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  • Cloning, Molecular  (69)
  • American Association for the Advancement of Science (AAAS)  (69)
  • Blackwell Publishing Ltd
  • 1995-1999  (63)
  • 1980-1984  (6)
  • 1996  (63)
  • 1980  (6)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (69)
  • Blackwell Publishing Ltd
Years
  • 1995-1999  (63)
  • 1980-1984  (6)
Year
  • 1
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    IRAK: a kinase associated with the interleukin-1 receptor (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    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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  • 2
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    Binding of zinc finger protein ZPR1 to the epidermal growth factor receptor (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 3
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    Myc and Max homologs in Drosophila (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
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  • 4
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    KUZ, a conserved metalloprotease-disintegrin protein with two roles in Drosophila neurogenesis (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 5
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    PER protein in silkmoths marches to different drummer (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1996 Nov 22;274(5291):1306.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8966602" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Clocks ; Bombyx/genetics/*metabolism ; Brain/metabolism ; Cell Nucleus/metabolism ; *Circadian Rhythm ; Cloning, Molecular ; *Drosophila Proteins ; Drosophila melanogaster/genetics/metabolism ; Gene Expression Regulation ; Genes, Insect ; Neurons/*metabolism ; Nuclear Proteins/genetics/*metabolism ; Period Circadian Proteins ; Proteins/genetics/metabolism ; RNA, Antisense/metabolism ; RNA, Messenger/metabolism
    Print ISSN: 0036-8075
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  • 6
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    Protein kinase N (PKN) and PKN-related protein rhophilin as targets of small GTPase Rho (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 7
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    Association of Src tyrosine kinase with a human potassium channel mediated by SH3 domain (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 8
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    Functional analysis of the genes of yeast chromosome V by genetic footprinting (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-20
    Description: Genetic footprinting was used to assess the phenotypic effects of Ty1 transposon insertions in 268 predicted genes of chromosome V of Saccharomyces cerevisiae. When seven selection protocols were used, Ty1 insertions in more than half the genes tested (157 of 268) were found to result in a detectable reduction in fitness. Results could not be obtained for fewer than 3 percent of the genes tested (7 of 268). Previously known mutant phenotypes were confirmed, and, for about 30 percent of the genes, new mutant phenotypes were identified.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, V -- Chou, K N -- Lashkari, D -- Botstein, D -- Brown, P O -- 1PO1 HG00205-05/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1996 Dec 20;274(5295):2069-74.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA. Medicine, Stanford, CA 94305, USA. pbrown@cmgm.stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8953036" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosomes, Fungal/*genetics ; Cloning, Molecular ; Culture Media ; DNA Footprinting ; DNA Transposable Elements ; DNA, Fungal/genetics ; Gene Library ; *Genes, Fungal ; Mutagenesis, Insertional ; Phenotype ; Polymerase Chain Reaction ; Saccharomyces cerevisiae/*genetics/growth & development/physiology
    Print ISSN: 0036-8075
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  • 9
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    A quasi-monoclonal mouse (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-14
    Description: As a model for studying the generation of antibody diversity, a gene-targeted mouse was produced that is hemizygous for a rearranged V(D)J segment at the immunoglobulin (Ig) heavy chain locus, the other allele being nonfunctional. The mouse also has no functional kappa light chain allele. The heavy chain, when paired with any lambda light chain, is specific for the hapten (4-hydroxy-3-nitrophenyl) acetyl (NP). The primary repertoire of this quasi-monoclonal mouse is monospecific, but somatic hypermutation and secondary rearrangements change the specificity of 20 percent of the antigen receptors on B cells. The serum concentrations of the Ig isotypes are similar to those in nontransgenic littermates, but less than half of the serum IgM binds to NP, and none of the other isotypes do. Thus, neither network interactions nor random activation of a small fraction of the B cell population can account for serum Ig concentrations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cascalho, M -- Ma, A -- Lee, S -- Masat, L -- Wabl, M -- 1R01 GM37699/GM/NIGMS NIH HHS/ -- P60 AR20684/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1649-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of California, San Francisco 94143-0670, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658139" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/*genetics/immunology ; *Antigens, CD ; Antigens, CD43 ; Antigens, CD45/immunology ; B-Lymphocytes/cytology/immunology ; Base Sequence ; Cell Line ; Cloning, Molecular ; Dna ; Flow Cytometry ; Gene Rearrangement, B-Lymphocyte, Heavy Chain ; Haptens/immunology ; Immunoglobulin Heavy Chains/*genetics/immunology ; Immunoglobulin Isotypes/genetics ; Immunoglobulin J-Chains/genetics ; Immunoglobulin Light Chains/genetics/immunology ; Immunoglobulin Variable Region/genetics ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Mice, Knockout/genetics/*immunology ; Molecular Sequence Data ; Nitrophenols/immunology ; Phenylacetates ; Recombinant Proteins/genetics/immunology ; Sialoglycoproteins/immunology
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  • 10
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    Tricorn protease--the core of a modular proteolytic system (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 11
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    Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 12
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    A new receptor for growth hormone-release peptide (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Conn, P M -- Bowers, C Y -- New York, N.Y. -- Science. 1996 Aug 16;273(5277):923.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Oregon Regional Primate Research Center, Beaverton, OR 97006-3499, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8711477" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; Growth Hormone/pharmacology/*secretion ; Growth Hormone-Releasing Hormone/metabolism ; Hormones/metabolism/pharmacology ; Humans ; Hypothalamus/metabolism ; Insulin-Like Growth Factor I/analysis ; Oligopeptides/*metabolism/pharmacology ; Receptors, Cell Surface/chemistry/*metabolism ; *Receptors, G-Protein-Coupled ; Receptors, Ghrelin ; Receptors, Neuropeptide/metabolism ; Receptors, Pituitary Hormone-Regulating Hormone/metabolism ; Recombinant Proteins/pharmacology
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  • 13
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    CKI1, a histidine kinase homolog implicated in cytokinin signal transduction (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 14
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    PKD2, a gene for polycystic kidney disease that encodes an integral membrane protein (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Fly sex drive traced to fru gene (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1996 Dec 13;274(5294):1836.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8984640" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; Drosophila melanogaster/*genetics/physiology ; Female ; Gene Expression Regulation ; *Genes, Insect ; Male ; Neurons/metabolism ; RNA Splicing ; *Sexual Behavior, Animal
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  • 16
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    Small-conductance, calcium-activated potassium channels from mammalian brain (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 17
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    Cold-induced expression of delta 9-desaturase in carp by transcriptional and posttranslational mechanisms (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    A neural tetraspanin, encoded by late bloomer, that facilitates synapse formation (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    The rf2 nuclear restorer gene of male-sterile T-cytoplasm maize (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Life's last domain (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1996 Aug 23;273(5278):1043-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8711482" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Evolution ; Chromosomes, Bacterial ; Cloning, Molecular ; DNA, Bacterial/*genetics ; Gene Library ; *Genome, Bacterial ; Methane/metabolism ; Methanococcus/classification/*genetics/physiology ; Pressure ; Protein Biosynthesis ; Sequence Analysis, DNA ; Temperature ; Transcription, Genetic
