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  • Phosphorylation  (55)
  • American Association for the Advancement of Science (AAAS)  (55)
  • American Institute of Physics
  • American Meteorological Society
  • International Union of Crystallography
  • 1995-1999  (55)
  • 1996  (55)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (55)
  • American Institute of Physics
  • American Meteorological Society
  • International Union of Crystallography
  • Springer  (3)
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  • 1995-1999  (55)
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  • 1
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    IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-alpha- and obesity-induced insulin resistance (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-02
    Description: Tumor necrosis factor-alpha (TNF-alpha) is an important mediator of insulin resistance in obesity and diabetes through its ability to decrease the tyrosine kinase activity of the insulin receptor (IR). Treatment of cultured murine adipocytes with TNF-alpha was shown to induce serine phosphorylation of insulin receptor substrate 1 (IRS-1) and convert IRS-1 into an inhibitor of the IR tyrosine kinase activity in vitro. Myeloid 32D cells, which lack endogenous IRS-1, were resistant to TNF-alpha-mediated inhibition of IR signaling, whereas transfected 32D cells that express IRS-1 were very sensitive to this effect of TNF-alpha. An inhibitory form of IRS-1 was observed in muscle and fat tissues from obese rats. These results indicate that TNF-alpha induces insulin resistance through an unexpected action of IRS-1 to attenuate insulin receptor signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hotamisligil, G S -- Peraldi, P -- Budavari, A -- Ellis, R -- White, M F -- Spiegelman, B M -- DK 42539/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1996 Feb 2;271(5249):665-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Biology, Dana-Farber Cancer Institute, Boston, MA, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8571133" target="_blank"〉PubMed〈/a〉
    Keywords: Adipocytes/*metabolism ; Adipose Tissue/metabolism ; Animals ; Cells, Cultured ; Insulin/pharmacology ; Insulin Receptor Substrate Proteins ; Insulin Resistance/*physiology ; Male ; Mice ; Muscle, Skeletal/metabolism ; Obesity/*metabolism ; Phosphoproteins/metabolism/*physiology ; Phosphorylation ; Rats ; Rats, Zucker ; Receptor, Insulin/*antagonists & inhibitors/metabolism ; Serine/metabolism ; Signal Transduction ; Tumor Necrosis Factor-alpha/*pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Identification of BIME as a subunit of the anaphase-promoting complex (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-15
    Description: The initiation of anaphase and exit from mitosis require the activation of a proteolytic system that ubiquitinates and degrades cyclin B. The regulated component of this system is a large ubiquitin ligase complex, termed the anaphase-promoting complex (APC) or cyclosome. Purified Xenopus laevis APC was found to be composed of eight major subunits, at least four of which became phosphorylated in mitosis. In addition to CDC27, CDC16, and CDC23, APC contained a homolog of Aspergillus nidulans BIME, a protein essential for anaphase. Because mutation of bimE can bypass the interphase arrest induced by either nimA mutation or unreplicated DNA, it appears that ubiquitination catalyzed by APC may also negatively regulate entry into mitosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peters, J M -- King, R W -- Hoog, C -- Kirschner, M W -- New York, N.Y. -- Science. 1996 Nov 15;274(5290):1199-201.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8895470" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Anaphase ; Animals ; Aspergillus/chemistry/cytology/metabolism ; Cell Cycle Proteins/*chemistry/metabolism ; Cyclins/metabolism ; Electrophoresis, Polyacrylamide Gel ; Fungal Proteins/analysis/*chemistry/genetics/metabolism ; Ligases/*chemistry/metabolism ; *Mitosis ; Molecular Sequence Data ; Mutation ; Ovum ; Phosphorylation ; Ubiquitin-Protein Ligases ; Xenopus laevis
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  • 3
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    Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-16
    Description: A signaling pathway has been elucidated whereby growth factors activate the transcription factor cyclic adenosine monophosphate response element-binding protein (CREB), a critical regulator of immediate early gene transcription. Growth factor-stimulated CREB phosphorylation at serine-133 is mediated by the RAS-mitogen-activated protein kinase (MAPK) pathway. MAPK activates CREB kinase, which in turn phosphorylates and activates CREB. Purification, sequencing, and biochemical characterization of CREB kinase revealed that it is identical to a member of the pp90(RSK) family, RSK2. RSK2 was shown to mediate growth factor induction of CREB serine-133 phosphorylation both in vitro and in vivo. These findings identify a cellular function for RSK2 and define a mechanism whereby growth factor signals mediated by RAS and MAPK are transmitted to the nucleus to activate gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xing, J -- Ginty, D D -- Greenberg, M E -- CA43855/CA/NCI NIH HHS/ -- NS34814-01/NS/NINDS NIH HHS/ -- P30-HD18655/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 16;273(5277):959-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Biological and Biomedical Sciences, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8688081" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Line ; Cell Nucleus/metabolism ; Cyclic AMP Response Element-Binding Protein/*metabolism ; Epidermal Growth Factor/pharmacology ; *Gene Expression Regulation ; Growth Substances/*pharmacology ; Humans ; Molecular Sequence Data ; Nerve Growth Factors/pharmacology ; PC12 Cells ; Phosphorylation ; Protein-Serine-Threonine Kinases/*metabolism ; Rats ; Ribosomal Protein S6 Kinases ; *Signal Transduction ; Tetradecanoylphorbol Acetate/pharmacology ; Transcriptional Activation ; Transfection ; Tumor Cells, Cultured ; ras Proteins/metabolism
    Print ISSN: 0036-8075
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  • 4
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    IRAK: a kinase associated with the interleukin-1 receptor (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-23
    Description: The pleiotropic biological activities of interleukin-1 (IL-1) are mediated by its type I receptor (IL-1RI). When the ligand binds, IL-1RI initiates a signaling cascade that results in the activation of the transcription regulator nuclear factor kappa B (NF-kappa B). A protein kinase designated IRAK (IL-1 receptor-associated kinase) was purified, and its complementary DNA was molecularly cloned. When human embryonic kidney cells (cell line 293) over-expressing IL-1RI or HeLa cells were exposed to IL-1, IRAK rapidly associated with the IL-1RI complex and was phosphorylated. The primary amino acid sequence of IRAK shares similarity with that of Pelle, a protein kinase that is essential for the activation of a NF-kappa B homolog in Drosophila.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cao, Z -- Henzel, W J -- Gao, X -- New York, N.Y. -- Science. 1996 Feb 23;271(5252):1128-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Department, Tularik, Incorporated, South San Francisco, CA 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599092" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cloning, Molecular ; DNA, Complementary/genetics ; Drosophila ; *Drosophila Proteins ; HeLa Cells ; Humans ; Interleukin-1/*metabolism/pharmacology ; Interleukin-1 Receptor-Associated Kinases ; Molecular Sequence Data ; Phosphorylation ; Protein Kinases/chemistry/genetics/isolation & purification/*metabolism ; Protein-Serine-Threonine Kinases/chemistry ; Receptors, Interleukin-1/*metabolism ; Transfection
    Print ISSN: 0036-8075
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  • 5
