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  • Articles  (64)
  • Signal Transduction  (64)
  • American Association for the Advancement of Science (AAAS)  (64)
  • American Association of Petroleum Geologists (AAPG)
  • Emerald
  • Frontiers Media
  • 2020-2022
  • 1995-1999  (64)
  • 1996  (64)
  • Physics  (64)
  • Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • Articles  (64)
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  • American Association for the Advancement of Science (AAAS)  (64)
  • American Association of Petroleum Geologists (AAPG)
  • Emerald
  • Frontiers Media
Years
  • 2020-2022
  • 1995-1999  (64)
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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
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  • 2
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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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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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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  • 5
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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
    Print ISSN: 0036-8075
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  • 6
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    Does leptin contribute to diabetes caused by obesity? (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 7
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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)
    Details
    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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  • 8
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    Horizontal cells of the primate retina: cone specificity without spectral opponency (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
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  • 9
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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
    Print ISSN: 0036-8075
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  • 10
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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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  • 11
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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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  • 12
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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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  • 13
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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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 14
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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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  • 15
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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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  • 16
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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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  • 17
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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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  • 18
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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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  • 19
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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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  • 20
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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)
    Details
    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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  • 21
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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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  • 22
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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
    Print ISSN: 0036-8075
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  • 23
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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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  • 24
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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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  • 25
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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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  • 26
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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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  • 27
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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
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    Interfering with apoptosis: Ca(2+)-binding protein ALG-2 and Alzheimer's disease gene ALG-3 (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-26
    Description: Two apoptosis-linked genes, named ALG-2 and ALG-3, were identified by means of a functional selection strategy. ALG-2 codes for a Ca(2+)-binding protein required for T cell receptor-, Fas-, and glucocorticoid-induced cell death. ALG-3, a partial complementary DNA that is homologous to the familial Alzheimer's disease gene STM2, rescues a T cell hybridoma from T cell receptor- and Fas-induced apoptosis. These findings suggest that ALG-2 may mediate Ca(2+)-regulated signals along the death pathway and that cell death may play a role in Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vito, P -- Lacana, E -- D'Adamio, L -- New York, N.Y. -- Science. 1996 Jan 26;271(5248):521-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉T Cell Molecular Biology Unit, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8560270" target="_blank"〉PubMed〈/a〉
    Keywords: Alkaloids/pharmacology ; Alzheimer Disease/*genetics ; Amino Acid Sequence ; Animals ; Antigens, CD95/metabolism ; *Apoptosis/drug effects ; Apoptosis Regulatory Proteins ; Calcium/metabolism ; Calcium-Binding Proteins/chemistry/genetics/*physiology ; Cell Line ; Cloning, Molecular ; DNA, Complementary ; Dactinomycin/pharmacology ; Dexamethasone/pharmacology ; Fas Ligand Protein ; Hybridomas ; Interleukin-2/metabolism ; Membrane Glycoproteins/metabolism ; Membrane Proteins/chemistry/genetics/*physiology ; Mice ; Molecular Sequence Data ; Presenilin-2 ; Receptors, Antigen, T-Cell/physiology ; Signal Transduction ; Staurosporine ; T-Lymphocytes ; Transfection ; Up-Regulation
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    An essential role for NF-kappaB in preventing TNF-alpha-induced cell death (1996)
    American Association for the Advancement of Science (AAAS)
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    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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    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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    Regulation of rate of cartilage differentiation by Indian hedgehog and PTH-related protein (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-02
