterial chemotaxis receptors appears to require a conformational change within a receptor dimer. Dimers were engineered of the cytoplasmic domain of the Escherichia coli aspartate receptor that stimulated the kinase CheA in vitro. The folding free energy of the leucine-zipper dimerization domain was harnessed to twist the dimer interface of the receptor, which markedly affected the extent of CheA activation. Response to this twist was attenuated by modification of receptor regulatory sites, in the same manner as adaptation resets sensitivity to ligand in vivo. These results suggest that the normal allosteric activation of the chemotaxis receptor has been mimicked in a system that lacks both ligand-binding and transmembrane domains. The most stimulatory receptor dimer formed a species of tetrameric size.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cochran, A G -- Kim, P S -- T32 AI07348-07/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Feb 23;271(5252):1113-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599087" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/chemistry/*metabolism ; Chemoreceptor Cells ; Chemotaxis ; Cytoplasm/metabolism ; Enzyme Activation ; Escherichia coli/*metabolism ; *Escherichia coli Proteins ; Leucine Zippers ; Ligands ; Membrane Proteins/chemistry/*metabolism ; Methylation ; Molecular Sequence Data ; Phosphorylation ; Protein Conformation ; Protein Kinases/metabolism ; Protein Structure, Secondary ; Receptors, Amino Acid/chemistry/*metabolism ; *Receptors, Cell Surface ; Recombinant Fusion Proteins/chemistry/metabolism ; *Signal Transduction
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  • 38
    Publication Date: 1996-01-05
    Description: Developing insects repeatedly shed their cuticle by means of a stereotyped behavior called ecdysis, thought to be initiated by the brain peptide eclosion hormone. Here an ecdysis-triggering hormone, Mas-ETH, is described from the tobacco hornworm Manduca sexta. Mas-ETH contains 26 amino acids and is produced by a segmentally distributed endocrine system of epitracheal glands (EGs). The EGs undergo a marked reduction in volume, appearance, and immunohistochemical staining during ecdysis, at which time Mas-ETH is found in the hemolymph. Injection of EGs extract or synthetic Mas-ETH into pharate larvae, pupae, or adults initiates preecdysis within 2 to 10 minutes, followed by ecdysis. Sensitivity to injected Mas-ETH appears much earlier before ecdysis and occurs with shorter latency than that reported for eclosion hormone. The isolated central nervous system responds to Mas-ETH, but not to eclosion hormone, with patterned motor bursting corresponding to in vivo preecdysis and ecdysis. Mas-ETH may be an immediate blood-borne trigger for ecdysis through a direct action on the nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zitnan, D -- Kingan, T G -- Hermesman, J L -- Adams, M E -- New York, N.Y. -- Science. 1996 Jan 5;271(5245):88-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Entomology, University of California, Riverside 92521, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539606" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Central Nervous System/drug effects/physiology ; Endocrine Glands/chemistry/cytology/physiology ; Hemolymph/chemistry ; Insect Hormones/chemistry/isolation & purification/pharmacology/*physiology ; Larva/physiology ; Manduca/*chemistry/physiology ; Molecular Sequence Data ; Molecular Weight ; *Molting ; Motor Neurons/drug effects/physiology ; Peptides/chemistry/isolation & purification/pharmacology/*physiology ; Pupa/physiology
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  • 39
    Publication Date: 1996-11-22
    Description: Large macromolecular assemblies have evolved as a means of compartmentalizing reactions in organisms lacking membrane-bounded compartments. A tricorn-shaped protease was isolated from the archaeon Thermoplasma and was shown to form a multisubunit proteolytic complex. The 120-kilodalton monomer assembled to form a hexameric toroid that could assemble further into a capsid structure. Tricorn protease appeared to act as the core of a proteolytic system; when it interacted with several smaller proteins, it displayed multicatalytic activities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tamura, T -- Tamura, N -- Cejka, Z -- Hegerl, R -- Lottspeich, F -- Baumeister, W -- New York, N.Y. -- Science. 1996 Nov 22;274(5291):1385-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institute for Biochemistry, D-82152 Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8910281" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cloning, Molecular ; Cysteine Endopeptidases/metabolism ; Endopeptidases/*chemistry/genetics/isolation & purification/*metabolism ; Genes, Bacterial ; Microscopy, Electron ; Models, Molecular ; Molecular Sequence Data ; Molecular Weight ; Multienzyme Complexes/metabolism ; Peptides/metabolism ; Proteasome Endopeptidase Complex ; *Protein Conformation ; Protein Folding ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry/metabolism ; Substrate Specificity ; Thermoplasma/*enzymology
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  • 40
    Publication Date: 1996-02-16
    Description: Variants of lambda repressor and cytochrome b562 translated from messenger RNAs without stop codons were modified by carboxyl terminal addition of an ssrA-encoded peptide tag and subsequently degraded by carboxyl terminal-specific proteases present in both the cytoplasm and periplasm of Escherichia coli. The tag appears to be added to the carboxyl terminus of the nascent polypeptide chain by cotranslational switching of the ribosome from the damaged messenger RNA to ssrA RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keiler, K C -- Waller, P R -- Sauer, R T -- AI-15706/AI/NIAID NIH HHS/ -- AI-16892/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Feb 16;271(5251):990-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139-4307, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8584937" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine ; Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Codon, Terminator ; Cytochrome b Group/genetics/*metabolism ; *DNA-Binding Proteins ; Endopeptidases/metabolism ; Escherichia coli/genetics/metabolism ; *Escherichia coli Proteins ; Molecular Sequence Data ; Peptides/metabolism ; Protein Biosynthesis ; *Protein Processing, Post-Translational ; RNA, Bacterial/genetics/*metabolism ; RNA, Messenger/genetics/*metabolism ; Repressor Proteins/genetics/*metabolism ; Viral Proteins ; Viral Regulatory and Accessory Proteins
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  • 41
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-03-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taubes, G -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1493-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599100" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*metabolism ; Amino Acid Sequence ; Amyloid beta-Peptides/*chemistry/metabolism ; Amyloid beta-Protein Precursor/chemistry/genetics/metabolism ; Amyloidosis/*metabolism ; Animals ; Brain Chemistry ; Humans ; Prealbumin/chemistry/genetics ; Prion Diseases/*metabolism ; *Protein Folding
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  • 42
    Publication Date: 1996-06-28
    Description: A chloroplast RNA polymerase sigma factor is encoded by a nuclear gene, sigA, in the red alga Cyanidium caldarium RK-1. The encoded protein functions as an RNA polymerase sigma factor in vitro and it is localized to the chloroplast in vivo. SigA shows high sequence similarity to the sigma factors of cyanobacteria, which is indicative of the ancestral endosymbiotic event and subsequent transfer of the sigA gene to the nuclear genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tanaka, K -- Oikawa, K -- Ohta, N -- Kuroiwa, H -- Kuroiwa, T -- Takahashi, H -- New York, N.Y. -- Science. 1996 Jun 28;272(5270):1932-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular and Cellular Biosciences, University of Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658165" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Blotting, Southern ; Cell Nucleus/genetics ; Chloroplasts/*enzymology/genetics ; DNA-Directed RNA Polymerases/chemistry/*genetics/isolation & ; purification/metabolism ; Molecular Sequence Data ; Recombinant Proteins/isolation & purification/metabolism ; Rhodophyta/enzymology/*genetics/ultrastructure ; Sequence Alignment ; Sigma Factor/chemistry/*genetics/isolation & purification/metabolism
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  • 43
    Publication Date: 1996-07-12
    Description: The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate (GTP)-bound, active form of RhoA (GTP.RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP.RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kimura, K -- Ito, M -- Amano, M -- Chihara, K -- Fukata, Y -- Nakafuku, M -- Yamamori, B -- Feng, J -- Nakano, T -- Okawa, K -- Iwamatsu, A -- Kaibuchi, K -- New York, N.Y. -- Science. 1996 Jul 12;273(5272):245-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Signal Transduction, Nara Institute of Science and Technology, Ikoma 630-01, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662509" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Actins/metabolism ; Amino Acid Sequence ; Animals ; Cattle ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/*metabolism ; Intracellular Signaling Peptides and Proteins ; Isopropyl Thiogalactoside/pharmacology ; Mice ; Molecular Sequence Data ; Muscle Contraction ; Muscle, Smooth/physiology ; Myosin Light Chains/metabolism ; Myosin-Light-Chain Phosphatase ; Oxazoles/pharmacology ; Phosphoprotein Phosphatases/*antagonists & inhibitors/metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/*metabolism ; rho-Associated Kinases ; rhoA GTP-Binding Protein
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  • 44
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-03-15
    Description: Active transport of proteins and RNAs between the nucleus and cytoplasm is a major process in eukaryotic cells. Recently, factors that recognize transport substrates and mediate nuclear import or export have been characterized, revealing interactions that target substrates to the nuclear pore complexes, through which translocation occurs. Translocation requires energy, and for the import process this energy is at least partly consumed by the action of the small guanosine triphosphatase Ran. In the first half of the review, some of the well-established general background information on nucleocytoplasmic transport is discussed. The second half describes recent information on the mechanistic details of nuclear import and export as well as major unresolved issues such as how directionality is conferred on either import or export. The whole review is slanted toward discussion of metazoan cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gorlich, D -- Mattaj, I W -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1513-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome/Cancer Research Campaign Institute, Cambridge, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599106" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Transport, Active ; Cell Nucleus/*metabolism ; Cytoplasm/*metabolism ; GTP-Binding Proteins/metabolism ; Humans ; Karyopherins ; Molecular Sequence Data ; Nuclear Proteins/metabolism ; Protein Sorting Signals/metabolism ; Proteins/*metabolism ; RNA/*metabolism ; RNA Cap-Binding Proteins ; RNA-Binding Proteins/metabolism ; ran GTP-Binding Protein
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  • 45
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-07-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Corey, D P -- Garcia-Anoveros, J -- New York, N.Y. -- Science. 1996 Jul 19;273(5273):323-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Boston, MA 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8685718" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Caenorhabditis elegans/genetics/*physiology ; Genes, Helminth ; Helminth Proteins/chemistry/genetics/*physiology ; Molecular Sequence Data ; Muscle Contraction ; Mutation ; Phenotype ; Sensation/genetics/*physiology ; Sodium Channels/chemistry/genetics/*physiology ; Touch/genetics/physiology
    Print ISSN: 0036-8075
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  • 46
    Publication Date: 1996-07-26
    Description: B and T lymphocytes undergoing apoptosis in response to anti-immunoglobulin M antibodies and dexamethasone, respectively, were found to have increased amounts of messenger RNA for the inositol 1,4,5-trisphosphate receptor (IP3R) and increased amounts of IP3R protein. Immunohistochemical analysis revealed that the augmented receptor population was localized to the plasma membrane. Type 3 IP3R (IP3R3) was selectively increased during apoptosis, with no enhancement of type 1 IP3R (IP3R1). Expression of IP3R3 antisense constructs in S49 T cells blocked dexamethasone-induced apoptosis, whereas IP3R3 sense, IP3R1 sense, or IP3R1 antisense control constructs did not block cell death. Thus, the increases in IP3R3 may be causally related to apoptosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Khan, A A -- Soloski, M J -- Sharp, A H -- Schilling, G -- Sabatini, D M -- Li, S H -- Ross, C A -- Snyder, S H -- AI-20922/AI/NIAID NIH HHS/ -- AI-37934/AI/NIAID NIH HHS/ -- MH43040/MH/NIMH NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Jul 26;273(5274):503-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662540" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Apoptosis ; B-Lymphocytes/*cytology/metabolism ; Base Sequence ; Calcium/metabolism ; Calcium Channels/genetics/immunology/*metabolism ; Cell Line ; Cell Membrane/metabolism ; Cells, Cultured ; DNA, Antisense ; Dexamethasone/pharmacology ; Immunoblotting ; Inositol 1,4,5-Trisphosphate/*metabolism ; Inositol 1,4,5-Trisphosphate Receptors ; Mice ; Molecular Sequence Data ; Receptors, Cytoplasmic and Nuclear/genetics/immunology/*metabolism ; T-Lymphocytes/*cytology/metabolism ; Transfection ; Tumor Cells, Cultured