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    Binding of zinc finger protein ZPR1 to the epidermal growth factor receptor (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-21
    Description: ZPR1 is a zinc finger protein that binds to the cytoplasmic tyrosine kinase domain of the epidermal growth factor receptor (EGFR). Deletion analysis demonstrated that this binding interaction is mediated by the zinc fingers of ZPR1 and subdomains X and XI of the EGFR tyrosine kinase. Treatment of mammalian cells with EGF caused decreased binding of ZPR1 to the EGFR and the accumulation of ZPR1 in the nucleus. The effect of EGF to regulate ZPR1 binding is dependent on tyrosine phosphorylation of the EGFR. ZPR1 therefore represents a prototype for a class of molecule that binds to the EGFR and is released from the receptor after activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Galcheva-Gargova, Z -- Konstantinov, K N -- Wu, I H -- Klier, F G -- Barrett, T -- Davis, R J -- R01-CA58396/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 21;272(5269):1797-802.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650580" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry/*metabolism/secretion ; Cell Line ; Cell Nucleus/metabolism ; Cloning, Molecular ; Cytoplasm/metabolism ; Epidermal Growth Factor/pharmacology ; Humans ; Immunoblotting ; Male ; Mice ; Molecular Sequence Data ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein Structure, Secondary ; RNA, Messenger/genetics/metabolism ; Receptor, Epidermal Growth Factor/chemistry/*metabolism ; Testis/metabolism ; Type C Phospholipases/metabolism ; Vanadates/pharmacology ; *Zinc Fingers ; src Homology Domains
    Print ISSN: 0036-8075
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  • 6
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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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  • 7
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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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  • 8
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    Identification of a putative target for Rho as the serine-threonine kinase protein kinase N (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-02
    Description: Rho, a Ras-like small guanosine triphosphatase, has been implicated in cytoskeletal responses to extracellular signals such as lysophosphatidic acid (LPA) to form stress fibers and focal contacts. The form of RhoA bound to guanosine triphosphate directly bound to and activated a serine-threonine kinase, protein kinase N (PKN). Activated RhoA formed a complex with PKN and activated it in COS-7 cells. PKN was phosphorylated in Swiss 3T3 cells stimulated with LPA, and this phosphorylation was blocked by treatment of cells with botulinum C3 exoenzyme. Activation of Rho may be linked directly to a serine-threonine kinase pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Amano, M -- Mukai, H -- Ono, Y -- Chihara, K -- Matsui, T -- Hamajima, Y -- Okawa, K -- Iwamatsu, A -- Kaibuchi, K -- New York, N.Y. -- Science. 1996 Feb 2;271(5249):648-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Signal Transduction, Nara Institute of Science and Technology, Ikoma, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8571127" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; ADP Ribose Transferases/pharmacology ; Amino Acid Sequence ; Animals ; *Botulinum Toxins ; Cell Line ; Chromatography, Affinity ; Enzyme Activation ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/*metabolism ; Guanosine Triphosphate/metabolism ; Lysophospholipids/pharmacology ; Mice ; Molecular Sequence Data ; Phosphorylation ; Protein Kinase C/*metabolism ; Recombinant Fusion Proteins/metabolism ; rhoA GTP-Binding Protein
    Print ISSN: 0036-8075
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  • 9
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    Phosphoinositides as regulators in membrane traffic (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-15
    Description: Phosphorylated products of phosphatidylinositol play critical roles in the regulation of membrane traffic, in addition to their classical roles as second messengers in signal transduction at the cell surface. Growing evidence suggests that phosphorylation-dephosphorylation of the polar heads of phosphoinositides (polyphosphorylated inositol lipids) in specific intracellular locations signals either the recruitment or the activation of proteins essential for vesicular transport. Cross talk between phosphatidylinositol metabolites and guanosine triphosphatases is an important feature of these regulatory mechanisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉De Camilli, P -- Emr, S D -- McPherson, P S -- Novick, P -- CA-46128/CA/NCI NIH HHS/ -- CA-58689/CA/NCI NIH HHS/ -- GM-32703/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1533-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599109" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Transport ; Cell Membrane/*metabolism ; Coated Vesicles/metabolism ; Endocytosis ; Exocytosis ; GTP Phosphohydrolases/metabolism ; Golgi Apparatus/metabolism ; Inositol Phosphates/*metabolism ; Intracellular Membranes/*metabolism ; Membrane Proteins/*metabolism ; Phosphatidylinositols/*metabolism ; Phosphorylation ; Yeasts/metabolism
    Print ISSN: 0036-8075
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  • 10
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    BTK as a mediator of radiation-induced apoptosis in DT-40 lymphoma B cells (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-23
    Description: Bruton's tyrosine kinase (BTK) is a member of the SRC-related TEC family of protein tyrosine kinases (PTKs). DT-40 lymphoma B cells, rendered BTK-deficient through targeted disruption of the btk gene by homologous recombination knockout, did not undergo radiation-induced apoptosis, but cells with disrupted lyn or syk genes did. Introduction of the wild-type, or a SRC homology 2 domain or a plecstrin homology domain mutant (but not a kinase domain mutant), human btk gene into BTK-deficient cells restored the apoptotic response to radiation. Thus, BTK is the PTK responsible for triggering radiation-induced apoptosis of lymphoma B cells, and its kinase domain is indispensable for the apoptotic response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Uckun, F M -- Waddick, K G -- Mahajan, S -- Jun, X -- Takata, M -- Bolen, J -- Kurosaki, T -- R01-CA-42111/CA/NCI NIH HHS/ -- R01-CA-42633/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 23;273(5278):1096-100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Signal Transduction Laboratory, Biotherapy Institute, University of Minnesota, Roseville, MN 55113, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8688094" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; B-Lymphocytes/cytology/enzymology/*radiation effects ; Chickens ; Gamma Rays ; Gene Targeting ; Humans ; Immunoglobulin M/immunology ; Lymphoma, B-Cell/enzymology/*pathology ; Phosphorylation ; Protein-Tyrosine Kinases/chemistry/genetics/*metabolism ; Receptors, Antigen, B-Cell/immunology/physiology ; Tumor Cells, Cultured ; src Homology Domains
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  • 11
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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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  • 12
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    Identification of an asymmetrically localized sensor histidine kinase responsible for temporally and spatially regulated transcription (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-25