    Description: Proper regulation of chondrocyte differentiation is necessary for the morphogenesis of skeletal elements, yet little is known about the molecular regulation of this process. A chicken homolog of Indian hedgehog (Ihh), a member of the conserved Hedgehog family of secreted proteins that is expressed during bone formation, has now been isolated. Ihh has biological properties similar to those of Sonic hedgehog (Shh), including the ability to regulate the conserved targets Patched (Ptc) and Gli. Ihh is expressed in the prehypertrophic chondrocytes of cartilage elements, where it regulates the rate of hypertrophic differentiation. Misexpression of Ihh prevents proliferating chondrocytes from initiating the hypertrophic differentiation process. The direct target of Ihh signaling is the perichondrium, where Gli and Ptc flank the expression domain of Ihh. Ihh induces the expression of a second signal, parathyroid hormone-related protein (PTHrP), in the periarticular perichondrium. Analysis of PTHrP (-/-) mutant mice indicated that the PTHrP protein signals to its receptor in the prehypertrophic chondrocytes, thereby blocking hypertrophic differentiation. In vitro application of Hedgehog or PTHrP protein to normal or PTHrP (-/-) limb explants demonstrated that PTHrP mediates the effects of Ihh through the formation of a negative feedback loop that modulates the rate of chondrocyte differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vortkamp, A -- Lee, K -- Lanske, B -- Segre, G V -- Kronenberg, H M -- Tabin, C J -- DK47038/DK/NIDDK NIH HHS/ -- DK4723/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 2;273(5275):613-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662546" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Bone Development ; Cartilage/*cytology/metabolism ; Cell Differentiation ; Cell Division ; Chick Embryo ; Cloning, Molecular ; Culture Techniques ; Extremities/embryology ; Feedback ; Gene Expression Regulation ; Growth Plate/*cytology/metabolism ; Hedgehog Proteins ; Mice ; Molecular Sequence Data ; Morphogenesis ; *Osteogenesis ; Parathyroid Hormone ; Parathyroid Hormone-Related Protein ; Phenotype ; Proteins/pharmacology/*physiology ; Receptor, Parathyroid Hormone, Type 1 ; Receptors, Parathyroid Hormone/physiology ; Signal Transduction ; *Trans-Activators
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    Arabidopsis AUX1 gene: a permease-like regulator of root gravitropism (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-08-16
    Description: The plant hormone auxin regulates various developmental processes including root formation, vascular development, and gravitropism. Mutations within the AUX1 gene confer an auxin-resistant root growth phenotype and abolish root gravitropic curvature. Polypeptide sequence similarity to amino acid permeases suggests that AUX1 mediates the transport of an amino acid-like signaling molecule. Indole-3-acetic acid, the major form of auxin in higher plants, is structurally similar to tryptophan and is a likely substrate for the AUX1 gene product. The cloned AUX1 gene can restore the auxin-responsiveness of transgenic aux1 roots. Spatially, AUX1 is expressed in root apical tissues that regulate root gravitropic curvature.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bennett, M J -- Marchant, A -- Green, H G -- May, S T -- Ward, S P -- Millner, P A -- Walker, A R -- Schulz, B -- Feldmann, K A -- New York, N.Y. -- Science. 1996 Aug 16;273(5277):948-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of Warwick, Coventry, CV4 7AL, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8688077" target="_blank"〉PubMed〈/a〉
    Keywords: 2,4-Dichlorophenoxyacetic Acid/pharmacology ; Amino Acid Sequence ; Amino Acid Transport Systems ; Amino Acids/metabolism ; Arabidopsis/chemistry/*genetics/growth & development/metabolism ; *Arabidopsis Proteins ; Biological Transport ; Cloning, Molecular ; DNA, Bacterial/genetics ; *Genes, Plant ; Genetic Complementation Test ; *Gravitropism ; Indoleacetic Acids/metabolism/pharmacology ; Membrane Transport Proteins/chemistry ; Molecular Sequence Data ; Molecular Weight ; Mutation ; Plant Proteins/chemistry/*genetics/metabolism ; Plant Roots/*growth & development/metabolism ; Sequence Alignment ; Signal Transduction
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    A role for brassinosteroids in light-dependent development of Arabidopsis (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-04-19
    Description: Although steroid hormones are important for animal development, the physiological role of plant steroids is unknown. The Arabidopsis DET2 gene encodes a protein that shares significant sequence identity with mammalian steroid 5 alpha-reductases. A mutation of glutamate 204, which is absolutely required for the activity of human steroid reductase, abolishes the in vivo activity of DET2 and leads to defects in light-regulated development that can be ameliorated by application of a plant steroid, brassinolide. Thus, DET2 may encode a reductase in the brassinolide biosynthetic pathway, and brassinosteroids may constitute a distinct class of phytohormones with an important role in light-regulated development of higher plants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, J -- Nagpal, P -- Vitart, V -- McMorris, T C -- Chory, J -- New York, N.Y. -- Science. 1996 Apr 19;272(5260):398-401.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Plant Biology Laboratory, Salk Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8602526" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Oxo-5-alpha-Steroid 4-Dehydrogenase/chemistry ; Amino Acid Sequence ; Animals ; Arabidopsis/genetics/*growth & development/metabolism ; *Arabidopsis Proteins ; Brassinosteroids ; Cholestanols/*metabolism/pharmacology ; Chromosome Mapping ; *Genes, Plant ; Humans ; Light ; Molecular Sequence Data ; Mutation ; Oxidation-Reduction ; Phenotype ; Plant Growth Regulators/biosynthesis/*metabolism ; Plant Proteins/*genetics ; Rats ; Sequence Alignment ; Signal Transduction ; Steroids, Heterocyclic/*metabolism/pharmacology
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    Developmental control of cell cycle regulators: a fly's perspective (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-12-06
    Description: During early development in many species, maternally supplied gene products permit the cell cycle to run at maximum velocity, subdividing the fertilized egg into smaller and smaller cells. As development proceeds, zygotic controls are activated that first limit divisions to defined spatial and temporal domains, coordinating them with morphogenesis, and then halt proliferation altogether, to allow cell differentiation. Analysis of the regulation of cyclin-dependent kinases (Cdks) in Drosophila has provided insights into how this embryonic program of cell proliferation is controlled at the molecular level and how it is linked to developmental cues. Recent studies have also begun to reveal how cell proliferation is controlled during the second phase of Drosophila development, which occurs in imaginal tissues. In contrast to their embryonic progenitors, imaginal cells proliferate with a cycle that requires cell growth and is linked to patterning processes controlled by secreted cell signaling molecules. The functions of these signaling molecules appear to be nearly as conserved between vertebrates and invertebrates as the cell cycle control apparatus itself, suggesting that the mechanisms that coordinate growth, patterning, and cell proliferation in developing tissues have ancient origins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Edgar, B A -- Lehner, C F -- R01 GM51186/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Dec 6;274(5293):1646-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA 98109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8939845" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Body Patterning ; *Cell Cycle ; Cell Cycle Proteins/metabolism ; Cell Division ; Cyclin-Dependent Kinases/metabolism ; Cyclins/metabolism ; DNA Replication ; Drosophila/*cytology/embryology ; Gene Expression Regulation, Developmental ; Mitosis ; Signal Transduction ; Zygote/physiology