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  • 21
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    Guiding neurons to the cortex (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1996 Nov 15;274(5290):1100-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8966585" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/abnormalities/embryology ; Brain Diseases/genetics ; Cell Adhesion Molecules, Neuronal/*genetics/physiology ; Cell Movement ; Cerebral Cortex/cytology/*embryology ; Cloning, Molecular ; Cyclin-Dependent Kinase 5 ; *Cyclin-Dependent Kinases ; Extracellular Matrix Proteins/*genetics/physiology ; Female ; Humans ; Intellectual Disability/genetics ; Male ; Mice ; Mice, Neurologic Mutants ; Nerve Tissue Proteins/genetics/physiology ; Neurons/*physiology ; Protein-Serine-Threonine Kinases/physiology ; Serine Endopeptidases
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  • 22
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    DNA replication fork pause sites dependent on transcription (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-05-17
    Description: Replication fork pause (RFP) sites transiently arresting replication fork movement were mapped to transfer RNA (tRNA) genes of Saccharomyces cerevisiae in vivo. RFP sites are polar, stalling replication forks only when they oppose the direction of tRNA transcription. Mutant tRNA genes defective in assembly of transcription initiation complexes and a temperature-sensitive RNA polymerase III mutant (rpc160-41) defective in initiation of transcription do not stall replication forks, suggesting that transcription is required for RFP activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Deshpande, A M -- Newlon, C S -- GM35679/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 May 17;272(5264):1030-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Micobiology and Molecular Genetics, UMDNJ Medical School and UMDNJ-Graduate School of Biomedical Sciences, Newark, NJ 07103, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638128" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cloning, Molecular ; *DNA Replication ; Genes, Fungal ; Molecular Sequence Data ; Point Mutation ; RNA Polymerase III/metabolism ; RNA, Fungal/*genetics ; RNA, Transfer/*genetics ; Repetitive Sequences, Nucleic Acid ; Replication Origin ; Saccharomyces cerevisiae/genetics/*metabolism ; Sequence Deletion ; Temperature ; Transcription Factors/metabolism ; *Transcription, Genetic
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  • 23
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    Altered growth and branching patterns in synpolydactyly caused by mutations in HOXD13 (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Researchers nail down leptin receptor (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1996 Feb 16;271(5251):913.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8584929" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carrier Proteins/biosynthesis/chemistry/*genetics ; Chromosome Mapping ; Cloning, Molecular ; Diabetes Mellitus/*genetics ; Humans ; Leptin ; Mice ; Mutation ; Obesity/*genetics ; Proteins/genetics ; RNA, Messenger/genetics ; Rats ; *Receptors, Cell Surface ; Receptors, Cytokine/biosynthesis/chemistry/*genetics ; Receptors, Leptin
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  • 25
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    Role of the nuclear transport factor p10 in nuclear import (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-05
    Description: The nuclear import factor p10 was cloned from Saccharomyces cerevisiae and found to be essential. The protein p10 can bind directly to several peptide repeat-containing nucleoporins. It also binds to the guanosine triphosphatase (GTPase) Ran in its guanosine diphosphate (GDP)-bound form and to karyopherin beta. Assembly of the karyopherin heterodimer on immobilized nucleoporin yielded cooperative binding of p10 and Ran-GDP. Addition of GTP to this pentameric complex led to dissociation of karyopherin (chi, presumably via in situ formation of Ran-GTP from Ran-GDP. Thus, p10 appears to coordinate the Ran-dependent association and dissociation reactions underlying nuclear import.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nehrbass, U -- Blobel, G -- New York, N.Y. -- Science. 1996 Apr 5;272(5258):120-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8600522" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Transport, Active ; Carrier Proteins/genetics/*metabolism ; Cell Nucleus/*metabolism ; Cloning, Molecular ; GTP-Binding Proteins/metabolism ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Molecular Sequence Data ; Nuclear Envelope/metabolism ; Nuclear Proteins/*metabolism ; *Nucleocytoplasmic Transport Proteins ; Saccharomyces cerevisiae/genetics/*metabolism ; Saccharomyces cerevisiae Proteins ; alpha Karyopherins ; beta Karyopherins ; ran GTP-Binding Protein
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  • 26
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    Interfering with apoptosis: Ca(2+)-binding protein ALG-2 and Alzheimer's disease gene ALG-3 (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    CRINKLY4: A TNFR-like receptor kinase involved in maize epidermal differentiation (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    High mutation frequencies among Escherichia coli and Salmonella pathogens (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-15
    Description: Here it is reported that the incidence of mutators among isolates of pathogenic Escherichia coli and Salmonella enterica is high (over 1 percent). These findings counter the theory, founded on studies with laboratory-attenuated strains, that suggests mutators are rare among bacterial populations. Defects in methyl-directed mismatch repair underlie all mutator phenotypes described here. Of nine independently derived hypermutable strains, seven contained a defective mutS allele. Because these mutant alleles increase the mutation rate and enhance recombination among diverse species, these studies may help explain both the rapid emergence of antibiotic resistance and the penetrance of virulence genes within the prokaryotic community.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉LeClerc, J E -- Li, B -- Payne, W L -- Cebula, T A -- New York, N.Y. -- Science. 1996 Nov 15;274(5290):1208-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Branch, Center for Food Safety and Applied Nutrition (HFS-235), Food and Drug Administration, Washington, DC 20204, USA. tac@vax8.cfsan.fda.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8895473" target="_blank"〉PubMed〈/a〉
    Keywords: *Adenosine Triphosphatases ; Bacterial Proteins/genetics ; Biological Evolution ; Cloning, Molecular ; DNA Repair/genetics ; *DNA-Binding Proteins ; Disease Outbreaks ; Drug Resistance, Microbial/genetics ; Escherichia coli/*genetics/*pathogenicity ; Escherichia coli Infections/epidemiology/microbiology ; Escherichia coli O157/genetics/pathogenicity ; *Escherichia coli Proteins ; Food Microbiology ; Genetic Complementation Test ; Humans ; Molecular Sequence Data ; MutS DNA Mismatch-Binding Protein ; *Mutation ; Phenotype ; Polymerase Chain Reaction ; Recombination, Genetic ; Salmonella/*genetics/*pathogenicity ; Salmonella Food Poisoning/epidemiology/microbiology ; Selection, Genetic ; Sequence Deletion ; Sigma Factor/genetics ; Virulence/genetics
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    Site-directed hydroxyl radical probing of the rRNA neighborhood of ribosomal protein S5 (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-14
    Description: Cysteine residues were introduced into three different positions distributed on the surface of ribosomal protein S5, to serve as targets for derivatization with an Fe(II)-ethyl-enediaminetetraacetic acid linker. Hydroxyl radicals generated locally from the tethered Fe(II) in intermediate ribonucleoprotein particles or in 30S ribosomal subunits reconstituted from derivatized S5 caused cleavage of the RNA, resulting in characteristically different cleavage patterns for the three different tethering positions. These findings provide constraints for the three-dimensional folding of 16S ribosomal RNA (rRNA) and for the orientation of S5 in the 30S subunit, and they further suggest that antibiotic resistance and accuracy mutations in S5 may involve perturbation of 16S rRNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heilek, G M -- Noller, H F -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1659-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular Biology of RNA, Sinsheimer Laboratories, University of California, Santa Cruz 95064, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658142" target="_blank"〉PubMed〈/a〉