    Description: Caulobacter crescentus undergoes asymmetric cell division, resulting in a stalked cell and a motile swarmer cell. The genes encoding external components of the flagellum are expressed in the swarmer compartment of the predivisional cell through the localized activation of the transcription factor FlbD. The mechanisms responsible for the temporal and spatial activation of FlbD were determined through identification of FlbE, a histidine kinase required for FlbD activity. FlbE is asymmetrically distributed in the predivisional cell. It is located at the pole of the stalked compartment and at the site of cell division in the swarmer compartment. These findings suggest that FlbE and FlbD are activated in response to a morphological change in the cell resulting from cell division events.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wingrove, J A -- Gober, J W -- GM-07104/GM/NIGMS NIH HHS/ -- GM48417/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):597-601.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry and the Molecular Biology Institute, University of California, Los Angeles, CA 90095-1569, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8849449" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/genetics/*metabolism ; Caulobacter crescentus/cytology/*genetics/physiology ; Cell Division ; DNA-Binding Proteins/genetics/*metabolism ; Gene Expression Regulation, Bacterial ; Genes, Bacterial ; Mutation ; Phosphorylation ; Promoter Regions, Genetic ; Protein Kinases/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Transcription Factors/genetics/*metabolism ; *Transcription, Genetic
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  • 13
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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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 14
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    Rho returns: its targets in focal adhesions (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bussey, H -- New York, N.Y. -- Science. 1996 Jul 12;273(5272):203.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, McGill University, Montreal, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8668997" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*metabolism ; Fungal Proteins/metabolism ; GTP Phosphohydrolases/metabolism ; GTP-Binding Proteins/*metabolism ; Humans ; Intracellular Signaling Peptides and Proteins ; Myosin-Light-Chain Phosphatase ; Myosins/*metabolism ; Phosphoprotein Phosphatases/antagonists & inhibitors/metabolism ; Phosphorylation ; Polysaccharides/biosynthesis ; Protein-Serine-Threonine Kinases/*metabolism ; Yeasts/metabolism ; *rho GTP-Binding Proteins ; rho-Associated Kinases ; rhoA GTP-Binding Protein
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  • 15
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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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  • 16
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    Imitation of Escherichia coli aspartate receptor signaling in engineered dimers of the cytoplasmic domain (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-23
    Description: Transmembrane signaling by bacterial chemotaxis receptors appears to require a conformational change within a receptor dimer. Dimers were engineered of the cytoplasmic domain of the Escherichia coli aspartate receptor that stimulated the kinase CheA in vitro. The folding free energy of the leucine-zipper dimerization domain was harnessed to twist the dimer interface of the receptor, which markedly affected the extent of CheA activation. Response to this twist was attenuated by modification of receptor regulatory sites, in the same manner as adaptation resets sensitivity to ligand in vivo. These results suggest that the normal allosteric activation of the chemotaxis receptor has been mimicked in a system that lacks both ligand-binding and transmembrane domains. The most stimulatory receptor dimer formed a species of tetrameric size.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cochran, A G -- Kim, P S -- T32 AI07348-07/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Feb 23;271(5252):1113-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599087" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/chemistry/*metabolism ; Chemoreceptor Cells ; Chemotaxis ; Cytoplasm/metabolism ; Enzyme Activation ; Escherichia coli/*metabolism ; *Escherichia coli Proteins ; Leucine Zippers ; Ligands ; Membrane Proteins/chemistry/*metabolism ; Methylation ; Molecular Sequence Data ; Phosphorylation ; Protein Conformation ; Protein Kinases/metabolism ; Protein Structure, Secondary ; Receptors, Amino Acid/chemistry/*metabolism ; *Receptors, Cell Surface ; Recombinant Fusion Proteins/chemistry/metabolism ; *Signal Transduction
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  • 17
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    Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase) (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-12
    Description: The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate (GTP)-bound, active form of RhoA (GTP.RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP.RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kimura, K -- Ito, M -- Amano, M -- Chihara, K -- Fukata, Y -- Nakafuku, M -- Yamamori, B -- Feng, J -- Nakano, T -- Okawa, K -- Iwamatsu, A -- Kaibuchi, K -- New York, N.Y. -- Science. 1996 Jul 12;273(5272):245-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Signal Transduction, Nara Institute of Science and Technology, Ikoma 630-01, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662509" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Actins/metabolism ; Amino Acid Sequence ; Animals ; Cattle ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/*metabolism ; Intracellular Signaling Peptides and Proteins ; Isopropyl Thiogalactoside/pharmacology ; Mice ; Molecular Sequence Data ; Muscle Contraction ; Muscle, Smooth/physiology ; Myosin Light Chains/metabolism ; Myosin-Light-Chain Phosphatase ; Oxazoles/pharmacology ; Phosphoprotein Phosphatases/*antagonists & inhibitors/metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/*metabolism ; rho-Associated Kinases ; rhoA GTP-Binding Protein
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  • 18
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    Activation of Pyk2 by stress signals and coupling with JNK signaling pathway (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-09
    Description: The c-Jun amino-terminal kinase (JNK) is activated by various heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors, inflammatory cytokines, and stress signals. Yet, upstream mediators that link extracellular signals with the JNK signaling pathway are currently unknown. The tyrosine kinase Pyk2 was activated by tumor necrosis factor alpha, by ultraviolet irradiation, and by changes in osmolarity. Overexpression of Pyk2 led to activation of JNK, and a dominant-negative mutant of Pyk2 interfered with ultraviolet light- or osmotic shock-induced activation of JNK. Pyk2 represents a cell type-specific, stress-sensitive mediator of the JNK signaling pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tokiwa, G -- Dikic, I -- Lev, S -- Schlessinger, J -- New York, N.Y. -- Science. 1996 Aug 9;273(5276):792-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, New York University Medical Center, 550 First Avenue, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8670418" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anisomycin/pharmacology ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Egtazic Acid/pharmacology ; Enzyme Activation ; Focal Adhesion Kinase 2 ; GTP Phosphohydrolases/metabolism ; GTP-Binding Proteins/metabolism ; HL-60 Cells ; Humans ; JNK Mitogen-Activated Protein Kinases ; *Mitogen-Activated Protein Kinases ; Osmolar Concentration ; PC12 Cells ; Phosphorylation ; Protein-Tyrosine Kinases/*metabolism ; Rats ; *Signal Transduction ; Sorbitol/pharmacology ; Transfection ; Tumor Necrosis Factor-alpha/pharmacology ; Ultraviolet Rays
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  • 19
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    Protection against osmotic stress by cGMP-mediated myosin phosphorylation (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-12