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    Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP Kinase (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-05-31
    Description: CHOP, a member of the C/EBP family of transcription factors, mediates effects of cellular stress on growth and differentiation. It accumulates under conditions of stress and undergoes inducible phosphorylation on two adjacent serine residues (78 and 81). In vitro, CHOP is phosphorylated on these residues by p38 mitogen-activated protein kinase (MAP kinase). A specific inhibitor of p38 MAP kinase, SB203580, abolished the stress-inducible in vivo phosphorylation of CHOP. Phosphorylation of CHOP on these residues enhanced its ability to function as a transcriptional activator and was also required for the full inhibitory effect of CHOP on adipose cell differentiation. CHOP thus serves as a link between a specific stress-activated protein kinase, p38, and cellular growth and differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, X Z -- Ron, D -- New York, N.Y. -- Science. 1996 May 31;272(5266):1347-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Skirball Institute of Biomolecular Medicine, New York University Medical Center, 10016, NY, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650547" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Adipocytes/cytology ; Amino Acid Sequence ; Animals ; *CCAAT-Enhancer-Binding Proteins ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Differentiation ; Cell Division ; Culture Media ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Enzyme Inhibitors/pharmacology ; Imidazoles/pharmacology ; Methyl Methanesulfonate/pharmacology ; Mice ; *Mitogen-Activated Protein Kinases ; Molecular Sequence Data ; Phosphorylation ; Pyridines/pharmacology ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Transcription Factor CHOP ; Transcription Factors/chemistry/genetics/*metabolism ; Transcriptional Activation ; p38 Mitogen-Activated Protein Kinases
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    Shaking out the cause of addiction (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-08-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hyman, S E -- New York, N.Y. -- Science. 1996 Aug 2;273(5275):611-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institute of Mental Health, Rockville, MD 20857, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8701316" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cyclic AMP/metabolism ; Cyclic AMP Response Element-Binding Protein/genetics/*physiology ; Drug Tolerance ; Locus Coeruleus/metabolism/physiology ; Mice ; Mice, Knockout ; Narcotics/*administration & dosage/adverse effects/pharmacology ; Neuronal Plasticity ; Neurons/physiology ; Opioid-Related Disorders/*etiology/metabolism ; Receptors, Opioid, mu/metabolism ; Signal Transduction ; Substance Withdrawal Syndrome/etiology/metabolism ; Up-Regulation
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    Cancer cell cycles (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-12-06
    Description: Uncontrolled cell proliferation is the hallmark of cancer, and tumor cells have typically acquired damage to genes that directly regulate their cell cycles. Genetic alterations affecting p16(INK4a) and cyclin D1, proteins that govern phosphorylation of the retinoblastoma protein (RB) and control exit from the G1 phase of the cell cycle, are so frequent in human cancers that inactivation of this pathway may well be necessary for tumor development. Like the tumor suppressor protein p53, components of this "RB pathway," although not essential for the cell cycle per se, may participate in checkpoint functions that regulate homeostatic tissue renewal throughout life.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sherr, C J -- New York, N.Y. -- Science. 1996 Dec 6;274(5293):1672-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Tumor Cell Biology, St. Jude Children's Research Hospital, 332 North Lauderdale, Memphis, TN 38105, USA. sherr@stjude.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8939849" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carrier Proteins/genetics/metabolism ; *Cell Cycle ; Cyclin-Dependent Kinase Inhibitor p16 ; Cyclin-Dependent Kinases/antagonists & inhibitors/metabolism ; Cyclins/metabolism ; G1 Phase ; Gene Expression Regulation, Neoplastic ; Genes, Tumor Suppressor ; Humans ; Neoplasms/genetics/metabolism/*pathology ; Proto-Oncogenes ; Retinoblastoma Protein/metabolism ; S Phase ; Signal Transduction ; Tumor Suppressor Protein p53/metabolism
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    Hyperresponsive B cells in CD22-deficient mice (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-11-01
    Description: CD22 is a surface glycoprotein of B lymphocytes that is rapidly phosphorylated on cytoplasmic tyrosines after antigen receptor cross-linking. Splenic B cells from mice with a disrupted CD22 gene were found to be hyperresponsive to receptor signaling: Heightened calcium fluxes and cell proliferation were obtained at lower ligand concentrations. The mice gave an augmented immune response, had an expanded peritoneal B-1 cell population, and contained increased serum titers of autoantibody. Thus, CD22 is a negative regulator of antigen receptor signaling whose onset of expression at the mature B cell stage may serve to raise the antigen concentration threshold required for B cell triggering.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Keefe, T L -- Williams, G T -- Davies, S L -- Neuberger, M S -- New York, N.Y. -- Science. 1996 Nov 1;274(5288):798-801.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8864124" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Antinuclear/blood ; Antibody Formation ; Antigens, CD/genetics/*immunology/metabolism ; Antigens, Differentiation, B-Lymphocyte/genetics/*immunology/metabolism ; B-Lymphocytes/*immunology/metabolism ; Calcium/metabolism ; *Cell Adhesion Molecules ; Female ; Gene Targeting ; Immunization ; Immunoglobulin M/blood ; Immunophenotyping ; *Lectins ; Lymphocyte Activation ; Male ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Phosphorylation ; Receptors, Antigen, B-Cell/immunology/physiology ; Sialic Acid Binding Ig-like Lectin 2 ; Signal Transduction ; Transfection
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    Expanding the eukaryote's cast of chaperones (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-12-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1996 Dec 6;274(5293):1613-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8984629" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Isomerases/physiology ; Carrier Proteins/*physiology ; *Cyclophilins ; DNA-Binding Proteins/physiology ; Fungal Proteins/*physiology ; HSP90 Heat-Shock Proteins/physiology ; Heat-Shock Proteins/physiology ; Molecular Chaperones/*physiology ; *Peptidylprolyl Isomerase ; Protein Conformation ; Protein Denaturation ; *Protein Folding ; Signal Transduction ; Tacrolimus Binding Proteins
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    Control of memory formation through regulated expression of a CaMKII transgene (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-06