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  • 47
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-11-08
    Description: Mutations in the p53 tumor suppressor are among the most frequently observed genetic alterations in human cancer and map to the 200-amino acid core domain of the protein. The core domain contains the sequence-specific DNA binding activity and the in vitro 53BP2 protein binding activity of p53. The crystal structure of the p53 core domain bound to the 53BP2 protein, which contains an SH3 (Src homology 3) domain and four ankyrin repeats, revealed that (i) the SH3 domain binds the L3 loop of p53 in a manner distinct from that of previously characterized SH3-polyproline peptide complexes, and (ii) an ankyrin repeat, which forms an L-shaped structure consisting of a beta hairpin and two alpha helices, binds the L2 loop of p53. The structure of the complex shows that the 53BP2 binding site on the p53 core domain consists of evolutionarily conserved regions that are frequently mutated in cancer and that it overlaps the site of DNA binding. The six most frequently observed p53 mutations disrupt 53BP2 binding in vitro. The structure provides evidence that the 53BP2-p53 complex forms in vivo and may have a critical role in the p53 pathway of tumor suppression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gorina, S -- Pavletich, N P -- CA65698/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 8;274(5289):1001-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8875926" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Ankyrins/*chemistry ; Apoptosis Regulatory Proteins ; Binding Sites ; Carrier Proteins/*chemistry/metabolism ; Crystallography, X-Ray ; DNA/metabolism ; Humans ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Neoplasms/genetics ; Protein Binding ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry/metabolism ; Tumor Suppressor Protein p53/*chemistry/genetics/metabolism ; *src Homology Domains
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  • 48
    Publication Date: 1996-02-09
    Description: Genetic studies indicated that the Drosophila melanogaster protein REAPER (RPR) controls apoptosis during embryo development. Induction of RPR expression in Drosophila Schneider cells rapidly stimulated apoptosis. RPR-mediated apoptosis was blocked by N-benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone (Z-VAD-fmk), which suggests that an interleukin-1 beta converting enzyme (ICE)-like protease is required for RPR function. RPR-induced apoptosis was associated with increased ceramide production that was also blocked by Z-VAD-fmk, which suggests that ceramide generation requires an ICE-like protease as well. Thus, the intracellular RPR protein uses cell death signaling pathways similar to those used by the vertebrate transmembrane receptors Fas (CD95) and tumor necrosis factor receptor type 1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pronk, G J -- Ramer, K -- Amiri, P -- Williams, L T -- New York, N.Y. -- Science. 1996 Feb 9;271(5250):808-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chiron Corporation, Emeryville, CA 94608, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8628997" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Chloromethyl Ketones/pharmacology ; Amino Acid Sequence ; Animals ; *Apoptosis/drug effects ; Caspase 1 ; Cell Line ; Ceramides/*metabolism/pharmacology ; Copper/pharmacology ; Copper Sulfate ; Cysteine Endopeptidases/*metabolism ; *Drosophila Proteins ; Drosophila melanogaster/*cytology/embryology/genetics/metabolism ; Enzyme Activation ; Gene Expression ; Molecular Sequence Data ; Peptides/genetics/*physiology ; Protease Inhibitors/pharmacology ; Signal Transduction ; Transfection
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  • 49
    Publication Date: 1996-08-30
    Description: Pycnodysostosis, an autosomal recessive osteochondrodysplasia characterized by osteosclerosis and short stature, maps to chromosome 1q21. Cathepsin K, a cysteine protease gene that is highly expressed in osteoclasts, localized to the pycnodysostosis region. Nonsense, missense, and stop codon mutations in the gene encoding cathepsin K were identified in patients. Transient expression of complementary DNA containing the stop codon mutation resulted in messenger RNA but no immunologically detectable protein. Thus, pycnodysostosis results from gene defects in a lysosomal protease with highest expression in osteoclasts. These findings suggest that cathepsin K is a major protease in bone resorption, providing a possible rationale for the treatment of disorders such as osteoporosis and certain forms of arthritis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gelb, B D -- Shi, G P -- Chapman, H A -- Desnick, R J -- R01 DK31775/DK/NIDDK NIH HHS/ -- R01 HL44816/HL/NHLBI NIH HHS/ -- R37 DK34045/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Aug 30;273(5279):1236-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Human Genetics and Division of Pediatric Cardiology, Mount Sinai School of Medicine, New York, NY 10029, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703060" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Bone Matrix/metabolism ; Bone Resorption ; Cathepsin K ; Cathepsins/deficiency/*genetics/metabolism ; Chromosome Mapping ; Chromosomes, Human, Pair 1 ; Codon, Terminator ; Dinucleoside Phosphates/genetics ; Humans ; Lysosomal Storage Diseases/enzymology/*genetics ; Lysosomes/*enzymology ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutation ; Osteochondrodysplasias/enzymology/*genetics ; Osteoclasts/*enzymology ; Transfection
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  • 50
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-11-08
    Description: Although cytokinin plays a central role in plant development, little is known about cytokinin signal transduction. Five Arabidopsis thaliana mutants that exhibit typical cytokinin responses, including rapid cell division and shoot formation in tissue culture in the absence of exogenous cytokinin, were isolated by activation transferred DNA tagging. A gene, CKI1, which was tagged in four of the five mutants and induced typical cytokinin responses after introduction and overexpression in plants, was cloned. CKI1 encodes a protein similar to the two-component regulators. These results suggest that CKI1 is involved in cytokinin signal transduction, possibly as a cytokinin receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kakimoto, T -- New York, N.Y. -- Science. 1996 Nov 8;274(5289):982-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8875940" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/genetics/*physiology ; *Arabidopsis Proteins ; Cloning, Molecular ; Cytokinins/pharmacology/*physiology ; DNA, Bacterial/genetics ; DNA, Complementary/genetics ; DNA, Plant/genetics ; Ethylenes/metabolism ; Genes, Plant ; Molecular Sequence Data ; Mutation ; Open Reading Frames ; Plant Proteins/chemistry/metabolism ; Polymorphism, Restriction Fragment Length ; Protein Kinases/chemistry/genetics/*physiology ; *Receptors, Cell Surface ; Sequence Homology, Amino Acid ; *Signal Transduction ; Transformation, Genetic
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  • 51
    Publication Date: 1996-05-31
    Description: A second gene for autosomal dominant polycystic kidney disease was identified by positional cloning. Nonsense mutations in this gene (PKD2) segregated with the disease in three PKD2 families. The predicted 968-amino acid sequence of the PKD2 gene product has six transmembrane spans with intracellular amino- and carboxyl-termini. The PKD2 protein has amino acid similarity with PKD1, the Caenorhabditis elegans homolog of PKD1, and the family of voltage-activated calcium (and sodium) channels, and it contains a potential calcium-binding domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mochizuki, T -- Wu, G -- Hayashi, T -- Xenophontos, S L -- Veldhuisen, B -- Saris, J J -- Reynolds, D M -- Cai, Y -- Gabow, P A -- Pierides, A -- Kimberling, W J -- Breuning, M H -- Deltas, C C -- Peters, D J -- Somlo, S -- DK02015/DK/NIDDK NIH HHS/ -- DK48383/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1996 May 31;272(5266):1339-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Renal Division, Department of Medicine and Molecular Genetics, Albert Einstein College of Medicine, Bronx, NY 10461, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650545" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Caenorhabditis elegans/chemistry/genetics ; Calcium Channels/chemistry/genetics ; Chromosome Mapping ; Chromosomes, Human, Pair 4 ; Cloning, Molecular ; Consensus Sequence ; Crystallography, X-Ray ; Female ; Glycosylation ; Humans ; Male ; Membrane Proteins/chemistry/*genetics/physiology ; Molecular Sequence Data ; Mutation ; Pedigree ; Phenotype ; Polycystic Kidney, Autosomal Dominant/*genetics ; Polymorphism, Single-Stranded Conformational ; Proteins/chemistry/genetics ; Sodium Channels/chemistry/genetics ; TRPP Cation Channels
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  • 52
    Publication Date: 1996-09-20
    Description: Members of a previously unidentified family of potassium channel subunits were cloned from rat and human brain. The messenger RNAs encoding these subunits were widely expressed in brain with distinct yet overlapping patterns, as well as in several peripheral tissues. Expression of the messenger RNAs in Xenopus oocytes resulted in calcium-activated, voltage-independent potassium channels. The channels that formed from the various subunits displayed differential sensitivity to apamin and tubocurare. The distribution, function, and pharmacology of these channels are consistent with the SK class of small-conductance, calcium-activated potassium channels, which contribute to the afterhyperpolarization in central neurons and other cell types.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kohler, M -- Hirschberg, B -- Bond, C T -- Kinzie, J M -- Marrion, N V -- Maylie, J -- Adelman, J P -- New York, N.Y. -- Science. 1996 Sep 20;273(5282):1709-14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute, L-474, Oregon Health Sciences University, 3181 Southwest Sam Jackson Road, Portland, OR 97201, USA. J. Maylie, Department of Obstetrics and Gyne.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8781233" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antisense Elements (Genetics) ; Apamin/pharmacology ; *Brain Chemistry ; Calcium/*metabolism/pharmacology ; Cloning, Molecular ; Electric Conductivity ; Female ; Humans ; Membrane Potentials ; Molecular Sequence Data ; Neurons/*physiology ; Oocytes ; Patch-Clamp Techniques ; Potassium/metabolism ; Potassium Channel Blockers ; Potassium Channels/analysis/chemistry/*physiology ; *Potassium Channels, Calcium-Activated ; RNA, Messenger/analysis/genetics ; Rats ; Rats, Sprague-Dawley ; Small-Conductance Calcium-Activated Potassium Channels ; Xenopus
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  • 53
    Publication Date: 1996-02-09
    Description: Poikilothermic animals respond to chronic cold by increasing phosphoglyceride unsaturation to restore the fluidity of cold-rigidified membranes. Despite the importance of this compensatory response, the enzymes involved have not been clearly identified, and the mechanisms that control their activity are unknown. In carp liver, cold induces an 8- to 10-fold increase in specific activity of the microsomal stearoyl coenzyme A desaturase. Cold-induced up-regulation of gene transcription resulted in a 10-fold increase in desaturase transcript amounts after 48 to 60 hours. However, this increase was preceded by the activation of latent desaturase, probably by a posttranslational mechanism. These two mechanisms may act sequentially to match desaturase expression to the demands imposed by a progressive decrease in temperature.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tiku, P E -- Gracey, A Y -- Macartney, A I -- Beynon, R J -- Cossins, A R -- New York, N.Y. -- Science. 1996 Feb 9;271(5250):815-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Environmental and Evolutionary Biology, University of Liverpool, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8629000" target="_blank"〉PubMed〈/a〉
    Keywords: Acclimatization ; Amino Acid Sequence ; Animals ; Antisense Elements (Genetics) ; Carps/*metabolism ; Cloning, Molecular ; Cold Temperature ; Enzyme Activation ; Microsomes, Liver/*enzymology ; Molecular Sequence Data ; Protein Processing, Post-Translational ; RNA, Messenger/genetics/metabolism ; Stearoyl-CoA Desaturase/*biosynthesis/genetics/*metabolism ; *Transcription, Genetic ; Up-Regulation
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  • 54
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-01-12