    Description: Conventional myosin functions universally as a generator of motive force in eukaryotic cells. Analysis of mutants of the microorganism Dictyostelium discoideum revealed that myosin also provides resistance against high external osmolarities. An osmo-induced increase of intracellular guanosine 3',5'-monophosphate was shown to mediate phosphorylation of three threonine residues on the myosin tail, which caused a relocalization of myosin required to resist osmotic stress. This redistribution of myosin allowed cells to adopt a spherical shape and may provide physical strength to withstand extensive cell shrinkage in high osmolarities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuwayama, H -- Ecke, M -- Gerisch, G -- Van Haastert, P J -- New York, N.Y. -- Science. 1996 Jan 12;271(5246):207-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Groningen, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539621" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/chemistry ; Actins/analysis ; Animals ; Cyclic GMP/analogs & derivatives/*metabolism/pharmacology ; Cytoplasm/chemistry ; Dictyostelium/genetics/*physiology/ultrastructure ; Glucose/pharmacology ; Guanylate Cyclase/metabolism ; Myosins/analysis/*metabolism ; Osmotic Pressure ; Phosphorylation ; Pseudopodia/chemistry/ultrastructure ; Threonine/metabolism ; Water-Electrolyte Balance
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  • 20
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    Rapid degradation of the G1 cyclin Cln2 induced by CDK-dependent phosphorylation (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-15
    Description: Cyclins regulate the major cell cycle transitions in eukaryotes through association with cyclin-dependent protein kinases (CDKs). In yeast, G1 cyclins are essential, rate-limiting activators of cell cycle initiation. G1-specific accumulation of one G1 cyclin, Cln2, results from periodic gene expression coupled with rapid protein turnover. Site-directed mutagenesis of CLN2 revealed that its phosphorylation provides a signal that promotes rapid degradation. Cln2 phosphorylation is dependent on the Cdc28 protein kinase, the CDK that it activates. These findings suggest that Cln2 is rendered self-limiting by virtue of its ability to activate its cognate CDK subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lanker, S -- Valdivieso, M H -- Wittenberg, C -- GM43487/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1597-601.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599119" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; CDC28 Protein Kinase, S cerevisiae/*metabolism ; Cyclins/genetics/*metabolism ; Enzyme Activation ; Fungal Proteins/genetics/metabolism ; *G1 Phase ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutation ; Phenotype ; Phosphorylation ; Saccharomyces cerevisiae/cytology/metabolism ; Saccharomyces cerevisiae Proteins
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  • 21
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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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  • 22
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    Resetting the Drosophila clock by photic regulation of PER and a PER-TIM complex (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-22
    Description: Circadian clocks can be reset by light stimulation. To investigate the mechanism of this phase shifting, the effects of light pulses on the protein and messenger RNA products of the Drosophila clock gene period (per) were measured. Photic stimuli perturbed the timing of the PER protein and messenger RNA cycles in a manner consistent with the direction and magnitude of the phase shift. In addition, the recently identified clock protein TIM (for timeless) interacted with PER in vivo, and this association was rapidly decreased by light. This disruption of the PER-TIM complex in the cytoplasm was accompanied by a delay in PER phosphorylation and nuclear entry and disruption in the nucleus by an advance in PER phosphorylation and disappearance. These results suggest a mechanism for how a unidirectional environmental signal elicits a bidirectional clock response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, C -- Parikh, V -- Itsukaichi, T -- Bae, K -- Edery, I -- New York, N.Y. -- Science. 1996 Mar 22;271(5256):1740-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate Program in Molecular Genetics and Microbiology, Center for Advanced Biotechnology and Medicine, Rutgers University, Piscataway, NJ 08854, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596938" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Clocks/genetics ; Brain/metabolism ; Cell Nucleus/metabolism ; *Circadian Rhythm/genetics ; Cytoplasm/metabolism ; Darkness ; *Drosophila Proteins ; Drosophila melanogaster/genetics/metabolism/*physiology ; Gene Expression Regulation ; Genes, Insect ; *Light ; Neurons/metabolism ; Nuclear Proteins/genetics/*metabolism ; Period Circadian Proteins ; Phosphorylation ; Photoreceptor Cells, Invertebrate/metabolism ; Proteins/genetics/*metabolism ; RNA, Messenger/genetics/metabolism
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  • 23
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    STATs find that hanging together can be stimulating (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-08-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leung, S -- Li, X -- Stark, G R -- New York, N.Y. -- Science. 1996 Aug 9;273(5276):750-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Research Institute, Cleveland Clinic Foundation, Cleveland, OH 44195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8701326" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/metabolism ; Cytokines/*metabolism ; DNA-Binding Proteins/chemistry/metabolism ; Humans ; Interferon-alpha/metabolism ; Interferon-gamma/metabolism ; Phosphorylation ; Receptor, Interferon alpha-beta ; Receptors, Interferon/metabolism ; STAT1 Transcription Factor ; STAT4 Transcription Factor ; *Signal Transduction ; Trans-Activators/chemistry/*metabolism ; Transcription Factors/metabolism ; *Transcriptional Activation ; src Homology Domains
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  • 24
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    Linkage of replication to start by the Cdk inhibitor Sic1 (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-26
    Description: In Saccharomyces cerevisiae, three G1 cyclins (Clns) are important for Start, the event committing cells to division. Sic1, an inhibitor of C1b-Cdc28 kinases, became phosphorylated at Start, and this phosphorylation depended on the activity of Clns. Sic1 was subsequently lost, which depended on the activity of Clns and the ubiquitin-conjugating enzyme Cdc34. Inactivation of Sic1 was the only nonredundant essential function of Clns, because a sic1 deletion rescued the inviability of the cln1 cln2 cln3 triple mutant. In sic1 mutants, DNA replication became uncoupled from budding. Thus, Sic1 may be a substrate of Cln-Cdc28 complexes, and phosphorylation and proteolysis of Sic1 may regulate commitment to replication at Start.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schneider, B L -- Yang, Q H -- Futcher, A B -- GM39978/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Apr 26;272(5261):560-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614808" target="_blank"〉PubMed〈/a〉
    Keywords: Anaphase-Promoting Complex-Cyclosome ; CDC28 Protein Kinase, S cerevisiae/antagonists & inhibitors/metabolism ; Cell Cycle ; Cyclin-Dependent Kinase Inhibitor Proteins ; Cyclins/metabolism ; *DNA Replication ; DNA, Fungal/biosynthesis ; Enzyme Inhibitors/*metabolism ; Fungal Proteins/*metabolism ; Ligases/metabolism ; Phosphorylation ; Saccharomyces cerevisiae/cytology/*metabolism ; *Saccharomyces cerevisiae Proteins ; Ubiquitin-Conjugating Enzymes ; *Ubiquitin-Protein Ligase Complexes ; Ubiquitin-Protein Ligases
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  • 25
