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  • Mutation  (141)
  • Signal Transduction  (64)
  • Crystallography, X-Ray  (48)
  • American Association for the Advancement of Science (AAAS)  (227)
  • American Meteorological Society
  • PANGAEA
  • 2015-2019
  • 2000-2004
  • 1995-1999  (227)
  • 1996  (227)
Collection
Keywords
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  • American Association for the Advancement of Science (AAAS)  (227)
  • American Meteorological Society
  • PANGAEA
  • Springer  (4)
  • Wiley-Blackwell  (1)
Years
  • 2015-2019
  • 2000-2004
  • 1995-1999  (227)
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  • 1
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    IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-alpha- and obesity-induced insulin resistance (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-02
    Description: Tumor necrosis factor-alpha (TNF-alpha) is an important mediator of insulin resistance in obesity and diabetes through its ability to decrease the tyrosine kinase activity of the insulin receptor (IR). Treatment of cultured murine adipocytes with TNF-alpha was shown to induce serine phosphorylation of insulin receptor substrate 1 (IRS-1) and convert IRS-1 into an inhibitor of the IR tyrosine kinase activity in vitro. Myeloid 32D cells, which lack endogenous IRS-1, were resistant to TNF-alpha-mediated inhibition of IR signaling, whereas transfected 32D cells that express IRS-1 were very sensitive to this effect of TNF-alpha. An inhibitory form of IRS-1 was observed in muscle and fat tissues from obese rats. These results indicate that TNF-alpha induces insulin resistance through an unexpected action of IRS-1 to attenuate insulin receptor signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hotamisligil, G S -- Peraldi, P -- Budavari, A -- Ellis, R -- White, M F -- Spiegelman, B M -- DK 42539/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1996 Feb 2;271(5249):665-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Biology, Dana-Farber Cancer Institute, Boston, MA, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8571133" target="_blank"〉PubMed〈/a〉
    Keywords: Adipocytes/*metabolism ; Adipose Tissue/metabolism ; Animals ; Cells, Cultured ; Insulin/pharmacology ; Insulin Receptor Substrate Proteins ; Insulin Resistance/*physiology ; Male ; Mice ; Muscle, Skeletal/metabolism ; Obesity/*metabolism ; Phosphoproteins/metabolism/*physiology ; Phosphorylation ; Rats ; Rats, Zucker ; Receptor, Insulin/*antagonists & inhibitors/metabolism ; Serine/metabolism ; Signal Transduction ; Tumor Necrosis Factor-alpha/*pharmacology
    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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    Estimating the age of the common ancestor of men from the ZFY intron (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fu, Y X -- Li, W H -- New York, N.Y. -- Science. 1996 May 31;272(5266):1356-7; author reply 1361-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650550" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bayes Theorem ; Biological Evolution ; Confidence Intervals ; DNA-Binding Proteins/*genetics ; *Genetics, Population ; Hominidae/*genetics ; Humans ; Introns/*genetics ; Kruppel-Like Transcription Factors ; Male ; Mutation ; Population Density ; Probability ; Time Factors ; Transcription Factors/*genetics ; Y Chromosome/*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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  • 3
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    Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-13
    Description: The structure of the Staphylococcus aureus alpha-hemolysin pore has been determined to 1.9 A resolution. Contained within the mushroom-shaped homo-oligomeric heptamer is a solvent-filled channel, 100 A in length, that runs along the sevenfold axis and ranges from 14 A to 46 A in diameter. The lytic, transmembrane domain comprises the lower half of a 14-strand antiparallel beta barrel, to which each protomer contributes two beta strands, each 65 A long. The interior of the beta barrel is primarily hydrophilic, and the exterior has a hydrophobic belt 28 A wide. The structure proves the heptameric subunit stoichiometry of the alpha-hemolysin oligomer, shows that a glycine-rich and solvent-exposed region of a water-soluble protein can self-assemble to form a transmembrane pore of defined structure, and provides insight into the principles of membrane interaction and transport activity of beta barrel pore-forming toxins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Song, L -- Hobaugh, M R -- Shustak, C -- Cheley, S -- Bayley, H -- Gouaux, J E -- New York, N.Y. -- Science. 1996 Dec 13;274(5294):1859-66.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Chicago, 920 East 58 Street, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8943190" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Toxins/*chemistry/metabolism ; Cell Membrane/chemistry/metabolism ; Crystallography, X-Ray ; Hemolysin Proteins/*chemistry/metabolism ; Hydrogen Bonding ; Lipid Bilayers/*chemistry ; Membrane Potentials ; Models, Molecular ; Molecular Sequence Data ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Staphylococcus aureus/*chemistry
    Print ISSN: 0036-8075
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  • 4
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    DNA looping and lac repressor-CAP interaction (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perros, M -- Steitz, T A -- New York, N.Y. -- Science. 1996 Dec 13;274(5294):1929-30; author reply 1931-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8984647" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Crystallography, X-Ray ; Cyclic AMP Receptor Protein/*metabolism ; DNA, Bacterial/chemistry/*metabolism ; Escherichia coli/genetics ; *Lac Operon ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Operator Regions, Genetic ; *Promoter Regions, Genetic ; Protein Binding ; Protein Conformation ; Repressor Proteins/chemistry/*metabolism
    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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  • 5
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    Identification of BIME as a subunit of the anaphase-promoting complex (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-15
    Description: The initiation of anaphase and exit from mitosis require the activation of a proteolytic system that ubiquitinates and degrades cyclin B. The regulated component of this system is a large ubiquitin ligase complex, termed the anaphase-promoting complex (APC) or cyclosome. Purified Xenopus laevis APC was found to be composed of eight major subunits, at least four of which became phosphorylated in mitosis. In addition to CDC27, CDC16, and CDC23, APC contained a homolog of Aspergillus nidulans BIME, a protein essential for anaphase. Because mutation of bimE can bypass the interphase arrest induced by either nimA mutation or unreplicated DNA, it appears that ubiquitination catalyzed by APC may also negatively regulate entry into mitosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peters, J M -- King, R W -- Hoog, C -- Kirschner, M W -- New York, N.Y. -- Science. 1996 Nov 15;274(5290):1199-201.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8895470" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Anaphase ; Animals ; Aspergillus/chemistry/cytology/metabolism ; Cell Cycle Proteins/*chemistry/metabolism ; Cyclins/metabolism ; Electrophoresis, Polyacrylamide Gel ; Fungal Proteins/analysis/*chemistry/genetics/metabolism ; Ligases/*chemistry/metabolism ; *Mitosis ; Molecular Sequence Data ; Mutation ; Ovum ; Phosphorylation ; Ubiquitin-Protein Ligases ; Xenopus laevis
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Stimulation of membrane ruffling and MAP kinase activation by distinct effectors of RAS (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-09
    Description: The RAS guanine nucleotide binding proteins activate multiple signaling events that regulate cell growth and differentiation. In quiescent fibroblasts, ectopic expression of activated H-RAS (H-RASV12, where V12 indicates valine-12) induces membrane ruffling, mitogen-activated protein (MAP) kinase activation, and stimulation of DNA synthesis. A mutant of activated H-RAS, H-RASV12C40 (where C40 indicates cysteine-40), was identified that was defective for MAP kinase activation and stimulation of DNA synthesis, but retained the ability to induce membrane ruffling. Another mutant of activated H-RAS, H-RASV12S35 (where S35 indicates serine-35), which activates MAP kinase, was defective for stimulation of membrane ruffling and induction of DNA synthesis. Expression of both mutants resulted in a stimulation of DNA synthesis that was comparable to that induced by H-RASV12. These results indicate that membrane ruffling and activation of MAP kinase represent distinct RAS effector pathways and that input from both pathways is required for the mitogenic activity of RAS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Joneson, T -- White, M A -- Wigler, M H -- Bar-Sagi, D -- CA 55360/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Feb 9;271(5250):810-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Microbiology, State University of New York at Stony Brook 11794, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8628998" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Division ; Cell Line ; Cell Membrane/*ultrastructure ; DNA/biosynthesis ; Enzyme Activation ; GTP-Binding Proteins/genetics/metabolism ; Microinjections ; Mutation ; Plasmids ; Protein-Serine-Threonine Kinases/*metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-raf ; Rats ; Signal Transduction ; rac GTP-Binding Proteins ; ras Proteins/genetics/*metabolism
    Print ISSN: 0036-8075
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  • 7
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    Antigen presentation and T cell development in H2-M-deficient mice (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-01
    Description: HLA-DM (DM) facilitates peptide loading of major histocompatibility complex class II molecules in human cell lines. Mice lacking functional H2-M, the mouse equivalent of DM, have normal amounts of class II molecules at the cell surface, but most of these are associated with invariant chain-derived CLIP peptides. These mice contain large numbers of CD4+ T cells, which is indicative of positive selection in the thymus. Their CD4+ cells were unresponsive to self H2-M-deficient antigen-presenting cells (APCs) but were hyperreactive to wild-type APCs. H2-M-deficient APCs failed to elicit proliferative responses from wild-type T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fung-Leung, W P -- Surh, C D -- Liljedahl, M -- Pang, J -- Leturcq, D -- Peterson, P A -- Webb, S R -- Karlsson, L -- New York, N.Y. -- Science. 1996 Mar 1;271(5253):1278-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉R. W. Johnson Pharmaceutical Research Institute, San Diego, CA 92121, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638109" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigen Presentation ; Antigen-Presenting Cells/*immunology ; Antigens, Differentiation, B-Lymphocyte/immunology/metabolism ; Base Sequence ; CD4-Positive T-Lymphocytes/*immunology ; Cells, Cultured ; Gene Targeting ; Histocompatibility Antigens Class II/genetics/*immunology/metabolism ; Isoantigens/immunology ; Lymphocyte Activation ; Mice ; Molecular Sequence Data ; Mutation
    Print ISSN: 0036-8075
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  • 8
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    Modulation of virulence factor expression by pathogen target cell contact (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-30
    Description: Upon contact with the eukaryotic cell, Yersinia pseudotuberculosis increased the rate of transcription of virulence genes (yop), as determined by in situ monitoring of light emission from individual bacteria expressing luciferase under the control of the yopE promoter. The microbe-host interaction triggered export of LcrQ, a negative regulator of Yop expression, via the Yop-type III secretion system. The intracellular concentration of LcrQ was thereby lowered, resulting in increased expression of Yops. These results suggest a key role for the type III secretion system of pathogenic bacteria to coordinate secretion with expression of virulence factors after physical contact with the target cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pettersson, J -- Nordfelth, R -- Dubinina, E -- Bergman, T -- Gustafsson, M -- Magnusson, K E -- Wolf-Watz, H -- New York, N.Y. -- Science. 1996 Aug 30;273(5279):1231-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Molecular Biology, University of Umea, S-901 87 Umea, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703058" target="_blank"〉PubMed〈/a〉
    Keywords: *Bacterial Adhesion ; Bacterial Outer Membrane Proteins/biosynthesis/*genetics/secretion ; Bacterial Proteins/genetics/*secretion ; Calcium/metabolism ; Culture Media ; Cytosol/metabolism ; *Gene Expression Regulation, Bacterial ; HeLa Cells ; Humans ; Mutation ; Up-Regulation ; Virulence/*genetics ; Yersinia pseudotuberculosis/genetics/metabolism/*pathogenicity
    Print ISSN: 0036-8075
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  • 9
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    Cooperative DNA binding and sequence-selective recognition conferred by the STAT amino-terminal domain (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-09
    Description: STAT proteins (signal transducers and activators of transcription) activate distinct target genes despite having similar DNA binding preferences. The transcriptional specificity of STAT proteins was investigated on natural STAT binding sites near the interferon-gamma gene. These sites are arranged in multiple copies and required cooperative interactions for STAT binding. The conserved amino-terminal domain of STAT proteins was required for cooperative DNA binding, although this domain was not essential for dimerization or binding to a single site. Cooperative binding interactions enabled the STAT proteins to recognize variations of the consensus site. These sites can be specific for the different STAT proteins and may function to direct selective transcriptional activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xu, X -- Sun, Y L -- Hoey, T -- New York, N.Y. -- Science. 1996 Aug 9;273(5276):794-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tularik, Two Corporate Drive, South San Francisco, CA 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8670419" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Cell Line ; DNA/*metabolism ; DNA-Binding Proteins/chemistry/immunology/*metabolism ; Interferon-gamma/genetics ; Introns ; Molecular Sequence Data ; Mutation ; Oligodeoxyribonucleotides/metabolism ; Promoter Regions, Genetic ; STAT1 Transcription Factor ; STAT4 Transcription Factor ; Sequence Deletion ; Signal Transduction ; Trans-Activators/chemistry/immunology/*metabolism ; *Transcriptional Activation
    Print ISSN: 0036-8075
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  • 10
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    Functional evidence for indirect recognition of G.U in tRNA(Ala) by alanyl-tRNA synthetase (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-12
    Description: The structural features of the G.U wobble pair in Escherichia coli alanine transfer RNA (tRNA(Ala)) that are associated with aminoacylation by alanyl-tRNA synthetase (AlaRS) were investigated in vivo for wild-type tRNA(Ala) and mutant tRNAs with G.U substitutions. tRNA(Ala) with G.U, C.A, or G.A gave similar amounts of charged tRNA(Ala) and supported viability of E. coli lacking chromosomal tRNA(Ala) genes. tRNA(Ala) with G.C was inactive. Recognition of G.U by AlaRS thus requires more than the functional groups on G.U in a regular helix and may involve detection of a helical distortion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gabriel, K -- Schneider, J -- McClain, W H -- GM42123/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 12;271(5246):195-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Bacteriology, University of Wisconsin, Madison 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539617" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine-tRNA Ligase/*metabolism ; Anticodon ; Base Composition ; Base Sequence ; Escherichia coli/genetics/growth & development ; Genes, Bacterial ; Guanine/chemistry ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; Plasmids ; RNA, Transfer, Ala/chemistry/genetics/*metabolism ; Uracil/chemistry