    Description: The digestive vacuole of Plasmodium falciparum is the site of hemoglobin degradation, heme polymerization into crystalline hemozoin, and antimalarial drug accumulation. Antibodies identified histidine-rich protein II (HRP II) in purified digestive vacuoles. Recombinant or native HRP II promoted the formation of hemozoin, and chloroquine inhibited the reaction. The related HRP III also polymerized heme, and an additional HRP was identified in vacuoles. It is proposed that after secretion by the parasite into the host erythrocyte cytosol, HRPs are brought into the acidic digestive vacuole along with hemoglobin. After hemoglobin proteolysis, HRPs bind the liberated heme and mediate hemozoin formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sullivan, D J Jr -- Gluzman, I Y -- Goldberg, D E -- AI-31615/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 12;271(5246):219-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Medicine, Washington University School of Medicine, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539625" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Fluorescent Antibody Technique, Indirect ; Heme/metabolism ; Hemeproteins/*biosynthesis ; Hemoglobins/metabolism ; Immunoblotting ; Molecular Sequence Data ; Plasmodium falciparum/*metabolism ; Proteins/chemistry/*metabolism ; Protozoan Proteins/chemistry/*metabolism ; Recombinant Proteins/metabolism ; Vacuoles/metabolism
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  • 55
    Publication Date: 1996-03-29
    Description: In Drosophila, the Wingless and Notch signaling pathways function in m any of the same developmental patterning events. Genetic analysis demonstrates that the dishevelled gene, which encodes a molecule previously implicated in implementation of the Winglass signal, interacts antagonistically with Notch and one of its known ligands, Delta. A direct physical interaction between Dishevelled and the Notch carboxyl terminus, distal to the cdc10/ankyrin repeats, suggests a mechanism for this interaction. It is proposed that Dishevelled, in addition to transducing the Wingless signal, blocks Notch signaling directly, thus providing a molecular mechanism for the inhibitory cross talk observed between these pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Axelrod, J D -- Matsuno, K -- Artavanis-Tsakonas, S -- Perrimon, N -- New York, N.Y. -- Science. 1996 Mar 29;271(5257):1826-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596950" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Clone Cells ; Drosophila/genetics/growth & development/*metabolism ; *Drosophila Proteins ; Genes, Insect ; Intracellular Signaling Peptides and Proteins ; Membrane Proteins/antagonists & inhibitors/genetics/*metabolism ; Molecular Sequence Data ; Mutation ; Phenotype ; *Phosphoproteins ; Proteins/genetics/*metabolism ; Proto-Oncogene Proteins/genetics/*metabolism ; Pupa/metabolism ; Receptors, Notch ; *Signal Transduction ; Wings, Animal/cytology/growth & development ; Wnt1 Protein
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  • 56
    Publication Date: 1996-03-29
    Description: Upon contacting its postsynaptic target, a neuronal growth cone transforms into a presynaptic terminal. A membrane component on the growth cone that facilitates synapse formation was identified by means of a complementary DNA-based screen followed by genetic analysis. The late bloomer (lbl) gene in Drosophila encodes a member of the tetraspanin family of cell surface proteins. LBL protein is transiently expressed on motor axons, growth cones, and terminal arbors. In lbl mutant embryos, the growth cone of the RP3 motoneuron contacts its target muscles, but synapse formation is delayed and neighboring motoneurons display an increase in ectopic sprouting.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kopczynski, C C -- Davis, G W -- Goodman, C S -- New York, N.Y. -- Science. 1996 Mar 29;271(5257):1867-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, Berkeley 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596956" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Axons/metabolism/ultrastructure ; Cloning, Molecular ; Drosophila/embryology/genetics/physiology ; *Drosophila Proteins ; *Genes, Insect ; Membrane Proteins/chemistry/genetics/*physiology ; Molecular Sequence Data ; Motor Neurons/cytology/metabolism/*physiology ; Muscles/innervation ; Mutation ; Nerve Tissue Proteins/chemistry/genetics/*physiology ; Neuromuscular Junction/*physiology ; Presynaptic Terminals/*physiology/ultrastructure ; Signal Transduction
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  • 57
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-05-31
    Description: The T cytoplasm of maize serves as a model for the nuclear restoration of cytoplasmic male sterility. The rf2 gene, one of two nuclear genes required for fertility restoration in male-sterile T-cytoplasm (cmsT) maize, was cloned. The protein predicted by the rf2 sequence is a putative aldehyde dehydrogenase, which suggests several mechanisms that might explain Rf2-mediated fertility restoration in cmsT maize. Aldehyde dehydrogenase may be involved in the detoxification of acetaldehyde produced by ethanolic fermentation during pollen development, may play a role in energy metabolism, or may interact with URF13, the mitochondrial protein associated with male sterility in cmsT maize.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cui, X -- Wise, R P -- Schnable, P S -- New York, N.Y. -- Science. 1996 May 31;272(5266):1334-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology and Genetics, Iowa State University, Ames, 50011, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650543" target="_blank"〉PubMed〈/a〉
    Keywords: Acetaldehyde/metabolism ; Aldehyde Dehydrogenase/chemistry/*genetics/metabolism ; Alleles ; Amino Acid Sequence ; Cell Nucleus ; Cloning, Molecular ; Crosses, Genetic ; Cytoplasm/genetics/physiology ; Energy Metabolism ; *Genes, Plant ; Intracellular Membranes/metabolism ; Mitochondria/genetics/metabolism ; *Mitochondrial Proteins ; Molecular Sequence Data ; Nuclear Proteins/chemistry/*genetics/metabolism ; Plant Proteins/genetics/metabolism ; Pollen/physiology ; Zea mays/*genetics/*physiology
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  • 58
    Publication Date: 1996-05-24
    Description: The crystal structure of bovine heart cytochrome c oxidase at 2.8 A resolution with an R value of 19.9 percent reveals 13 subunits, each different from the other, five phosphatidyl ethanolamines, three phosphatidyl glycerols and two cholates, two hemes A, and three copper, one magnesium, and one zinc. Of 3606 amino acid residues in the dimer, 3560 have been converged to a reasonable structure by refinement. A hydrogen-bonded system, including a propionate of a heme A (heme a), part of peptide backbone, and an imidazole ligand of CuA, could provide an electron transfer pathway between CuA and heme a. Two possible proton pathways for pumping, each spanning from the matrix to the cytosolic surfaces, were identified, including hydrogen bonds, internal cavities likely to contain water molecules, and structures that could form hydrogen bonds with small possible conformational change of amino acid side chains. Possible channels for chemical protons to produce H2O, for removing the produced water, and for O2, respectively, were identified.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tsukihara, T -- Aoyama, H -- Yamashita, E -- Tomizaki, T -- Yamaguchi, H -- Shinzawa-Itoh, K -- Nakashima, R -- Yaono, R -- Yoshikawa, S -- New York, N.Y. -- Science. 1996 May 24;272(5265):1136-44.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Protein Research, Osaka University, Suita, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638158" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cattle ; Cell Nucleus/genetics ; Copper/analysis ; Crystallography, X-Ray ; Electron Transport ; Electron Transport Complex IV/*chemistry/genetics/metabolism ; Heme/analogs & derivatives/analysis ; Hydrogen Bonding ; Iron/analysis ; Membrane Proteins/chemistry ; Mitochondria, Heart/genetics ; Models, Molecular ; Molecular Sequence Data ; Molecular Weight ; Myocardium/enzymology ; Nucleotides/metabolism ; Oxidation-Reduction ; Oxygen/metabolism ; Phospholipids/analysis ; *Protein Conformation ; Protein Structure, Secondary ; Proton Pumps ; Water/metabolism
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  • 59
    Publication Date: 1996-01-19
    Description: About 90 percent of human pancreatic carcinomas show allelic loss at chromosome 18q. To identify candidate tumor suppressor genes on 18q, a panel of pancreatic carcinomas were analyzed for convergent sites of homozygous deletion. Twenty-five of 84 tumors had homozygous deletions at 18q21.1, a site that excludes DCC (a candidate suppressor gene for colorectal cancer) and includes DPC4, a gene similar in sequence to a Drosophila melanogaster gene (Mad) implicated in a transforming growth factor-beta (TGF-beta)-like signaling pathway. Potentially inactivating mutations in DPC4 were identified in six of 27 pancreatic carcinomas that did not have homozygous deletions at 18q21.1. These results identify DPC4 as a candidate tumor suppressor gene whose inactivation may play a role in pancreatic and possibly other human cancers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hahn, S A -- Schutte, M -- Hoque, A T -- Moskaluk, C A -- da Costa, L T -- Rozenblum, E -- Weinstein, C L -- Fischer, A -- Yeo, C J -- Hruban, R H -- Kern, S E -- CA62924/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 19;271(5247):350-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8553070" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Division ; Chromosome Mapping ; *Chromosomes, Human, Pair 18 ; *DNA-Binding Proteins ; Gene Deletion ; Gene Expression ; *Genes, Tumor Suppressor ; Genetic Markers ; Humans ; Mice ; Molecular Sequence Data ; Mutation ; Neoplasm Transplantation ; Pancreatic Neoplasms/*genetics/pathology ; Proteins/chemistry/*genetics/physiology ; Signal Transduction ; Smad4 Protein ; *Trans-Activators ; Transforming Growth Factor beta/physiology ; Transplantation, Heterologous ; Tumor Cells, Cultured
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  • 60
    Publication Date: 1996-03-15
    Description: Cyclins regulate the major cell cycle transitions in eukaryotes through association with cyclin-dependent protein kinases (CDKs). In yeast, G1 cyclins are essential, rate-limiting activators of cell cycle initiation. G1-specific accumulation of one G1 cyclin, Cln2, results from periodic gene expression coupled with rapid protein turnover. Site-directed mutagenesis of CLN2 revealed that its phosphorylation provides a signal that promotes rapid degradation. Cln2 phosphorylation is dependent on the Cdc28 protein kinase, the CDK that it activates. These findings suggest that Cln2 is rendered self-limiting by virtue of its ability to activate its cognate CDK subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lanker, S -- Valdivieso, M H -- Wittenberg, C -- GM43487/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1597-601.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599119" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; CDC28 Protein Kinase, S cerevisiae/*metabolism ; Cyclins/genetics/*metabolism ; Enzyme Activation ; Fungal Proteins/genetics/metabolism ; *G1 Phase ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutation ; Phenotype ; Phosphorylation ; Saccharomyces cerevisiae/cytology/metabolism ; Saccharomyces cerevisiae Proteins
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  • 61
    Publication Date: 1996-04-26
    Description: Hox genes regulate patterning during limb development. It is believed that they function in the determination of the timing and extent of local growth rates. Here, it is demonstrated that synpolydactyly, an inherited human abnormality of the hands and feet, is caused by expansions of a polyalanine stretch in the amino-terminal region of HOXD13. The homozygous phenotype includes the transformation of metacarpal and metatarsal bones to short carpal- and tarsal-like bones. The mutations identify the polyalanine stretch outside of the DNA binding domain of HOXD13 as a region necessary for proper protein function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Muragaki, Y -- Mundlos, S -- Upton, J -- Olsen, B R -- AR36819/AR/NIAMS NIH HHS/ -- AR36820/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Apr 26;272(5261):548-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614804" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Chromosome Mapping ; Chromosomes, Human, Pair 2 ; Cloning, Molecular ; Female ; Fingers/*abnormalities/embryology ; *Genes, Homeobox ; Genetic Linkage ; Homeodomain Proteins/chemistry/*genetics/physiology ; Humans ; Male ; Molecular Sequence Data ; Morphogenesis ; Multigene Family ; Mutation ; Pedigree ; Peptides/chemistry ; Polydactyly/embryology/*genetics/radiography ; Polymerase Chain Reaction ; Syndactyly/embryology/*genetics/radiography ; Toes/*abnormalities/embryology ; *Transcription Factors
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  • 62
    Publication Date: 1996-06-28