    Keywords: Anti-Bacterial Agents/pharmacology ; Cloning, Molecular ; Cysteine/chemistry ; Edetic Acid/analogs & derivatives ; Escherichia coli ; Ferrous Compounds/chemistry ; Hydroxyl Radical/*chemistry ; Models, Molecular ; Molecular Probes ; Mutagenesis, Site-Directed ; Nucleic Acid Conformation ; Organometallic Compounds ; Protein Conformation ; RNA, Ribosomal/*chemistry ; RNA, Ribosomal, 16S/chemistry/drug effects ; Ribosomal Proteins/*chemistry/genetics ; Spectinomycin/pharmacology
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    Regulation of rate of cartilage differentiation by Indian hedgehog and PTH-related protein (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-02
    Description: Proper regulation of chondrocyte differentiation is necessary for the morphogenesis of skeletal elements, yet little is known about the molecular regulation of this process. A chicken homolog of Indian hedgehog (Ihh), a member of the conserved Hedgehog family of secreted proteins that is expressed during bone formation, has now been isolated. Ihh has biological properties similar to those of Sonic hedgehog (Shh), including the ability to regulate the conserved targets Patched (Ptc) and Gli. Ihh is expressed in the prehypertrophic chondrocytes of cartilage elements, where it regulates the rate of hypertrophic differentiation. Misexpression of Ihh prevents proliferating chondrocytes from initiating the hypertrophic differentiation process. The direct target of Ihh signaling is the perichondrium, where Gli and Ptc flank the expression domain of Ihh. Ihh induces the expression of a second signal, parathyroid hormone-related protein (PTHrP), in the periarticular perichondrium. Analysis of PTHrP (-/-) mutant mice indicated that the PTHrP protein signals to its receptor in the prehypertrophic chondrocytes, thereby blocking hypertrophic differentiation. In vitro application of Hedgehog or PTHrP protein to normal or PTHrP (-/-) limb explants demonstrated that PTHrP mediates the effects of Ihh through the formation of a negative feedback loop that modulates the rate of chondrocyte differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vortkamp, A -- Lee, K -- Lanske, B -- Segre, G V -- Kronenberg, H M -- Tabin, C J -- DK47038/DK/NIDDK NIH HHS/ -- DK4723/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 2;273(5275):613-22.〈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/8662546" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Bone Development ; Cartilage/*cytology/metabolism ; Cell Differentiation ; Cell Division ; Chick Embryo ; Cloning, Molecular ; Culture Techniques ; Extremities/embryology ; Feedback ; Gene Expression Regulation ; Growth Plate/*cytology/metabolism ; Hedgehog Proteins ; Mice ; Molecular Sequence Data ; Morphogenesis ; *Osteogenesis ; Parathyroid Hormone ; Parathyroid Hormone-Related Protein ; Phenotype ; Proteins/pharmacology/*physiology ; Receptor, Parathyroid Hormone, Type 1 ; Receptors, Parathyroid Hormone/physiology ; Signal Transduction ; *Trans-Activators
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    Gastric mucosa abnormalities and tumorigenesis in mice lacking the pS2 trefoil protein (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-11
    Description: To determine the function of the pS2 trefoil protein, which is normally expressed in the gastric mucosa, the mouse pS2 (mpS2) gene was inactivated. The antral and pyloric gastric mucosa of mpS2-null mice was dysfunctional and exhibited severe hyperplasia and dysplasia. All homozygous mutant mice developed antropyloric adenoma, and 30 percent developed multifocal intraepithelial or intramucosal carcinomas. The small intestine was characterized by enlarged villi and an abnormal infiltrate of lymphoid cells. These results indicate that mpS2 is essential for normal differentiation of the antral and pyloric gastric mucosa and may function as a gastric-specific tumor suppressor gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lefebvre, O -- Chenard, M P -- Masson, R -- Linares, J -- Dierich, A -- LeMeur, M -- Wendling, C -- Tomasetto, C -- Chambon, P -- Rio, M C -- New York, N.Y. -- Science. 1996 Oct 11;274(5285):259-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS/INSERM/Universite Louis Pasteur/College de France, Communaute Urbaine de Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8824193" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoma/etiology/pathology ; Animals ; Base Sequence ; Cell Differentiation ; Cloning, Molecular ; Female ; Gastric Mucosa/cytology/*pathology ; Gene Targeting ; Genes, Tumor Suppressor ; Intestinal Mucosa/cytology/*pathology ; Male ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Neoplasm Proteins/genetics/*physiology ; Phenotype ; *Proteins ; Pyloric Antrum ; Stomach Neoplasms/*etiology/pathology ; Tumor Suppressor Proteins
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    Arabidopsis AUX1 gene: a permease-like regulator of root gravitropism (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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
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    Cdc13p: a single-strand telomeric DNA-binding protein with a dual role in yeast telomere maintenance (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-11
    Description: The CDC13 gene has previously been implicated in the maintenance of telomere integrity in Saccharomyces cerevisiae. With the use of two classes of mutations, here it is shown that CDC13 has two discrete roles at the telomere. The cdc13-2est mutation perturbs a function required in vivo for telomerase regulation but not in vitro for enzyme activity, whereas cdc13-1ts defines a separate essential role at the telomere. In vitro, purified Cdc13p binds to single-strand yeast telomeric DNA. Therefore, Cdc13p is a telomere-binding protein required to protect the telomere and mediate access of telomerase to the chromosomal terminus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nugent, C I -- Hughes, T R -- Lue, N F -- Lundblad, V -- New York, N.Y. -- Science. 1996 Oct 11;274(5285):249-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Human Genetics and Cell and Molecular Biology Program, 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/8824190" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Cloning, Molecular ; Cyclin B ; Cyclins/genetics/*metabolism ; DNA, Fungal/metabolism ; DNA, Single-Stranded/metabolism ; DNA-Binding Proteins/*metabolism ; Fungal Proteins/genetics ; Genes, Fungal ; Molecular Sequence Data ; Mutation ; Phenotype ; Saccharomyces cerevisiae/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Telomerase/genetics/*metabolism ; Telomere/*metabolism
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    A K+ channel worthy of attention (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-09-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hille, B -- New York, N.Y. -- Science. 1996 Sep 20;273(5282):1677.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, University of Washington, Seattle, 98195-7290, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8830412" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Attention/*physiology ; Calcium/*metabolism ; Cloning, Molecular ; Cyclic AMP/metabolism ; Humans ; Norepinephrine/metabolism ; Phosphorylation ; Potassium Channels/metabolism/*physiology ; *Potassium Channels, Calcium-Activated ; Rats ; Small-Conductance Calcium-Activated Potassium Channels
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    Identification of D-peptide ligands through mirror-image phage display (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    NF-AT-Driven interleukin-4 transcription potentiated by NIP45 (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Compensatory ahpC gene expression in isoniazid-resistant Mycobacterium tuberculosis (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    A subfamily of P-type ATPases with aminophospholipid transporting activity (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Signal transduction by DR3, a death domain-containing receptor related to TNFR-1 and CD95 (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-08
    Description: Tumor necrosis factor receptor-1 (TNFR-1) and CD95 (also called Fas or APO-1) are cytokine receptors that engage the apoptosis pathway through a region of intracellular homology, designated the "death domain." Another death domain-containing member of the TNFR family, death receptor 3 (DR3), was identified and was shown to induce both apoptosis and activation of nuclear factor kappaB. Expression of DR3 appears to be restricted to tissues enriched in lymphocytes. DR3 signal transduction is mediated by a complex of intracellular signaling molecules including TRADD, TRAF2, FADD, and FLICE. Thus, DR3 likely plays a role in regulating lymphocyte homeostasis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chinnaiyan, A M -- O'Rourke, K -- Yu, G L -- Lyons, R H -- Garg, M -- Duan, D R -- Xing, L -- Gentz, R -- Ni, J -- Dixit, V M -- GM-07863/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 8;274(5289):990-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of Michigan Medical School, Ann Arbor, MI 48109, USA. Sciences Inc., 9620 Medical Center Driv.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8875942" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Antigens, CD95/chemistry/physiology ; *Apoptosis ; Carrier Proteins/metabolism ; Caspase 8 ; Caspase 9 ; *Caspases ; Cloning, Molecular ; Cysteine Endopeptidases/metabolism ; Fas-Associated Death Domain Protein ; Gene Library ; Humans ; Lymphocytes ; Molecular Sequence Data ; NF-kappa B/*physiology ; Organ Specificity ; Proteins/metabolism ; RNA, Messenger/analysis/genetics ; Receptors, Tumor Necrosis Factor/chemistry/genetics/*physiology ; Receptors, Tumor Necrosis Factor, Member 25 ; Sequence Alignment ; *Signal Transduction ; TNF Receptor-Associated Factor 1 ; TNF Receptor-Associated Factor 2 ; Transfection ; Tumor Cells, Cultured