    Print ISSN: 0036-8075
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  • 11
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    Intestinal secretory defects and dwarfism in mice lacking cGMP-dependent protein kinase II (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-20
    Description: Cyclic guanosine 3',5'-monophosphate (cGMP)-dependent protein kinases (cGKs) mediate cellular signaling induced by nitric oxide and cGMP. Mice deficient in the type II cGK were resistant to Escherichia coli STa, an enterotoxin that stimulates cGMP accumulation and intestinal fluid secretion. The cGKII-deficient mice also developed dwarfism that was caused by a severe defect in endochondral ossification at the growth plates. These results indicate that cGKII plays a central role in diverse physiological processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pfeifer, A -- Aszodi, A -- Seidler, U -- Ruth, P -- Hofmann, F -- Fassler, R -- New York, N.Y. -- Science. 1996 Dec 20;274(5295):2082-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut f-ur Pharmakologie und Toxikologie, Technische Universitat Munchen, Biedersteiner Strasse 29, D-80802 M-unchen, Germany. pfeifer@ipt.med.tu-muenchen.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8953039" target="_blank"〉PubMed〈/a〉
    Keywords: 8-Bromo Cyclic Adenosine Monophosphate/pharmacology ; Animals ; Bacterial Toxins/toxicity ; Body Water/secretion ; *Bone Development ; Crosses, Genetic ; Cyclic GMP/analogs & derivatives/metabolism/pharmacology ; Cyclic GMP-Dependent Protein Kinases/deficiency/genetics/*metabolism ; Diarrhea/physiopathology ; Dwarfism/*enzymology/genetics/pathology ; Enterotoxins/toxicity ; Escherichia coli Proteins ; Female ; Gene Deletion ; Growth Plate/enzymology/pathology ; Intestinal Mucosa/*secretion ; Male ; Mice ; Mice, Inbred C57BL ; Osteogenesis ; Signal Transduction
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  • 12
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    G protein-mediated neuronal DNA fragmentation induced by familial Alzheimer's disease-associated mutants of APP (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-31
    Description: Missense mutations in the 695-amino acid form of the amyloid precursor protein (APP695) cosegregate with disease phenotype in families with dominantly inherited Alzheimer's disease. These mutations convert valine at position 642 to isoleucine, phenylalanine, or glycine. Expression of these mutant proteins, but not of normal APP695, was shown to induce nucleosomal DNA fragmentation in neuronal cells. Induction of DNA fragmentation required the cytoplasmic domain of the mutants and appeared to be mediated by heterotrimeric guanosine triphosphate-binding proteins (G proteins).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamatsuji, T -- Matsui, T -- Okamoto, T -- Komatsuzaki, K -- Takeda, S -- Fukumoto, H -- Iwatsubo, T -- Suzuki, N -- Asami-Odaka, A -- Ireland, S -- Kinane, T B -- Giambarella, U -- Nishimoto, I -- New York, N.Y. -- Science. 1996 May 31;272(5266):1349-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cardiovascular Research Center, Massachusetts General Hospital, Department of Medicine, Harvard Medical School, Charlestown, MA 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650548" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*genetics/metabolism ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/chemistry/genetics/*physiology ; Animals ; Apoptosis ; Base Sequence ; Culture Media, Conditioned ; DNA/*metabolism ; GTP-Binding Proteins/*physiology ; Humans ; Hybrid Cells ; Mice ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutation ; Neurons/cytology/*metabolism ; Nucleosomes/*metabolism ; Peptide Fragments/metabolism ; Rats ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 13
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    Checkpoints take the next step (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carr, A M -- New York, N.Y. -- Science. 1996 Jan 19;271(5247):314-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Cell Mutation Unit, Sussex University, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8553064" target="_blank"〉PubMed〈/a〉
    Keywords: Ataxia Telangiectasia Mutated Proteins ; *Cell Cycle ; *Cell Cycle Proteins ; Checkpoint Kinase 2 ; *DNA Damage ; DNA Replication ; DNA-Binding Proteins ; Humans ; *Mitosis ; Mutation ; Phosphorylation ; Protein Kinases/genetics/*metabolism ; *Protein-Serine-Threonine Kinases ; Proteins/genetics/metabolism ; Saccharomyces cerevisiae/cytology/metabolism ; *Saccharomyces cerevisiae Proteins ; Schizosaccharomyces/cytology/metabolism ; Signal Transduction ; Tumor Suppressor Proteins
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  • 14
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    Sterol esterification in yeast: a two-gene process (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-31
    Description: Unesterified sterol modulates the function of eukaryotic membranes. In human cells, sterol is esterified to a storage form by acyl-coenzyme A (CoA): cholesterol acyl transferase (ACAT). Here, two genes are identified, ARE1 and ARE2, that encode ACAT-related enzymes in yeast. The yeast enzymes are 49 percent identical to each other and exhibit 23 percent identity to human ACAT. Deletion of ARE2 reduced sterol ester levels to approximately 25 percent of normal levels, whereas disruption of ARE1 did not affect sterol ester biosynthesis. Deletion of both genes resulted in a viable cell with undetectable esterified sterol. Measurements of [14C]acetate incorporation into saponified lipids indicated down-regulation of sterol biosynthesis in the are1 are2 mutant cells. With the use of a consensus sequence to the yeast and human genes, an additional number of the ACAT gene family was identified in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, H -- Bard, M -- Bruner, D A -- Gleeson, A -- Deckelbaum, R J -- Aljinovic, G -- Pohl, T M -- Rothstein, R -- Sturley, S L -- GM 50237/GM/NIGMS NIH HHS/ -- HG00861/HG/NHGRI NIH HHS/ -- R01 AI38598/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 May 31;272(5266):1353-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Human Nutrition, Columbia University College of Physicians and Surgeons, New York, 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650549" target="_blank"〉PubMed〈/a〉
    Keywords: Acetates/metabolism ; Acyltransferases/chemistry/*genetics/metabolism ; Amino Acid Sequence ; Base Sequence ; Cell Membrane/metabolism ; Cholesterol Esters/metabolism ; Cyclin-Dependent Kinase 8 ; *Cyclin-Dependent Kinases ; DNA, Complementary/genetics ; Ergosterol/metabolism ; Esterification ; *Genes, Fungal ; Homeostasis ; Humans ; Molecular Sequence Data ; Mutation ; Oleic Acid ; Oleic Acids/metabolism ; Saccharomyces cerevisiae/*genetics/metabolism ; Saccharomyces cerevisiae Proteins ; Sterol O-Acyltransferase/*genetics/metabolism ; Sterols/*metabolism ; Transformation, Genetic
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  • 15
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    A permease-oxidase complex involved in high-affinity iron uptake in yeast (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-15
    Description: Iron must cross biological membranes to reach essential intracellular enzymes. Two proteins in the plasma membrane of yeast--a multicopper oxidase, encoded by the FET3 gene, and a permease, encoded by the FTR1 gene--were shown to mediate high-affinity iron uptake. FET3 expression was required for FTR1 protein to be transported to the plasma membrane. FTR1 expression was required for apo-FET3 protein to be loaded with copper and thus acquire oxidase activity. FTR1 protein also played a direct role in iron transport. Mutations in a conserved sequence motif of FTR1 specifically blocked iron transport.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stearman, R -- Yuan, D S -- Yamaguchi-Iwai, Y -- Klausner, R D -- Dancis, A -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1552-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institutes of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599111" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Biological Transport ; Carrier Proteins/chemistry/*genetics/*metabolism ; Cell Membrane/metabolism ; *Ceruloplasmin ; Copper/metabolism/pharmacology ; Endoplasmic Reticulum/metabolism ; Ferric Compounds/metabolism ; Ferritins/chemistry/metabolism ; Ferrous Compounds/metabolism ; Genes, Fungal ; Golgi Apparatus/metabolism ; Iron/*metabolism ; Membrane Transport Proteins/chemistry/*genetics/*metabolism ; Models, Biological ; Molecular Sequence Data ; Multienzyme Complexes/*metabolism ; Mutation ; Open Reading Frames ; Oxidation-Reduction ; Oxidoreductases/*metabolism ; Saccharomyces cerevisiae/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Transformation, Genetic
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  • 16
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    Structural basis of ligand discrimination by two related RNA aptamers resolved by NMR spectroscopy (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-05-31
    Description: In a previous study, an RNA aptamer for the specific recognition of arginine was evolved from a parent sequence that bound citrulline specifically. The two RNAs differ at only 3 positions out of 44. The solution structures of the two aptamers complexed to their cognate amino acids have now been determined by two-dimensional nuclear magnetic resonance spectroscopy. Both aptamers contain two asymmetrical internal loops that are not well ordered in the free RNA but that fold into a compact structure upon ligand binding. Those nucleotides common to both RNAs include a conserved cluster of purine residues, three of which form an uneven plane containing a G:G pair, and two other residues nearly perpendicular to that surface. Two of the three variant nucleotides are stacked on the cluster of purines and form a triple contact to the amino acid side chain, whereas the edge of the third variant nucleotide is capping the binding pocket.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, Y -- Kochoyan, M -- Burgstaller, P -- Westhof, E -- Famulok, M -- New York, N.Y. -- Science. 1996 May 31;272(5266):1343-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre de Biochimie Structurale (CBS), Unite Mixte de Recherche, CNRS 9955, Montpellier, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650546" target="_blank"〉PubMed〈/a〉
    Keywords: Arginine/chemistry/*metabolism ; Base Composition ; Base Sequence ; Citrulline/chemistry/*metabolism ; Crystallography, X-Ray ; Hydrogen Bonding ; Ligands ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Mutation ; *Nucleic Acid Conformation ; RNA/*chemistry/genetics/*metabolism
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  • 17
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    Crystal structure of a group I ribozyme domain: principles of RNA packing (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-09-20
    Description: Group I self-splicing introns catalyze their own excision from precursor RNAs by way of a two-step transesterification reaction. The catalytic core of these ribozymes is formed by two structural domains. The 2.8-angstrom crystal structure of one of these, the P4-P6 domain of the Tetrahymena thermophila intron, is described. In the 160-nucleotide domain, a sharp bend allows stacked helices of the conserved core to pack alongside helices of an adjacent region. Two specific long-range interactions clamp the two halves of the domain together: a two-Mg2+-coordinated adenosine-rich corkscrew plugs into the minor groove of a helix, and a GAAA hairpin loop binds to a conserved 11-nucleotide internal loop. Metal- and ribose-mediated backbone contacts further stabilize the close side-by-side helical packing. The structure indicates the extent of RNA packing required for the function of large ribozymes, the spliceosome, and the ribosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cate, J H -- Gooding, A R -- Podell, E -- Zhou, K -- Golden, B L -- Kundrot, C E -- Cech, T R -- Doudna, J A -- 5T32GM08283-07/GM/NIGMS NIH HHS/ -- GM22778-21/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Sep 20;273(5282):1678-85.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA. doudna@csb.yale.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8781224" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine/chemistry ; Animals ; Base Composition ; Base Sequence ; Binding Sites ; Catalysis ; Crystallography, X-Ray ; Hydrogen Bonding ; *Introns ; Magnesium/chemistry ; Models, Molecular ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Phosphates/chemistry ; Phylogeny ; RNA Splicing ; RNA, Catalytic/*chemistry/metabolism ; RNA, Protozoan/*chemistry/metabolism ; Ribose/chemistry ; Tetrahymena thermophila/genetics
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  • 18
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    Molecular genetic insights into cardiovascular disease (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-05-03
    Description: The recent application of molecular genetic tools to inherited forms of cardiovascular disease has provided important insight into the molecular mechanisms underlying cardiac arrhythmias, cardiomyopathies, and vascular diseases. These studies point to defects in ion channels, contractile proteins, structural proteins, and signaling molecules as key players in disease pathogenesis. Genetic testing is now available for a subset of inherited cardiovascular diseases, and new mechanism-based therapies may be available in the near future. This remarkable progress and the implications it may have for more common forms of cardiovascular disease are reviewed here.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keating, M T -- Sanguinetti, M C -- New York, N.Y. -- Science. 1996 May 3;272(5262):681-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Utah, Salt Lake City, 84112, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614827" target="_blank"〉PubMed〈/a〉
    Keywords: Arrhythmias, Cardiac/diagnosis/*genetics ; Cardiomyopathies/diagnosis/*genetics ; Contractile Proteins/genetics ; Genetic Predisposition to Disease ; Genetic Testing ; Humans ; Ion Channels/genetics ; Mutation ; Myocardium/metabolism ; Prognosis ; Risk Factors ; Vascular Diseases/diagnosis/*genetics
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  • 19
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    Control of C. elegans larval development by neuronal expression of a TGF-beta homolog (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-22
    Description: The Caenorhabditis elegans dauer larva is specialized for dispersal without growth and is formed under conditions of overcrowding and limited food. The daf-7 gene, required for transducing environmental cues that support continuous development with plentiful food, encodes a transforming growth factor-beta (TGF-beta) superfamily member. A daf-7 reporter construct is expressed in the ASI chemosensory neurons. Dauer-inducing pheromone inhibits daf-7 expression and promotes dauer formation, whereas food reactivates daf-7 expression and promotes recovery from the dauer state. When the food/pheromone ratio is high, the level of daf-7 mRNA peaks during the L1 larval stage, when commitment to non-dauer development is made.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ren, P -- Lim, C S -- Johnsen, R -- Albert, P S -- Pilgrim, D -- Riddle, D L -- HD11239/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 22;274(5291):1389-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Program and Division of Biological Sciences, 311 Tucker Hall, University of Missouri, Columbia, MO 65211, USA. riddle@biosci.mbp.missouri.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8910282" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Caenorhabditis elegans/genetics/*growth & development/metabolism ; *Caenorhabditis elegans Proteins ; Genes, Helminth ; Genes, Reporter ; Green Fluorescent Proteins ; Helminth Proteins/chemistry/genetics/*physiology ; Humans ; Larva/growth & development/metabolism ; Ligands ; Luminescent Proteins/genetics ; Molecular Sequence Data ; Mutation ; Neurons, Afferent/*metabolism ; Phenotype ; Pheromones/pharmacology ; Temperature ; Transforming Growth Factor beta/chemistry/genetics/*physiology ; Transgenes