    Description: One of the major limitations in the use of genetically modified mice for studying cognitive functions is the lack of regional and temporal control of gene function. To overcome these limitations, a forebrain-specific promoter was combined with the tetracycline transactivator system to achieve both regional and temporal control of transgene expression. Expression of an activated calcium-independent form of calcium-calmodulin-dependent kinase II (CaMKII) resulted in a loss of hippocampal long-term potentiation in response to 10-hertz stimulation and a deficit in spatial memory, a form of explicit memory. Suppression of transgene expression reversed both the physiological and the memory deficit. When the transgene was expressed at high levels in the lateral amygdala and the striatum but not other forebrain structures, there was a deficit in fear conditioning, an implicit memory task, that also was reversible. Thus, the CaMKII signaling pathway is critical for both explicit and implicit memory storage, in a manner that is independent of its potential role in development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mayford, M -- Bach, M E -- Huang, Y Y -- Wang, L -- Hawkins, R D -- Kandel, E R -- New York, N.Y. -- Science. 1996 Dec 6;274(5293):1678-83.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Neurobiology and Behavior, College of Physicians and Surgeons of Columbia University, and Howard Hughes Medical Institute, 722 West 168 Street, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8939850" target="_blank"〉PubMed〈/a〉
    Keywords: Amygdala/physiology ; Animals ; Brain/*physiology ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 ; Calcium-Calmodulin-Dependent Protein Kinases/genetics/*metabolism ; Conditioning (Psychology) ; Corpus Striatum/physiology ; Doxycycline/pharmacology ; Fear ; *Gene Expression Regulation, Enzymologic ; Genes, Reporter ; Hippocampus/physiology ; Long-Term Potentiation ; Maze Learning ; Memory/*physiology ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Neuronal Plasticity ; Promoter Regions, Genetic ; Prosencephalon/physiology ; Signal Transduction ; Transgenes
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  • 41
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    Modulation of insulin activities by leptin (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-15
    Description: Leptin mediates its effects on food intake through the hypothalamic form of its receptor OB-R. Variants of OB-R are found in other tissues, but their function is unknown. Here, an OB-R variant was found in human hepatic cells. Exposure of these cells to leptin, at concentrations comparable with those present in obese individuals, caused attenuation of several insulin-induced activities, including tyrosine phosphorylation of the insulin receptor substrate-1 (IRS-1), association of the adapter molecule growth factor receptor-bound protein 2 with IRS-1, and down-regulation of gluconeogenesis. In contrast, leptin increased the activity of IRS-1-associated phosphatidylinositol 3-kinase. These in vitro studies raise the possibility that leptin modulates insulin activities in obese individuals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, B -- Novick, D -- Rubinstein, M -- New York, N.Y. -- Science. 1996 Nov 15;274(5290):1185-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, The Weizmann Institute of Science, Rehovot 76100, Israel. lvrub@weizmann.weizmann.ac.il〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8895466" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Carrier Proteins/genetics/metabolism ; Cell Line ; Down-Regulation/drug effects ; GRB2 Adaptor Protein ; Gene Expression Regulation, Enzymologic/drug effects ; Gluconeogenesis/drug effects ; Glucose/metabolism ; Humans ; Insulin/*pharmacology ; Insulin Antagonists ; Insulin Receptor Substrate Proteins ; Leptin ; Liver/cytology/metabolism ; Phosphatidylinositol 3-Kinases ; Phosphoenolpyruvate Carboxykinase (GTP)/genetics/metabolism ; Phosphoproteins/metabolism ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor)/metabolism ; Phosphotyrosine/metabolism ; Proteins/metabolism/*pharmacology ; Receptor, Epidermal Growth Factor/metabolism ; Receptor, Insulin/metabolism ; *Receptors, Cell Surface ; Receptors, Leptin ; Signal Transduction ; Tumor Cells, Cultured
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    Pass the butter (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martin, G -- New York, N.Y. -- Science. 1996 Oct 11;274(5285):203-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy, University of California, San Francisco, 94143-0452, USA. gmartin@itsa.ucsf.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8927979" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cholesterol/*metabolism ; *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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  • 43
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    Requirement of CDC42 for Salmonella-induced cytoskeletal and nuclear responses (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-20
    Description: The bacterial pathogen Salmonella typhimurium triggers host cell signaling pathways that lead to cytoskeletal and nuclear responses required for pathogenesis. Here, the role of the small guanosine triphosphate (GTP)-binding protein CDC42Hs in these responses was examined. Expression of a dominant interfering mutant of CDC42 (CDC42HsN17) prevented S. typhimurium-induced cytoskeletal reorganization and subsequent macropinocytosis and bacterial internalization into host cells. Cells expressing constitutively active CDC42 (CDC42HsV12) internalized an S. typhimurium mutant unable to trigger host cell responses. Furthermore, expression of CDC42HsN17 prevented S. typhimurium-induced JNK kinase activation. These results indicate that CDC42 is required for bacterial invasion and induction of nuclear responses in host cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, L M -- Hobbie, S -- Galan, J E -- GM52543/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Dec 20;274(5295):2115-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Microbiology, School of Medicine, State University of New York at Stony Brook, Stony Brook, NY, 11794-5222, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8953049" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; COS Cells ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Cycle Proteins/genetics/*physiology ; Cell Nucleus/*metabolism ; Cytoskeleton/*ultrastructure ; Enzyme Activation ; GTP-Binding Proteins/genetics/*physiology ; JNK Mitogen-Activated Protein Kinases ; *Mitogen-Activated Protein Kinases ; Pinocytosis ; Salmonella typhimurium/*physiology ; Signal Transduction ; Transfection ; cdc42 GTP-Binding Protein ; rac GTP-Binding Proteins
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  • 44
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    Coordination of three signaling enzymes by AKAP79, a mammalian scaffold protein (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-15
    Description: Multivalent binding proteins, such as the yeast scaffold protein Sterile-5, coordinate the location of kinases by serving as platforms for the assembly of signaling units. Similarly, in mammalian cells the cyclic adenosine 3',5'-monophosphate-dependent protein kinase (PKA) and phosphatase 2B [calcineurin (CaN)] are complexed by an A kinase anchoring protein, AKAP79. Deletion analysis and binding studies demonstrate that a third enzyme, protein kinase C (PKC), binds AKAP79 at a site distinct from those bound by PKA or CaN. The subcellular distributions of PKC and AKAP79 were similar in neurons. Thus, AKAP79 appears to function as a scaffold protein for three multifunctional enzymes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klauck, T M -- Faux, M C -- Labudda, K -- Langeberg, L K -- Jaken, S -- Scott, J D -- CA538841/CA/NCI NIH HHS/ -- GM48231/GM/NIGMS NIH HHS/ -- GM50152/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1589-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute, Oregon Health Sciences University, Portland, 97201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599116" target="_blank"〉PubMed〈/a〉