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    The cytolytic P2Z receptor for extracellular ATP identified as a P2X receptor (P2X7) (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-03
    Description: The P2Z receptor is responsible for adenosine triphosphate (ATP)-dependent lysis of macrophages through the formation of membrane pores permeable to large molecules. Other ATP-gated channels, the P2X receptors, are permeable only to small cations. Here, an ATP receptor, the P2X7 receptor, was cloned from rat brain and exhibited both these properties. This protein is homologous to other P2X receptors but has a unique carboxyl-terminal domain that was required for the lytic actions of ATP. Thus, the P2X7 (or P2Z) receptor is a bifunctional molecule that could function in both fast synaptic transmission and the ATP-mediated lysis of antigen-presenting cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Surprenant, A -- Rassendren, F -- Kawashima, E -- North, R A -- Buell, G -- New York, N.Y. -- Science. 1996 May 3;272(5262):735-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Glaxo Institute for Molecular Biology, Geneva, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614837" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/analogs & derivatives/*metabolism/pharmacology ; Amino Acid Sequence ; Animals ; Base Sequence ; Cations, Divalent/pharmacology ; Cell Death ; Cell Line ; Cloning, Molecular ; DNA, Complementary/genetics ; Electric Conductivity ; Humans ; Ion Channels/physiology ; Mice ; Molecular Sequence Data ; Patch-Clamp Techniques ; Rats ; Receptors, Purinergic P2/chemistry/genetics/*physiology ; Receptors, Purinergic P2X7 ; Transfection
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    Researchers find the reset button for the fruit fly clock (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1996 Mar 22;271(5256):1671-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596926" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Clocks/genetics ; *Circadian Rhythm/genetics ; Cloning, Molecular ; *Drosophila Proteins ; Drosophila melanogaster/genetics/*physiology ; Gene Expression Regulation ; Genes, Insect ; *Light ; Mutation ; Nuclear Proteins/genetics/*metabolism ; Period Circadian Proteins ; Proteins/genetics/*metabolism ; RNA, Messenger/genetics/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    No "End of History" for photolyases (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sancar, A -- New York, N.Y. -- Science. 1996 Apr 5;272(5258):48-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of Nor Carolina School of Medicine, Chapel Hill, 27599, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8600535" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; Cryptochromes ; DNA/*metabolism/radiation effects ; DNA Damage ; DNA Repair ; Deoxyribodipyrimidine Photo-Lyase/chemistry/genetics/*metabolism ; Drosophila/enzymology/genetics ; *Drosophila Proteins ; *Eye Proteins ; *Flavoproteins ; Humans ; *Photoreceptor Cells, Invertebrate ; Plant Proteins/chemistry/metabolism ; Pyrimidine Dimers/*metabolism ; Receptors, G-Protein-Coupled ; Signal Transduction ; Ultraviolet Rays
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    TAB1: an activator of the TAK1 MAPKKK in TGF-beta signal transduction (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-24
    Description: Transforming growth factor-beta (TGF-beta) regulates many aspects of cellular function. A member of the mitogen-activated protein kinase kinase kinase (MAPKKK) family, TAK1, was previously identified as a mediator in the signaling pathway of TGF-beta superfamily members. The yeast two-hybrid system has now revealed two human proteins, termed TAB1 and TAB2 (for TAK1 binding protein), that interact with TAK1. TAB1 and TAK1 were co-immunoprecipitated from mammalian cells. Overproduction of TAB1 enhanced activity of the plasminogen activator inhibitor 1 gene promoter, which is regulated by TGF-beta, and increased the kinase activity of TAK1. TAB1 may function as an activator of the TAK1 MAPKKK in TGF-beta signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shibuya, H -- Yamaguchi, K -- Shirakabe, K -- Tonegawa, A -- Gotoh, Y -- Ueno, N -- Irie, K -- Nishida, E -- Matsumoto, K -- New York, N.Y. -- Science. 1996 May 24;272(5265):1179-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638164" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/chemistry/*metabolism ; Cell Line ; Cloning, Molecular ; Enzyme Activation ; Genes, Reporter ; Humans ; *Intracellular Signaling Peptides and Proteins ; *MAP Kinase Kinase Kinases ; Mice ; Molecular Sequence Data ; Plasminogen Activator Inhibitor 1/genetics ; Promoter Regions, Genetic ; Protein-Serine-Threonine Kinases/*metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/genetics/metabolism ; *Signal Transduction ; Transfection ; Transformation, Genetic ; Transforming Growth Factor beta/*metabolism
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    An RNA polymerase II elongation factor encoded by the human ELL gene (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-29
    Description: The human ELL gene on chromosome 19 undergoes frequent translocations with the trithorax-like MLL gene on chromosome 11 in acute myeloid leukemias. Here, ELL was shown to encode a previously uncharacterized elongation factor that can increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by polymerase at multiple sites along the DNA. Functionally, ELL resembles Elongin (SIII), a transcription elongation factor regulated by the product of the von Hippel-Lindau (VHL) tumor suppressor gene. The discovery of a second elongation factor implicated in oncogenesis provides further support for a close connection between the regulation of transcription elongation and cell growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shilatifard, A -- Lane, W S -- Jackson, K W -- Conaway, R C -- Conaway, J W -- GM41628/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Mar 29;271(5257):1873-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Molecular and Cell Biology, Oklahoma Medical Research Foundation, Oklahoma City, 73104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596958" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cloning, Molecular ; DNA-Binding Proteins/chemistry/*genetics/metabolism ; Genes, Tumor Suppressor ; Histone-Lysine N-Methyltransferase ; Humans ; Leukemia/genetics ; Molecular Sequence Data ; Myeloid-Lymphoid Leukemia Protein ; *Neoplasm Proteins ; *Peptide Elongation Factors ; *Proto-Oncogenes ; RNA Polymerase II/*metabolism ; RNA, Messenger/genetics/metabolism ; Rats ; Recombinant Proteins/metabolism ; Transcription Factors/chemistry/*genetics/metabolism ; Transcription, Genetic ; Transcriptional Elongation Factors ; Translocation, Genetic ; von Hippel-Lindau Disease/genetics
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    Sequence similarity between the 73-kilodalton protein of mammalian CPSF and a subunit of yeast polyadenylation factor I (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-29
    Description: The 3' ends of most eukaryotic messenger RNAs are generated by endonucleolytic cleavage and polyadenylation. In mammals, the cleavage and polyadenylation specificity factor (CPSF) plays a central role in both steps of the processing reaction. Here, the cloning of the 73-kilodalton subunit of CPSF is reported. Sequence analyses revealed that a yeast protein (Ysh1) was highly similar to the 73-kD polypeptide. Ysh1 constitutes a new subunit of polyadenylation factor I (PFI), which has a role in yeast pre-mRNA 3'-end formation. This finding was unexpected because in contrast to CPSF, PFI is only required for the polyadenylation reaction. These results contribute to the understanding of how 3'-end processing factors may have evolved.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jenny, A -- Minvielle-Sebastia, L -- Preker, P J -- Keller, W -- New York, N.Y. -- Science. 1996 Nov 29;274(5292):1514-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Biozentrum, University of Basel, CH-4056 Basel, Switzerland. Keller2@ubaclu.unibas.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8929409" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cloning, Molecular ; Evolution, Molecular ; Fungal Proteins/*chemistry/genetics/metabolism ; Humans ; Molecular Sequence Data ; Molecular Weight ; Poly A/metabolism ; Polynucleotide Adenylyltransferase/metabolism ; RNA Precursors/metabolism ; RNA Processing, Post-Transcriptional ; RNA, Fungal/metabolism ; RNA, Messenger/metabolism ; RNA-Binding Proteins/*chemistry/genetics/metabolism ; Sequence Homology, Amino Acid ; mRNA Cleavage and Polyadenylation Factors