    Description: Homozygous weaver mice are profoundly ataxic because of the loss of granule cell neurons during cerebellar development. This granule cell loss appears to be caused by a genetic defect in the pore region (Gly156--〉Ser) of the heterotrimeric guanine nucleotide-binding protein (G protein)-gated inwardly rectifying potassium (K+) channel subunit (GIRK2). A related subunit, GIRK1, associates with GIRK2 to constitute a neuronal G protein-gated inward rectifier K+ channel. The weaver allele of the GIRK2 subunit (wvGIRK2) caused loss of K+ selectivity when expressed either as wvGIRK2 homomultimers or as GIRK1-wvGIRK2 heteromultimers. The mutation also let to loss of sensitivity to G protein betagamma dimers. Expression of wvGIRK2 subunits let to increased cell death, presumably as a result of basal nonselective channel opening.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Navarro, B -- Kennedy, M E -- Velimirovic, B -- Bhat, D -- Peterson, A S -- Clapham, D E -- New York, N.Y. -- Science. 1996 Jun 28;272(5270):1950-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Mayo Foundation, Rochester, Minnesota 55905, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658170" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antisense Elements (Genetics) ; CHO Cells ; Cell Death ; Cell Line ; Cerebellum/cytology/*metabolism ; Cricetinae ; G Protein-Coupled Inwardly-Rectifying Potassium Channels ; GTP-Binding Proteins/*physiology ; Membrane Potentials ; Mice ; Mice, Neurologic Mutants ; Molecular Sequence Data ; Neurons/cytology/metabolism ; Oocytes/cytology ; Patch-Clamp Techniques ; Point Mutation ; Potassium Channels/genetics/*metabolism ; *Potassium Channels, Inwardly Rectifying ; Transfection
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  • 63
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-01-26
    Description: Two apoptosis-linked genes, named ALG-2 and ALG-3, were identified by means of a functional selection strategy. ALG-2 codes for a Ca(2+)-binding protein required for T cell receptor-, Fas-, and glucocorticoid-induced cell death. ALG-3, a partial complementary DNA that is homologous to the familial Alzheimer's disease gene STM2, rescues a T cell hybridoma from T cell receptor- and Fas-induced apoptosis. These findings suggest that ALG-2 may mediate Ca(2+)-regulated signals along the death pathway and that cell death may play a role in Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vito, P -- Lacana, E -- D'Adamio, L -- New York, N.Y. -- Science. 1996 Jan 26;271(5248):521-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉T Cell Molecular Biology Unit, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8560270" target="_blank"〉PubMed〈/a〉
    Keywords: Alkaloids/pharmacology ; Alzheimer Disease/*genetics ; Amino Acid Sequence ; Animals ; Antigens, CD95/metabolism ; *Apoptosis/drug effects ; Apoptosis Regulatory Proteins ; Calcium/metabolism ; Calcium-Binding Proteins/chemistry/genetics/*physiology ; Cell Line ; Cloning, Molecular ; DNA, Complementary ; Dactinomycin/pharmacology ; Dexamethasone/pharmacology ; Fas Ligand Protein ; Hybridomas ; Interleukin-2/metabolism ; Membrane Glycoproteins/metabolism ; Membrane Proteins/chemistry/genetics/*physiology ; Mice ; Molecular Sequence Data ; Presenilin-2 ; Receptors, Antigen, T-Cell/physiology ; Signal Transduction ; Staurosporine ; T-Lymphocytes ; Transfection ; Up-Regulation
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  • 64
    Publication Date: 1996-09-13
    Description: The solution structure of a human immunodeficiency virus type-1 (HIV-1) Rev peptide bound to stem-loop IIB of the Rev response element (RRE) RNA was solved by nuclear magnetic resonance spectroscopy. The Rev peptide has an alpha-helical conformation and binds in the major groove of the RNA near a purine-rich internal loop. Several arginine side chains make base-specific contacts, and an asparagine residue contacts a G.A base pair. The phosphate backbone adjacent to a G.G base pair adopts an unusual structure that allows the peptide to access a widened major groove. The structure formed by the two purine-purine base pairs of the RRE creates a distinctive binding pocket that the peptide can use for specific recognition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Battiste, J L -- Mao, H -- Rao, N S -- Tan, R -- Muhandiram, D R -- Kay, L E -- Frankel, A D -- Williamson, J R -- GM-08344/GM/NIGMS NIH HHS/ -- GM-39589/GM/NIGMS NIH HHS/ -- GM-53320/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Sep 13;273(5281):1547-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703216" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arginine/chemistry ; Asparagine/chemistry ; Base Composition ; Base Sequence ; *DNA-Binding Proteins ; Fungal Proteins/chemistry ; Gene Products, rev/*chemistry/*metabolism ; *Genes, env ; HIV-1/*chemistry ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Protein Kinases/chemistry ; *Protein Structure, Secondary ; RNA, Viral/*chemistry/genetics/metabolism ; *Saccharomyces cerevisiae Proteins ; Threonine/chemistry ; rev Gene Products, Human Immunodeficiency Virus
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  • 65
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-12-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hasegawa, M -- Fitch, W M -- New York, N.Y. -- Science. 1996 Dec 6;274(5293):1750; author reply 1751-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8984636" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Evolution, Molecular ; Models, Statistical ; Mutation ; Proteins/*chemistry/genetics
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  • 66
    Publication Date: 1996-07-19
    Description: Vaccination with naked DNA elicits cellular and humoral immune responses that have a T helper cell type 1 bias. However, plasmid vectors expressing large amounts of gene product do not necessarily induce immune responses to the encoded antigens. Instead, the immunogenicity of plasmid DNA (pDNA) requires short immunostimulatory DNA sequences (ISS) that contain a CpG dinucleotide in a particular base context. Human monocytes transfected with pDNA or double-stranded oligonucleotides containing the ISS, but not those transfected with ISS-deficient pDNA or oligonucleotides, transcribed large amounts of interferon-alpha, interferon-beta, and interleukin-12. Although ISS are necessary for gene vaccination, they down-regulate gene expression and thus may interfere with gene replacement therapy by inducing proinflammatory cytokines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sato, Y -- Roman, M -- Tighe, H -- Lee, D -- Corr, M -- Nguyen, M D -- Silverman, G J -- Lotz, M -- Carson, D A -- Raz, E -- AI36214/AI/NIAID NIH HHS/ -- AI37305/AI/NIAID NIH HHS/ -- AR41897/AR/NIAMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Jul 19;273(5273):352-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine and The Sam and Rose Stein Institute for Research on Aging, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0663, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662521" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Ampicillin Resistance/*genetics ; Animals ; *Antibody Formation ; Base Sequence ; CpG Islands ; Cytokines/*biosynthesis ; DNA/chemistry/genetics/*immunology ; Female ; Gene Expression Regulation ; Genetic Vectors ; Humans ; Injections, Intradermal ; Interferons/biosynthesis ; Interleukin-12/biosynthesis ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Monocytes/immunology ; Plasmids/genetics/*immunology ; Th1 Cells/immunology ; Transfection ; *Vaccination ; beta-Galactosidase/*immunology
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  • 67
    Publication Date: 1996-09-06
    Description: The maize crinkly4 (cr4) mutation affects leaf epidermis differentiation such that cell size and morphology are altered, and surface functions are compromised, allowing graft-like fusions between organs. In the seed, loss of cr4 inhibits aleurone formation in a pattern that reflects the normal progression of differentiation over the developing endosperm surface. The cr4 gene was isolated by transposon tagging and found to encode a putative receptor kinase. The extracellular domain contains a cysteine-rich region similar to the ligand binding domain in mammalian tumor necrosis factor receptors (TNFRs) and seven copies of a previously unknown 39-amino acid repeat. The results suggest a role for cr4 in a differentiation signal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Becraft, P W -- Stinard, P S -- McCarty, D R -- New York, N.Y. -- Science. 1996 Sep 6;273(5280):1406-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, Iowa State University, Ames, IA 50011, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703079" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Differentiation ; Cloning, Molecular ; DNA Transposable Elements ; Genes, Plant ; Molecular Sequence Data ; Mutagenesis ; Phenotype ; Plant Leaves/cytology ; *Plant Proteins ; Protein Kinases/chemistry/genetics/*physiology ; Protein-Serine-Threonine Kinases/chemistry ; Receptors, Tumor Necrosis Factor/chemistry ; Seeds/cytology ; Zea mays/chemistry/*cytology/genetics/growth & development
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  • 68
    Publication Date: 1996-01-26
    Description: Amino acid sequence data from 57 different enzymes were used to determine the divergence times of the major biological groupings. Deuterostomes and protostomes split about 670 million years ago and plants, animals, and fungi last shared a common ancestor about a billion years ago. With regard to these protein sequences, plants are slightly more similar to animals than are the fungi. In contrast, phylogenetic analysis of the same sequences indicates that fungi and animals shared a common ancestor more recently than either did with plants, the greater difference resulting from the fungal lineage changing faster than the animal and plant lines over the last 965 million years. The major protist lineages have been changing at a somewhat faster rate than other eukaryotes and split off about 1230 million years ago. If the rate of change has been approximately constant, then prokaryotes and eukaryotes last shared a common ancestor about 2 billion years ago, archaebacterial sequences being measurably more similar to eukaryotic ones than are eubacterial ones.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doolittle, R F -- Feng, D F -- Tsang, S -- Cho, G -- Little, E -- HL-26873/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 26;271(5248):470-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular Genetics University of California, San Diego, La Jolla 92093-0634, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8560259" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Archaea/classification/enzymology ; Bacteria/classification/enzymology ; Cyanobacteria/classification/enzymology ; Enzymes/*chemistry ; *Eukaryotic Cells/classification/enzymology ; *Evolution, Molecular ; Fossils ; Fungi/classification/enzymology ; Humans ; Phylogeny ; Plants/classification/enzymology ; *Prokaryotic Cells/classification/enzymology ; Sequence Alignment
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  • 69
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-05-10
    Description: The molecular structure of the Escherichia coli RecA protein in the absence of DNA revealed two disordered or mobile loops that were proposed to be DNA binding sites. A short peptide spanning one of these loops was shown to carry out the key reaction mediated by the whole RecA protein: pairing (targeting) of a single-stranded DNA to its homologous site on a duplex DNA. In the course of the reaction the peptide bound to both substrate DNAs, unstacked the single-stranded DNA, and assumed a beta structure. These events probably recapitulate the underlying molecular pathway or mechanism used by homologous recombination proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Voloshin, O N -- Wang, L -- Camerini-Otero, R D -- New York, N.Y. -- Science. 1996 May 10;272(5263):868-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-1810, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8629021" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; DNA, Single-Stranded/chemistry/genetics/*metabolism ; DNA, Superhelical/chemistry/genetics/*metabolism ; DNA-Binding Proteins/chemistry/metabolism ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/chemistry/metabolism ; Peptide Fragments/chemistry/*metabolism ; Protein Conformation ; Protein Structure, Secondary ; Rec A Recombinases/chemistry/*metabolism ; *Recombination, Genetic
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  • 70
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-03-15
    Description: Most major systems that transport proteins across a membrane share the following features: an amino-terminal transient signal sequence on the transported protein, a targeting system on the cis side of the membrane, a hetero-oligomeric transmembrane channel that is gated both across and within the plane of the membrane, a peripherally attached protein translocation motor that is powered by the hydrolysis of nucleoside triphosphate, and a protein folding system on the trans side of the membrane. These transport systems are divided into two families: export systems that export proteins out of the cytosol, and import systems that transport proteins into cytosol-like compartments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schatz, G -- Dobberstein, B -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1519-26.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biozentrum der Universitat Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599107" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacteria/metabolism ; Biological Transport ; Cell Membrane/*metabolism ; Chloroplasts/metabolism ; Cytosol/metabolism ; Endoplasmic Reticulum/metabolism ; GTP Phosphohydrolases/metabolism ; Intracellular Membranes/*metabolism ; Membrane Proteins/metabolism ; Microbodies/metabolism ; Mitochondria/metabolism ; Molecular Chaperones/metabolism ; Molecular Sequence Data ; Protein Folding ; Protein Sorting Signals/metabolism ; Proteins/*metabolism