    Keywords: A Kinase Anchor Proteins ; *Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Brain/enzymology ; Calcineurin ; Calmodulin/pharmacology ; Calmodulin-Binding Proteins/*metabolism ; *Carrier Proteins ; Cattle ; Cell Line ; Cyclic AMP-Dependent Protein Kinases/analysis/antagonists & ; inhibitors/*metabolism ; Fungal Proteins/metabolism ; Humans ; Molecular Sequence Data ; Neurons/chemistry ; Phosphoprotein Phosphatases/*metabolism ; Phosphorylation ; Protein Kinase C/analysis/antagonists & inhibitors/*metabolism ; Proteins/analysis/*metabolism/pharmacology ; Recombinant Proteins ; *Saccharomyces cerevisiae Proteins ; Signal Transduction ; Synapses/physiology
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  • 45
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    Ultraviolet light and osmotic stress: activation of the JNK cascade through multiple growth factor and cytokine receptors (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-15
    Description: Exposure of mammalian cells to ultraviolet (UV) light or high osmolarity strongly activates the c-Jun amino-terminal protein kinase (JNK) cascade, causing induction of many target genes. Exposure to UV light or osmotic shock induced clustering and internalization of cell surface receptors for epidermal growth factor (EGF), tumor necrosis factor (TNF), and interleukin-1 (IL-1). Activation of the EGF and TNF receptors was also detected biochemically. Whereas activation of each receptor alone resulted in modest activation of JNK, coadministration of EGF, IL-1, and TNF resulted in a strong synergistic response equal to that caused by exposure to osmotic shock or UV light. Inhibition of clustering or receptor down-regulation attenuated both the osmotic shock and UV responses. Physical stresses may perturb the cell surface or alter receptor conformation, thereby subverting signaling pathways normally used by growth factors and cytokines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rosette, C -- Karin, M -- New York, N.Y. -- Science. 1996 Nov 15;274(5290):1194-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Program in Biomedical Sciences, School of Medicine, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0636, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8895468" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Dimerization ; Enzyme Activation ; Epidermal Growth Factor/pharmacology ; Fluorescent Antibody Technique, Indirect ; GRB2 Adaptor Protein ; HeLa Cells ; Humans ; Interleukin-1/pharmacology ; JNK Mitogen-Activated Protein Kinases ; *Mitogen-Activated Protein Kinases ; *Osmotic Pressure ; Phosphorylation ; Proteins/metabolism ; Receptor, Epidermal Growth Factor/*metabolism ; Receptors, Interleukin-1/*metabolism ; Receptors, Tumor Necrosis Factor/*metabolism ; Signal Transduction ; TNF Receptor-Associated Factor 1 ; Temperature ; Tumor Necrosis Factor-alpha/pharmacology ; *Ultraviolet Rays
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  • 46
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    Cellular microbiology emerging (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cossart, P -- Boquet, P -- Normark, S -- Rappuoli, R -- New York, N.Y. -- Science. 1996 Jan 19;271(5247):315-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Unite des Interactions Bacteries-Cellules, Institut Pasteur, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8553065" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*metabolism ; Animals ; Bacteria/*pathogenicity ; Bacterial Physiological Phenomena ; Bacterial Toxins/toxicity ; Cell Membrane/*physiology/ultrastructure ; Cytoskeleton/*physiology ; Endocytosis ; Humans ; Signal Transduction ; Trypanosoma cruzi/*pathogenicity/physiology ; Vacuoles/metabolism
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  • 47
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    Receptor tails unlock developmental checkpoints for B lymphocytes (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roth, P E -- DeFranco, A L -- New York, N.Y. -- Science. 1996 Jun 21;272(5269):1752-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of California, San Francisco-Hooper Foundation, 94143, USA. proth@itsa.ucsf.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650572" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibody Formation ; Antigens, CD/*physiology ; Antigens, CD79 ; B-Lymphocytes/*cytology/*immunology ; Gene Rearrangement, B-Lymphocyte ; Gene Targeting ; Genes, Immunoglobulin ; Mice ; Receptors, Antigen, B-Cell/*physiology ; Signal Transduction
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  • 48
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    Activation of Gal4p by galactose-dependent interaction of galactokinase and Gal80p (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-14
    Description: Yeast galactokinase (Gal1p) is an enzyme and a regulator of transcription. In addition to phosphorylating galactose, Gal1p activates Gal4p, the activator of GAL genes, but the mechanism of this regulation has been unclear. Here, biochemical and genetic evidence is presented to show that Gal1p activates Gal4p by direct interaction with the Gal4p inhibitor Gal80p. Interaction requires galactose, adenosine triphosphate, and the regulatory function of Gal1p. These data indicate that Gal1p-Gal80p complex formation results in the inactivation of Gal80p, thereby transmitting the galactose signal to Gal4p.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zenke, F T -- Engles, R -- Vollenbroich, V -- Meyer, J -- Hollenberg, C P -- Breunig, K D -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1662-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Mikrobiologie, Heinrich-Heine-Universitat Dusseldorf, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658143" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Coenzymes/metabolism ; DNA-Binding Proteins ; Fungal Proteins/*metabolism ; Galactokinase/genetics/*metabolism ; Galactose/*metabolism ; Kluyveromyces/genetics/metabolism ; Molecular Sequence Data ; Mutation ; Repressor Proteins/*metabolism ; Saccharomyces cerevisiae/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Signal Transduction ; Transcription Factors/*metabolism
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  • 49
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    Molecular mimicry of human cytokine and cytokine response pathway genes by KSHV (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-12-06
    Description: Four virus proteins similar to two human macrophage inflammatory protein (MIP) chemokines, interleukin-6 (IL-6), and interferon regulatory factor (IRF) are encoded by the Kaposi's sarcoma-associated herpesvirus (KSHV) genome. vIL-6 was functional in B9 proliferation assays and primarily expressed in KSHV-infected hematopoietic cells rather than KS lesions. HIV-1 transmission studies showed that vMIP-I is similar to human MIP chemokines in its ability to inhibit replication of HIV-1 strains dependent on the CCR5 co-receptor. These viral genes may form part of the response to host defenses contributing to virus-induced neoplasia and may have relevance to KSHV and HIV-I interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moore, P S -- Boshoff, C -- Weiss, R A -- Chang, Y -- CA67391/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Dec 6;274(5293):1739-44.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Public Health, Columbia University, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8939871" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Division ; Cell Line ; Chemokine CCL4 ; Gene Expression ; Genes, Viral ; HIV-1/physiology ; Herpesvirus 4, Human/physiology ; Herpesvirus 8, Human/*genetics/physiology ; Humans ; Interleukin-6/chemistry/genetics ; Lymph Nodes/virology ; Lymphoma, B-Cell/virology ; Macrophage Inflammatory Proteins/chemistry/genetics ; Mice ; *Molecular Mimicry ; Molecular Sequence Data ; Receptors, CCR5 ; Receptors, Cytokine/metabolism ; Receptors, HIV/metabolism ; Sarcoma, Kaposi/virology ; Sequence Alignment ; Signal Transduction ; Tetradecanoylphorbol Acetate/pharmacology ; Tumor Cells, Cultured ; Viral Nonstructural Proteins/chemistry/*genetics/physiology ; Virus Replication