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    Molecular cloning and disease association of hepatitis G virus: a transfusion-transmissible agent (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-26
    Description: An RNA virus, designated hepatitis G virus (HGV), was identified from the plasma of a patient with chronic hepatitis. Extension from an immunoreactive complementary DNA clone yielded the entire genome (9392 nucleotides) encoding a polyprotein of 2873 amino acids. The virus is closely related to GB virus C (GBV-C) and distantly related to hepatitis C virus, GBV-A, and GBV-B. HGV was associated with acute and chronic hepatitis. Persistent viremia was detected for up to 9 years in patients with hepatitis. The virus is transfusion-transmissible. It has a global distribution and is present within the volunteer blood donor population in the United States.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Linnen, J -- Wages, J Jr -- Zhang-Keck, Z Y -- Fry, K E -- Krawczynski, K Z -- Alter, H -- Koonin, E -- Gallagher, M -- Alter, M -- Hadziyannis, S -- Karayiannis, P -- Fung, K -- Nakatsuji, Y -- Shih, J W -- Young, L -- Piatak, M Jr -- Hoover, C -- Fernandez, J -- Chen, S -- Zou, J C -- Morris, T -- Hyams, K C -- Ismay, S -- Lifson, J D -- Hess, G -- Foung, S K -- Thomas, H -- Bradley, D -- Margolis, H -- Kim, J P -- New York, N.Y. -- Science. 1996 Jan 26;271(5248):505-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genelabs Technologies, Redwood City, CA 94063, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8560265" target="_blank"〉PubMed〈/a〉
    Keywords: Acute Disease ; Amino Acid Sequence ; Base Sequence ; Blood Donors ; Blood Transfusion/*adverse effects ; Blood-Borne Pathogens ; Chronic Disease ; Cloning, Molecular ; Consensus Sequence ; Disease Transmission, Infectious ; Flaviviridae/genetics ; Genome, Viral ; Hepatitis Viruses/chemistry/*genetics/isolation & purification ; Hepatitis, Viral, Human/epidemiology/transmission/*virology ; Humans ; Molecular Sequence Data ; Polymerase Chain Reaction ; RNA Viruses/chemistry/*genetics/isolation & purification ; RNA, Viral/blood/genetics ; Sequence Alignment ; United States/epidemiology ; Viral Proteins/chemistry/genetics ; Viremia/epidemiology/virology
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    Interaction between a putative mechanosensory membrane channel and a collagen (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-19
    Description: The degenerin family of proteins in Caenorhabditis elegans is homologous to subunits of the mammalian amiloride-sensitive epithelial sodium channels. Mutations in nematode degenerins cause cell death, probably because of defects in channel function. Genetic evidence was obtained that the unc-105 gene product represents a degenerin homolog affecting C. elegans muscles and that this putative channel interacts with type IV collagen in the extracellular matrix underlying the muscle cell. This interaction may serve as a mechanism of stretch-activated muscle contraction, and this system could provide a molecular model for the activation of mechanosensitive ion channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, J -- Schrank, B -- Waterston, R H -- GM23883/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 19;273(5273):361-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, 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/8662524" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Base Sequence ; Caenorhabditis elegans/chemistry/genetics/*metabolism ; *Caenorhabditis elegans Proteins ; Cloning, Molecular ; Collagen/*metabolism ; Extracellular Matrix/metabolism ; Genes, Helminth ; Genetic Complementation Test ; Helminth Proteins/chemistry/genetics/*metabolism/*physiology ; Ion Channel Gating ; Models, Biological ; Molecular Sequence Data ; Muscle Contraction ; Muscles/physiology ; Mutation ; Sensation ; Signal Transduction ; Sodium Channels/chemistry/genetics/*metabolism/*physiology ; Suppression, Genetic
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    HIV quasispecies and resampling (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, S L -- Rodrigo, A G -- Shankarappa, R -- Learn, G H -- Hsu, L -- Davidov, O -- Zhao, L P -- Mullins, J I -- New York, N.Y. -- Science. 1996 Jul 26;273(5274):415-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8677432" target="_blank"〉PubMed〈/a〉
    Keywords: Cloning, Molecular ; DNA, Viral/genetics ; *Genetic Variation ; HIV/classification/*genetics ; Humans ; Leukocytes, Mononuclear/virology ; Polymerase Chain Reaction ; Probability ; Sample Size ; Sequence Analysis, DNA
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    Interleukin-1 research (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-09-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hopp, T P -- New York, N.Y. -- Science. 1996 Sep 27;273(5283):1781.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8815535" target="_blank"〉PubMed〈/a〉
    Keywords: Cloning, Molecular ; *Interleukin-1/chemistry/genetics/isolation & purification ; *Research
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    Accessing genetic information with high-density DNA arrays (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-25
    Description: Rapid access to genetic information is central to the revolution taking place in molecular genetics. The simultaneous analysis of the entire human mitochondrial genome is described here. DNA arrays containing up to 135,000 probes complementary to the 16.6-kilobase human mitochondrial genome were generated by light-directed chemical synthesis. A two-color labeling scheme was developed that allows simultaneous comparison of a polymorphic target to a reference DNA or RNA. Complete hybridization patterns were revealed in a matter of minutes. Sequence polymorphisms were detected with single-base resolution and unprecedented efficiency. The methods described are generic and can be used to address a variety of questions in molecular genetics including gene expression, genetic linkage, and genetic variability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chee, M -- Yang, R -- Hubbell, E -- Berno, A -- Huang, X C -- Stern, D -- Winkler, J -- Lockhart, D J -- Morris, M S -- Fodor, S P -- 5RO1HG00813/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):610-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Affymetrix, 3380 Central Expressway, Santa Clara, CA 95051, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8849452" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Base Composition ; Base Sequence ; Cloning, Molecular ; DNA, Mitochondrial/*genetics ; Fluorescein ; Fluoresceins ; Gene Expression ; Genetic Variation ; *Genome ; Humans ; Mitochondria/*genetics ; *Nucleic Acid Hybridization ; *Oligonucleotide Probes ; Phycoerythrin ; Polymerase Chain Reaction ; Polymorphism, Genetic ; Sequence Analysis, DNA
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    A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-19
    Description: Trapoxin is a microbially derived cyclotetrapeptide that inhibits histone deacetylation in vivo and causes mammalian cells to arrest in the cell cycle. A trapoxin affinity matrix was used to isolate two nuclear proteins that copurified with histone deacetylase activity. Both proteins were identified by peptide microsequencing, and a complementary DNA encoding the histone deacetylase catalytic subunit (HD1) was cloned from a human Jurkat T cell library. As the predicted protein is very similar to the yeast transcriptional regulator Rpd3p, these results support a role for histone deacetylase as a key regulator of eukaryotic transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taunton, J -- Hassig, C A -- Schreiber, S L -- New York, N.Y. -- Science. 1996 Apr 19;272(5260):408-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8602529" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Anti-Bacterial Agents/metabolism/pharmacology ; Cattle ; Cell Cycle/drug effects ; Cloning, Molecular ; Enzyme Inhibitors/metabolism/pharmacology ; Fungal Proteins/chemistry/genetics/*metabolism ; *Gene Expression Regulation ; Histone Deacetylase Inhibitors ; Histone Deacetylases/chemistry/genetics/isolation & purification/*metabolism ; Humans ; Hydroxamic Acids/metabolism/pharmacology ; Molecular Sequence Data ; Molecular Weight ; *Peptides ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins ; T-Lymphocytes/enzymology ; Transcription Factors/chemistry/genetics/isolation & purification/*metabolism ; *Transcription, Genetic ; Tumor Cells, Cultured
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    GS28, a 28-kilodalton Golgi SNARE that participates in ER-Golgi transport (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-24