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  • 71
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-03-29
    Description: Cell cycle phase transitions in eukaryotic cells are driven by regulation of the activity of protein kinases known as cyclin-dependent kinases (Cdks). A broad spectrum of Cdk-inhibitory activity associated with a 28-kilodalton protein (p28lck1) was induced in cells treated with the drug lovastatin or upon density-mediated growth arrest and was periodic in the cell cycle, with peak activity in G1. The p28lck1 protein was shown to be identical to p27Kip1, and the periodic or induced inhibitory activity resulted from a periodic accumulation of the protein. Variations in the amount of p27 protein occurred, whereas the abundance of the p27 messenger RNA remained unchanged. In every instance investigated, the posttranscriptional alteration of p27 protein levels was achieved in part by a mechanism of translational control, although in density-arrested fibroblasts and thymidine-arrested HeLa cells the half-life of the protein was also changed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hengst, L -- Reed, S I -- GM46006/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Mar 29;271(5257):1861-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596954" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Cell Cycle ; *Cell Cycle Proteins ; Cell Line ; Cyclin-Dependent Kinase Inhibitor p27 ; Cyclin-Dependent Kinases/*antagonists & inhibitors ; Enzyme Inhibitors/metabolism ; G1 Phase ; Half-Life ; HeLa Cells ; Humans ; Lovastatin/pharmacology ; Microtubule-Associated Proteins/*biosynthesis/genetics/metabolism ; Molecular Sequence Data ; Protein Biosynthesis ; RNA, Messenger/genetics/metabolism ; S Phase ; Tumor Cells, Cultured ; *Tumor Suppressor Proteins
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  • 72
    Publication Date: 1996-06-14
    Description: The molybdoenzyme dimethylsulfoxide (DMSO) reductase contributes to the release of dimethylsulfide, a compound that has been implicated in cloud nucleation and global climate regulation. The crystal structure of DMSO reductase from Rhodobacter sphaeroides reveals a monooxo molybdenum cofactor containing two molybdopterin guanine dinucleotides that asymmetrically coordinate the molybdenum through their dithiolene groups. One of the pterins exhibits different coordination modes to the molybdenum between the oxidized and reduced states, whereas the side chain oxygen of Ser147 coordinates the metal in both states. The change in pterin coordination between the Mo(VI) and Mo(IV) forms suggests a mechanism for substrate binding and reduction by this enzyme. Sequence comparisons of DMSO reductase with a family of bacterial oxotransferases containing molybdopterin guanine dinucleotide indicate a similar polypeptide fold and active site with two molybdopterins within this family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schindelin, H -- Kisker, C -- Hilton, J -- Rajagopalan, K V -- Rees, D C -- GM00091/GM/NIGMS NIH HHS/ -- GM50775/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1615-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658134" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Coenzymes/*chemistry ; Crystallography, X-Ray ; *Iron-Sulfur Proteins ; Metalloproteins/*chemistry ; Models, Molecular ; Molecular Sequence Data ; Oxidation-Reduction ; Oxidoreductases/*chemistry/metabolism ; Protein Conformation ; Pteridines/*chemistry ; Rhodobacter sphaeroides/*enzymology ; Sequence Homology, Amino Acid
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  • 73
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-06-28
    Description: Vibrio cholerae, the causative agent of cholera, requires two coordinately regulated factors for full virulence: cholera toxin (CT), a potent enterotoxin, and toxin-coregulated pili (TCP), surface organelles required for intestinal colonization. The structural genes for CT are shown here to be encoded by a filamentous bacteriophage (designated CTXphi), which is related to coliphage M13. The CTXphi genome chromosomally integrated or replicated as a plasmid. CTXphi used TCP as its receptor and infected V. cholerae cells within the gastrointestinal tracts of mice more efficiently than under laboratory conditions. Thus, the emergence of toxigenic V. cholerae involves horizontal gene transfer that may depend on in vivo gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Waldor, M K -- Mekalanos, J J -- AI01321/AI/NIAID NIH HHS/ -- AI18045/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 28;272(5270):1910-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Shipley Institute of Medicine, Harvard Medical School, Boston, Massachusetts 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658163" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacteriophages/*genetics/physiology ; Base Sequence ; Cholera/*microbiology ; Cholera Toxin/*genetics ; DNA Primers ; Digestive System/microbiology ; Fimbriae, Bacterial/physiology/virology ; Gene Expression ; Genes, Bacterial ; *Lysogeny ; Mice ; Molecular Sequence Data ; Morphogenesis ; Mutation ; Transduction, Genetic ; Vibrio cholerae/genetics/*pathogenicity/*virology ; Virulence/genetics
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  • 74
    Publication Date: 1996-08-16
    Description: The plant hormone auxin regulates various developmental processes including root formation, vascular development, and gravitropism. Mutations within the AUX1 gene confer an auxin-resistant root growth phenotype and abolish root gravitropic curvature. Polypeptide sequence similarity to amino acid permeases suggests that AUX1 mediates the transport of an amino acid-like signaling molecule. Indole-3-acetic acid, the major form of auxin in higher plants, is structurally similar to tryptophan and is a likely substrate for the AUX1 gene product. The cloned AUX1 gene can restore the auxin-responsiveness of transgenic aux1 roots. Spatially, AUX1 is expressed in root apical tissues that regulate root gravitropic curvature.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bennett, M J -- Marchant, A -- Green, H G -- May, S T -- Ward, S P -- Millner, P A -- Walker, A R -- Schulz, B -- Feldmann, K A -- New York, N.Y. -- Science. 1996 Aug 16;273(5277):948-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of Warwick, Coventry, CV4 7AL, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8688077" target="_blank"〉PubMed〈/a〉
    Keywords: 2,4-Dichlorophenoxyacetic Acid/pharmacology ; Amino Acid Sequence ; Amino Acid Transport Systems ; Amino Acids/metabolism ; Arabidopsis/chemistry/*genetics/growth & development/metabolism ; *Arabidopsis Proteins ; Biological Transport ; Cloning, Molecular ; DNA, Bacterial/genetics ; *Genes, Plant ; Genetic Complementation Test ; *Gravitropism ; Indoleacetic Acids/metabolism/pharmacology ; Membrane Transport Proteins/chemistry ; Molecular Sequence Data ; Molecular Weight ; Mutation ; Plant Proteins/chemistry/*genetics/metabolism ; Plant Roots/*growth & development/metabolism ; Sequence Alignment ; Signal Transduction
    Print ISSN: 0036-8075
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  • 75
    Publication Date: 1996-10-25
    Description: The human genome is thought to harbor 50,000 to 100,000 genes, of which about half have been sampled to date in the form of expressed sequence tags. An international consortium was organized to develop and map gene-based sequence tagged site markers on a set of two radiation hybrid panels and a yeast artificial chromosome library. More than 16,000 human genes have been mapped relative to a framework map that contains about 1000 polymorphic genetic markers. The gene map unifies the existing genetic and physical maps with the nucleotide and protein sequence databases in a fashion that should speed the discovery of genes underlying inherited human disease. The integrated resource is available through a site on the World Wide Web at http://www.ncbi.nlm.nih.gov/SCIENCE96/.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schuler, G D -- Boguski, M S -- Stewart, E A -- Stein, L D -- Gyapay, G -- Rice, K -- White, R E -- Rodriguez-Tome, P -- Aggarwal, A -- Bajorek, E -- Bentolila, S -- Birren, B B -- Butler, A -- Castle, A B -- Chiannilkulchai, N -- Chu, A -- Clee, C -- Cowles, S -- Day, P J -- Dibling, T -- Drouot, N -- Dunham, I -- Duprat, S -- East, C -- Edwards, C -- Fan, J B -- Fang, N -- Fizames, C -- Garrett, C -- Green, L -- Hadley, D -- Harris, M -- Harrison, P -- Brady, S -- Hicks, A -- Holloway, E -- Hui, L -- Hussain, S -- Louis-Dit-Sully, C -- Ma, J -- MacGilvery, A -- Mader, C -- Maratukulam, A -- Matise, T C -- McKusick, K B -- Morissette, J -- Mungall, A -- Muselet, D -- Nusbaum, H C -- Page, D C -- Peck, A -- Perkins, S -- Piercy, M -- Qin, F -- Quackenbush, J -- Ranby, S -- Reif, T -- Rozen, S -- Sanders, C -- She, X -- Silva, J -- Slonim, D K -- Soderlund, C -- Sun, W L -- Tabar, P -- Thangarajah, T -- Vega-Czarny, N -- Vollrath, D -- Voyticky, S -- Wilmer, T -- Wu, X -- Adams, M D -- Auffray, C -- Walter, N A -- Brandon, R -- Dehejia, A -- Goodfellow, P N -- Houlgatte, R -- Hudson, J R Jr -- Ide, S E -- Iorio, K R -- Lee, W Y -- Seki, N -- Nagase, T -- Ishikawa, K -- Nomura, N -- Phillips, C -- Polymeropoulos, M H -- Sandusky, M -- Schmitt, K -- Berry, R -- Swanson, K -- Torres, R -- Venter, J C -- Sikela, J M -- Beckmann, J S -- Weissenbach, J -- Myers, R M -- Cox, D R -- James, M R -- Bentley, D -- Deloukas, P -- Lander, E S -- Hudson, T J -- HG00098/HG/NHGRI NIH HHS/ -- HG00206/HG/NHGRI NIH HHS/ -- HG00835/HG/NHGRI NIH HHS/ -- Wellcome Trust/United Kingdom -- etc. -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):540-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, 8600 Rockville Pike, Bethesda, MD 20894, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8849440" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; *Chromosome Mapping ; Chromosomes, Artificial, Yeast ; Computer Communication Networks ; DNA, Complementary/genetics ; Databases, Factual ; Gene Expression ; Genetic Markers ; *Genome, Human ; *Human Genome Project ; Humans ; Multigene Family ; RNA, Messenger/genetics ; Sequence Homology, Nucleic Acid ; Sequence Tagged Sites
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  • 76
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-02-23
    Description: Zinc ions are key structural components of a large number of proteins. The binding of zinc stabilizes the folded conformations of domains so that they may facilitate interactions between the proteins and other macromolecules such as DNA. The modular nature of some of these zinc-containing proteins has allowed the rational design of site-specific DNA binding proteins. The ability of zinc to be bound specifically within a range of tetrahedral sites appears to be responsible for the evolution of the side range of zinc-stabilized structural domains now known to exist. The lack of redox activity for the zinc ion and its binding and exchange kinetics also may be important in the use of zinc for specific functional roles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berg, J M -- Shi, Y -- New York, N.Y. -- Science. 1996 Feb 23;271(5252):1081-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599083" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; DNA/metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Engineering ; Transcription Factors/chemistry/*metabolism ; Zinc/chemistry/metabolism/*physiology ; Zinc Fingers/*physiology
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  • 77
    Publication Date: 1996-03-29
    Description: Genetically encoded libraries of peptides and oligonucleotides are well suited for the identification of ligands for many macromolecules. A major drawback of these techniques is that the resultant ligands are subject to degradation by naturally occurring enzymes. Here, a method is described that uses a biologically encoded library for the identification of D-peptide ligands, which should be resistant to proteolytic degradation. In this approach, a protein is synthesized in the D-amino acid configuration and used to select peptides from a phage display library expressing random L-amino acid peptides. For reasons of symmetry, the mirror images of these phage-displayed peptides interact with the target protein of the natural handedness. The value of this approach was demonstrated by the identification of a cyclic D-peptide that interacts with the Src homology 3 domain of c- SRC. Nuclear magnetic resonance studies indicate that the binding site for this D-peptide partially overlaps the site for the physiological ligands of this domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schumacher, T N -- Mayr, L M -- Minor, D L Jr -- Milhollen, M A -- Burgess, M W -- Kim, P S -- New York, N.Y. -- Science. 1996 Mar 29;271(5257):1854-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596952" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacteriophages ; Base Sequence ; Binding Sites ; Chickens ; Cloning, Molecular ; Gene Library ; Ligands ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; Peptides/chemistry/genetics/*metabolism ; Peptides, Cyclic/chemistry/genetics/*metabolism ; Proto-Oncogene Proteins pp60(c-src)/chemistry/*metabolism ; Stereoisomerism ; *src Homology Domains
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  • 78
    Publication Date: 1996-04-19