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  • 20
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    Kap104p: a karyopherin involved in the nuclear transport of messenger RNA binding proteins (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-25
    Description: A cytosolic yeast karyopherin, Kap104p, was isolated and shown to function in the nuclear import of a specific class of proteins. The protein bound directly to repeat-containing nucleoporins and to a cytosolic pool of two nuclear messenger RNA (mRNA) binding proteins, Nab2p and Nab4p. Depletion of Kap104p resulted in a rapid shift of Nab2p from the nucleus to the cytoplasm without affecting the localization of other nuclear proteins tested. This finding suggests that the major function of Kap104p lies in returning mRNA binding proteins to the nucleus after mRNA export.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aitchison, J D -- Blobel, G -- Rout, M P -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):624-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA. blobel@rockvax.rockefeller.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8849456" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Biological Transport ; Carrier Proteins/chemistry/isolation & purification/*metabolism ; Cell Nucleus/*metabolism ; Cytosol/chemistry/metabolism ; Fungal Proteins/*metabolism ; *Karyopherins ; Membrane Proteins/metabolism ; Molecular Sequence Data ; Mutation ; Nuclear Envelope/metabolism ; *Nuclear Pore Complex Proteins ; Nuclear Proteins/*metabolism ; *Nucleocytoplasmic Transport Proteins ; RNA, Messenger/genetics/metabolism ; RNA-Binding Proteins/*metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/*metabolism ; *Saccharomyces cerevisiae Proteins ; Temperature ; beta Karyopherins
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  • 21
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    Does leptin contribute to diabetes caused by obesity? (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-11-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taylor, S I -- Barr, V -- Reitman, M -- New York, N.Y. -- Science. 1996 Nov 15;274(5290):1151-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Diabetes Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-1829, USA. simeon_taylor@nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8966588" target="_blank"〉PubMed〈/a〉
    Keywords: Adipocytes/physiology ; Animals ; Carrier Proteins/metabolism ; Diabetes Mellitus/*etiology ; Diabetes Mellitus, Type 2/*etiology ; Gene Expression Regulation, Enzymologic ; Humans ; Insulin/*metabolism ; Insulin Antagonists ; Insulin Receptor Substrate Proteins ; Insulin Resistance ; Leptin ; Liver/metabolism ; Mice ; Mice, Obese ; Obesity/physiopathology ; Phosphoenolpyruvate Carboxykinase (GTP)/genetics ; Phosphoproteins/metabolism ; Phosphorylation ; Proteins/pharmacology/*secretion ; Receptor, Insulin/metabolism ; *Receptors, Cell Surface ; Receptors, Leptin ; Signal Transduction
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  • 22
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    New 'Alzheimer's mouse' produced (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-10-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1996 Oct 11;274(5285):177-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8927978" target="_blank"〉PubMed〈/a〉
    Keywords: *Alzheimer Disease/genetics/metabolism/pathology ; Amyloid beta-Peptides/blood/metabolism ; Amyloid beta-Protein Precursor/*genetics ; Animals ; Brain/pathology ; Brain Chemistry ; *Disease Models, Animal ; Learning Disorders/etiology ; Memory Disorders/etiology ; Mice ; Mice, Inbred C57BL ; *Mice, Transgenic ; Mutation ; Peptide Fragments/blood/metabolism ; Transgenes
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  • 23
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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)
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    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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  • 24
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    Control of the gene optomotor-blind in Drosophila wing development by decapentaplegic and wingless (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-03-15
    Description: Diffusible factors of several protein families control appendage outgrowth and patterning in both insects and vertebrates. In Drosophila wing development, the gene decapentaplegic (dpp) is expressed along the anteroposterior compartment boundary. Early wingless (wg) expression is involved in setting up the dorsoventral boundary. Interaction between dpp- and wg-expressing cells promotes appendage outgrowth. Here, it is shown that optomotor-blind (omb) expression is required for distal wing development and is controlled by both dpp and wg. Ectopic omb expression can lead to the growth of additional wings. Thus, omb is essential for wing development and is controlled by two signaling pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grimm, S -- Pflugfelder, G O -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1601-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Theodor-Boveri-Institut (Biozentrum), Lehrstuhl fur Genetik, Universitat Wurzburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599120" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA-Binding Proteins/*genetics/physiology ; Drosophila/*genetics/growth & development ; *Drosophila Proteins ; *Gene Expression Regulation, Developmental ; Genes, Insect ; Insect Hormones/*genetics/physiology ; Larva/genetics/growth & development ; Mutation ; Nerve Tissue Proteins/*genetics/physiology ; Phenotype ; Proto-Oncogene Proteins/*genetics/physiology ; Signal Transduction ; *T-Box Domain Proteins ; Wings, Animal/*growth & development ; Wnt1 Protein
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  • 25
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    Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-07-12
    Description: Rapamycin, a potent immunosuppressive agent, binds two proteins: the FK506-binding protein (FKBP12) and the FKBP-rapamycin-associated protein (FRAP). A crystal structure of the ternary complex of human FKBP12, rapamycin, and the FKBP12-rapamycin-binding (FRB) domain of human FRAP at a resolution of 2.7 angstroms revealed the two proteins bound together as a result of the ability of rapamycin to occupy two different hydrophobic binding pockets simultaneously. The structure shows extensive interactions between rapamycin and both proteins, but fewer interactions between the proteins. The structure of the FRB domain of FRAP clarifies both rapamycin-independent and -dependent effects observed for mutants of FRAP and its homologs in the family of proteins related to the ataxia-telangiectasia mutant gene product, and it illustrates how a small cell-permeable molecule can mediate protein dimerization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Choi, J -- Chen, J -- Schreiber, S L -- Clardy, J -- CA59021/CA/NCI NIH HHS/ -- GM38625/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 12;273(5272):239-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Baker Laboratory, Cornell University, Ithaca, NY 14853-1301, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662507" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Carrier Proteins/chemistry/genetics/*metabolism ; Crystallography, X-Ray ; DNA-Binding Proteins/chemistry/*metabolism ; Heat-Shock Proteins/chemistry/*metabolism ; Humans ; *Immunophilins ; Models, Molecular ; Mutation ; *Phosphotransferases (Alcohol Group Acceptor) ; Polyenes/*chemistry/*metabolism ; *Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry/metabolism ; Sirolimus ; TOR Serine-Threonine Kinases ; Tacrolimus Binding Proteins
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  • 26
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    Horizontal cells of the primate retina: cone specificity without spectral opponency (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-02-02
    Description: The chromatic dimensions of human color vision have a neural basis in the retina. Ganglion cells, the output neurons of the retina, exhibit spectral opponency; they are excited by some wavelengths and inhibited by others. The hypothesis that the opponent circuitry emerges from selective connections between horizontal cell interneurons and cone photoreceptors sensitive to long, middle, and short wavelengths (L-, M-, and S-cones) was tested by physiologically and anatomically characterizing cone connections of horizontal cell mosaics in macaque monkeys. H1 horizontal cells received input only from L- and M-cones, whereas H2 horizontal cells received a strong input from S-cones and a weaker input from L- and M-cones. All cone inputs were the same sign, and both horizontal cell types lacked opponency. Despite cone type selectivity, the horizontal cell cannot be the locus of an opponent transformation in primates, including humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dacey, D M -- Lee, B B -- Stafford, D K -- Pokorny, J -- Smith, V C -- New York, N.Y. -- Science. 1996 Feb 2;271(5249):656-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Structure, University of Washington, Seattle 98195-7420, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8571130" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Color Perception/*physiology ; Dendrites/ultrastructure ; Humans ; Interneurons/cytology/*physiology ; Macaca fascicularis ; Macaca mulatta ; Macaca nemestrina ; Photic Stimulation ; Retinal Cone Photoreceptor Cells/*physiology ; Retinal Ganglion Cells/*physiology ; Signal Transduction ; Visual Pathways
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Circadian rhythms in cultured mammalian retina (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-19
    Description: Many retinal functions are circadian, but in most instances the location of the clock that drives the rhythm is not known. Cultured neural retinas of the golden hamster (Mesocricetus auratus) exhibited circadian rhythms of melatonin synthesis for at least 5 days at 27 degrees celsius. The rhythms were entrained by light cycles applied in vitro and were free-running in constant darkness. Retinas from hamsters homozygous for the circadian mutation tau, which shortens the free-running period of the circadian activity rhythm by 4 hours, showed a shortened free-running period of melatonin synthesis. The mammalian retina contains a genetically programmed circadian oscillator that regulates its synthesis of melatonin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tosini, G -- Menaker, M -- HD13162/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1996 Apr 19;272(5260):419-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of Virginia, Charlottesville, VA 22903, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8602533" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Clocks ; *Circadian Rhythm/genetics ; Cricetinae ; Culture Techniques ; Darkness ; Genes ; Light ; Melatonin/*biosynthesis ; Mesocricetus ; Mutation ; Retina/metabolism/*physiology ; Temperature
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    A fin-de siecle achievement: charting new waters in vertebrate biology (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grunwald, D J -- New York, N.Y. -- Science. 1996 Dec 6;274(5293):1634-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Human Genetics, Eccles Institute of Human Genetics, University of Utah, Salt Lake City 84112, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8984632" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Congenital Abnormalities/genetics ; *Embryonic Development ; Embryonic Induction ; *Genes ; Humans ; Morphogenesis ; *Mutation ; Phenotype ; Signal Transduction ; Syndrome ; Zebrafish/*embryology/*genetics
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  • 29
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    A mechanism of drug action revealed by structural studies of enoyl reductase (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-20
    Description: Enoyl reductase (ENR), an enzyme involved in fatty acid biosynthesis, is the target for antibacterial diazaborines and the front-line antituberculosis drug isoniazid. Analysis of the structures of complexes of Escherichia coli ENR with nicotinamide adenine dinucleotide and either thienodiazaborine or benzodiazaborine revealed the formation of a covalent bond between the 2' hydroxyl of the nicotinamide ribose and a boron atom in the drugs to generate a tight, noncovalently bound bisubstrate analog. This analysis has implications for the structure-based design of inhibitors of ENR, and similarities to other oxidoreductases suggest that mimicking this molecular linkage may have generic applications in other areas of medicinal chemistry.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baldock, C -- Rafferty, J B -- Sedelnikova, S E -- Baker, P J -- Stuitje, A R -- Slabas, A R -- Hawkes, T R -- Rice, D W -- New York, N.Y. -- Science. 1996 Dec 20;274(5295):2107-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, UK. D.Rice@sheffield.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8953047" target="_blank"〉PubMed〈/a〉
    Keywords: Anti-Bacterial Agents/*metabolism/pharmacology ; Binding Sites ; Boron Compounds/*metabolism/pharmacology ; Crystallography, X-Ray ; Drug Design ; Drug Resistance, Microbial ; Enoyl-(Acyl-Carrier-Protein) Reductase (NADH) ; Enzyme Inhibitors/*metabolism/pharmacology ; Escherichia coli/enzymology ; Escherichia coli Proteins ; Fatty Acid Synthase, Type II ; Fatty Acid Synthases/antagonists & inhibitors/*chemistry/metabolism ; Hydrogen Bonding ; Models, Molecular ; NAD/*metabolism ; Oxidoreductases/antagonists & inhibitors/*chemistry/metabolism ; Protein Conformation ; Protein Structure, Secondary
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    Flies unmask evolutionary warfare between the sexes (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1996 May 17;272(5264):953-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638139" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Drosophila/genetics/*physiology ; Female ; Genes, Insect ; Male ; Mutation ; Reproduction ; Sex Characteristics ; Sexual Behavior, Animal
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    Age-dependent diarrhea induced by a rotaviral nonstructural glycoprotein (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-05
    Description: The rotavirus nonstructural glycoprotein NSP4 is an intracellular receptor that mediates the acquisition of a transient membrane envelope as subviral particles bud into the endoplasmic reticulum. NSP4 also causes an increase in intracellular calcium in insect cells. Purified NSP4 or a peptide corresponding to NSP4 residues 114 to 135 induced diarrhea in young (6 to 10 days old) CD1 mice. This disease response was age-dependent, dose-dependent, and specific. Electrophysiologic data from intestinal mucosa showed that the NSP4 114-135 peptide potentiates chloride secretion by a calcium-dependent signaling pathway. Diarrhea is induced when NSP4, acting as a viral enterotoxin, triggers a signal transduction pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ball, J M -- Tian, P -- Zeng, C Q -- Morris, A P -- Estes, M K -- DK 30144/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1996 Apr 5;272(5258):101-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Virology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8600515" target="_blank"〉PubMed〈/a〉
    Keywords: *Aging ; Amino Acid Sequence ; Animals ; Calcium/metabolism ; Carbachol/pharmacology ; Chlorides/metabolism ; Colforsin/pharmacology ; Diarrhea/*etiology/prevention & control/virology ; Enterotoxins/*toxicity ; Glycoproteins/immunology/*toxicity ; Immune Sera/administration & dosage ; Immunization ; In Vitro Techniques ; Intestinal Mucosa/drug effects/secretion ; Mice ; Molecular Sequence Data ; Peptide Fragments/toxicity ; Receptors, Virus ; Rotavirus/*pathogenicity ; Rotavirus Infections/prevention & control/*virology ; Signal Transduction ; Toxins, Biological ; Viral Nonstructural Proteins/immunology/*toxicity
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    Sperm protein makes its mark upon the worm embryo (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1996 Jan 5;271(5245):33.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539595" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/*embryology/genetics ; *Caenorhabditis elegans Proteins ; *Embryonic Development ; Female ; Fertilization ; Genes, Helminth ; Helminth Proteins/genetics/*physiology ; Male ; Mutation ; *Nuclear Proteins ; Oocytes/physiology ; Spermatozoa/*chemistry/physiology