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    rad-dependent response of the chk1-encoded protein kinase at the DNA damage checkpoint (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-19
    Description: Exposure of eukaryotic cells to agents that generate DNA damage results in transient arrest of progression through the cell cycle. In fission yeast, the DNA damage checkpoint associated with cell cycle arrest before mitosis requires the protein kinase p56chk1. DNA damage induced by ultraviolet light, gamma radiation, or a DNA-alkylating agent has now been shown to result in phosphorylation of p56chk1. This phosphorylation decreased the mobility of p56chk1 on SDS-polyacrylamide gel electrophoresis and was abolished by a mutation in the p56chk1 catalytic domain, suggesting that it might represent autophosphorylation. Phosphorylation of p56chk1 did not occur when other checkpoint genes were inactive. Thus, p56chk1 appears to function downstream of several of the known Schizosaccharomyces pombe checkpoint gene products, including that encoded by rad3+, a gene with sequence similarity to the ATM gene mutated in patients with ataxia telangiectasia. The phosphorylation of p56chk1 provides an assayable biochemical response to activation of the DNA damage checkpoint in the G2 phase of the cell cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walworth, N C -- Bernards, R -- New York, N.Y. -- Science. 1996 Jan 19;271(5247):353-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Carcinogenesis, Netherlands Cancer Institute, Amsterdam.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8553071" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/genetics ; Ataxia Telangiectasia Mutated Proteins ; Base Sequence ; Cell Cycle Proteins ; *DNA Damage ; DNA Helicases/genetics ; DNA Replication ; DNA, Fungal/metabolism/radiation effects ; DNA-Binding Proteins ; Electrophoresis, Polyacrylamide Gel ; *G2 Phase ; Genes, Fungal ; Humans ; *Mitosis ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Protein Kinases/chemistry/genetics/*metabolism ; *Protein-Serine-Threonine Kinases ; Proteins/genetics ; Recombinant Fusion Proteins/chemistry/metabolism ; Saccharomyces cerevisiae Proteins ; Schizosaccharomyces/*cytology/genetics/radiation effects ; Tumor Suppressor Proteins ; Ultraviolet Rays
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    A K+ channel worthy of attention (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-09-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hille, B -- New York, N.Y. -- Science. 1996 Sep 20;273(5282):1677.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, University of Washington, Seattle, 98195-7290, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8830412" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Attention/*physiology ; Calcium/*metabolism ; Cloning, Molecular ; Cyclic AMP/metabolism ; Humans ; Norepinephrine/metabolism ; Phosphorylation ; Potassium Channels/metabolism/*physiology ; *Potassium Channels, Calcium-Activated ; Rats ; Small-Conductance Calcium-Activated Potassium Channels
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 27
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    The p21(RAS) farnesyltransferase alpha subunit in TGF-beta and activin signaling (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-23
    Description: The alpha subunit of p21(RAS) farnesyltransferase (FNTA), which is also shared by geranylgeranyltransferase, was isolated as a specific cytoplasmic interactor of the transforming growth factor-beta (TGF-beta) and activin type I receptors with the use of the yeast two-hybrid system. FNTA interacts specifically with ligand-free TGF-beta type l receptor but is phosphorylated and released upon ligand binding. Furthermore, the release is dependent on the kinase activity of the TGF-beta type II receptor. Thus, the growth inhibitory and differentiative pathways activated by TGF-beta and activin involve novel mechanisms of serine-threonine receptor phosphorylation-dependent release of cytoplasmic interactors and regulation of the activation of small G proteins, such as p21(RAS).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, T -- Danielson, P D -- Li, B Y -- Shah, P C -- Kim, S D -- Donahoe, P K -- HD28138/HD/NICHD NIH HHS/ -- R01 HD3081/HD/NICHD NIH HHS/ -- R01 HD32112/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1996 Feb 23;271(5252):1120-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pediatric Surgical Research Laboratories, Massachusetts General Hospital, Boston, MA 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599089" target="_blank"〉PubMed〈/a〉
    Keywords: Activin Receptors ; *Activin Receptors, Type I ; Activins ; *Alkyl and Aryl Transferases ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Humans ; Inhibins/*metabolism ; Ligands ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism ; Receptors, Growth Factor/metabolism ; Receptors, Transforming Growth Factor beta/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Transferases/*metabolism ; Transforming Growth Factor beta/*metabolism
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  • 28
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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)
    Details
    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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    Extracellular protein kinases (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ehrlich, Y H -- New York, N.Y. -- Science. 1996 Jan 19;271(5247):278-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8553056" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Membrane/*enzymology ; Long-Term Potentiation ; Phosphorylation ; Protein Kinases/*metabolism ; Receptors, Glutamate/*metabolism
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  • 30
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    Inhibition of adipogenesis through MAP kinase-mediated phosphorylation of PPARgamma (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-20
    Description: Adipocyte differentiation is an important component of obesity and other metabolic diseases. This process is strongly inhibited by many mitogens and oncogenes. Several growth factors that inhibit fat cell differentiation caused mitogen-activated protein (MAP) kinase-mediated phosphorylation of the dominant adipogenic transcription factor peroxisome proliferator-activated receptor gamma (PPARgamma) and reduction of its transcriptional activity. Expression of PPARgamma with a nonphosphorylatable mutation at this site (serine-112) yielded cells with increased sensitivity to ligand-induced adipogenesis and resistance to inhibition of differentiation by mitogens. These results indicate that covalent modification of PPARgamma by serum and growth factors is a major regulator of the balance between cell growth and differentiation in the adipose cell lineage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hu, E -- Kim, J B -- Sarraf, P -- Spiegelman, B M -- R37DK31405/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1996 Dec 20;274(5295):2100-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute and Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8953045" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Adipocytes/*cytology/metabolism ; Animals ; Blood ; Calcium-Calmodulin-Dependent Protein Kinases/antagonists & inhibitors/*metabolism ; Cell Differentiation ; Cell Line ; Enzyme Inhibitors/pharmacology ; Epidermal Growth Factor/pharmacology ; Flavonoids/pharmacology ; Insulin/pharmacology ; Ligands ; Mice ; Mitogens/pharmacology ; Mutation ; Phosphorylation ; Rats ; Receptors, Cytoplasmic and Nuclear/chemistry/genetics/*metabolism ; Tetradecanoylphorbol Acetate/pharmacology ; Transcription Factors/chemistry/genetics/*metabolism ; Transcription, Genetic/drug effects ; Transfection
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  • 31
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    A role for phosphoinositide 3-kinase in bacterial invasion (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-01