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  • 50
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    Aberrant B cell development and immune response in mice with a compromised BCR complex (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-21
    Description: The immunoglobulin alpha (Ig-alpha)-Ig-beta heterodimer is the signaling component of the antigen receptor complex on B cells (BCR) and B cell progenitors (pre-BCR). A mouse mutant that lacks most of the Ig-alpha cytoplasmic tail exhibits only a small impairment in early B cell development but a severe block in the generation of the peripheral B cell pool, revealing a checkpoint in B cell maturation that ensures the expression of a functional BCR on mature B cells. B cells that do develop demonstrate a differential dependence on Ig-alpha signaling in antibody responses such that a signaling-competent Ig-alpha appears to be critical for the response to T-independent, but not T-dependent, antigens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Torres, R M -- Flaswinkel, H -- Reth, M -- Rajewsky, K -- New York, N.Y. -- Science. 1996 Jun 21;272(5269):1804-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genetics, University of Cologne, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650582" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibody Formation ; Antigens/immunology ; Antigens, CD/chemistry/immunology/*physiology ; Antigens, CD79 ; Antigens, T-Independent/immunology ; B-Lymphocytes/*cytology/*immunology ; Bone Marrow Cells ; Cell Lineage ; Gene Rearrangement, B-Lymphocyte ; Gene Targeting ; Genes, Immunoglobulin ; Hematopoietic Stem Cells/cytology/immunology ; Lymphoid Tissue/cytology/immunology ; Mice ; Mice, Inbred C57BL ; Receptors, Antigen, B-Cell/chemistry/immunology/*physiology ; Signal Transduction
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    Genetic susceptibility to Leishmania: IL-12 responsiveness in TH1 cell development (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-16
    Description: The genetic background of T lymphocytes influences development of the T helper (TH) phenotype, resulting in either resistance or susceptibility of certain mouse strains to pathogens such as Leishmania major. With an in vitro model system, a difference in maintenance of responsiveness of T cells to interleukin-12 (IL-12) was detected between BALB/c and B10.D2 mice. Although naive T cells from both strains initially responded to IL-12, BALB/c T cells lost IL-12 responsiveness after stimulation with antigen in vitro, even when cocultured with B10.D2 T cells. Thus, susceptibility of BALB/c mice to infection with L. major may derive from the loss of the ability to generate IL-12-induced TH1 responses rather than from an IL-4-induced TH2 response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guler, M L -- Gorham, J D -- Hsieh, C S -- Mackey, A J -- Steen, R G -- Dietrich, W F -- Murphy, K M -- AI31238/AI/NIAID NIH HHS/ -- AI34580/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Feb 16;271(5251):984-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Washington University School of Medicine, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8584935" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Coculture Techniques ; Genetic Predisposition to Disease ; Immunity, Innate/genetics ; Interferon-gamma/biosynthesis ; Interleukin-12/*pharmacology ; Interleukin-4/biosynthesis ; Leishmania major/*immunology ; Leishmaniasis, Cutaneous/*immunology ; Lymphocyte Activation ; Mice ; Mice, Inbred BALB C ; Mice, Transgenic ; Phenotype ; Receptors, Interleukin-2/biosynthesis ; Signal Transduction ; Th1 Cells/*immunology ; Th2 Cells/immunology
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  • 52
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    Role of Rho in chemoattractant-activated leukocyte adhesion through integrins (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-16
    Description: Heterotrimeric guanine nucleotide binding protein (G protein)-linked receptors of the chemoattractant subfamily can trigger adhesion through leukocyte integrins, and in this role they are thought to regulate immune cell-cell interactions and trafficking. In lymphoid cells transfected with formyl peptide or interleukin-8 receptors, agonist stimulation activated nucleotide exchange on the small guanosine triphosphate-binding protein RhoA in seconds. Inactivation of Rho by C3 transferase exoenzyme blocked agonist-induced lymphocyte alpha4beta1 adhesion to vascular cell adhesion molecule-1 and neutrophil beta2 integrin adhesion to fibrinogen. These findings suggest that Rho participates in signaling from chemoattractant receptors to trigger rapid adhesion in leukocytes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Laudanna, C -- Campbell, J J -- Butcher, E C -- 1F32 AI08930/AI/NIAID NIH HHS/ -- 5T32 CA09302/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Feb 16;271(5251):981-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Immunology and Vascular Biology, Department of Pathology, Stanford University, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8584934" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD/genetics ; B-Lymphocytes/*physiology ; *Cell Adhesion ; Cells, Cultured ; Chemotactic Factors/*pharmacology ; GTP-Binding Proteins/metabolism/*physiology ; Guanosine 5'-O-(3-Thiotriphosphate)/metabolism ; Guanosine Diphosphate/metabolism ; Integrin alpha4beta1 ; Integrins/*physiology ; Interleukin-8/pharmacology ; Mice ; Molecular Sequence Data ; N-Formylmethionine Leucyl-Phenylalanine/pharmacology ; Receptors, Formyl Peptide ; Receptors, Immunologic/genetics ; Receptors, Interleukin/genetics ; Receptors, Interleukin-8A ; Receptors, Lymphocyte Homing/*physiology ; Receptors, Peptide/genetics ; Signal Transduction ; Tetradecanoylphorbol Acetate/pharmacology ; Transfection ; Vascular Cell Adhesion Molecule-1/*physiology ; rhoA GTP-Binding Protein
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    No "End of History" for photolyases (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sancar, A -- New York, N.Y. -- Science. 1996 Apr 5;272(5258):48-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of Nor Carolina School of Medicine, Chapel Hill, 27599, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8600535" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; Cryptochromes ; DNA/*metabolism/radiation effects ; DNA Damage ; DNA Repair ; Deoxyribodipyrimidine Photo-Lyase/chemistry/genetics/*metabolism ; Drosophila/enzymology/genetics ; *Drosophila Proteins ; *Eye Proteins ; *Flavoproteins ; Humans ; *Photoreceptor Cells, Invertebrate ; Plant Proteins/chemistry/metabolism ; Pyrimidine Dimers/*metabolism ; Receptors, G-Protein-Coupled ; Signal Transduction ; Ultraviolet Rays
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    Cell cycle checkpoints: preventing an identity crisis (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-06
    Description: Cell cycle checkpoints are regulatory pathways that control the order and timing of cell cycle transitions and ensure that critical events such as DNA replication and chromosome segregation are completed with high fidelity. In addition, checkpoints respond to damage by arresting the cell cycle to provide time for repair and by inducing transcription of genes that facilitate repair. Checkpoint loss results in genomic instability and has been implicated in the evolution of normal cells into cancer cells. Recent advances have revealed signal transduction pathways that transmit checkpoint signals in response to DNA damage, replication blocks, and spindle damage. Checkpoint pathways have components shared among all eukaryotes, underscoring the conservation of cell cycle regulatory machinery.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Elledge, S J -- GM44664/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Dec 6;274(5293):1664-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Howard Hughes Medical Institute, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8939848" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Cycle ; Cyclin-Dependent Kinases/antagonists & inhibitors/metabolism ; Cyclins/metabolism ; DNA Damage ; DNA Repair ; DNA Replication ; Gene Expression Regulation ; Saccharomyces cerevisiae/cytology/genetics/metabolism ; Schizosaccharomyces/cytology/metabolism ; Signal Transduction ; Spindle Apparatus/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 55