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    HERG sequence correction (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Trudeau, M C -- Warmke, J W -- Ganetzky, B -- Robertson, G A -- New York, N.Y. -- Science. 1996 May 24;272(5265):1087.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638148" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Humans ; Mutation ; Potassium Channels/*genetics ; *Potassium Channels, Inwardly Rectifying
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    Protein matchmaker may lead new gene therapy to the altar (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balter, M -- New York, N.Y. -- Science. 1996 Jul 12;273(5272):183.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8668994" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carrier Proteins/chemistry/*metabolism ; Crystallography, X-Ray ; DNA-Binding Proteins/chemistry/*metabolism ; *Gene Expression Regulation ; Genetic Therapy ; Growth Hormone/*genetics ; Heat-Shock Proteins/chemistry/*metabolism ; Humans ; *Immunophilins ; Mice ; *Phosphotransferases (Alcohol Group Acceptor) ; Polyenes/chemistry/*metabolism ; Sirolimus ; TOR Serine-Threonine Kinases ; Tacrolimus Binding Proteins
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  • 35
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    Cell killing by the Drosophila gene reaper (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-02-09
    Description: The reaper gene (rpr) is important for the activation of apoptosis in Drosophila. To investigate whether rpr expression is sufficient to induce apoptosis, transgenic flies were generated that express rpr complementary DNA or the rpr open reading frame in cells that normally live. Transcription of rpr from a heat-inducible promoter rapidly caused wide-spread ectopic apoptosis and organismal death. Ectopic overexpression of rpr in the developing retina resulted in eye ablation. The occurrence of cell death was highly sensitive to the dosage of the transgene. Because cell death induced by the protein encoded by rpr (RPR) could be blocked by the baculovirus p35 protein, RPR appears to activate a death program mediated by a ced-3/ICE (interleukin-1 converting enzyme)-like protease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉White, K -- Tahaoglu, E -- Steller, H -- New York, N.Y. -- Science. 1996 Feb 9;271(5250):805-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cutaneous Biology Research Center, Massachusetts General Hospital, Charlestown 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8628996" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; *Apoptosis ; Caspase 1 ; Cysteine Endopeptidases/metabolism ; DNA, Complementary/genetics ; Drosophila/cytology/embryology/*genetics ; *Drosophila Proteins ; Gene Dosage ; Gene Expression ; *Genes, Insect ; Hot Temperature ; Inhibitor of Apoptosis Proteins ; Mutation ; Open Reading Frames ; Peptides/*genetics/physiology ; Photoreceptor Cells, Invertebrate/cytology ; Transgenes ; Viral Proteins/genetics/physiology
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    Requirement for the adapter protein GRB2 in EGF receptor endocytosis (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-28
    Description: Activated epidermal growth factor (EGF) receptors induce the formation of various complexes of intracellular signaling proteins that are mediated by SRC homology 2 (SH2) and SH3 domains. The activated receptors are also rapidly internalized into the endocytotic compartment and degraded in lysosomes. EGF stimulation of canine epithelial cells induced a rapid and transient association of the SH3-SH2-SH3 protein GRB2 with dynamin, a guanosine triphosphatase that regulates endocytosis. Disruption of GRB2 interactions by microinjection of a peptide corresponding to the GRB2 SH2 domain or its phosphopeptide ligand blocked EGF receptor endocytosis; other SH2 domains that bind EGF receptors or antibodies that neutralize RAS did not. Both activation and termination of EGF signaling appear to be regulated by the diverse interactions of GRB2.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Z -- Moran, M F -- New York, N.Y. -- Science. 1996 Jun 28;272(5270):1935-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Banting and Best Department of Medical Research, University of Toronto, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658166" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Animals ; Antibodies, Monoclonal ; Cell Line ; Dogs ; Dynamins ; *Endocytosis/drug effects ; Epidermal Growth Factor/pharmacology ; GRB2 Adaptor Protein ; GTP Phosphohydrolases/metabolism ; Microinjections ; Peptide Fragments/pharmacology ; Proteins/*metabolism ; Receptor, Epidermal Growth Factor/*metabolism ; Receptors, Transferrin/metabolism ; Recombinant Fusion Proteins/pharmacology ; Signal Transduction ; ras Proteins/immunology/physiology ; src Homology Domains/physiology
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    Evidence that Spt6p controls chromatin structure by a direct interaction with histones (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-06-07
    Description: Genetic analysis has implicated SPT6, an essential gene of Saccharomyces cerevisiae, in the control of chromatin structure. Mutations in SPT6 and particular mutations in histone genes are able to overcome transcriptional defects in strains lacking the Snf/Swi protein complex. Here it is shown that an spt6 mutation causes changes in chromatin structure in vivo. In addition, both in vivo and in vitro experiments provide evidence that Spt6p interacts directly with histones and primarily with histone H3. Consistent with these findings, Spt6p is capable of nucleosome assembly in vitro.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bortvin, A -- Winston, F -- GM32967/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 7;272(5267):1473-6.〈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/8633238" target="_blank"〉PubMed〈/a〉
    Keywords: Chromatin/chemistry/genetics/metabolism/*ultrastructure ; DNA, Fungal/metabolism ; Fungal Proteins/genetics/metabolism/*physiology ; Histones/chemistry/genetics/*metabolism ; Humans ; Mutation ; Nuclear Proteins/genetics/metabolism/*physiology ; Nucleosomes/metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/*genetics/metabolism ; *Saccharomyces cerevisiae Proteins ; Transcription, Genetic ; Transcriptional Elongation Factors
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    Gene perplexes epilepsy researchers (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Brien, C -- New York, N.Y. -- Science. 1996 Mar 22;271(5256):1672.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596927" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Chromosome Mapping ; Chromosomes, Human, Pair 21/*genetics ; Cystatin B ; Cystatins/*genetics ; Cysteine Proteinase Inhibitors/*genetics ; Epilepsies, Myoclonic/*genetics ; Female ; Humans ; Male ; Mutation ; Pedigree ; RNA, Messenger/genetics/metabolism
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    Evidence for physical and functional association between EMB-5 and LIN-12 in Caenorhabditis elegans (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-05
    Description: The Caenorhabditis elegans LIN-12 and GLP-1 proteins are members of the LIN-12/Notch family of receptors for intercellular signals that specify cell fate. Evidence presented here suggests that the intracellular domains of LIN-12 and GLP-1 interact with the C. elegans EMB-5 protein and that the emb-5 gene functions in the same pathway as the lin-12 and glp-1 genes. EMB-5 is similar in sequence to a yeast protein that controls chromatin structure. Hence, a direct consequence of LIN-12 or GLP-1 activation may be an alteration of chromatin structure that produces changes in transcriptional activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hubbard, E J -- Dong, Q -- Greenwald, I -- GM37602/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 5;273(5271):112-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Columbia University College of Physicians and Surgeons, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658178" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/*cytology/embryology/genetics/*metabolism ; *Caenorhabditis elegans Proteins ; Cell Lineage ; Chromatin/metabolism ; Gene Expression Regulation, Developmental ; Genes, Helminth ; Helminth Proteins/genetics/*metabolism ; Meiosis ; Membrane Proteins/genetics/*metabolism ; Mitosis ; Mutation ; Receptors, Notch ; *Signal Transduction ; Temperature ; Transcription Factors/genetics/*metabolism
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  • 40
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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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    Initiation of runaway cell death in an Arabidopsis mutant by extracellular superoxide (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-09-27
    Description: Reactive oxygen intermediates (ROIs) regulate apoptosis during normal development and disease in animals. ROIs are also implicated in hypersensitive resistance responses of plants against pathogens. Arabidopsis lsd1 mutants exhibited impaired control of cell death in the absence of pathogen and could not control the spread of cell death once it was initiated. Superoxide was necessary and sufficient to initiate lesion formation; it accumulated before the onset of cell death and subsequently in live cells adjacent to spreading lsd1 lesions. Thus, runaway cell death seen in lsd1 plants reflected abnormal accumulation of superoxide and lack of responsiveness to signals derived from it.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jabs, T -- Dietrich, R A -- Dangl, J L -- New York, N.Y. -- Science. 1996 Sep 27;273(5283):1853-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Delbruck Laboratory, Carl von Linne Weg 10, 50829 Koln, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8791589" target="_blank"〉PubMed〈/a〉
    Keywords: *Apoptosis ; Arabidopsis/*cytology/genetics/metabolism ; Cell Membrane/enzymology ; Enzyme Inhibitors/pharmacology ; Gene Expression Regulation, Plant ; Genes, Plant ; Glutathione Transferase/genetics/metabolism ; Mutation ; NADH, NADPH Oxidoreductases/antagonists & inhibitors/metabolism ; NADPH Oxidase ; Onium Compounds/pharmacology ; Peroxidases/genetics/metabolism ; Plant Leaves/cytology/metabolism ; RNA, Messenger/genetics/metabolism ; RNA, Plant/genetics/metabolism ; Reactive Oxygen Species/metabolism ; Superoxide Dismutase/genetics ; Superoxides/*metabolism
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    Transcription factor IIA: a structure with multiple functions (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jacobson, R H -- Tjian, R -- New York, N.Y. -- Science. 1996 May 10;272(5263):827-8.〈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/8629011" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Crystallography, X-Ray ; DNA/*chemistry/metabolism ; DNA-Binding Proteins/*chemistry/metabolism ; Humans ; Models, Molecular ; Nucleic Acid Conformation ; Protein Conformation ; Protein Structure, Secondary ; TATA Box ; TATA-Box Binding Protein ; Transcription Factor TFIIA ; Transcription Factor TFIID ; Transcription Factors/*chemistry/genetics/*metabolism ; *Transcription, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Antagonistic interactions between wingless and decapentaplegic responsible for dorsal-ventral pattern in the Drosophila Leg (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-09-06
    Description: Subdivision of the limb primordia of Drosophila into anterior and posterior compartments triggers cell interactions that pattern the legs and wings. A comparable compartment-based mechanism is used to pattern the dorsal-ventral axis of the wing. Evidence is presented here for a mechanism based on cell interaction, rather than on compartment formation, that distinguishes dorsal from ventral in the leg. Mutual repression by Wingless and Decapentaplegic signaling systems generates a stable regulatory circuit by which each gene maintains its own expression in a spatially restricted domain. Compartment-independent patterning mechanisms may be used by other organisms during development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brook, W J -- Cohen, S M -- New York, N.Y. -- Science. 1996 Sep 6;273(5280):1373-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, Meyerhofstr 1, 69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703069" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; Cell Lineage ; Drosophila/*genetics/growth & development ; *Drosophila Proteins ; Extremities/growth & development ; *Gene Expression Regulation, Developmental ; *Genes, Insect ; Insect Hormones/*genetics/physiology ; Molecular Sequence Data ; Morphogenesis ; Proto-Oncogene Proteins/*genetics/physiology ; Signal Transduction ; Wnt1 Protein
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    Streetcar carries evolution modelers around roadblocks (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, N -- New York, N.Y. -- Science. 1996 Mar 8;271(5254):1365-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596907" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Game Theory ; Genes ; Genetics, Population ; Humans ; *Models, Biological ; Models, Genetic ; Mutation
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Will a twist of viral fate lead to a new cancer treatment? (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1996 Oct 18;274(5286):342-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8927990" target="_blank"〉PubMed〈/a〉
    Keywords: Adenovirus E1B Proteins/*genetics/metabolism ; Adenoviruses, Human/genetics/*physiology ; Animals ; Clinical Trials, Phase I as Topic ; Cytopathogenic Effect, Viral ; Genes, Viral ; *Genes, p53 ; Head and Neck Neoplasms/*therapy/virology ; Humans ; Mice ; Mutation ; Neoplasm Transplantation ; Neoplasms, Experimental/*therapy/virology ; Tumor Suppressor Protein p53/metabolism ; Virus Replication
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    Molecular orientation and two-component nature of the crystalline fraction of spider dragline silk (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-05
    Description: The molecular origin of the exceptional mechanical properties of spider silk is unclear. This paper presents solid-state 2H nuclear magnetic resonance data from unoriented, oriented, and supercontracted fibers, indicating that the crystalline fraction of dragline silk consists of two types of alanine-rich regions, one that is highly oriented and one that is poorly oriented and less densely packed. A new model for the molecular-level structure of individual silk molecules and their arrangement in the fibers is proposed. These data suggest that it will be necessary to control the secondary structure of individual polymer molecules in order to obtain optimum properties in bio-inspired polymers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Simmons, A H -- Michal, C A -- Jelinski, L W -- New York, N.Y. -- Science. 1996 Jan 5;271(5245):84-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Advanced Technology in Biotechnology, Cornell University, Ithaca, NY 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539605" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine/analysis ; Algorithms ; Amino Acid Sequence ; Animals ; Crystallization ; Crystallography, X-Ray ; *Fibroins ; Glycine/analysis ; *Insect Proteins ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Peptides/analysis ; Protein Conformation ; Protein Structure, Secondary ; Proteins/*chemistry ; Silk ; Spiders/*chemistry
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 47
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    Identification of an asymmetrically localized sensor histidine kinase responsible for temporally and spatially regulated transcription (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-25