    Description: Listeria monocytogenes is a bacterial pathogen that invades cultured nonphagocytic cells. Inhibitors and a dominant negative mutation were used to demonstrate that efficient entry requires the phosphoinositide (PI) 3-kinase p85alpha-p110. Infection with L. monocytogenes caused rapid increases in cellular amounts of PI(3, 4)P2 and PI(3,4,5)P3, indicating that invading bacteria stimulated PI 3-kinase activity. This stimulation required the bacterial protein InlB, host cell tyrosine phosphorylation, and association of p85alpha with one or more tyrosine-phosphorylated proteins. This role for PI 3-kinase in bacterial entry may have parallels in some endocytic events.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ireton, K -- Payrastre, B -- Chap, H -- Ogawa, W -- Sakaue, H -- Kasuga, M -- Cossart, P -- New York, N.Y. -- Science. 1996 Nov 1;274(5288):780-2.〈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/8864117" target="_blank"〉PubMed〈/a〉
    Keywords: Androstadienes/pharmacology ; Animals ; Bacterial Proteins/physiology ; Cell Line ; Chromones/pharmacology ; Cytochalasin D/pharmacology ; Enzyme Activation ; Enzyme Inhibitors/pharmacology ; Genistein ; Humans ; Isoflavones/pharmacology ; Listeria monocytogenes/*enzymology/*pathogenicity ; Membrane Proteins/physiology ; Morpholines/pharmacology ; Phosphatidylinositol 3-Kinases ; Phosphatidylinositol Phosphates/metabolism ; Phosphoproteins/metabolism ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor)/antagonists & inhibitors/*metabolism ; Phosphotyrosine/metabolism ; Tumor Cells, Cultured
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  • 32
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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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  • 33
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    A protein phosphorylation switch at the conserved allosteric site in GP (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-09-13
    Description: A phosphorylation-initiated mechanism of local protein refolding activates yeast glycogen phosphorylase (GP). Refolding of the phosphorylated amino-terminus was shown to create a hydrophobic cluster that wedges into the subunit interface of the enzyme to trigger activation. The phosphorylated threonine is buried in the allosteric site. The mechanism implicates glucose 6-phosphate, the allosteric inhibitor, in facilitating dephosphorylation by dislodging the buried covalent phosphate through binding competition. Thus, protein phosphorylation-dephosphorylation may also be controlled through regulation of the accessibility of the phosphorylation site to kinases and phosphatases. In mammalian glycogen phosphorylase, phosphorylation occurs at a distinct locus. The corresponding allosteric site binds a ligand activator, adenosine monophosphate, which triggers activation by a mechanism analogous to that of phosphorylation in the yeast enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, K -- Rath, V L -- Dai, S C -- Fletterick, R J -- Hwang, P K -- DK32822/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1996 Sep 13;273(5281):1539-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California at San Francisco, 513 Parnassus, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703213" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Monophosphate/metabolism ; Allosteric Site ; Amino Acid Sequence ; Animals ; Crystallography, X-Ray ; Enzyme Activation ; Enzyme Inhibitors/metabolism/pharmacology ; Glucose-6-Phosphate ; Glucosephosphates/metabolism/pharmacology ; Models, Molecular ; Molecular Sequence Data ; Phosphorylases/antagonists & inhibitors/*chemistry/*metabolism ; Phosphorylation ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Saccharomyces cerevisiae/enzymology
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  • 34
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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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  • 35
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    Direct regulation of ZAP-70 by SHP-1 in T cell antigen receptor signaling (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-24
    Description: The threshold at which antigen triggers lymphocyte activation is set by the enzymes that regulate tyrosine phosphorylation. Upon T cell activation, the protein tyrosine phosphatase SHP-1 was found to bind to the protein tyrosine kinase ZAP-70. This interaction resulted in an increase in SHP-1 phosphatase activity and a decrease in ZAP-70 kinase activity. Expression of a dominant negative mutant of SHP-1 in T cells increased the sensitivity of the antigen receptor. Thus, SHP-1 functions as a negative regulator of the T cell antigen receptor and in setting the threshold of activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Plas, D R -- Johnson, R -- Pingel, J T -- Matthews, R J -- Dalton, M -- Roy, G -- Chan, A C -- Thomas, M L -- New York, N.Y. -- Science. 1996 May 24;272(5265):1173-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Center for Immunology, Washington University Medical School, St Louis, Missouri 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638162" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; HeLa Cells ; Humans ; Intracellular Signaling Peptides and Proteins ; Lymphocyte Activation ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck) ; Mutation ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein Tyrosine Phosphatase, Non-Receptor Type 11 ; Protein Tyrosine Phosphatase, Non-Receptor Type 6 ; Protein Tyrosine Phosphatases/genetics/*metabolism ; Protein-Tyrosine Kinases/*metabolism ; Receptors, Antigen, T-Cell/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; T-Lymphocytes/immunology/*metabolism ; Transfection ; Tumor Cells, Cultured ; ZAP-70 Protein-Tyrosine Kinase ; src-Family Kinases/metabolism
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  • 36
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    Coordination of three signaling enzymes by AKAP79, a mammalian scaffold protein (1996)
    American Association for the Advancement of Science (AAAS)
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    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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  • 37
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    Crystal structure of the dual specificity protein phosphatase VHR (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-31
    Description: Dual specificity protein phosphatases (DSPs) regulate mitogenic signal transduction and control the cell cycle. Here, the crystal structure of a human DSP, vaccinia H1-related phosphatase (or VHR), was determined at 2.1 angstrom resolution. A shallow active site pocket in VHR allows for the hydrolysis of phosphorylated serine, threonine, or tyrosine protein residues, whereas the deeper active site of protein tyrosine phosphatases (PTPs) restricts substrate specificity to only phosphotyrosine. Positively charged crevices near the active site may explain the enzyme's preference for substrates with two phosphorylated residues. The VHR structure defines a conserved structural scaffold for both DSPs and PTPs. A "recognition region," connecting helix alpha1 to strand beta1, may determine differences in substrate specificity between VHR, the PTPs, and other DSPs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yuvaniyama, J -- Denu, J M -- Dixon, J E -- Saper, M A -- AI 34095/AI/NIAID NIH HHS/ -- DK18024/DK/NIDDK NIH HHS/ -- DK18849/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 May 31;272(5266):1328-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biophysics Research Division and Department of Biological Chemistry, University of Michigan, Ann Arbor 48109-1055, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650541" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; Dual Specificity Phosphatase 3 ; Humans ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Phosphorylation ; Phosphoserine/metabolism ; Phosphothreonine/metabolism ; Phosphotyrosine/metabolism ; *Protein Conformation ; Protein Folding ; *Protein Structure, Secondary ; Protein Tyrosine Phosphatases/*chemistry/metabolism ; Sequence Alignment ; Substrate Specificity ; Water/metabolism ; Yersinia/enzymology