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    An orphan nuclear hormone receptor that lacks a DNA binding domain and heterodimerizes with other receptors (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-31
    Description: SHP is an orphan member of the nuclear hormone receptor superfamily that contains the dimerization and ligand-binding domain found in other family members but lacks the conserved DNA binding domain. In the yeast two-hybrid system, SHP interacted with several conventional and orphan members of the receptor superfamily, including retinoid receptors, the thyroid hormone receptor, and the orphan receptor MB67. SHP also interacted directly with these receptors in vitro. In mammalian cells, SHP specifically inhibited transactivation by the superfamily members with which it interacted. These results suggest that SHP functions as a negative regulator of receptor-dependent signaling pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seol, W -- Choi, H S -- Moore, D D -- DK46546/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1996 May 31;272(5266):1336-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Massachusetts General Hospital, Boston, 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650544" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; DAX-1 Orphan Nuclear Receptor ; DNA/*metabolism ; DNA-Binding Proteins/chemistry/metabolism ; Humans ; Mice ; Molecular Sequence Data ; Receptors, Cytoplasmic and Nuclear/chemistry/*metabolism ; Receptors, Retinoic Acid/chemistry/metabolism ; Receptors, Thyroid Hormone/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; *Repressor Proteins ; Retinoid X Receptors ; Signal Transduction ; Transcription Factors/chemistry/metabolism ; Transcriptional Activation/drug effects ; Tumor Cells, Cultured
    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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  • 56
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    Interaction between a putative mechanosensory membrane channel and a collagen (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-19
    Description: The degenerin family of proteins in Caenorhabditis elegans is homologous to subunits of the mammalian amiloride-sensitive epithelial sodium channels. Mutations in nematode degenerins cause cell death, probably because of defects in channel function. Genetic evidence was obtained that the unc-105 gene product represents a degenerin homolog affecting C. elegans muscles and that this putative channel interacts with type IV collagen in the extracellular matrix underlying the muscle cell. This interaction may serve as a mechanism of stretch-activated muscle contraction, and this system could provide a molecular model for the activation of mechanosensitive ion channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, J -- Schrank, B -- Waterston, R H -- GM23883/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 19;273(5273):361-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Washington University School of Medicine, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662524" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Base Sequence ; Caenorhabditis elegans/chemistry/genetics/*metabolism ; *Caenorhabditis elegans Proteins ; Cloning, Molecular ; Collagen/*metabolism ; Extracellular Matrix/metabolism ; Genes, Helminth ; Genetic Complementation Test ; Helminth Proteins/chemistry/genetics/*metabolism/*physiology ; Ion Channel Gating ; Models, Biological ; Molecular Sequence Data ; Muscle Contraction ; Muscles/physiology ; Mutation ; Sensation ; Signal Transduction ; Sodium Channels/chemistry/genetics/*metabolism/*physiology ; Suppression, Genetic
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    Hierarchical control of lymphocyte survival (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boise, L H -- Thompson, C B -- New York, N.Y. -- Science. 1996 Oct 4;274(5284):67-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gwen Knapp Center for Lupus and Immunology Research, Howard Hughes Medical Institute, University of Chicago, Illinois 60637-5420, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8848725" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens/immunology ; Antigens, CD95/physiology ; *Apoptosis ; *Cell Survival ; Cytokines/physiology ; *Lymphocyte Activation ; Lymphocytes/*cytology/*immunology ; Proto-Oncogene Proteins/physiology ; Proto-Oncogene Proteins c-bcl-2 ; Receptors, Antigen/physiology ; Receptors, Cell Surface/physiology ; Signal Transduction
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    Regulation of interferon-gamma-activated STAT1 by the ubiquitin-proteasome pathway (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-09-20
    Description: STAT proteins (signal transducers and activators of transcription) are latent cytoplasmic transcription factors that are phosphorylated by Janus kinases in response to cytokines. Phosphorylated STAT proteins translocate to the nucleus, where they transiently turn on specific sets of cytokine-inducible genes. The mechanism that controls the amounts of activated STAT proteins is not understood. STAT1 proteins activated by interferon-gamma treatment in HeLa cells were shown to be stabilized by a proteasome inhibitor and ubiquitinated in vivo. Thus, the amount of activated STAT1 may be negatively regulated by the ubiquitin-proteasome pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, T K -- Maniatis, T -- AI20642/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Sep 20;273(5282):1717-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8781235" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Nucleus/metabolism ; Cysteine Endopeptidases/*metabolism ; Cysteine Proteinase Inhibitors/pharmacology ; DNA/metabolism ; DNA-Binding Proteins/*metabolism ; HeLa Cells ; Humans ; Immunoblotting ; Interferon-gamma/*pharmacology ; Leupeptins/pharmacology ; Multienzyme Complexes/*metabolism ; Mutation ; Phosphorylation ; Proteasome Endopeptidase Complex ; STAT1 Transcription Factor ; Signal Transduction ; Trans-Activators/*metabolism ; Tumor Cells, Cultured ; Ubiquitins/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Dissecting how presinilins function--and malfunction (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1996 Dec 13;274(5294):1838-40.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8984642" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*etiology/genetics/metabolism/pathology ; Amyloid beta-Peptides/*metabolism ; Amyloid beta-Protein Precursor/chemistry/*metabolism ; Animals ; Apoptosis ; Brain/pathology ; Caenorhabditis elegans ; Endoplasmic Reticulum/metabolism ; Humans ; Membrane Proteins/genetics/metabolism/*physiology ; Mice ; Mutation ; Neurons/pathology ; Peptide Fragments/*metabolism ; Presenilin-1 ; Presenilin-2 ; Protein Folding ; Receptors, Notch ; Signal Transduction
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    Multiple extracellular elements of CCR5 and HIV-1 entry: dissociation from response to chemokines (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-13