    Description: Caulobacter crescentus undergoes asymmetric cell division, resulting in a stalked cell and a motile swarmer cell. The genes encoding external components of the flagellum are expressed in the swarmer compartment of the predivisional cell through the localized activation of the transcription factor FlbD. The mechanisms responsible for the temporal and spatial activation of FlbD were determined through identification of FlbE, a histidine kinase required for FlbD activity. FlbE is asymmetrically distributed in the predivisional cell. It is located at the pole of the stalked compartment and at the site of cell division in the swarmer compartment. These findings suggest that FlbE and FlbD are activated in response to a morphological change in the cell resulting from cell division events.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wingrove, J A -- Gober, J W -- GM-07104/GM/NIGMS NIH HHS/ -- GM48417/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):597-601.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry and the Molecular Biology Institute, University of California, Los Angeles, CA 90095-1569, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8849449" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/genetics/*metabolism ; Caulobacter crescentus/cytology/*genetics/physiology ; Cell Division ; DNA-Binding Proteins/genetics/*metabolism ; Gene Expression Regulation, Bacterial ; Genes, Bacterial ; Mutation ; Phosphorylation ; Promoter Regions, Genetic ; Protein Kinases/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Transcription Factors/genetics/*metabolism ; *Transcription, Genetic
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    Identification of MAP kinase domains by redirecting stress signals into growth factor responses (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-14
    Description: Mitogen-activated protein kinase (MAPK) cascades, termed MAPK modules, channel extracellular signals into specific cellular responses. Chimeric molecules were constructed between p38 and p44 MAPKs, which transduce stress and growth factor signals, respectively. A discrete region of 40 residues located in the amono-terminal p38MAPK lobe directed the specificity of response to extracellular signals, whereas the p44MAPK chimera, expressed in vivo, redirected stress signals into early mitogenic responses, demonstrating the functional independence of these domains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brunet, A -- Pouyssegur, J -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1652-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre de Biochemie-CNRS, UMR134, Parc Valrose, Faculte des Sciences, Nice, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658140" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Anisomycin/pharmacology ; Binding Sites ; Calcium-Calmodulin-Dependent Protein Kinases/genetics/*metabolism ; Cell Division ; Cell Line ; Cricetinae ; Cricetulus ; Enzyme Activation ; Gene Expression Regulation ; Genes, fos ; Growth Substances/metabolism ; Mice ; Mitogen-Activated Protein Kinase 3 ; *Mitogen-Activated Protein Kinases ; Molecular Sequence Data ; Phosphorylation/drug effects ; Protein Kinases/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Recombinant Fusion Proteins/genetics/metabolism ; Ribosomal Protein S6 Kinases ; Signal Transduction ; Sorbitol/pharmacology ; Substrate Specificity ; p38 Mitogen-Activated Protein Kinases
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    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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    Molecular pathways controlling heart development (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-03
    Description: Heart formation requires complex interactions among cells from multiple embryonic origins. Recent studies have begun to reveal the genetic pathways that control cardiac morphogenesis. Many of the genes within these pathways are conserved across vast phylogenetic distances, which has allowed cardiac development to be dissected in organisms ranging from flies to mammals. Studies of cardiac development have also revealed the molecular defects underlying several congenital cardiac malformations in humans and may ultimately provide opportunities for genetic testing and intervention.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Olson, E N -- Srivastava, D -- New York, N.Y. -- Science. 1996 May 3;272(5262):671-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Oncology, University of Texas Southwestern Medical Center, Dallas, 75235-9148, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614825" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; *Gene Expression Regulation, Developmental ; Genes ; Genes, Regulator ; Heart/*embryology ; Heart Conduction System/embryology ; Heart Defects, Congenital/embryology/*genetics/pathology ; Humans ; Morphogenesis ; Mutation ; Myocardium/cytology ; Neural Crest/cytology ; Transcription Factors/physiology ; Transcription, Genetic
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    Worm genes imply a master clock (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1996 May 17;272(5264):949-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638138" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/*genetics ; Animals ; Biological Clocks/*genetics ; Caenorhabditis elegans/*genetics/physiology ; *Genes, Helminth ; Longevity/genetics ; Mutation
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    Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-09
    Description: Bruton's tyrosine kinase (BTK) is pivotal in B cell activation and development through its participation in the signaling pathways of multiple hematopoietic receptors. The mechanisms controlling BTK activation were studied here by examination of the biochemical consequences of an interaction between BTK and SRC family kinases. This interaction of BTK with SRC kinases transphosphorylated BTK on tyrosine at residue 551, which led to BTK activation. BTK then autophosphorylated at a second site. The same two sites were phosphorylated upon B cell antigen receptor cross-linking. The activated BTK was predominantly membrane-associated, which suggests that BTK integrates distinct receptor signals resulting in SRC kinase activation and BTK membrane targeting.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rawlings, D J -- Scharenberg, A M -- Park, H -- Wahl, M I -- Lin, S -- Kato, R M -- Fluckiger, A C -- Witte, O N -- Kinet, J P -- AR01912/AR/NIAMS NIH HHS/ -- AR36834/AR/NIAMS NIH HHS/ -- CA09120-20/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Feb 9;271(5250):822-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, University of California, Los Angeles 90095-1662, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8629002" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; B-Lymphocytes/*enzymology ; Cell Line, Transformed ; Cell Membrane/enzymology ; Enzyme Activation ; Immunoglobulin M/immunology ; Lymphocyte Activation ; Mice ; Mutation ; Phosphopeptides/analysis ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein-Tyrosine Kinases/chemistry/genetics/*metabolism ; Receptors, Antigen, B-Cell/metabolism ; Signal Transduction ; src-Family Kinases/*metabolism
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    Lord of the rings: GroES structure (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mayhew, M -- Hartl, F U -- New York, N.Y. -- Science. 1996 Jan 12;271(5246):161-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539614" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Chaperonin 10/*chemistry/metabolism ; Chaperonin 60/metabolism ; Crystallography, X-Ray ; Mycobacterium leprae/*chemistry ; *Protein Conformation ; *Protein Folding ; Protein Structure, Secondary
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    Diversity and pattern in the developing spinal cord (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-15
    Description: The generation of distinct neuronal cell types in appropriate numbers and at precise positions underlies the assembly of neural circuits that encode animal behavior. Despite the complexity of the vertebrate central nervous system, advances have been made in defining the principles that control the diversification and patterning of its component cells. A combination of molecular genetic, biochemical, and embryological assays has begun to reveal the identity and mechanism of action of molecules that induce and pattern neural tissue and the role of transcription factors in establishing generic and specific neuronal fates. Some of these advances are discussed here, focusing on the spinal cord as a model system for analyzing the molecular control of central nervous system development in vertebrates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tanabe, Y -- Jessell, T M -- New York, N.Y. -- Science. 1996 Nov 15;274(5290):1115-23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Center for Neurobiology and Behavior, Columbia University, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8895454" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Body Patterning ; Cell Differentiation ; Ectoderm/cytology/physiology ; *Embryonic Induction ; Gene Expression Regulation, Developmental ; Motor Neurons/cytology/physiology ; Neurons/*cytology/physiology ; Notochord/physiology ; Signal Transduction ; Spinal Cord/cytology/*embryology ; Transcription Factors/physiology
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    Selector genes, polymorphisms, and evolution (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tautz, D -- New York, N.Y. -- Science. 1996 Jan 12;271(5246):160-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Zoologisches Institut, Universitat Munchen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539613" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; DNA-Binding Proteins/*genetics ; Drosophila/drug effects/*genetics ; *Drosophila Proteins ; Ether/pharmacology ; *Genes, Homeobox ; Genes, Insect ; *Genes, Regulator ; Homeodomain Proteins/*genetics ; Homeostasis ; Mutation ; *Polymorphism, Genetic ; *Transcription Factors
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    Regulation of an early developmental checkpoint in the B cell pathway by Ig beta (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-19
    Description: Many of the cell fate decisions in precursor B cells and more mature B cells are controlled by membrane immunoglobulin (Ig)M heavy chain (mu) and the Ig alpha-Ig beta signal transducers. The role of Ig beta in regulating early B cell development was examined in mice that lack Ig beta (Ig beta-/-). These mice had a complete block in B cell development at the immature CD43+B220+ stage. Immunoglobulin heavy chain diversity (DH) and joining (JH) segments rearranged, but variable (VH) to DJH recombination and immunoglobulin messenger RNA expression were compromised. These experiments define an unexpected, early requirement for Ig(beta) to produce B cells that can complete VDJH recombination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gong, S -- Nussenzweig, M C -- New York, N.Y. -- Science. 1996 Apr 19;272(5260):411-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Rockefeller University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8602530" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/genetics/*physiology ; Antigens, CD79 ; B-Lymphocytes/cytology/*immunology ; Gene Expression ; *Gene Rearrangement, B-Lymphocyte, Heavy Chain ; Gene Targeting ; Genes, Immunoglobulin ; Immunoglobulin Heavy Chains/*genetics ; Immunoglobulin Joining Region/genetics ; Immunoglobulin Light Chains/*genetics ; Immunoglobulin Variable Region/genetics ; Immunoglobulin mu-Chains/biosynthesis/genetics/physiology ; Lymph Nodes ; Mice ; Mice, Inbred C57BL ; Mutation ; RNA, Messenger/genetics ; Receptors, Antigen, B-Cell/physiology ; *Recombination, Genetic ; Signal Transduction
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  • 57
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    Cholesterol modification of hedgehog signaling proteins in animal development (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-11
    Description: Hedgehog (Hh) proteins comprise a family of secreted signaling molecules essential for patterning a variety of structures in animal embryogenesis. During biosynthesis, Hh undergoes an autocleavage reaction, mediated by its carboxyl-terminal domain, that produces a lipid-modified amino-terminal fragment responsible for all known Hh signaling activity. Here it is reported that cholesterol is the lipophilic moiety covalently attached to the amino-terminal signaling domain during autoprocessing and that the carboxyl-terminal domain acts as an intramolecular cholesterol transferase. This use of cholesterol to modify embryonic signaling proteins may account for some of the effects of perturbed cholesterol biosynthesis on animal development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Porter, J A -- Young, K E -- Beachy, P A -- New York, N.Y. -- Science. 1996 Oct 11;274(5285):255-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8824192" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cells, Cultured ; Cholesterol/*metabolism ; Dithiothreitol/pharmacology ; Drosophila ; *Drosophila Proteins ; *Embryonic Induction ; Embryonic and Fetal Development ; Hedgehog Proteins ; Humans ; Protein Processing, Post-Translational ; Proteins/genetics/*metabolism ; Signal Transduction ; *Trans-Activators
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    Diffusional mobility of Golgi proteins in membranes of living cells (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-09
    Description: The mechanism by which Golgi membrane proteins are retained within the Golgi complex in the midst of a continuous flow of protein and lipid is not yet understood. The diffusional mobilities of mammalian Golgi membrane proteins fused with green fluorescent protein from Aequorea victoria were measured in living HeLa cells with the fluorescence photobleaching recovery technique. The diffusion coefficients ranged from 3 x 10(-9) square centimeters per second to 5 x 10(-9) square centimeters per second, with greater than 90 percent of the chimeric proteins mobile. Extensive lateral diffusion of the chimeric proteins occurred between Golgi stacks. Thus, the chimeras diffuse rapidly and freely in Golgi membranes, which suggests that Golgi targeting and retention of these molecules does not depend on protein immobilization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cole, N B -- Smith, C L -- Sciaky, N -- Terasaki, M -- Edidin, M -- Lippincott-Schwartz, J -- R37 AI14584/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 9;273(5276):797-801.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Building 18T, 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/8670420" target="_blank"〉PubMed〈/a〉
    Keywords: Aluminum Compounds/pharmacology ; Diffusion ; Endoplasmic Reticulum/metabolism ; Fluorides/pharmacology ; Golgi Apparatus/*metabolism ; Green Fluorescent Proteins ; HeLa Cells ; Humans ; Intracellular Membranes/metabolism ; Luminescent Proteins ; Mannosidases/*metabolism ; Membrane Proteins/*metabolism ; Microscopy, Confocal ; Mutation ; N-Acetyllactosamine Synthase/*metabolism ; Receptors, Peptide/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism
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    Mechanosensation and the DEG/ENaC ion channels (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Corey, D P -- Garcia-Anoveros, J -- New York, N.Y. -- Science. 1996 Jul 19;273(5273):323-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Boston, MA 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8685718" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Caenorhabditis elegans/genetics/*physiology ; Genes, Helminth ; Helminth Proteins/chemistry/genetics/*physiology ; Molecular Sequence Data ; Muscle Contraction ; Mutation ; Phenotype ; Sensation/genetics/*physiology ; Sodium Channels/chemistry/genetics/*physiology ; Touch/genetics/physiology
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    Uncoupling of GTP binding from target stimulation by a single mutation in the transducin alpha subunit (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-08
    Description: Glutamic acid-203 of the alpha subunit of transducin (alphaT) resides within a domain that undergoes a guanosine triphosphate (GTP)-induced conformational change that is essential for effector recognition. Changing the glutamic acid to an alanine in bovine alpha(T) yielded an alpha subunit (alpha(T)E203A) that was fully dependent on rhodopsin for GTP-guanosine diphosphate (GDP) exchange and showed GTP hydrolytic activity similar to that measured for wild-type alpha(T). However, unlike the wild-type protein, the GDP-bound form of alpha(T)E203A was constitutively active toward the effector of transducin, the cyclic guanosine monophosphate phosphodiesterase. Thus, the alpha(T)E203A mutant represents a short-circuited protein switch that no longer requires GTP for the activation of the effector target phosphodiesterase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mittal, R -- Erickson, J W -- Cerione, R A -- New York, N.Y. -- Science. 1996 Mar 8;271(5254):1413-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Cornell University, Ithaca, NY 14853-6401, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596913" target="_blank"〉PubMed〈/a〉