    Description: Little is known about the integral membrane proteins that participate in the early secretory pathway of mammalian cells. The complementary DNA encoding a 28-kilodalton protein (p28) of the cis-Golgi was cloned and sequenced. The protein was predicted to contain a central coiled-coil domain with a carboxyl-terminal membrane anchor. An in vitro assay for endoplasmic reticulum-Golgi transport was used to show that p28 participates in the docking and fusion stage of this transport event. Biochemical studies established that p28 is a core component of the Golgi SNAP receptor (SNARE) complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Subramaniam, V N -- Peter, F -- Philp, R -- Wong, S H -- Hong, W -- New York, N.Y. -- Science. 1996 May 24;272(5265):1161-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Membrane Biology Laboratory, Institute of Molecular and Cell Biology, National University of Singapore.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638159" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Biological Transport ; Carrier Proteins/analysis ; Cell Line ; Cloning, Molecular ; DNA, Complementary/genetics ; Egtazic Acid/pharmacology ; Endoplasmic Reticulum/*metabolism ; Golgi Apparatus/*chemistry/metabolism ; *Membrane Glycoproteins ; Membrane Proteins/analysis/*chemistry/genetics/isolation & ; purification/*metabolism ; Molecular Sequence Data ; N-Ethylmaleimide-Sensitive Proteins ; SNARE Proteins ; Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins ; *Vesicular Transport Proteins ; Vesicular stomatitis Indiana virus ; Viral Envelope Proteins/metabolism
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    Probing flowers' genetic past (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-09-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1996 Sep 6;273(5280):1339.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8801629" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*genetics/growth & development ; Cloning, Molecular ; *Genes, Plant
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    Complementary DNA for 12-kilodalton B cell growth factor: misassigned (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kovanen, P E -- Harju, L -- Timonen, T -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):629-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8928011" target="_blank"〉PubMed〈/a〉
    Keywords: Cells, Cultured ; Cloning, Molecular ; DNA Probes ; DNA, Complementary/*genetics ; Humans ; Interleukin-4/*genetics ; Leukocytes, Mononuclear/chemistry ; Lymphocyte Activation ; Lymphokines/*genetics ; Molecular Sequence Data ; RNA Probes ; RNA, Messenger/genetics ; Repetitive Sequences, Nucleic Acid
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Similarity among the Drosophila (6-4)photolyase, a human photolyase homolog, and the DNA photolyase-blue-light photoreceptor family (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-05
    Description: Ultraviolet light (UV)-induced DNA damage can be repaired by DNA photolyase in a light-dependent manner. Two types of photolyase are known, one specific for cyclobutane pyrimidine dimers (CPD photolyase) and another specific for pyrimidine (6-4) pyrimidone photoproducts[(6-4)photolyase]. In contrast to the CPD photolyase, which has been detected in a wide variety of organisms, the (6-4)photolyase has been found only in Drosophila melanogaster. In the present study a gene encoding the Drosophila(6-4)photolyase ws cloned, and the deduced amino acid sequence of the product was found to be similar to the CPD photolyase and to the blue-light photoreceptor of plants. A homolog of the Drosophila (6-4)photolyase gene was also cloned from human cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Todo, T -- Ryo, H -- Yamamoto, K -- Toh, H -- Inui, T -- Ayaki, H -- Nomura, T -- Ikenaga, M -- New York, N.Y. -- Science. 1996 Apr 5;272(5258):109-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Radiation Biology Center, Kyoto University, Kyoto, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8600518" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cloning, Molecular ; DNA Repair ; DNA, Complementary/genetics ; Deoxyribodipyrimidine Photo-Lyase/*chemistry/genetics/metabolism ; Drosophila melanogaster/*enzymology/genetics ; Flavin-Adenine Dinucleotide/metabolism ; Genes, Insect ; Humans ; Light ; Molecular Sequence Data ; Photoreceptor Cells, Invertebrate/*chemistry ; Plant Proteins/*chemistry ; Recombinant Proteins/chemistry/metabolism ; Sequence Alignment ; Ultraviolet Rays
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    Purification and molecular cloning of Plx1, a Cdc25-regulatory kinase from Xenopus egg extracts (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-09-06
    Description: Cdc2, the cyclin-dependent kinase that controls mitosis, is negatively regulated by phosphorylation on its threonine-14 and tyrosine-15 residues. Cdc25, the phosphatase that dephosphorylates both of these residues, undergoes activation and phosphorylation by multiple kinases at mitosis. Plx1, a kinase that associates with and phosphorylates the amino-terminal domain of Cdc25, was purified extensively from Xenopus egg extracts. Cloning of its complementary DNA revealed that Plx1 is related to the Polo family of protein kinases. Recombinant Plx1 phosphorylated Cdc25 and stimulated its activity in a purified system. Cdc25 phosphorylated by Plx1 reacted strongly with MPM-2, a monoclonal antibody to mitotic phosphoproteins. These studies indicate that Plx1 may participate in control of mitotic progression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kumagai, A -- Dunphy, W G -- New York, N.Y. -- Science. 1996 Sep 6;273(5280):1377-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, 216-76, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703070" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; CDC2 Protein Kinase/metabolism ; Cell Cycle Proteins/chemistry/*metabolism ; Cloning, Molecular ; Cyclins/metabolism ; Enzyme Activation ; Molecular Sequence Data ; Mutation ; Oocytes/enzymology ; Peptide Mapping ; Phosphoprotein Phosphatases/chemistry/*metabolism ; Phosphorylation ; Phosphoserine/analysis ; Phosphothreonine/analysis ; Protein-Serine-Threonine Kinases/chemistry/genetics/*isolation & ; purification/metabolism ; Recombinant Proteins/metabolism ; Xenopus ; *Xenopus Proteins ; cdc25 Phosphatases
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    Enzymatic synthesis of a quorum-sensing autoinducer through use of defined substrates (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-14
    Description: Many bacteria, including several pathogens of plants and humans, use a pheromone called an autoinducer to regulate gene expression in a cell density-dependent manner. Agrobacterium autoinducer [AAI, N-(3-oxo-octanoyl)-L-homoserine lactone] of A. tumefaciens is synthesized by the Tral protein, which is encoded by the tumor-inducing plasmid. Purified hexahistidinyl-Tral (H6-Tral) used S-adenosylmethionine to make the homoserine lactone moiety of AAI, but did not use related compounds. H6-Tral used 3-oxo-octanoyl-acyl carrier protein to make the 3-oxo-octanoyl moiety of AAI, but did not use 3-oxo-octanoyl-coenzyme A. These results demonstrate the enzymatic synthesis of an autoinducer through the use of purified substrates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉More, M I -- Finger, L D -- Stryker, J L -- Fuqua, C -- Eberhard, A -- Winans, S C -- GM42893/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1655-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Microbiology, Cornell University, Ithaca, New York 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658141" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase/antagonists & inhibitors/metabolism ; Acyl Carrier Protein/metabolism ; Agrobacterium tumefaciens/*genetics/metabolism ; Base Sequence ; Cerulenin/pharmacology ; Chromatography, Gel ; Chromatography, High Pressure Liquid ; Cloning, Molecular ; DNA Helicases/*metabolism ; DNA Primers ; Escherichia coli ; Escherichia coli Proteins ; Fatty Acids/metabolism ; *Gene Expression Regulation, Bacterial/drug effects ; Homoserine/*analogs & derivatives/biosynthesis ; Malonyl Coenzyme A/metabolism ; Molecular Sequence Data ; NADP/metabolism ; Plasmids ; S-Adenosylmethionine/metabolism
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    Phenotypes of mouse diabetes and rat fatty due to mutations in the OB (leptin) receptor (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-16
    Description: Mice harboring mutations in the obese (ob) and diabetes (db) genes display similar phenotypes, and it has been proposed that these genes encode the ligand and receptor, respectively, for a physiologic pathway that regulates body weight. The cloning of ob, and the demonstration that it encodes a secreted protein (leptin) that binds specifically to a receptor (OB-R) in the brain, have validated critical aspects of this hypothesis. Here it is shown by genetic mapping and genomic analysis that mouse db, rat fatty (a homolog of db), and the gene encoding the OB-R are the same gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chua, S C Jr -- Chung, W K -- Wu-Peng, X S -- Zhang, Y -- Liu, S M -- Tartaglia, L -- Leibel, R L -- DK26687/DK/NIDDK NIH HHS/ -- DK47473/DK/NIDDK NIH HHS/ -- HD28047/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1996 Feb 16;271(5251):994-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Human Behavior and Metabolism, Rockefeller University, New York 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8584938" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Blotting, Southern ; Carrier Proteins/*genetics ; Chromosome Mapping ; Cloning, Molecular ; DNA Mutational Analysis ; Diabetes Mellitus/*genetics ; Genetic Markers ; Leptin ; Mice ; Mice, Inbred C57BL ; Mice, Inbred Strains ; Molecular Sequence Data ; Obesity/*genetics ; Phenotype ; Polymerase Chain Reaction ; Proteins/genetics ; Rats ; Rats, Inbred Strains ; *Receptors, Cell Surface ; Receptors, Cytokine/*genetics ; Receptors, Leptin