    Description: The human beta-chemokine receptor CCR5 is an important cofactor for entry of human immunodeficiency virus-type 1 (HIV-1). The murine form of CCR5, despite its 82 percent identity to the human form, was not functional as an HIV-1 coreceptor. HIV-1 entry function could be reconstituted by fusion of various individual elements derived from the extracellular region of human CCR5 onto murine CCR5. Analysis of chimeras containing elements from human CCR5 and human CCR2B suggested that a complex structure rather than single contact sites is responsible for facilitation of viral entry. Further, certain chimeras lacking the domains necessary to signal in response to their natural chemokine ligands retained vigorous HIV-1 coreceptor activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Atchison, R E -- Gosling, J -- Monteclaro, F S -- Franci, C -- Digilio, L -- Charo, I F -- Goldsmith, M A -- HL52773/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1996 Dec 13;274(5294):1924-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gladstone Institute of Virology and Immunology, School of Medicine, University of California, San Francisco, Post Office Box 419100, San Francisco, CA 94141-9100, USA. mark_goldsmith@quickmail.ucsf.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8943208" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD4/metabolism ; COS Cells ; HIV-1/*metabolism ; Humans ; Inositol Phosphates/metabolism ; Ligands ; Mice ; Receptors, CCR2 ; Receptors, CCR5 ; *Receptors, Chemokine ; Receptors, Cytokine/chemistry/genetics/*metabolism ; Receptors, HIV/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Transfection
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    Putting the brakes on bone growth (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1996 Aug 2;273(5275):579.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8701309" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Bone Development ; Cartilage/*cytology/metabolism ; Cell Differentiation ; Cell Division ; Chick Embryo ; Feedback ; Growth Plate/*cytology/metabolism ; Hedgehog Proteins ; Humans ; Mice ; *Osteogenesis ; Parathyroid Hormone ; Parathyroid Hormone-Related Protein ; Proteins/*metabolism/pharmacology/*physiology ; Signal Transduction ; *Trans-Activators
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    Patterning the vertebrate neuraxis (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-15
    Description: Neuraxial patterning is a continuous process that extends over a protracted period of development. During gastrulation a crude anteroposterior pattern, detectable by molecular markers, is conferred on the neuroectoderm by signals from the endomesoderm that are largely inseparable from those of neural induction itself. This coarse-grained pattern is subsequently reinforced and refined by diverse, locally acting mechanisms. Segmentation and long-range signaling from organizing centers are prominent among the emerging principles governing regional pattern.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lumsden, A -- Krumlauf, R -- New York, N.Y. -- Science. 1996 Nov 15;274(5290):1109-15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Neurobiology, United Medical and Dental Schools, Guy's Hospital, London SE1 9RT, UK. a.lumsden@umds.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8895453" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Body Patterning ; Central Nervous System/cytology/*embryology/physiology ; *Embryonic Induction ; Gene Expression Regulation, Developmental ; Genes, Homeobox ; Mesencephalon/cytology/embryology/physiology ; Mesoderm/physiology ; Neurons/cytology/physiology ; Prosencephalon/cytology/embryology/physiology ; Rhombencephalon/cytology/embryology/physiology ; Signal Transduction ; Spinal Cord/cytology/embryology/physiology ; Tretinoin/physiology
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    Reduction of morphine abstinence in mice with a mutation in the gene encoding CREB (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-02
    Description: Chronic morphine administration induces an up-regulation of several components of the cyclic adenosine 5'-monophosphate (cAMP) signal transduction cascade. The behavioral and biochemical consequences of opiate withdrawal were investigated in mice with a genetic disruption of the alpha and Delta isoforms of the cAMP-responsive element-binding protein (CREB). In CREBalphadelta mutant mice the main symptoms of morphine withdrawal were strongly attenuated. No change in opioid binding sites or in morphine-induced analgesia was observed in these mutant mice, and the increase of adenylyl cyclase activity and immediate early gene expression after morphine withdrawal was normal. Thus, CREB-dependent gene transcription is a factor in the onset of behavioral manifestations of opiate dependence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maldonado, R -- Blendy, J A -- Tzavara, E -- Gass, P -- Roques, B P -- Hanoune, J -- Schutz, G -- New York, N.Y. -- Science. 1996 Aug 2;273(5275):657-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departement de Pharmacochimie Moleculaire et Structurale, Unite de Recherche Associee D1500 CNRS, Universite Rene Descartes, Faculte de Pharmacie, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662559" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/metabolism ; Analgesia ; Animals ; Behavior, Animal ; Cerebral Cortex/enzymology ; Cyclic AMP Response Element-Binding Protein/*genetics/*physiology ; Drug Tolerance ; Gene Expression Regulation ; Gene Targeting ; Genes, Immediate-Early ; Locus Coeruleus/metabolism ; Mice ; Morphine/*administration & dosage/adverse effects/pharmacology ; Morphine Dependence/*etiology/metabolism ; Mutation ; Naloxone/pharmacology ; Receptors, Opioid/metabolism ; Signal Transduction ; Substance Withdrawal Syndrome/*physiopathology
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    Small peptides as potent mimetics of the protein hormone erythropoietin (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-26
    Description: Random phage display peptide libraries and affinity selective methods were used to isolate small peptides that bind to and activate the receptor for the cytokine erythropoietin (EPO). In a panel of in vitro biological assays, the peptides act as full agonists and they can also stimulate erythropoiesis in mice. These agonists are represented by a 14- amino acid disulfide-bonded, cyclic peptide with the minimum consensus sequence YXCXXGPXTWXCXP, where X represents positions allowing occupation by several amino acids. The amino acid sequences of these peptides are not found in the primary sequence of EPO. The signaling pathways activated by these peptides appear to be identical to those induced by the natural ligand. This discovery may form the basis for the design of small molecule mimetics of EPO.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wrighton, N C -- Farrell, F X -- Chang, R -- Kashyap, A K -- Barbone, F P -- Mulcahy, L S -- Johnson, D L -- Barrett, R W -- Jolliffe, L K -- Dower, W J -- New York, N.Y. -- Science. 1996 Jul 26;273(5274):458-64.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Affymax Research Institute, 4001 Miranda Avenue, Palo Alto, CA 94304, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662529" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacteriophages ; Cell Division/drug effects ; Cell Line ; Cloning, Molecular ; Erythropoiesis/drug effects ; Erythropoietin/chemistry/*metabolism/*pharmacology ; Humans ; Ligands ; Mice ; *Molecular Mimicry ; Molecular Sequence Data ; Mutagenesis ; Peptides, Cyclic/chemistry/*metabolism/*pharmacology ; Phosphorylation ; Protein Structure, Secondary ; Receptors, Erythropoietin/*agonists/chemistry/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Signal Transduction ; Solubility ; Tyrosine/metabolism
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