    Keywords: 3',5'-Cyclic-GMP Phosphodiesterases/*metabolism ; Adenosine Diphosphate Ribose/metabolism ; Alanine/chemistry ; Animals ; Base Sequence ; Cattle ; Enzyme Activation ; Glutamic Acid/chemistry ; Guanosine 5'-O-(3-Thiotriphosphate)/metabolism ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/*metabolism ; Molecular Sequence Data ; Mutation ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Fusion Proteins ; Rhodopsin/metabolism ; Transducin/chemistry/genetics/*metabolism
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    A chloride channel model? (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, C -- New York, N.Y. -- Science. 1996 Nov 1;274(5288):738.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Biochemistry, Braindeis University, Waltham, MA 02254, USA. cmiller@binah.cc.brandeis.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8966555" target="_blank"〉PubMed〈/a〉
    Keywords: Chloride Channels/*chemistry ; Chlorides/chemistry ; Crystallography, X-Ray ; Extracellular Matrix Proteins/*chemistry ; Glutamine/chemistry ; Glycoproteins/*chemistry ; Matrilin Proteins ; *Protein Conformation ; *Protein Structure, Secondary
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    Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2 (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-08
    Description: Mutations in the p53 tumor suppressor are among the most frequently observed genetic alterations in human cancer and map to the 200-amino acid core domain of the protein. The core domain contains the sequence-specific DNA binding activity and the in vitro 53BP2 protein binding activity of p53. The crystal structure of the p53 core domain bound to the 53BP2 protein, which contains an SH3 (Src homology 3) domain and four ankyrin repeats, revealed that (i) the SH3 domain binds the L3 loop of p53 in a manner distinct from that of previously characterized SH3-polyproline peptide complexes, and (ii) an ankyrin repeat, which forms an L-shaped structure consisting of a beta hairpin and two alpha helices, binds the L2 loop of p53. The structure of the complex shows that the 53BP2 binding site on the p53 core domain consists of evolutionarily conserved regions that are frequently mutated in cancer and that it overlaps the site of DNA binding. The six most frequently observed p53 mutations disrupt 53BP2 binding in vitro. The structure provides evidence that the 53BP2-p53 complex forms in vivo and may have a critical role in the p53 pathway of tumor suppression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gorina, S -- Pavletich, N P -- CA65698/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 8;274(5289):1001-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8875926" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Ankyrins/*chemistry ; Apoptosis Regulatory Proteins ; Binding Sites ; Carrier Proteins/*chemistry/metabolism ; Crystallography, X-Ray ; DNA/metabolism ; Humans ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Neoplasms/genetics ; Protein Binding ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry/metabolism ; Tumor Suppressor Protein p53/*chemistry/genetics/metabolism ; *src Homology Domains
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    A mouse model of familial hypertrophic cardiomyopathy (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-05-03
    Description: A mouse model of familial hypertrophic cardiomyopathy (FHC) was generated by the introduction of an Arg 403 --〉 Gln mutation into the alpha cardiac myosin heavy chain (MHC) gene. Homozygous alpha MHC 403/403 mice died 7 days after birth, and sedentary heterozygous alpha MHC 403/+ mice survived for 1 year. Cardiac histopathology and dysfunction in the alpha MHC 403/+ mice resembled human FHC. Cardiac dysfunction preceded histopathologic changes, and myocyte disarray, hypertrophy, and fibrosis increased with age. Young male alpha MHC 403/+ mice showed more evidence of disease than did their female counterparts. Preliminary results suggested that exercise capacity may have been compromised in the alpha MHC 403/+ mice. This mouse model may help to define the natural history of FHC.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Geisterfer-Lowrance, A A -- Christe, M -- Conner, D A -- Ingwall, J S -- Schoen, F J -- Seidman, C E -- Seidman, J G -- New York, N.Y. -- Science. 1996 May 3;272(5262):731-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614836" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cardiac Output ; Cardiomyopathy, Hypertrophic/*genetics/pathology/physiopathology ; *Disease Models, Animal ; Female ; Gene Transfer Techniques ; Heart/*physiopathology ; Heterozygote ; Homozygote ; Humans ; Male ; Mice ; Mice, Mutant Strains ; Molecular Sequence Data ; Mutation ; Myocardium/chemistry/*pathology ; Myosin Heavy Chains/*genetics ; Physical Exertion ; Sex Characteristics ; Ventricular Function, Left
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    Requirement of an ICE-like protease for induction of apoptosis and ceramide generation by REAPER (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-02-09
    Description: Genetic studies indicated that the Drosophila melanogaster protein REAPER (RPR) controls apoptosis during embryo development. Induction of RPR expression in Drosophila Schneider cells rapidly stimulated apoptosis. RPR-mediated apoptosis was blocked by N-benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone (Z-VAD-fmk), which suggests that an interleukin-1 beta converting enzyme (ICE)-like protease is required for RPR function. RPR-induced apoptosis was associated with increased ceramide production that was also blocked by Z-VAD-fmk, which suggests that ceramide generation requires an ICE-like protease as well. Thus, the intracellular RPR protein uses cell death signaling pathways similar to those used by the vertebrate transmembrane receptors Fas (CD95) and tumor necrosis factor receptor type 1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pronk, G J -- Ramer, K -- Amiri, P -- Williams, L T -- New York, N.Y. -- Science. 1996 Feb 9;271(5250):808-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chiron Corporation, Emeryville, CA 94608, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8628997" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Chloromethyl Ketones/pharmacology ; Amino Acid Sequence ; Animals ; *Apoptosis/drug effects ; Caspase 1 ; Cell Line ; Ceramides/*metabolism/pharmacology ; Copper/pharmacology ; Copper Sulfate ; Cysteine Endopeptidases/*metabolism ; *Drosophila Proteins ; Drosophila melanogaster/*cytology/embryology/genetics/metabolism ; Enzyme Activation ; Gene Expression ; Molecular Sequence Data ; Peptides/genetics/*physiology ; Protease Inhibitors/pharmacology ; Signal Transduction ; Transfection
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    Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-30
    Description: Pycnodysostosis, an autosomal recessive osteochondrodysplasia characterized by osteosclerosis and short stature, maps to chromosome 1q21. Cathepsin K, a cysteine protease gene that is highly expressed in osteoclasts, localized to the pycnodysostosis region. Nonsense, missense, and stop codon mutations in the gene encoding cathepsin K were identified in patients. Transient expression of complementary DNA containing the stop codon mutation resulted in messenger RNA but no immunologically detectable protein. Thus, pycnodysostosis results from gene defects in a lysosomal protease with highest expression in osteoclasts. These findings suggest that cathepsin K is a major protease in bone resorption, providing a possible rationale for the treatment of disorders such as osteoporosis and certain forms of arthritis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gelb, B D -- Shi, G P -- Chapman, H A -- Desnick, R J -- R01 DK31775/DK/NIDDK NIH HHS/ -- R01 HL44816/HL/NHLBI NIH HHS/ -- R37 DK34045/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Aug 30;273(5279):1236-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Human Genetics and Division of Pediatric Cardiology, Mount Sinai School of Medicine, New York, NY 10029, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703060" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Bone Matrix/metabolism ; Bone Resorption ; Cathepsin K ; Cathepsins/deficiency/*genetics/metabolism ; Chromosome Mapping ; Chromosomes, Human, Pair 1 ; Codon, Terminator ; Dinucleoside Phosphates/genetics ; Humans ; Lysosomal Storage Diseases/enzymology/*genetics ; Lysosomes/*enzymology ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutation ; Osteochondrodysplasias/enzymology/*genetics ; Osteoclasts/*enzymology ; Transfection
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    CKI1, a histidine kinase homolog implicated in cytokinin signal transduction (1996)
    American Association for the Advancement of Science (AAAS)
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    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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    PKD2, a gene for polycystic kidney disease that encodes an integral membrane protein (1996)
    American Association for the Advancement of Science (AAAS)
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    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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    Form follows function when plants harvest light (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-06-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moffat, A S -- New York, N.Y. -- Science. 1996 Jun 21;272(5269):1743-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650571" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carotenoids/*chemistry/metabolism ; Crystallography, X-Ray ; Dinoflagellida/*chemistry/metabolism ; Light ; Photosynthesis ; *Protein Conformation ; Protozoan Proteins/*chemistry/metabolism
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    Fly gene discovery gets at root of branching structures (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-12-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1996 Dec 20;274(5295):2011.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8984660" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Body Patterning ; *Drosophila Proteins ; Drosophila melanogaster/embryology/*genetics ; Fibroblast Growth Factors/chemistry ; Gene Expression Regulation, Developmental ; *Genes, Insect ; Insect Proteins/chemistry/*genetics/metabolism/physiology ; Larva/growth & development ; Morphogenesis ; Mutation ; *Protein-Tyrosine Kinases ; Receptors, Fibroblast Growth Factor/genetics/metabolism ; Trachea/embryology
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    Hedgehog's patterning call is patched through, smoothly (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1996 Nov 22;274(5291):1304-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8966601" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Body Patterning ; Carcinoma, Basal Cell/genetics/therapy ; Hedgehog Proteins ; Humans ; Membrane Proteins/genetics/*metabolism ; Mutation ; Proteins/*metabolism ; Receptors, Cell Surface/*metabolism/physiology ; *Receptors, G-Protein-Coupled ; Signal Transduction ; Skin Neoplasms/genetics/therapy ; *Trans-Activators
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    Interaction between Wingless and Notch signaling pathways mediated by dishevelled (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-29
    Description: In Drosophila, the Wingless and Notch signaling pathways function in m any of the same developmental patterning events. Genetic analysis demonstrates that the dishevelled gene, which encodes a molecule previously implicated in implementation of the Winglass signal, interacts antagonistically with Notch and one of its known ligands, Delta. A direct physical interaction between Dishevelled and the Notch carboxyl terminus, distal to the cdc10/ankyrin repeats, suggests a mechanism for this interaction. It is proposed that Dishevelled, in addition to transducing the Wingless signal, blocks Notch signaling directly, thus providing a molecular mechanism for the inhibitory cross talk observed between these pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Axelrod, J D -- Matsuno, K -- Artavanis-Tsakonas, S -- Perrimon, N -- New York, N.Y. -- Science. 1996 Mar 29;271(5257):1826-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596950" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Clone Cells ; Drosophila/genetics/growth & development/*metabolism ; *Drosophila Proteins ; Genes, Insect ; Intracellular Signaling Peptides and Proteins ; Membrane Proteins/antagonists & inhibitors/genetics/*metabolism ; Molecular Sequence Data ; Mutation ; Phenotype ; *Phosphoproteins ; Proteins/genetics/*metabolism ; Proto-Oncogene Proteins/genetics/*metabolism ; Pupa/metabolism ; Receptors, Notch ; *Signal Transduction ; Wings, Animal/cytology/growth & development ; Wnt1 Protein
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    Liver failure and defective hepatocyte regeneration in interleukin-6-deficient mice (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-22
    Description: Liver regeneration stimulated by a loss of liver mass leads to hepatocyte and nonparenchymal cell proliferation and rapid restoration of liver parenchyma. Mice with targeted disruption of the interleukin-6 (IL-6) gene had impaired liver regeneration characterized by liver necrosis and failure. There was a blunted DNA synthetic response in hepatocytes of these mice but not in nonparenchymal liver cells. Furthermore, there were discrete G1 phase (prereplicative stage in the cell cycle) abnormalities including absence of STAT3 (signal transducer and activator of transcription protein 3) activation and depressed AP-1, Myc, and cyclin D1 expression. Treatment of IL-6-deficient mice with a single preoperative dose of IL-6 returned STAT3 binding, gene expression, and hepatocyte proliferation to near normal and prevented liver damage, establishing that IL-6 is a critical component of the regenerative response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cressman, D E -- Greenbaum, L E -- DeAngelis, R A -- Ciliberto, G -- Furth, E E -- Poli, V -- Taub, R -- DK44237/DK/NIDDK NIH HHS/ -- DK49210/DK/NIDDK NIH HHS/ -- DK49629/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Nov 22;274(5291):1379-83.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics and Medicine, University of Pennsylvania School of Medicine, 705a Stellar-Chance, 422 Curie Boulevard, Philadelphia, PA 19104-6145, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8910279" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cyclin D1 ; Cyclins/biosynthesis ; DNA/biosynthesis/metabolism ; DNA-Binding Proteins/metabolism ; G1 Phase ; Gene Expression Regulation ; Gene Targeting ; Genes, Immediate-Early ; Hepatectomy ; Interleukin-6/deficiency/genetics/pharmacology/*physiology ; Liver/*cytology/metabolism/pathology ; Liver Failure/*etiology/pathology ; *Liver Regeneration ; Mice ; Mice, Inbred C57BL ; Mitosis ; Mutation ; Necrosis ; Oncogene Proteins/biosynthesis ; Proto-Oncogene Proteins c-myc/biosynthesis ; STAT3 Transcription Factor ; Trans-Activators/metabolism ; Transcription Factor AP-1/biosynthesis
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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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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    New virus variant killed Serengeti cats (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1996 Feb 2;271(5249):596.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8571120" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Distemper/transmission/*virology ; Distemper Virus, Canine/classification/*genetics ; Dogs ; *Genome, Viral ; Humans ; Lions/*virology ; Mutation ; Species Specificity ; Tanzania
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-24