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    PTH/PTHrP receptor in early development and Indian hedgehog-regulated bone growth (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-02
    Description: The PTH/PTHrP receptor binds to two ligands with distinct functions: the calcium-regulating hormone, parathyroid hormone (PTH), and the paracrine factor, PTH-related protein (PTHrP). Each ligand, in turn, is likely to activate more than one receptor. The functions of the PTH/PTHrP receptor were investigated by deletion of the murine gene by homologous recombination. Most PTH/PTHrP receptor (-/-) mutant mice died in mid-gestation, a phenotype not observed in PTHrP (-/-) mice, perhaps because of the effects of maternal PTHrP. Mice that survived exhibited accelerated differentiation of chondrocytes in bone, and their bones, grown in explant culture, were resistant to the effects of PTHrP and Sonic hedgehog. These results suggest that the PTH/PTHrP receptor mediates the effects of Indian Hedgehog and PTHrP on chondrocyte differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lanske, B -- Karaplis, A C -- Lee, K -- Luz, A -- Vortkamp, A -- Pirro, A -- Karperien, M -- Defize, L H -- Ho, C -- Mulligan, R C -- Abou-Samra, A B -- Juppner, H -- Segre, G V -- Kronenberg, H M -- DK 47038/DK/NIDDK NIH HHS/ -- DK 47237/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 2;273(5275):663-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Endocrine Unit, Massachusetts General Hospital and Harvard Medical School, Boston, MA 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662561" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Bone Development ; Cartilage/*cytology/metabolism ; Cell Differentiation ; Cell Division ; Cloning, Molecular ; Culture Techniques ; Feedback ; Gene Deletion ; Gene Targeting ; Growth Plate/*cytology/metabolism ; Hedgehog Proteins ; Mice ; Mice, Inbred C57BL ; Osteoblasts/cytology ; *Osteogenesis ; Parathyroid Hormone ; Parathyroid Hormone-Related Protein ; Protein Biosynthesis ; Proteins/pharmacology/physiology ; Receptor, Parathyroid Hormone, Type 1 ; Receptors, Parathyroid Hormone/genetics/*physiology ; Stem Cells ; *Trans-Activators
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    The immunological evolution of catalysis (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-02-23
    Description: The germline genes used by the mouse to generate the esterolytic antibody 48G7 were cloned and expressed in an effort to increase our understanding of the detailed molecular mechanisms by which the immune system evolves catalytic function. The nine replacement mutations that were fixed during affinity maturation increased affinity for the transition state analogue by a factor of 10(4), primarily the result of a decrease in the dissociation rate of the hapten-antibody complex. There was a corresponding increase in the rate of reaction of antibody with substrate, k(cat)/k(m), from 1.7 x 10(2)M(-1) min(-1) to 1.4 x 10(4)M(-1) min(-1). The three-dimensional crystal structure of the 48G7-transition state analogue complex at 2.0 angstroms resolution indicates that one of the nine residues in which somatic mutations have been fixed directly contact the hapten. Thus, in the case of 48G7, affinity maturation appears to play a conformational role, either in reorganizing the active site geometry of limiting side-chain and backbone flexibility of the germline antibody. The crystal structure and analysis of somatic and directed active site mutants underscore the role of transition state stabilization in the evolution of this catalytic antibody.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Patten, P A -- Gray, N S -- Yang, P L -- Marks, C B -- Wedemayer, G J -- Boniface, J J -- Stevens, R C -- Schultz, P G -- R01 AL24695/PHS HHS/ -- New York, N.Y. -- Science. 1996 Feb 23;271(5252):1086-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, 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/8599084" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Catalytic/chemistry/genetics/*immunology/metabolism ; Antibody Affinity ; Antigen-Antibody Complex ; Antigen-Antibody Reactions ; Base Sequence ; Binding Sites ; Catalysis ; Cloning, Molecular ; Crystallization ; Crystallography, X-Ray ; *Evolution, Molecular ; Genes, Immunoglobulin ; Haptens/immunology ; Immunoglobulin Fab Fragments/genetics/immunology ; Immunoglobulin Heavy Chains/genetics/immunology ; Immunoglobulin Light Chains/genetics/immunology ; Mice ; Molecular Sequence Data ; Mutation ; Protein Conformation
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    A cellular homolog of hepatitis delta antigen: implications for viral replication and evolution (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-04
    Description: Hepatitis delta virus (HDV) is a pathogenic human virus whose RNA genome and replication cycle resemble those of plant viroids. However, viroid genomes contain no open reading frames, whereas HDV RNA encodes a single protein, hepatitis delta antigen (HDAg), which is required for viral replication. A cellular gene whose product interacts with HDAg has now been identified, and this interaction was found to affect viral genomic replication in intact cells. DNA sequence analysis revealed that this protein, termed delta-interacting protein A (DIPA), is a cellular homolog of HDAg. These observations demonstrate that a host gene product can modulate HDV replication and suggest that HDV may have evolved from a primitive viroidlike RNA through capture of a cellular transcript.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brazas, R -- Ganem, D -- New York, N.Y. -- Science. 1996 Oct 4;274(5284):90-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of California, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8810253" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; *Biological Evolution ; Carrier Proteins/*chemistry/genetics/metabolism ; Cell Line ; Cloning, Molecular ; Genome, Viral ; Hepatitis Antigens/*chemistry/genetics/*metabolism ; Hepatitis Delta Virus/*genetics/physiology ; Hepatitis delta Antigens ; Humans ; Liver/chemistry ; Molecular Sequence Data ; RNA, Messenger/genetics ; RNA, Viral/genetics ; Repressor Proteins ; Sequence Alignment ; Transfection ; Tumor Cells, Cultured ; Viroids/genetics ; Virus Replication
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    Small peptides as potent mimetics of the protein hormone erythropoietin (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-07-26
    Description: Random phage display peptide libraries and affinity selective methods were used to isolate small peptides that bind to and activate the receptor for the cytokine erythropoietin (EPO). In a panel of in vitro biological assays, the peptides act as full agonists and they can also stimulate erythropoiesis in mice. These agonists are represented by a 14- amino acid disulfide-bonded, cyclic peptide with the minimum consensus sequence YXCXXGPXTWXCXP, where X represents positions allowing occupation by several amino acids. The amino acid sequences of these peptides are not found in the primary sequence of EPO. The signaling pathways activated by these peptides appear to be identical to those induced by the natural ligand. This discovery may form the basis for the design of small molecule mimetics of EPO.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wrighton, N C -- Farrell, F X -- Chang, R -- Kashyap, A K -- Barbone, F P -- Mulcahy, L S -- Johnson, D L -- Barrett, R W -- Jolliffe, L K -- Dower, W J -- New York, N.Y. -- Science. 1996 Jul 26;273(5274):458-64.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Affymax Research Institute, 4001 Miranda Avenue, Palo Alto, CA 94304, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662529" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacteriophages ; Cell Division/drug effects ; Cell Line ; Cloning, Molecular ; Erythropoiesis/drug effects ; Erythropoietin/chemistry/*metabolism/*pharmacology ; Humans ; Ligands ; Mice ; *Molecular Mimicry ; Molecular Sequence Data ; Mutagenesis ; Peptides, Cyclic/chemistry/*metabolism/*pharmacology ; Phosphorylation ; Protein Structure, Secondary ; Receptors, Erythropoietin/*agonists/chemistry/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Signal Transduction ; Solubility ; Tyrosine/metabolism
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    Human homolog of patched, a candidate gene for the basal cell nevus syndrome (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-06-14