    Description: Although steroid hormones are important for animal development, the physiological role of plant steroids is unknown. The Arabidopsis DET2 gene encodes a protein that shares significant sequence identity with mammalian steroid 5 alpha-reductases. A mutation of glutamate 204, which is absolutely required for the activity of human steroid reductase, abolishes the in vivo activity of DET2 and leads to defects in light-regulated development that can be ameliorated by application of a plant steroid, brassinolide. Thus, DET2 may encode a reductase in the brassinolide biosynthetic pathway, and brassinosteroids may constitute a distinct class of phytohormones with an important role in light-regulated development of higher plants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, J -- Nagpal, P -- Vitart, V -- McMorris, T C -- Chory, J -- New York, N.Y. -- Science. 1996 Apr 19;272(5260):398-401.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Plant Biology Laboratory, Salk Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8602526" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Oxo-5-alpha-Steroid 4-Dehydrogenase/chemistry ; Amino Acid Sequence ; Animals ; Arabidopsis/genetics/*growth & development/metabolism ; *Arabidopsis Proteins ; Brassinosteroids ; Cholestanols/*metabolism/pharmacology ; Chromosome Mapping ; *Genes, Plant ; Humans ; Light ; Molecular Sequence Data ; Mutation ; Oxidation-Reduction ; Phenotype ; Plant Growth Regulators/biosynthesis/*metabolism ; Plant Proteins/*genetics ; Rats ; Sequence Alignment ; Signal Transduction ; Steroids, Heterocyclic/*metabolism/pharmacology
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  • 79
    Publication Date: 1996-08-23
    Description: A previously unknown redox cofactor has been identified in the active site of lysyl oxidase from the bovine aorta. Edman sequencing, mass spectrometry, ultraviolet-visible spectra, and resonance Raman studies showed that this cofactor is a quinone. Its structure is derived from the crosslinking of the epsilon-amino group of a peptidyl lysine with the modified side chain of a tyrosyl residue, and it has been designated lysine tyrosylquinone. This quinone appears to be the only example of a mammalian cofactor formed from the crosslinking of two amino acid side chains. This discovery expands the range of known quino-cofactor structures and has implications for the mechanism of their biogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, S X -- Mure, M -- Medzihradszky, K F -- Burlingame, A L -- Brown, D E -- Dooley, D M -- Smith, A J -- Kagan, H M -- Klinman, J P -- GM27659/GM/NIGMS NIH HHS/ -- GM39296/GM/NIGMS NIH HHS/ -- P41 RR01614/RR/NCRR NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Aug 23;273(5278):1078-84.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8688089" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Aorta/enzymology ; Binding Sites ; Cattle ; Chromatography, High Pressure Liquid ; Lysine/*analogs & derivatives/chemistry/metabolism ; Mass Spectrometry ; Molecular Sequence Data ; Molecular Weight ; Mutagenesis, Site-Directed ; Oxidation-Reduction ; Protein-Lysine 6-Oxidase/*chemistry/genetics/isolation & purification/metabolism ; Quinones/*chemistry/metabolism ; Spectrophotometry, Ultraviolet ; Spectrum Analysis, Raman
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  • 80
    Publication Date: 1996-03-29
    Description: Eukaryotic initiation factor 5A(eIF-5A) is a cellular cofactor require d for the function of the human immunodeficiency virus type-1 (HIV-1) Rev trans-activator protein. The majority of a set of eIF-5A mutants did not support growth of yeast cells having an inactivated genomic copy of eIF-5A, indicating that the introduced mutation eliminated eIF-5A activity. Two nonfunctional mutants, eIF-5AM13 and eIF-5AM14, retained their binding capacity for the HIV-1 Rev response element:Rev complex. Both mutants were constitutively expressed in human T cells. When these T cells were infected with replication-competent HIV-1, virus replication was inhibited. The eIF-5AM13 and eIF5AM14 proteins blocked Rev trans-activation and Rev-mediated nuclear export.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bevec, D -- Jaksche, H -- Oft, M -- Wohl, T -- Himmelspach, M -- Pacher, A -- Schebesta, M -- Koettnitz, K -- Dobrovnik, M -- Csonga, R -- Lottspeich, F -- Hauber, J -- New York, N.Y. -- Science. 1996 Mar 29;271(5257):1858-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sandoz Research Institute, Department of Immunodermatology, Vienna, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596953" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Nucleus/metabolism ; Cells, Cultured ; Gene Products, rev/*metabolism ; Genes, env ; HIV-1/*physiology ; HeLa Cells ; Humans ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Peptide Initiation Factors/genetics/metabolism/*physiology ; *RNA-Binding Proteins ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/genetics/growth & development ; T-Lymphocytes/metabolism/*virology ; Transcriptional Activation ; Virus Replication ; rev Gene Products, Human Immunodeficiency Virus
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  • 81
    Publication Date: 1996-02-23
    Description: The alpha subunit of p21(RAS) farnesyltransferase (FNTA), which is also shared by geranylgeranyltransferase, was isolated as a specific cytoplasmic interactor of the transforming growth factor-beta (TGF-beta) and activin type I receptors with the use of the yeast two-hybrid system. FNTA interacts specifically with ligand-free TGF-beta type l receptor but is phosphorylated and released upon ligand binding. Furthermore, the release is dependent on the kinase activity of the TGF-beta type II receptor. Thus, the growth inhibitory and differentiative pathways activated by TGF-beta and activin involve novel mechanisms of serine-threonine receptor phosphorylation-dependent release of cytoplasmic interactors and regulation of the activation of small G proteins, such as p21(RAS).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, T -- Danielson, P D -- Li, B Y -- Shah, P C -- Kim, S D -- Donahoe, P K -- HD28138/HD/NICHD NIH HHS/ -- R01 HD3081/HD/NICHD NIH HHS/ -- R01 HD32112/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1996 Feb 23;271(5252):1120-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pediatric Surgical Research Laboratories, Massachusetts General Hospital, Boston, MA 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599089" target="_blank"〉PubMed〈/a〉
    Keywords: Activin Receptors ; *Activin Receptors, Type I ; Activins ; *Alkyl and Aryl Transferases ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Humans ; Inhibins/*metabolism ; Ligands ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism ; Receptors, Growth Factor/metabolism ; Receptors, Transforming Growth Factor beta/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Transferases/*metabolism ; Transforming Growth Factor beta/*metabolism
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  • 82
    Publication Date: 1996-12-13
    Description: The induction of cytokine gene transcription is mediated in part by the nuclear factor of activated T cells (NF-AT). Factors involved in the mechanisms of NF-AT-mediated transcription are not well understood. A nuclear factor that interacted with the Rel homology domain (RHD) of NF-ATp was identified with the use of a two-hybrid interaction trap. Designated NIP45 (NF-AT interacting protein), it has minimal similarity to any known genes. Transcripts encoding this factor were enriched in lymphoid tissues and testes. NIP45 synergized with NF-ATp and the proto-oncogene c-Maf to activate the interleukin-4 (IL-4) cytokine promoter; transient overexpression of NIP45 with NF-ATp and c-maf in B lymphoma cells induced measurable endogenous IL-4 protein production. The identification of NIP45 advances our understanding of gene activation of cytokines, critical mediators of the immune response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hodge, M R -- Chun, H J -- Rengarajan, J -- Alt, A -- Lieberson, R -- Glimcher, L H -- AI37833/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Dec 13;274(5294):1903-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Biology, Harvard School of Public Health and Department of Medicine, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8943202" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/chemistry/genetics/*metabolism ; Cell Line ; Cell Nucleus/metabolism ; Cloning, Molecular ; DNA-Binding Proteins/*metabolism ; Genes, Reporter ; Humans ; Interleukin-4/*genetics ; *Intracellular Signaling Peptides and Proteins ; Male ; Molecular Sequence Data ; NFATC Transcription Factors ; Nuclear Proteins/chemistry/genetics/*metabolism ; Promoter Regions, Genetic ; Recombinant Fusion Proteins/metabolism ; Spleen/metabolism ; Testis/metabolism ; Thymus Gland/metabolism ; Transcription Factors/*metabolism ; *Transcriptional Activation ; Transfection ; Tumor Cells, Cultured
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  • 83
    Publication Date: 1996-05-31
    Description: CHOP, a member of the C/EBP family of transcription factors, mediates effects of cellular stress on growth and differentiation. It accumulates under conditions of stress and undergoes inducible phosphorylation on two adjacent serine residues (78 and 81). In vitro, CHOP is phosphorylated on these residues by p38 mitogen-activated protein kinase (MAP kinase). A specific inhibitor of p38 MAP kinase, SB203580, abolished the stress-inducible in vivo phosphorylation of CHOP. Phosphorylation of CHOP on these residues enhanced its ability to function as a transcriptional activator and was also required for the full inhibitory effect of CHOP on adipose cell differentiation. CHOP thus serves as a link between a specific stress-activated protein kinase, p38, and cellular growth and differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, X Z -- Ron, D -- New York, N.Y. -- Science. 1996 May 31;272(5266):1347-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Skirball Institute of Biomolecular Medicine, New York University Medical Center, 10016, NY, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650547" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Adipocytes/cytology ; Amino Acid Sequence ; Animals ; *CCAAT-Enhancer-Binding Proteins ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Differentiation ; Cell Division ; Culture Media ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Enzyme Inhibitors/pharmacology ; Imidazoles/pharmacology ; Methyl Methanesulfonate/pharmacology ; Mice ; *Mitogen-Activated Protein Kinases ; Molecular Sequence Data ; Phosphorylation ; Pyridines/pharmacology ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Transcription Factor CHOP ; Transcription Factors/chemistry/genetics/*metabolism ; Transcriptional Activation ; p38 Mitogen-Activated Protein Kinases
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  • 84
    Publication Date: 1996-08-16
    Description: Small synthetic molecules termed growth hormone secretagogues (GHSs) act on the pituitary gland and the hypothalamus to stimulate and amplify pulsatile growth hormone (GH) release. A heterotrimeric GTP-binding protein (G protein)-coupled receptor (GPC-R) of the pituitary and arcuate ventro-medial and infundibular hypothalamus of swine and humans was cloned and was shown to be the target of the GHSs. On the basis of its pharmacological and molecular characterization, this GPC-R defines a neuroendocrine pathway for the control of pulsatile GH release and supports the notion that the GHSs mimic an undiscovered hormone.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Howard, A D -- Feighner, S D -- Cully, D F -- Arena, J P -- Liberator, P A -- Rosenblum, C I -- Hamelin, M -- Hreniuk, D L -- Palyha, O C -- Anderson, J -- Paress, P S -- Diaz, C -- Chou, M -- Liu, K K -- McKee, K K -- Pong, S S -- Chaung, L Y -- Elbrecht, A -- Dashkevicz, M -- Heavens, R -- Rigby, M -- Sirinathsinghji, D J -- Dean, D C -- Melillo, D G -- Patchett, A A -- Nargund, R -- Griffin, P R -- DeMartino, J A -- Gupta, S K -- Schaeffer, J M -- Smith, R G -- Van der Ploeg, L H -- New York, N.Y. -- Science. 1996 Aug 16;273(5277):974-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Merck Research Laboratories, Rahway, NJ 07065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8688086" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Codon ; DNA, Complementary/genetics ; GTP-Binding Proteins/metabolism ; Growth Hormone/*secretion ; Hormones/*metabolism ; Humans ; Hypothalamus, Middle/chemistry ; Indoles/*metabolism/pharmacology ; Macaca mulatta ; Molecular Sequence Data ; Oligopeptides/*metabolism ; Pituitary Gland/chemistry ; RNA, Complementary/genetics ; Rats ; Receptors, Cell Surface/analysis/chemistry/genetics/*metabolism ; *Receptors, G-Protein-Coupled ; Receptors, Ghrelin ; Spiro Compounds/*metabolism/pharmacology ; Swine
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  • 85
    Publication Date: 1996-05-10