    Description: The crystal structure of bovine heart cytochrome c oxidase at 2.8 A resolution with an R value of 19.9 percent reveals 13 subunits, each different from the other, five phosphatidyl ethanolamines, three phosphatidyl glycerols and two cholates, two hemes A, and three copper, one magnesium, and one zinc. Of 3606 amino acid residues in the dimer, 3560 have been converged to a reasonable structure by refinement. A hydrogen-bonded system, including a propionate of a heme A (heme a), part of peptide backbone, and an imidazole ligand of CuA, could provide an electron transfer pathway between CuA and heme a. Two possible proton pathways for pumping, each spanning from the matrix to the cytosolic surfaces, were identified, including hydrogen bonds, internal cavities likely to contain water molecules, and structures that could form hydrogen bonds with small possible conformational change of amino acid side chains. Possible channels for chemical protons to produce H2O, for removing the produced water, and for O2, respectively, were identified.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tsukihara, T -- Aoyama, H -- Yamashita, E -- Tomizaki, T -- Yamaguchi, H -- Shinzawa-Itoh, K -- Nakashima, R -- Yaono, R -- Yoshikawa, S -- New York, N.Y. -- Science. 1996 May 24;272(5265):1136-44.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Protein Research, Osaka University, Suita, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638158" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cattle ; Cell Nucleus/genetics ; Copper/analysis ; Crystallography, X-Ray ; Electron Transport ; Electron Transport Complex IV/*chemistry/genetics/metabolism ; Heme/analogs & derivatives/analysis ; Hydrogen Bonding ; Iron/analysis ; Membrane Proteins/chemistry ; Mitochondria, Heart/genetics ; Models, Molecular ; Molecular Sequence Data ; Molecular Weight ; Myocardium/enzymology ; Nucleotides/metabolism ; Oxidation-Reduction ; Oxygen/metabolism ; Phospholipids/analysis ; *Protein Conformation ; Protein Structure, Secondary ; Proton Pumps ; Water/metabolism
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    DPC4, a candidate tumor suppressor gene at human chromosome 18q21.1 (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-19
    Description: About 90 percent of human pancreatic carcinomas show allelic loss at chromosome 18q. To identify candidate tumor suppressor genes on 18q, a panel of pancreatic carcinomas were analyzed for convergent sites of homozygous deletion. Twenty-five of 84 tumors had homozygous deletions at 18q21.1, a site that excludes DCC (a candidate suppressor gene for colorectal cancer) and includes DPC4, a gene similar in sequence to a Drosophila melanogaster gene (Mad) implicated in a transforming growth factor-beta (TGF-beta)-like signaling pathway. Potentially inactivating mutations in DPC4 were identified in six of 27 pancreatic carcinomas that did not have homozygous deletions at 18q21.1. These results identify DPC4 as a candidate tumor suppressor gene whose inactivation may play a role in pancreatic and possibly other human cancers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hahn, S A -- Schutte, M -- Hoque, A T -- Moskaluk, C A -- da Costa, L T -- Rozenblum, E -- Weinstein, C L -- Fischer, A -- Yeo, C J -- Hruban, R H -- Kern, S E -- CA62924/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 19;271(5247):350-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8553070" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Division ; Chromosome Mapping ; *Chromosomes, Human, Pair 18 ; *DNA-Binding Proteins ; Gene Deletion ; Gene Expression ; *Genes, Tumor Suppressor ; Genetic Markers ; Humans ; Mice ; Molecular Sequence Data ; Mutation ; Neoplasm Transplantation ; Pancreatic Neoplasms/*genetics/pathology ; Proteins/chemistry/*genetics/physiology ; Signal Transduction ; Smad4 Protein ; *Trans-Activators ; Transforming Growth Factor beta/physiology ; Transplantation, Heterologous ; Tumor Cells, Cultured
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    Rapid degradation of the G1 cyclin Cln2 induced by CDK-dependent phosphorylation (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-15
    Description: Cyclins regulate the major cell cycle transitions in eukaryotes through association with cyclin-dependent protein kinases (CDKs). In yeast, G1 cyclins are essential, rate-limiting activators of cell cycle initiation. G1-specific accumulation of one G1 cyclin, Cln2, results from periodic gene expression coupled with rapid protein turnover. Site-directed mutagenesis of CLN2 revealed that its phosphorylation provides a signal that promotes rapid degradation. Cln2 phosphorylation is dependent on the Cdc28 protein kinase, the CDK that it activates. These findings suggest that Cln2 is rendered self-limiting by virtue of its ability to activate its cognate CDK subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lanker, S -- Valdivieso, M H -- Wittenberg, C -- GM43487/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1597-601.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599119" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; CDC28 Protein Kinase, S cerevisiae/*metabolism ; Cyclins/genetics/*metabolism ; Enzyme Activation ; Fungal Proteins/genetics/metabolism ; *G1 Phase ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutation ; Phenotype ; Phosphorylation ; Saccharomyces cerevisiae/cytology/metabolism ; Saccharomyces cerevisiae Proteins
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    Green light for steroid hormones (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Russell, D W -- New York, N.Y. -- Science. 1996 Apr 19;272(5260):370-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235-9046, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8602524" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Oxo-5-alpha-Steroid 4-Dehydrogenase/chemistry ; Arabidopsis/genetics/*growth & development/metabolism ; *Arabidopsis Proteins ; Brassinosteroids ; Cholestanols/*metabolism ; Cytochrome P-450 Enzyme System/genetics/metabolism ; *Genes, Plant ; Light ; Mutation ; Plant Growth Regulators/biosynthesis/*metabolism ; Plant Proteins/chemistry/*genetics/metabolism ; Steroids, Heterocyclic/*metabolism
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    Mutant mice and worms help solve mysteries of olfaction (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):500-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8928002" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/genetics/physiology ; Cyclic AMP/*physiology ; Inositol Phosphates/physiology ; Ion Channels/genetics/*physiology ; Mice ; Mice, Knockout ; Mutation ; Neurons, Afferent/physiology ; Odors ; Olfactory Receptor Neurons/*physiology ; Sensation/*physiology ; Sexual Behavior, Animal ; Signal Transduction ; Smell/*physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    AT-AC introns: an ATtACk on dogma (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mount, S M -- New York, N.Y. -- Science. 1996 Mar 22;271(5256):1690-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Maryland, College Park 20742-4415, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596928" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Composition ; Base Sequence ; Consensus Sequence ; Humans ; *Introns ; Molecular Sequence Data ; Mutation ; RNA Precursors/*genetics/metabolism ; *RNA Splicing ; RNA, Small Nuclear/metabolism ; Spliceosomes/metabolism
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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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    Genetic clues to Alzheimer's disease (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dewji, N N -- Singer, S J -- New York, N.Y. -- Science. 1996 Jan 12;271(5246):159-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Medicine, University of California at San Diego, La Jolla 92093-0322, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539612" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*genetics/metabolism ; Amyloid beta-Peptides/biosynthesis ; Amyloid beta-Protein Precursor/*genetics/metabolism ; Animals ; Brain/metabolism ; Caenorhabditis elegans/growth & development ; *Caenorhabditis elegans Proteins ; Drosophila/genetics/growth & development ; *Drosophila Proteins ; Eye Proteins/metabolism ; Female ; Helminth Proteins/genetics/metabolism ; Humans ; Membrane Glycoproteins/metabolism ; Membrane Proteins/*genetics/metabolism ; Mutation ; Neurons/metabolism ; Photoreceptor Cells, Invertebrate/growth & development/metabolism ; Presenilin-1 ; Presenilin-2 ; *Receptor Protein-Tyrosine Kinases ; Receptors, Notch ; *Receptors, Peptide ; Signal Transduction ; Vulva/growth & development/metabolism
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    An intriguing new lead on Huntington's disease (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1996 Mar 1;271(5253):1233-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638101" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*metabolism ; Glyceraldehyde-3-Phosphate Dehydrogenases/antagonists & inhibitors/*metabolism ; Glycolysis ; Humans ; Huntington Disease/genetics/*metabolism ; Mutation ; Nerve Tissue Proteins/chemistry/genetics/*metabolism ; Nervous System Diseases/metabolism ; Nuclear Proteins/chemistry/genetics/*metabolism ; Peptides/metabolism ; Repetitive Sequences, Nucleic Acid
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    Regulation of RAD53 by the ATM-like kinases MEC1 and TEL1 in yeast cell cycle checkpoint pathways (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-19
    Description: Mutants of the Saccharomyces cerevisiae ataxia telangiectasia mutated (ATM) homolog MEC1/SAD3/ESR1 were identified that could live only if the RAD53/SAD1 checkpoint kinase was overproduced. MEC1 and a structurally related gene, TEL1, have overlapping functions in response to DNA damage and replication blocks that in mutants can be provided by overproduction of RAD53. Both MEC1 and TEL1 were found to control phosphorylation of Rad53p in response to DNA damage. These results indicate that RAD53 is a signal transducer in the DNA damage and replication checkpoint pathways and functions downstream of two members of the ATM lipid kinase family. Because several members of this pathway are conserved among eukaryotes, it is likely that a RAD53-related kinase will function downstream of the human ATM gene product and play an important role in the mammalian response to DNA damage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sanchez, Y -- Desany, B A -- Jones, W J -- Liu, Q -- Wang, B -- Elledge, S J -- DK07696/DK/NIDDK NIH HHS/ -- GM44664/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 19;271(5247):357-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Verna and Mars McLean Department of Biochemistry, Department of Molecular and Human Genetics, Howard Hughes Medical Institute, 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/8553072" target="_blank"〉PubMed〈/a〉
    Keywords: Ataxia Telangiectasia Mutated Proteins ; Base Sequence ; *Cell Cycle ; *Cell Cycle Proteins ; Checkpoint Kinase 2 ; *DNA Damage ; DNA Replication ; DNA-Binding Proteins ; Fungal Proteins/*genetics/metabolism ; Gene Expression Regulation, Fungal ; *Genes, Fungal ; Intracellular Signaling Peptides and Proteins ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Protein Kinases/*genetics/metabolism ; *Protein-Serine-Threonine Kinases ; Proteins/genetics/metabolism ; Saccharomyces cerevisiae/cytology/*genetics/metabolism ; *Saccharomyces cerevisiae Proteins ; Signal Transduction ; Tumor Suppressor Proteins
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    Researchers nail down leptin receptor (1996)
    American Association for the Advancement of Science (AAAS)
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    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
    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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  • 86
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    In vitro development of primitive and definitive erythrocytes from different precursors (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-03
    Description: During mouse embryogenesis the production of "primitive" erythrocytes (EryP) precedes the production of "definitive" erythrocytes (EryD) in parallel with the transition of the hematopoietic site from the yolk sac to the fetal liver. On a macrophage colony-stimulating factor-deficient stromal cell line OP9, mouse embryonic stem cells were shown to give rise to EryP and EryD sequentially with a time course similar to that seen in murine ontogeny. Studies of the different growth factor requirements and limiting dilution analysis of precursor frequencies indicate that most EryP and EryD probably developed from different precursors by way of distinct differentiation pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakano, T -- Kodama, H -- Honjo, T -- New York, N.Y. -- Science. 1996 May 3;272(5262):722-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Chemistry, Faculty of Medicine, Kyoto University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614833" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Division ; Cell Line ; Cell Lineage ; Cell Separation ; Cells, Cultured ; Coculture Techniques ; Erythroid Precursor Cells/*cytology ; *Erythropoiesis ; Erythropoietin/pharmacology ; Kinetics ; Mice ; Signal Transduction ; Stem Cell Factor/physiology
    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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  • 87
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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
    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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  • 88
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    Dating the cenancester of organisms (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hasegawa, M -- Fitch, W M -- New York, N.Y. -- Science. 1996 Dec 6;274(5293):1750; author reply 1751-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8984636" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Evolution, Molecular ; Models, Statistical ; Mutation ; Proteins/*chemistry/genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 89
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    Estimating the age of the common ancestor of men from the ZFY intron (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Donnelly, P -- Tavare, S -- Balding, D J -- Griffiths, R C -- GM36232/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 May 31;272(5266):1357-9; author reply 1361-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650551" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA-Binding Proteins/*genetics ; *Genetics, Population ; Hominidae/*genetics ; Humans ; Introns/*genetics ; Kruppel-Like Transcription Factors ; Male ; Mutation ; Polymorphism, Genetic ; Population Density ; Probability ; Time Factors ; Transcription Factors/*genetics ; Y Chromosome/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 90
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    An essential role for NF-kappaB in preventing TNF-alpha-induced cell death (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-01
    Description: Studies on mice deficient in nuclear factor kappa B (NF-kappaB) subunits have shown that this transcription factor is important for lymphocyte responses to antigens and cytokine-inducible gene expression. In particular, the RelA (p65) subunit is required for induction of tumor necrosis factor-alpha (TNF-alpha)-dependent genes. Treatment of RelA-deficient (RelA-/-) mouse fibroblasts and macrophages with TNF-alpha resulted in a significant reduction in viability, whereas RelA+/+ cells were unaffected. Cytotoxicity to both cell types was mediated by TNF receptor 1. Reintroduction of RelA into RelA-/- fibroblasts resulted in enhanced survival, demonstrating that the presence of RelA is required for protection from TNF-alpha. These results have implications for the treatment of inflammatory and proliferative diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beg, A A -- Baltimore, D -- New York, N.Y. -- Science. 1996 Nov 1;274(5288):782-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8864118" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Antigens, CD/metabolism ; *Cell Death ; Cell Survival ; Cells, Cultured ; Gene Expression Regulation ; Humans ; Macrophages/cytology ; Mice ; NF-kappa B/genetics/*physiology ; Receptors, Tumor Necrosis Factor/metabolism ; Receptors, Tumor Necrosis Factor, Type I ; Signal Transduction ; Transcription Factor RelA ; Transfection ; Tumor Necrosis Factor-alpha/*pharmacology/physiology