    Description: The basal cell nevus syndrome (BCNS) is characterized by developmental abnormalities and by the postnatal occurrence of cancers, especially basal cell carcinomas (BCCs), the most common human cancer. Heritable mutations in BCNS patients and a somatic mutation in a sporadic BCC were identified in a human homolog of the Drosophila patched (ptc) gene. The ptc gene encodes a transmembrane protein that in Drosophila acts in opposition to the Hedgehog signaling protein, controlling cell fates, patterning, and growth in numerous tissues. The human PTC gene appears to be crucial for proper embryonic development and for tumor suppression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnson, R L -- Rothman, A L -- Xie, J -- Goodrich, L V -- Bare, J W -- Bonifas, J M -- Quinn, A G -- Myers, R M -- Cox, D R -- Epstein, E H Jr -- Scott, M P -- AR3995/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1668-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Biology, Howard Hughes Medical Institute, Stanford University School of Medicine, California 94305-5427, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658145" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Amino Acid Sequence ; Animals ; Basal Cell Nevus Syndrome/*genetics ; Base Sequence ; Cloning, Molecular ; DNA, Neoplasm ; Drosophila ; *Drosophila Proteins ; Female ; Frameshift Mutation ; *Genes, Tumor Suppressor ; Humans ; Insect Hormones/genetics ; Male ; Membrane Proteins/*genetics ; Middle Aged ; Molecular Sequence Data ; Polymerase Chain Reaction ; Polymorphism, Single-Stranded Conformational ; Protein Conformation ; Receptors, Cell Surface
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    Comparison of the nucleic acid sequence of anglerfish and mammalian insulin mRNA's from cloned cDNA's (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-12-19
    Description: Anglerfish (Lophius americanus) insulin complementary DNA was cloned in bacterial plasmids, and its sequence was determined. Fish insulin messenger RNA is larger (1.5 times) than the messenger RNA encoding mammalian (rat and human) insulin, in part because of a larger C peptide (an additional six amino acids or 18 nucleotides in length) but mainly because of increases in the 5' and 3' untranslated regions. Comparison of the fish, rat, and human insulin messenger RNA (from the complementary DNA) reveals that, in addition to the regions coding for the A and B peptides, sequence conservation is limited to a segment within the 5' untranslated region which may be involved in ribosomal binding, two small segments of the signal peptide, and two stretches of sequence in the 3' untranslated region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hobart, P M -- Shen, L P -- Crawford, R -- Pictet, R L -- Rutter, W J -- AM 21344/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1980 Dec 19;210(4476):1360-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7001633" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Biological Evolution ; Cloning, Molecular ; Codon ; Fishes/*genetics ; Insulin/*genetics ; Nucleic Acid Conformation ; Proinsulin/genetics ; Protein Biosynthesis ; Protein Precursors/genetics ; RNA, Messenger/*genetics
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    Genetic variation in the human insulin gene (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-08-01
    Description: Four recombinant lambda phages containing nucleotide sequences complementary to a cloned human preproinsulin DNA probe have been isolated from human DNA. Restriction analyses in conjunction with Southern hybridizations reveal two types of gene sequences. One isolate of each type was subjected to complete nucleotide sequence determination. The sequences contain the entire preproinsulin messenger RNA region, two intervening sequence. 260 nucleotides upstream from the messenger RNA capping site, and 35 nucleotides beyond the polyadenylate attachment site. Our results strongly suggest that these two gene types are allelic variants of a single insulin gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ullrich, A -- Dull, T J -- Gray, A -- Brosius, J -- Sures, I -- New York, N.Y. -- Science. 1980 Aug 1;209(4456):612-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6248962" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; *Dna ; DNA Restriction Enzymes ; DNA, Recombinant/metabolism ; *Genes ; Genetic Code ; *Genetic Variation ; Humans ; Insulin/*biosynthesis ; Nucleic Acid Hybridization ; Proinsulin/biosynthesis ; Rats ; Species Specificity
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Transformation by cloned Harvey murine sarcoma virus DNA: efficiency increased by long terminal repeat DNA (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-12-12
    Description: The coding sequences for the transforming (src) protein (p21) of Harvey murine sarcoma virus have been localized to a 1.3 kilobase pair segment near the 5' end of the viral genome. Ligation of the viral terminal repeat DNA to the left end of the src region DNA markedly enhanced the low transforming efficiency of the src region DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, E H -- Ellis, R W -- Scolnick, E M -- Lowy, D R -- New York, N.Y. -- Science. 1980 Dec 12;210(4475):1249-51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6254153" target="_blank"〉PubMed〈/a〉
    Keywords: *Cell Transformation, Viral ; Cloning, Molecular ; DNA, Viral/*genetics ; Genes, Viral ; Repetitive Sequences, Nucleic Acid ; Sarcoma Viruses, Murine/*genetics ; Transformation, Genetic ; Viral Proteins/genetics
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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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    Effect of interferon-alpha 1 from E. coli on some cell functions (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-09-19
    Description: Interferon-alpha 1 from Escherichia coli transformed with a hybrid plasmid containing a human leukocyte complementary DNA insert, induces resistance to virus in appropriate target cells. It also shares the following properties with natural leukocyte interferon (IFN). (i) It enhances natural killing activity of human lymphocytes, (ii) it enhances antibody-dependent cell-mediated cytotoxicity, (iii) it suppresses antigen- and mitogen-induced leukocyte migration inhibition, (iv) it inhibits growth of IFN-sensitive Burkitt lymphoma cells. Since these activities are exhibited by a cloned protein species, they are due to IFN itself and not to other human proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Masucci, M G -- Szigeti, R -- Klein, E -- Klein, G -- Gruest, J -- Montagnier, L -- Taira, H -- Hall, A -- Nagata, S -- Weissmann, C -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1431-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6158096" target="_blank"〉PubMed〈/a〉
    Keywords: Antibody-Dependent Cell Cytotoxicity/drug effects ; Cell Division/drug effects ; Cell Migration Inhibition ; Cloning, Molecular ; *DNA, Recombinant ; Escherichia coli ; Humans ; Hypersensitivity, Delayed/immunology ; Immunity, Cellular/drug effects ; Interferons/genetics/*pharmacology ; Structure-Activity Relationship
    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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    UCSD gene splicing incident ends unresolved (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-09-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wade, N -- New York, N.Y. -- Science. 1980 Sep 26;209(4464):1494-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7001622" target="_blank"〉PubMed〈/a〉
    Keywords: Advisory Committees ; California ; Cloning, Molecular ; Containment of Biohazards/*standards ; DNA, Viral/genetics ; History of Medicine ; Semliki forest virus/*genetics ; Sindbis Virus/*genetics ; Universities
    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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    Nucleotide sequence of human preproinsulin complementary DNA (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-04-04
    Description: Recombinant bacterial plasmids that contain DNA complementary to human preproinsulin messenger RNA have been constructed. One clone contains the entire preproinsulin coding region, as well as the 3' untranslated region of the messenger RNA and eight nucleotides of the 5' untranslated region. Additional sequence information for the 5' untranslated region was obtained with the use of insulinoma messenger RNA in conjunction with specific primers from the cloned DNA for enzymatic chain termination sequence analysis. The results confirm the amino acid sequence of human proinsulin previously determined, and predict the amino acid sequence of the human preproinsulin signal peptide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sures, I -- Goeddel, D V -- Gray, A -- Ullrich, A -- New York, N.Y. -- Science. 1980 Apr 4;208(4439):57-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6927840" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; DNA, Recombinant ; Humans ; Insulin ; Nucleic Acid Hybridization ; Nucleotides/*genetics ; Proinsulin/*genetics ; Protein Precursors/*genetics ; RNA, Messenger/*genetics
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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