    Description: A cofactor for HIV-1 (human immunodeficiency virus-type 1) fusion and entry was identified with the use of a novel functional complementary DNA (cDNA) cloning strategy. This protein, designated "fusin," is a putative G protein-coupled receptor with seven transmembrane segments. Recombinant fusin enabled CD4-expressing nonhuman cell types to support HIV-1 Env-mediated cell fusion and HIV-1 infection. Antibodies to fusin blocked cell fusion and infection with normal CD4-positive human target cells. Fusin messenger RNA levels correlated with HIV-1 permissiveness in diverse human cell types. Fusin acted preferentially for T cell line-tropic isolates, in comparison to its activity with macrophagetropic HIV-1 isolates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feng, Y -- Broder, C C -- Kennedy, P E -- Berger, E A -- New York, N.Y. -- Science. 1996 May 10;272(5263):872-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases (NIAID), NIH, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8629022" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Amino Acid Sequence ; Animals ; Antigens, CD4/*physiology ; CD4-Positive T-Lymphocytes/virology ; Cell Line ; Cell Membrane/virology ; Chemokines/physiology ; *Cloning, Molecular ; DNA, Complementary/genetics ; Disease Models, Animal ; GTP-Binding Proteins/metabolism ; Giant Cells ; HIV Envelope Protein gp120/physiology ; HIV-1/*pathogenicity/physiology ; HeLa Cells ; Humans ; Leukocytes, Mononuclear/virology ; Macrophages/virology ; *Membrane Fusion ; Membrane Proteins/genetics/*physiology ; Mice ; Molecular Sequence Data ; RNA, Messenger/metabolism ; Receptors, CXCR4 ; Recombinant Proteins ; Transfection
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  • 86
    Publication Date: 1996-06-14
    Description: Mutations that eliminate KatG catalase-peroxidase activity prevent activation of isoniazid and are a major mechanism of resistance to this principal drug for the treatment of Mycobacterium tuberculosis infections. However, the loss of KatG activity in clinical isolates seemed paradoxical because KatG is considered an important factor for the survival of the organism. Expression of either KatG or the recently identified alkyl hydroperoxidase AhpC was sufficient to protect bacilli against the toxic effects of organic peroxides. To survive during infection, isoniazid-resistant KatG mutants have apparently compensated for the loss of KatG catalase-peroxidase activity by a second mutation, resulting in hyperexpression of AhpC.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sherman, D R -- Mdluli, K -- Hickey, M J -- Arain, T M -- Morris, S L -- Barry, C E 3rd -- Stover, C K -- Z01 AI000783-11/Intramural NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1641-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Tuberculosis and Molecular Microbiology, PathoGenesis Corporation, Seattle, Washington 98119, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658136" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antitubercular Agents/*pharmacology ; *Bacterial Proteins ; Base Sequence ; Cloning, Molecular ; DNA, Bacterial ; Drug Resistance, Microbial/genetics ; Drug Synergism ; Enzyme Induction ; Gene Expression Regulation, Bacterial ; Hydrogen Peroxide/pharmacology ; Isoniazid/*pharmacology ; Molecular Sequence Data ; Mutation ; Mycobacterium bovis/drug effects/genetics ; Mycobacterium tuberculosis/*drug effects/*genetics ; Oxidoreductases/*genetics ; Peroxidases/biosynthesis/genetics/metabolism ; Peroxiredoxins ; Promoter Regions, Genetic
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  • 87
    Publication Date: 1996-08-09
    Description: The diphtheria toxin transmembrane (T) domain was spin-labeled at consecutive residues in a helical segment, TH9. After binding of the T domain to membranes at low pH, the nitroxide side chains generated by spin labeling were measured with respect to their frequency of collision with polar and nonpolar reagents. The data showed that the helical structure of TH9 in solution is conserved, with one face exposed to water and the other to the hydrophobic interior of the bilayer. Measurement of the depth of the nitroxide side chains from the membrane surfaces revealed an incremental change of about 5 angstroms per turn, which is consistent with a transmembrane orientation of an alpha helix. These results indicate that the helix forms the lining of a transmembrane water-filled channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oh, K J -- Zhan, H -- Cui, C -- Hideg, K -- Collier, R J -- Hubbell, W L -- AI-22021/AI/NIAID NIH HHS/ -- AI-22848/AI/NIAID NIH HHS/ -- EY-05216/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 9;273(5276):810-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Jules Stein Eye Institute and Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095-7008, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8670424" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Diphtheria Toxin/*chemistry/genetics ; Edetic Acid/analogs & derivatives ; Electron Spin Resonance Spectroscopy ; Hydrogen-Ion Concentration ; *Lipid Bilayers ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nickel ; Oxygen ; Phospholipids ; *Protein Structure, Secondary ; *Protein Structure, Tertiary ; Spin Labels
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  • 88
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-11-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Manley, J L -- Takagaki, Y -- New York, N.Y. -- Science. 1996 Nov 29;274(5292):1481-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Columbia University, New York, NY 10027, USA. jlm2@columbia.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8966619" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Conserved Sequence ; Evolution, Molecular ; Fungal Proteins/*chemistry/genetics/metabolism ; Humans ; Mammals/genetics/metabolism ; Oligoribonucleotides/metabolism ; Poly A/*metabolism ; RNA Precursors/*metabolism ; *RNA Processing, Post-Transcriptional ; RNA, Messenger/*metabolism ; RNA-Binding Proteins/*chemistry/genetics/metabolism ; Saccharomyces cerevisiae/chemistry/genetics ; mRNA Cleavage and Polyadenylation Factors
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  • 89
    Publication Date: 1996-03-22
    Description: Progressive myoclonus epilepsy of the Unverricht-Lundborg type (EPM1) is an autosomal recessive inherited form of epilepsy, previously linked to human chromosome 21q22.3. The gene encoding cystatin B was shown to be localized to this region, and levels of messenger RNA encoded by this gene were found to be decreased in cells from affected individuals. Two mutations, a 3' splice site mutation and a stop codon mutation, were identified in the gene encoding cystatin B in EPM1 patients but were not present in unaffected individuals. These results provide evidence that mutations in the gene encoding cystatin B are responsible for the primary defect in patients with EPM1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennacchio, L A -- Lehesjoki, A E -- Stone, N E -- Willour, V L -- Virtaneva, K -- Miao, J -- D'Amato, E -- Ramirez, L -- Faham, M -- Koskiniemi, M -- Warrington, J A -- Norio, R -- de la Chapelle, A -- Cox, D R -- Myers, R M -- HD-24610/HD/NICHD NIH HHS/ -- IF32GM17502/GM/NIGMS NIH HHS/ -- P50 HG-00206/HG/NHGRI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Mar 22;271(5256):1731-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Stanford University School of Medicine, Standford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596935" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Chromosome Mapping ; Chromosomes, Human, Pair 21/*genetics ; Codon, Terminator/genetics ; Cystatin B ; Cystatins/chemistry/*genetics ; Cysteine Proteinase Inhibitors/chemistry/*genetics ; Epilepsies, Myoclonic/*genetics ; Female ; Finland ; Gene Expression ; Genes, Recessive ; Humans ; Introns/genetics ; Linkage Disequilibrium ; Male ; Molecular Sequence Data ; Pedigree ; Point Mutation ; Polymerase Chain Reaction ; RNA, Messenger/genetics/metabolism ; Recombination, Genetic
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  • 90
    Publication Date: 1996-08-23
    Description: The complete 1.66-megabase pair genome sequence of an autotrophic archaeon, Methanococcus jannaschii, and its 58- and 16-kilobase pair extrachromosomal elements have been determined by whole-genome random sequencing. A total of 1738 predicted protein-coding genes were identified; however, only a minority of these (38 percent) could be assigned a putative cellular role with high confidence. Although the majority of genes related to energy production, cell division, and metabolism in M. jannaschii are most similar to those found in Bacteria, most of the genes involved in transcription, translation, and replication in M. jannaschii are more similar to those found in Eukaryotes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bult, C J -- White, O -- Olsen, G J -- Zhou, L -- Fleischmann, R D -- Sutton, G G -- Blake, J A -- FitzGerald, L M -- Clayton, R A -- Gocayne, J D -- Kerlavage, A R -- Dougherty, B A -- Tomb, J F -- Adams, M D -- Reich, C I -- Overbeek, R -- Kirkness, E F -- Weinstock, K G -- Merrick, J M -- Glodek, A -- Scott, J L -- Geoghagen, N S -- Venter, J C -- GM00783/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 23;273(5278):1058-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Microbiology Department, University of Illinois, Champaign-Urbana, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8688087" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/chemistry/*genetics ; Base Composition ; Base Sequence ; Biological Transport/genetics ; Carbon Dioxide/metabolism ; Chromosome Mapping ; Chromosomes, Bacterial/genetics ; DNA Replication ; DNA, Bacterial/*genetics ; Databases, Factual ; Energy Metabolism/genetics ; Genes, Bacterial ; *Genome, Bacterial ; Hydrogen/metabolism ; Methane/metabolism ; Methanococcus/*genetics/physiology ; Molecular Sequence Data ; Protein Biosynthesis ; Sequence Analysis, DNA ; Transcription, Genetic
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  • 91
    Publication Date: 1996-09-13
    Description: A phosphorylation-initiated mechanism of local protein refolding activates yeast glycogen phosphorylase (GP). Refolding of the phosphorylated amino-terminus was shown to create a hydrophobic cluster that wedges into the subunit interface of the enzyme to trigger activation. The phosphorylated threonine is buried in the allosteric site. The mechanism implicates glucose 6-phosphate, the allosteric inhibitor, in facilitating dephosphorylation by dislodging the buried covalent phosphate through binding competition. Thus, protein phosphorylation-dephosphorylation may also be controlled through regulation of the accessibility of the phosphorylation site to kinases and phosphatases. In mammalian glycogen phosphorylase, phosphorylation occurs at a distinct locus. The corresponding allosteric site binds a ligand activator, adenosine monophosphate, which triggers activation by a mechanism analogous to that of phosphorylation in the yeast enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, K -- Rath, V L -- Dai, S C -- Fletterick, R J -- Hwang, P K -- DK32822/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1996 Sep 13;273(5281):1539-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California at San Francisco, 513 Parnassus, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703213" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Monophosphate/metabolism ; Allosteric Site ; Amino Acid Sequence ; Animals ; Crystallography, X-Ray ; Enzyme Activation ; Enzyme Inhibitors/metabolism/pharmacology ; Glucose-6-Phosphate ; Glucosephosphates/metabolism/pharmacology ; Models, Molecular ; Molecular Sequence Data ; Phosphorylases/antagonists & inhibitors/*chemistry/*metabolism ; Phosphorylation ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Saccharomyces cerevisiae/enzymology
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  • 92
    Publication Date: 1996-06-14
    Description: DnaK and other members of the 70-kilodalton heat-shock protein (hsp70) family promote protein folding, interaction, and translocation, both constitutively and in response to stress, by binding to unfolded polypeptide segments. These proteins have two functional units: a substrate-binding portion binds the polypeptide, and an adenosine triphosphatase portion facilitates substrate exchange. The crystal structure of a peptide complex with the substrate-binding unit of DnaK has now been determined at 2.0 angstroms resolution. The structure consists of a beta-sandwich subdomain followed by alpha-helical segments. The peptide is bound to DnaK in an extended conformation through a channel defined by loops from the beta sandwich. An alpha-helical domain stabilizes the complex, but does not contact the peptide directly. This domain is rotated in the molecules of a second crystal lattice, which suggests a model of conformation-dependent substrate binding that features a latch mechanism for maintaining long lifetime complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhu, X -- Zhao, X -- Burkholder, W F -- Gragerov, A -- Ogata, C M -- Gottesman, M E -- Hendrickson, W A -- GM 34102/GM/NIGMS NIH HHS/ -- GM 37219/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1606-14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, College of Physicians and Surgeons, Columbia University, New York 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658133" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Chaperonins/chemistry/*metabolism ; Crystallography, X-Ray ; Escherichia coli ; *Escherichia coli Proteins ; HSP70 Heat-Shock Proteins/chemistry/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Peptides/metabolism ; Protein Binding ; Protein Conformation ; Sequence Homology, Amino Acid
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  • 93
    Publication Date: 1996-06-07