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  • 38
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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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    Regulation of a neuronal form of focal adhesion kinase by anandamide (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-09-20
    Description: Anandamide is an endogenous ligand for central cannabinoid receptors and is released after neuronal depolarization. Anandamide increased protein tyrosine phosphorylation in rat hippocampal slices and neurons in culture. The action of anandamide resulted from the inhibition of adenylyl cyclase and cyclic adenosine 3', 5'-monophosphate-dependent protein kinase. One of the proteins phosphorylated in response to anandamide was an isoform of pp125-focal adhesion kinase (FAK+) expressed preferentially in neurons. Focal adhesion kinase is a tyrosine kinase involved in the interactions between the integrins and actin-based cytoskeleton. Thus, anandamide may exert neurotrophic effects and play a role in synaptic plasticity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Derkinderen, P -- Toutant, M -- Burgaya, F -- Le Bert, M -- Siciliano, J C -- de Franciscis, V -- Gelman, M -- Girault, J A -- New York, N.Y. -- Science. 1996 Sep 20;273(5282):1719-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉INSERM U 114, Chaire de Neuropharmacologie, College de France, 11 place Marcelin Berthelot, 75231 Paris cedex 05, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8781236" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclase Inhibitors ; Adenylyl Cyclases/metabolism ; Amino Acid Sequence ; Animals ; Arachidonic Acid/pharmacology ; Arachidonic Acids/*pharmacology ; Cell Adhesion Molecules/*metabolism ; Cell Line ; Cells, Cultured ; Cyclic AMP/metabolism ; Cyclic AMP-Dependent Protein Kinases/antagonists & inhibitors/metabolism ; Endocannabinoids ; Focal Adhesion Kinase 1 ; Focal Adhesion Protein-Tyrosine Kinases ; Hippocampus/drug effects/*enzymology ; In Vitro Techniques ; Molecular Sequence Data ; Neuronal Plasticity/drug effects ; Neurons/drug effects/*enzymology ; Phosphorylation ; Phosphotyrosine/metabolism ; Polyunsaturated Alkamides ; Prosencephalon ; Protein-Tyrosine Kinases/*metabolism ; Rats ; Receptors, Cannabinoid ; Receptors, Drug/metabolism
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    Survival of cholinergic forebrain neurons in developing p75NGFR-deficient mice (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-06
    Description: The functions of the low-affinity p75 nerve growth factor receptor (p75(NGFR)) in the central nervous system were explored in vivo. In normal mice, approximately 25 percent of the cholinergic basal forebrain neurons did not express TrkA and died between postnatal day 6 and 15. This loss did not occur in p75(NGFR)-deficient mice or in normal mice systemically injected with a p75(NGFR)-inhibiting peptide. Control, but not p75(NGFR)-deficient, mice also had fewer cholinergic striatal interneurons. Apparently, p75(NGFR) mediates apoptosis of these developing neurons in the absence of TrkA, and modulation of p75(NGFR) can promote neuronal survival. Cholinergic basal forebrain neurons are involved in learning and memory.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Van der Zee, C E -- Ross, G M -- Riopelle, R J -- Hagg, T -- New York, N.Y. -- Science. 1996 Dec 6;274(5293):1729-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Neurobiology, Tupper Building, Dalhousie University, Halifax, Nova Scotia B3H 4H7, Canada. thagg@is.dal.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8939868" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Cell Survival ; Choline O-Acetyltransferase/metabolism ; DNA Fragmentation ; Interneurons/cytology ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Neostriatum/cytology ; Neurons/*cytology/enzymology ; Oligopeptides/pharmacology ; Parasympathetic Nervous System/*cytology ; Phosphorylation ; Prosencephalon/*cytology ; Proto-Oncogene Proteins/metabolism ; Purkinje Cells/cytology ; Receptor Protein-Tyrosine Kinases/metabolism ; Receptor, Nerve Growth Factor ; Receptor, trkA ; Receptors, Nerve Growth Factor/deficiency/metabolism/*physiology
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    Control of EGF receptor signaling by clathrin-mediated endocytosis (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-20
    Description: Epidermal growth factor receptor (EGFR) signaling was analyzed in mammalian cells conditionally defective for receptor-mediated endocytosis. EGF-dependent cell proliferation was enhanced in endocytosis-defective cells. However, early EGF-dependent signaling events were not uniformly up-regulated. A subset of signal transducers required the normal endocytic trafficking of EGFR for full activation. Thus, endocytic trafficking of activated EGFR plays a critical role not only in attenuating EGFR signaling but also in establishing and controlling specific signaling pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vieira, A V -- Lamaze, C -- Schmid, S L -- CA58689/CA/NCI NIH HHS/ -- CA69099/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Dec 20;274(5295):2086-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. slschmid@scripps.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8953040" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; *Adaptor Proteins, Vesicular Transport ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Cell Division/drug effects ; Cell Membrane/metabolism ; Clathrin/*physiology ; Coated Pits, Cell-Membrane/physiology ; Dynamins ; *Endocytosis ; Enzyme Activation ; Epidermal Growth Factor/metabolism/pharmacology ; GTP Phosphohydrolases/physiology ; HeLa Cells ; Humans ; Isoenzymes/metabolism ; Phosphatidylinositol 3-Kinases ; Phospholipase C gamma ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor)/metabolism ; Phosphotyrosine/metabolism ; Proteins/metabolism ; Receptor, Epidermal Growth Factor/*metabolism ; Shc Signaling Adaptor Proteins ; *Signal Transduction ; Type C Phospholipases/metabolism
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    Dependence of cyclin E-CDK2 kinase activity on cell anchorage (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-26
    Description: Most nonmalignant cells are anchorage-dependent; they require substrate attachment for growth and, in some instances, survival. This requirement is lost on oncogenic transformation. The cyclin E-CDK2 complex, which is required for the G1-S transition of the cell cycle, was activated in late G1 phase in attached human fibroblasts, but not in fibroblasts maintained in suspension. In transformed fibroblasts the complex was active regardless of attachment. The lack of cyclin E-CDK2 activity in suspended cells appeared to result from increased expression of CDK2 inhibitors and a concomitant decrease in phosphorylation of CDK2 on threonine-160. Suppression of cyclin E-CDK2 activity may thus underlie the anchorage dependence of cell growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fang, F -- Orend, G -- Watanabe, N -- Hunter, T -- Ruoslahti, E -- CA 28896/CA/NCI NIH HHS/ -- CA 60725/CA/NCI NIH HHS/ -- CA 67224/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Jan 26;271(5248):499-502.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉La Jolla Cancer Research Foundation, Cancer Center, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8560263" target="_blank"〉PubMed〈/a〉