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  • 91
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    Change of a catalytic reaction carried out by a DNA replication protein (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-11-01
    Description: The RepA protein of plasmid pC194 initiates and terminates rolling circle replication. At initiation, it forms a 5'-phosphotyrosyl DNA link, whereas at termination, a glutamate residue directs hydrolytic cleavage of the newly synthesized origin, and the resulting 3'-hydroxyl group undergoes transesterification with the phosphotyrosine link. The protein is thus released from DNA, and the termination is uncoupled from reinitiation of replication. Replacement of the glutamate with tyrosine in RepA altered this mechanism, so that termination occurred by two successive transesterifications and became coupled to reinitiation. This result suggests that various enzymes involved in DNA cleavage and rejoining may have similar mechanistic and evolutionary roots.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Noirot-Gros, M F -- Ehrlich, S D -- New York, N.Y. -- Science. 1996 Nov 1;274(5288):777-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genetique Microbienne, Institut National de la Recherche Agronomique, Domaine de Vilvert, 78352 Jouy en Josas Cedex, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8864116" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage phi X 174 ; Binding Sites ; *DNA Helicases ; *DNA Replication ; DNA, Bacterial/*metabolism ; DNA, Single-Stranded/metabolism ; DNA, Viral/metabolism ; *DNA-Binding Proteins ; Esterification ; Evolution, Molecular ; Glutamic Acid/metabolism ; Hydrolysis ; Mutation ; Plasmids ; Proteins/chemistry/genetics/*metabolism ; *Trans-Activators ; Tyrosine/metabolism ; Viral Proteins/metabolism
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  • 92
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    Rho1p, a yeast protein at the interface between cell polarization and morphogenesis (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-04-12
    Description: The enzyme that catalyzes the synthesis of the major structural component of the yeast cell wall, beta(1--〉3)-D-glucan synthase (also known as 1,3-beta-glucan synthase), requires a guanosine triphosphate (GTP) binding protein for activity. The GTP binding protein was identified as Rho1p. The rho1 mutants were defective in GTP stimulation of glucan synthase, and the defect was corrected by addition of purified or recombinant Rho1p. A protein missing in purified preparations from a rho1 strain was identified as Rho1p. Rho1p also regulates protein kinase C, which controls a mitogen-activated protein kinase cascade. Experiments with a dominant positive PKC1 gene showed that the two effects of Rho1p are independent of each other. The colocalization of Rho1p with actin patches at the site of bud emergence and the role of Rho1p in cell wall synthesis emphasize the importance of Rho1p in polarized growth and morphogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Drgonova, J -- Drgon, T -- Tanaka, K -- Kollar, R -- Chen, G C -- Ford, R A -- Chan, C S -- Takai, Y -- Cabib, E -- New York, N.Y. -- Science. 1996 Apr 12;272(5259):277-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory od Biochemistry and Metabolism, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8602514" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Polarity ; Cell Wall/metabolism ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/genetics/*metabolism ; Glucans/biosynthesis ; Glucosyltransferases/*metabolism ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Guanosine Triphosphate/metabolism ; *Membrane Proteins ; Morphogenesis ; Mutation ; Protein Kinase C/metabolism ; Recombinant Proteins/pharmacology ; Saccharomyces cerevisiae/cytology/genetics/growth & development/*metabolism ; Saccharomyces cerevisiae Proteins ; *Schizosaccharomyces pombe Proteins ; Temperature ; *beta-Glucans ; *rho GTP-Binding Proteins
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  • 93
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    Immunodeficiency in protein kinase cbeta-deficient mice (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-09
    Description: Cross-linking of the antigen receptor on lymphocytes by antigens or antibodies to the receptor results in activation of enzymes of the protein kinase C (PKC) family. Mice homozygous for a targeted disruption of the gene encoding the PKC-betaI and PKC-betaII isoforms develop an immunodeficiency characterized by impaired humoral immune responses and reduced cellular responses of B cells, which is similar to X-linked immunodeficiency in mice. Thus PKC-betaI and PKC-betaII play an important role in B cell activation and may be functionally linked to Bruton's tyrosine kinase in antigen receptor-mediated signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leitges, M -- Schmedt, C -- Guinamard, R -- Davoust, J -- Schaal, S -- Stabel, S -- Tarakhovsky, A -- New York, N.Y. -- Science. 1996 Aug 9;273(5276):788-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Delbruck-Laboratorium in der Max-Planck-Gesellschaft, Carl-von-Linne-Weg 10, D-50829 Koln, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8670417" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/*immunology ; Gene Targeting ; Genetic Linkage ; Immunoglobulin G/blood ; Immunoglobulin M/blood/immunology ; Immunoglobulins/*blood ; Immunologic Deficiency Syndromes/enzymology/*immunology ; Lymphocyte Activation ; Lymphocyte Count ; Mice ; Protein Kinase C/deficiency/genetics/*physiology ; Protein Kinase C beta ; Protein-Tyrosine Kinases/genetics/metabolism ; Receptors, Antigen, B-Cell/immunology ; Signal Transduction ; T-Lymphocytes/immunology ; X Chromosome
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  • 94
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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)
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    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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  • 95
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    New database (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-04-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vondrasek, J -- Wlodawer, A -- New York, N.Y. -- Science. 1996 Apr 19;272(5260):337-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8602518" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartic Acid Endopeptidases/*chemistry ; Computer Communication Networks ; Crystallography, X-Ray ; *Databases, Factual ; HIV Protease/*chemistry ; HIV-1/enzymology ; HIV-2/enzymology ; National Institutes of Health (U.S.) ; Simian Immunodeficiency Virus/enzymology ; United States
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  • 96
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    A cyclophilin function in Hsp90-dependent signal transduction (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-06
    Description: Cpr6 and Cpr7, the Saccharomyces cerevisiae homologs of cyclophilin-40 (CyP-40), were shown to form complexes with Hsp90, a protein chaperone that functions in several signal transduction pathways. Deletion of CPR7 caused severe growth defects when combined with mutations that decrease the amount of Hsp90 or Sti1, another component of the Hsp90 chaperone machinery. The activities of two heterologous Hsp90-dependent signal transducers expressed in yeast, glucocorticoid receptor and pp60(v-src) kinase, were adversely affected by cpr7 null mutations. These results suggest that CyP-40 cyclophilins play a general role in Hsp90-dependent signal transduction pathways under normal growth conditions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Duina, A A -- Chang, H C -- Marsh, J A -- Lindquist, S -- Gaber, R F -- GM25874/GM/NIGMS NIH HHS/ -- GM45739/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Dec 6;274(5293):1713-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, 2153 Sheridan Road, Evanston, IL 60208, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8939862" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Isomerases/genetics/metabolism/*physiology ; Carrier Proteins/genetics/metabolism/*physiology ; *Cyclophilins ; Fungal Proteins/genetics/metabolism/*physiology ; HSP90 Heat-Shock Proteins/genetics/metabolism/*physiology ; Heat-Shock Proteins ; Molecular Chaperones/genetics/metabolism/*physiology ; Mutation ; Oncogene Protein pp60(v-src)/metabolism ; *Peptidylprolyl Isomerase ; Proto-Oncogene Proteins pp60(c-src)/metabolism ; Receptors, Glucocorticoid/metabolism ; Saccharomyces cerevisiae/genetics/growth & development/metabolism/*physiology ; Saccharomyces cerevisiae Proteins ; *Signal Transduction
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  • 97
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    Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-06-14
    Description: The molybdoenzyme dimethylsulfoxide (DMSO) reductase contributes to the release of dimethylsulfide, a compound that has been implicated in cloud nucleation and global climate regulation. The crystal structure of DMSO reductase from Rhodobacter sphaeroides reveals a monooxo molybdenum cofactor containing two molybdopterin guanine dinucleotides that asymmetrically coordinate the molybdenum through their dithiolene groups. One of the pterins exhibits different coordination modes to the molybdenum between the oxidized and reduced states, whereas the side chain oxygen of Ser147 coordinates the metal in both states. The change in pterin coordination between the Mo(VI) and Mo(IV) forms suggests a mechanism for substrate binding and reduction by this enzyme. Sequence comparisons of DMSO reductase with a family of bacterial oxotransferases containing molybdopterin guanine dinucleotide indicate a similar polypeptide fold and active site with two molybdopterins within this family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schindelin, H -- Kisker, C -- Hilton, J -- Rajagopalan, K V -- Rees, D C -- GM00091/GM/NIGMS NIH HHS/ -- GM50775/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1615-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658134" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Coenzymes/*chemistry ; Crystallography, X-Ray ; *Iron-Sulfur Proteins ; Metalloproteins/*chemistry ; Models, Molecular ; Molecular Sequence Data ; Oxidation-Reduction ; Oxidoreductases/*chemistry/metabolism ; Protein Conformation ; Pteridines/*chemistry ; Rhodobacter sphaeroides/*enzymology ; Sequence Homology, Amino Acid
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  • 98
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    Conditional circadian dysfunction of the Arabidopsis early-flowering 3 mutant (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-11-01
    Description: Photoperiodic responses, such as the daylength-dependent control of reproductive development, are associated with a circadian biological clock. The photoperiod-insensitive early-flowering 3 (elf3) mutant of Arabidopsis thaliana lacks rhythmicity in two distinct circadian-regulated processes. This defect was apparent only when plants were assayed under constant light conditions. elf3 mutants retain rhythmicity in constant dark and anticipate light/dark transitions under most light/dark regimes. The conditional arrhythmic phenotype suggests that the circadian pacemaker is intact in darkness in elf3 mutant plants, but the transduction of light signals to the circadian clock is impaired.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hicks, K A -- Millar, A J -- Carre, I A -- Somers, D E -- Straume, M -- Meeks-Wagner, D R -- Kay, S A -- 1R01GM46006/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 1;274(5288):790-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8864121" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/growth & development/*physiology ; *Circadian Rhythm ; Darkness ; Gene Expression Regulation, Plant ; Genes, Plant ; *Light ; Movement ; Mutation ; Phenotype ; *Photoperiod ; Photosynthetic Reaction Center Complex Proteins/genetics ; Plant Leaves/physiology ; Plants, Genetically Modified
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  • 99
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    Enhanced fidelity of 3TC-selected mutant HIV-1 reverse transcriptase (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-01
    Description: Monotherapy with (-)2',3'-dideoxy-3'-thiacytidine (3TC) leads to the appearance of a drug-resistant variant of human immunodeficiency virus-type 1 (HIV-1) with the methionine-184 --〉 valine (M184V) substitution in the reverse transcriptase (RT). Despite resulting drug resistance, treatment for more than 48 weeks is associated with a lower plasma viral burden than that at baseline. Studies to investigate this apparent contradiction revealed the following. (i) Titers of HIV-neutralizing antibodies remained stable in 3TC-treated individuals in contrast to rapid declines in those treated with azidothymidine (AZT). (ii) Unlike wild-type HIV, growth of M184V HIV in cell culture in the presence of d4T, AZT, Nevirapine, Delavirdine, or Saquinavir did not select for variants displaying drug resistance. (iii) There was an increase in fidelity of nucleotide insertion by the M184V mutant compared with wild-type enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wainberg, M A -- Drosopoulos, W C -- Salomon, H -- Hsu, M -- Borkow, G -- Parniak, M -- Gu, Z -- Song, Q -- Manne, J -- Islam, S -- Castriota, G -- Prasad, V R -- P30 AI-27741/AI/NIAID NIH HHS/ -- R01 AI0-30861/AI/NIAID NIH HHS/ -- UO1AI-24845/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Mar 1;271(5253):1282-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉McGill AIDS Centre, Jewish General Hospital, Montreal, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638110" target="_blank"〉PubMed〈/a〉
    Keywords: Antiviral Agents/*pharmacology/therapeutic use ; Base Composition ; Base Sequence ; Deoxyribonucleotides/metabolism ; Drug Resistance, Microbial ; HIV Antibodies/blood/immunology ; HIV Infections/drug therapy/*virology ; HIV Protease Inhibitors/pharmacology ; HIV Reverse Transcriptase ; HIV-1/drug effects/*enzymology/genetics/immunology/physiology ; Humans ; Isoquinolines/pharmacology ; Lamivudine ; Molecular Sequence Data ; Mutation ; Neutralization Tests ; Quinolines/pharmacology ; RNA-Directed DNA Polymerase/drug effects/*genetics/metabolism ; Reverse Transcriptase Inhibitors/*pharmacology/therapeutic use ; Saquinavir ; Virus Replication/drug effects ; Zalcitabine/*analogs & derivatives/pharmacology/therapeutic use
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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    Population dynamics of immune responses to persistent viruses (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-05
    Description: Mathematical models, which are based on a firm understanding of biological interactions, can provide nonintuitive insights into the dynamics of host responses to infectious agents and can suggest new avenues for experimentation. Here, a simple mathematical approach is developed to explore the relation between antiviral immune responses, virus load, and virus diversity. The model results are compared to data on cytotoxic T cell responses and viral diversity in infections with the human T cell leukemia virus (HTLV-1) and the human immunodeficiency virus (HIV-1).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nowak, M A -- Bangham, C R -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1996 Apr 5;272(5258):74-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Oxford, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8600540" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Viral/immunology ; Antigenic Variation ; Antigens, Viral/immunology ; Cytokines/immunology ; Cytotoxicity, Immunologic ; Epitopes/immunology ; Genetic Variation ; HIV Infections/immunology/virology ; HIV-1/immunology/physiology ; HTLV-I Infections/immunology/virology ; Human T-lymphotropic virus 1/genetics/immunology/physiology ; Humans ; *Models, Biological ; Mutation ; Population Dynamics ; T-Lymphocytes, Cytotoxic/*immunology ; Virus Diseases/*immunology/virology ; Virus Physiological Phenomena ; Virus Replication ; Viruses/genetics/*immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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