    Description: The appearance of phosphatidylserine on the surface of animal cells triggers phagocytosis and blood coagulation. Normally, phosphatidylserine is confined to the inner leaflet of the plasma membrane by an aminophospholipid translocase, which has now been cloned and sequenced. The bovine enzyme is a member of a previously unrecognized subfamily of P-type adenosine triphosphatases (ATPases) that may have diverged from the primordial enzyme before the separation of the known families of ion-translocating ATPases. Studies in Saccharomyces cerevisiae suggest that aminophospholipid translocation is a general function of members of this family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tang, X -- Halleck, M S -- Schlegel, R A -- Williamson, P -- New York, N.Y. -- Science. 1996 Jun 7;272(5267):1495-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Amherst College, MA 01002, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8633245" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/chemistry/genetics/isolation & purification/*metabolism ; Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Animals ; Biological Transport ; Cattle ; Cell Membrane/metabolism ; Chromaffin Granules/enzymology ; Cloning, Molecular ; Molecular Sequence Data ; Molecular Weight ; Phosphatidylcholines/metabolism ; Phosphatidylethanolamines/metabolism ; Phosphatidylserines/metabolism ; Phospholipids/*metabolism ; Sequence Homology, Amino Acid
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  • 94
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-09-06
    Description: Complementary chromatic adaptation in cyanobacteria acts through photoreceptors to control the biosynthesis of light-harvesting complexes. The mutant FdBk, which appears black, cannot chromatically adapt and may contain a lesion in the apparatus that senses light quality. The complementing gene identified here, rcaE, encodes a deduced protein in which the amino-terminal region resembles the chromophore attachment domain of phytochrome photoreceptors and regions of plant ethylene receptors; the carboxyl- terminal half is similar to the histidine kinase domain of two-component sensor kinases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kehoe, D M -- Grossman, A R -- New York, N.Y. -- Science. 1996 Sep 6;273(5280):1409-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Biology, Carnegie Institution of Washington, 290 Panama Street, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703080" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Amino Acid Sequence ; Apoproteins/*chemistry ; *Arabidopsis Proteins ; Bacterial Proteins/chemistry ; Cyanobacteria/*chemistry/genetics/physiology ; Genetic Complementation Test ; Light ; *Light-Harvesting Protein Complexes ; Molecular Sequence Data ; Mutation ; Open Reading Frames ; Photosynthetic Reaction Center Complex Proteins/*chemistry/genetics/metabolism ; Phytochrome/*chemistry ; *Plant Proteins ; Protein Kinases/chemistry ; Receptors, Cell Surface/*chemistry ; Sequence Alignment
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  • 95
    Publication Date: 1996-08-30
    Description: The self-incompatibility (S) locus of flowering plants offers an example of extreme polymorphism maintained by balancing selection. Estimates of recent and long-term effective population size (Ne) were determined for two solanaceous species by examination of S-allele diversity. Estimates of recent Ne in two solanaceous species differed by an order of magnitude, consistent with differences in the species' ecology. In one species, the evidence was consistent with historical population restriction despite a large recent Ne. In the other, no severe bottleneck was indicated over millions of years. Bottlenecks are integral to founder-event speciation, and loci that are subject to balancing selection can be used to evaluate the frequency of this mode of speciation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Richman, A D -- Uyenoyama, M K -- Kohn, J R -- GM 37841/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 30;273(5279):1212-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0116, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703052" target="_blank"〉PubMed〈/a〉
    Keywords: *Alleles ; Amino Acid Sequence ; *Genes, Plant ; *Genetic Variation ; Molecular Sequence Data ; Phylogeny ; Plant Proteins/chemistry/*genetics ; Plants/classification/*genetics ; Polymerase Chain Reaction ; Selection, Genetic ; Sequence Alignment
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  • 96
    Publication Date: 1996-10-04
    Description: Identification and characterization of antigen-specific T lymphocytes during the course of an immune response is tedious and indirect. To address this problem, the peptide-major histocompatability complex (MHC) ligand for a given population of T cells was multimerized to make soluble peptide-MHC tetramers. Tetramers of human lymphocyte antigen A2 that were complexed with two different human immunodeficiency virus (HIV)-derived peptides or with a peptide derived from influenza A matrix protein bound to peptide-specific cytotoxic T cells in vitro and to T cells from the blood of HIV-infected individuals. In general, tetramer binding correlated well with cytotoxicity assays. This approach should be useful in the analysis of T cells specific for infectious agents, tumors, and autoantigens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Altman, J D -- Moss, P A -- Goulder, P J -- Barouch, D H -- McHeyzer-Williams, M G -- Bell, J I -- McMichael, A J -- Davis, M M -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1996 Oct 4;274(5284):94-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305-5428, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8810254" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Viral/*immunology ; Base Sequence ; CD8-Positive T-Lymphocytes/immunology ; Cell Line ; Coloring Agents ; Epitopes/immunology ; Flow Cytometry ; Gene Products, gag/immunology ; HIV Seropositivity/*immunology ; HLA-A2 Antigen/*immunology ; Humans ; Molecular Sequence Data ; Peptide Fragments/*immunology ; Phenotype ; RNA-Directed DNA Polymerase/immunology ; T-Lymphocytes, Cytotoxic/*immunology ; Viral Matrix Proteins/immunology
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 97
    Publication Date: 1996-10-25
    Description: The genome of the yeast Saccharomyces cerevisiae has been completely sequenced through a worldwide collaboration. The sequence of 12,068 kilobases defines 5885 potential protein-encoding genes, approximately 140 genes specifying ribosomal RNA, 40 genes for small nuclear RNA molecules, and 275 transfer RNA genes. In addition, the complete sequence provides information about the higher order organization of yeast's 16 chromosomes and allows some insight into their evolutionary history. The genome shows a considerable amount of apparent genetic redundancy, and one of the major problems to be tackled during the next stage of the yeast genome project is to elucidate the biological functions of all of these genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goffeau, A -- Barrell, B G -- Bussey, H -- Davis, R W -- Dujon, B -- Feldmann, H -- Galibert, F -- Hoheisel, J D -- Jacq, C -- Johnston, M -- Louis, E J -- Mewes, H W -- Murakami, Y -- Philippsen, P -- Tettelin, H -- Oliver, S G -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):546, 563-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Universite Catholique de Louvain, Unite de Biochimie Physiologique, Place Croix du Sud, 2/20, 1348 Louvain-la-Neuve, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8849441" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; *Chromosome Mapping ; Chromosomes, Fungal/genetics ; Computer Communication Networks ; DNA, Fungal/genetics ; Evolution, Molecular ; Fungal Proteins/chemistry/genetics/physiology ; Gene Library ; *Genes, Fungal ; *Genome, Fungal ; International Cooperation ; Multigene Family ; Open Reading Frames ; RNA, Fungal/genetics ; Saccharomyces cerevisiae/*genetics ; Sequence Analysis, DNA
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 98
    Publication Date: 1996-01-26
    Description: The current model of serine protease diversity theorizes that the earliest protease molecules were simple digestive enzymes that gained complex regulatory functions and restricted substrate specificities through evolution. Among the chymase group of serine proteases are enzymes that convert angiotensin I to angiotensin II, as well as others that simply degrade angiotensins. An ancestral chymase reconstructed with the use of phylogenetic inference, total gene synthesis, and protein expression had efficient and specific angiotensin II-forming activity (turnover number, about 700 per second). Thus, angiotensin II-forming activity is the more primitive state for chymases, and the loss of such activity occurred later in the evolution of some of these serine proteases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chandrasekharan, U M -- Sanker, S -- Glynias, M J -- Karnik, S S -- Husain, A -- HL33713/HL/NHLBI NIH HHS/ -- HL44201/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 26;271(5248):502-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Cardiology, Cleveland Clinic Foundation, OH 44195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8560264" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Angiotensin I/*metabolism ; Angiotensin II/*metabolism ; Angiotensins/metabolism ; Animals ; Binding Sites ; Chymases ; Evolution, Molecular ; Genes, Synthetic ; Humans ; Molecular Sequence Data ; Rats ; Serine Endopeptidases/chemistry/genetics/*metabolism ; Substrate Specificity
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 99
    Publication Date: 1996-04-12
    Description: Werner's syndrome (WS) is an inherited disease with clinical symptoms resembling premature aging. Early susceptibility to a number of major age-related diseases is a key feature of this disorder. The gene responsible for WS (known as WRN) was identified by positional cloning. The predicted protein is 1432 amino acids in length and shows significant similarity to DNA helicases. Four mutations in WS patients were identified. Two of the mutations are splice-junction mutations, with the predicted result being the exclusion of exons from the final messenger RNA. One of the these mutations, which results in a frameshift and a predicted truncated protein, was found in the homozygous state in 60 percent of Japanese WS patients examined. The other two mutations are nonsense mutations. The identification of a mutated putative helicase as the gene product of the WS gene suggests that defective DNA metabolism is involved in the complex process of aging in WS patients.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yu, C E -- Oshima, J -- Fu, Y H -- Wijsman, E M -- Hisama, F -- Alisch, R -- Matthews, S -- Nakura, J -- Miki, T -- Ouais, S -- Martin, G M -- Mulligan, J -- Schellenberg, G D -- P01 AG01751/AG/NIA NIH HHS/ -- R01 AG12019/AG/NIA NIH HHS/ -- T32 AG00057/AG/NIA NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Apr 12;272(5259):258-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Geriatric Research Education and Clinical Center, Veterans Affairs Puget Sound Health Care System, Seattle Division, WA 98108, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8602509" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/genetics ; Amino Acid Sequence ; Base Sequence ; Chromosome Mapping ; Chromosomes, Human, Pair 8/*genetics ; *Cloning, Molecular ; Codon, Terminator ; DNA/metabolism ; DNA Helicases/chemistry/*genetics ; DNA, Complementary/genetics ; Disease Susceptibility ; Exodeoxyribonucleases ; Exons/genetics ; Female ; Frameshift Mutation ; Heterozygote ; Homozygote ; Humans ; Male ; Molecular Sequence Data ; *Mutation ; Neoplasms/etiology/genetics ; RecQ Helicases ; Sequence Alignment ; Werner Syndrome/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 100
    Publication Date: 1996-03-15
    Description: Multivalent binding proteins, such as the yeast scaffold protein Sterile-5, coordinate the location of kinases by serving as platforms for the assembly of signaling units. Similarly, in mammalian cells the cyclic adenosine 3',5'-monophosphate-dependent protein kinase (PKA) and phosphatase 2B [calcineurin (CaN)] are complexed by an A kinase anchoring protein, AKAP79. Deletion analysis and binding studies demonstrate that a third enzyme, protein kinase C (PKC), binds AKAP79 at a site distinct from those bound by PKA or CaN. The subcellular distributions of PKC and AKAP79 were similar in neurons. Thus, AKAP79 appears to function as a scaffold protein for three multifunctional enzymes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klauck, T M -- Faux, M C -- Labudda, K -- Langeberg, L K -- Jaken, S -- Scott, J D -- CA538841/CA/NCI NIH HHS/ -- GM48231/GM/NIGMS NIH HHS/ -- GM50152/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1589-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute, Oregon Health Sciences University, Portland, 97201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599116" target="_blank"〉PubMed〈/a〉
    Keywords: A Kinase Anchor Proteins ; *Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Brain/enzymology ; Calcineurin ; Calmodulin/pharmacology ; Calmodulin-Binding Proteins/*metabolism ; *Carrier Proteins ; Cattle ; Cell Line ; Cyclic AMP-Dependent Protein Kinases/analysis/antagonists & ; inhibitors/*metabolism ; Fungal Proteins/metabolism ; Humans ; Molecular Sequence Data ; Neurons/chemistry ; Phosphoprotein Phosphatases/*metabolism ; Phosphorylation ; Protein Kinase C/analysis/antagonists & inhibitors/*metabolism ; Proteins/analysis/*metabolism/pharmacology ; Recombinant Proteins ; *Saccharomyces cerevisiae Proteins ; Signal Transduction ; Synapses/physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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