    Keywords: *CDC2-CDC28 Kinases ; *Cell Adhesion ; *Cell Cycle Proteins ; Cell Line ; Cell Line, Transformed ; Cell Nucleus/metabolism ; *Cell Transformation, Neoplastic ; Cyclin-Dependent Kinase 2 ; Cyclin-Dependent Kinase Inhibitor p21 ; Cyclin-Dependent Kinase Inhibitor p27 ; Cyclin-Dependent Kinase Inhibitor p57 ; Cyclin-Dependent Kinases/antagonists & inhibitors/*metabolism ; Cyclins/*metabolism ; Enzyme Inhibitors/metabolism ; *G1 Phase ; Humans ; Microtubule-Associated Proteins/metabolism ; Nuclear Proteins/metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/antagonists & inhibitors/*metabolism ; Tumor Cells, Cultured ; *Tumor Suppressor Proteins
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    Regulation of PHO4 nuclear localization by the PHO80-PHO85 cyclin-CDK complex (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-12
    Description: PHO4, a transcription factor required for induction of the PHO5 gene in response to phosphate starvation, is phosphorylated by the PHO80-PHO85 cyclin-CDK (cyclin-dependent kinase) complex when yeast are grown in phosphate-rich medium. PHO4 was shown to be concentrated in the nucleus when yeast were starved for phosphate and was predominantly cytoplasmic when yeast were grown in phosphate-rich medium. The sites of phosphorylation on PHO4 were identified, and phosphorylation was shown to be required for full repression of PHO5 transcription when yeast were grown in high phosphate. Thus, phosphorylation of PHO4 by PHO80-PHO85 turns off PHO5 transcription by regulating the nuclear localization of PHO4.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Neill, E M -- Kaffman, A -- Jolly, E R -- O'Shea, E K -- New York, N.Y. -- Science. 1996 Jan 12;271(5246):209-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California at San Francisco, School of Medicine 94143-0448, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539622" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Nucleus/*metabolism ; Culture Media ; Cyclin-Dependent Kinases/*metabolism ; Cyclins/*metabolism ; Cytoplasm/metabolism ; *DNA-Binding Proteins ; Dipeptides/metabolism ; Fungal Proteins/*metabolism ; Gene Expression Regulation, Fungal ; Membrane Transport Proteins/genetics ; Molecular Sequence Data ; Mutation ; *Phosphate Transport Proteins ; Phosphates/metabolism ; Phosphorylation ; *Repressor Proteins ; Saccharomyces cerevisiae/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Transcription Factors/*metabolism
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    A cyclin-dependent kinase-activating kinase (CAK) in budding yeast unrelated to vertebrate CAK (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-09-20
    Description: Progress through the cell cycle is governed by the cyclin-dependent kinases (CDKs), the activation of which requires phosphorylation by the CDK-activating kinase (CAK). In vertebrates, CAK is a trimeric enzyme containing CDK7, cyclin H, and MAT1. CAK from the budding yeast Saccharomyces cerevisiae was identified as an unusual 44-kilodalton protein kinase, Cak1, that is only distantly related to CDKs. Cak1 accounted for most CAK activity in yeast cell lysates, and its activity was constant throughout the cell cycle. The CAK1 gene was essential for cell viability. Thus, the major CAK in S. cerevisiae is distinct from the vertebrate enzyme, suggesting that budding yeast and vertebrates may have evolved different mechanisms of CDK activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Espinoza, F H -- Farrell, A -- Erdjument-Bromage, H -- Tempst, P -- Morgan, D O -- New York, N.Y. -- Science. 1996 Sep 20;273(5282):1714-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of California, San Francisco, 94143-0444, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8781234" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *CDC2-CDC28 Kinases ; CDC28 Protein Kinase, S cerevisiae/metabolism ; Cell Cycle ; Cyclin-Dependent Kinase 2 ; Cyclin-Dependent Kinases/metabolism ; Enzyme Activation ; Gene Deletion ; Genes, Fungal ; Humans ; Molecular Sequence Data ; Molecular Weight ; Phosphorylation ; Protein-Serine-Threonine Kinases/*chemistry/genetics/isolation & ; purification/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Saccharomyces cerevisiae/*enzymology/genetics
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    Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-25
    Description: Tat may stimulate transcriptional elongation by recruitment of a complex containing Tat-SF1 and a kinase to the human immunodeficiency virus-type 1 (HIV-1) promoter through a Tat-TAR interaction. A complementary DNA for the cellular activity, Tat-SF1, has been isolated. This factor is required for Tat trans-activation and is a substrate of an associated cellular kinase. Cotransfection with the complementary DNA for Tat-SF1 specifically modulates Tat activation. Tat-SF1 contains two RNA recognition motifs and a highly acidic carboxyl-terminal half. It is distantly related to EWS and FUS/TLS, members of a family of putative transcription factors with RNA recognition motifs that are associated with sarcomas.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, Q -- Sharp, P A -- AI32486/AI/NIAID NIH HHS/ -- CA14051/CA/NCI NIH HHS/ -- GM34277/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):605-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Cancer Research and 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/8849451" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; DNA, Complementary/genetics ; Electrophoresis, Polyacrylamide Gel ; Gene Expression ; Gene Products, tat/*genetics ; HIV Long Terminal Repeat ; HIV-1/*genetics ; HeLa Cells ; Heterogeneous-Nuclear Ribonucleoproteins ; Humans ; Immunoblotting ; Molecular Sequence Data ; Molecular Weight ; Neoplasm Proteins/chemistry ; Phosphorylation ; Promoter Regions, Genetic ; Protein Kinases/metabolism ; RNA, Viral/metabolism ; RNA-Binding Protein EWS ; RNA-Binding Protein FUS ; Ribonucleoproteins/chemistry ; Sequence Homology, Amino Acid ; Trans-Activators/chemistry/*genetics/metabolism ; *Transcriptional Activation ; Transfection ; tat Gene Products, Human Immunodeficiency Virus
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    Forskolin stimulation of water and cation permeability in aquaporin 1 water channels (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-30
    Description: Aquaporin 1, a six-transmembrane domain protein, is a water channel present in many fluid-secreting and -absorbing cells. In Xenopus oocytes injected with aquaporin 1 complementary RNA, the application of forskolin or cyclic 8-bromo- adenosine 3',5'-monophosphate increased membrane permeability to water and triggered a cationic conductance. The cationic conductance was also induced by direct injection of protein kinase A (PKA) catalytic subunit, reduced by the kinase inhibitor H7, and blocked by HgCl2, an inhibitor of aquaporin 1. The cationic permeability of the aquaporin 1 channel is activated by a cyclic adenosine monophosphate-dependent mechanism that may involve direct or indirect phosphorylation by PKA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yool, A J -- Stamer, W D -- Regan, J W -- EY09355/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 30;273(5279):1216-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Arizona, Tucson, AZ 85724-5051, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703053" target="_blank"〉PubMed〈/a〉
    Keywords: 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine ; 8-Bromo Cyclic Adenosine Monophosphate/pharmacology ; Animals ; Aquaporin 1 ; *Aquaporins ; Cations/*metabolism ; Cell Membrane Permeability/*drug effects ; Colforsin/*pharmacology ; Cyclic AMP/*metabolism ; Cyclic AMP-Dependent Protein Kinases/antagonists & inhibitors/metabolism ; Enzyme Inhibitors/pharmacology ; Ion Channels/drug effects/genetics/*metabolism ; Isoquinolines/pharmacology ; Mercuric Chloride/pharmacology ; Oocytes ; Patch-Clamp Techniques ; Phosphorylation ; Piperazines/pharmacology ; RNA, Complementary/genetics ; Water/*metabolism ; Xenopus
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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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    Purification and molecular cloning of Plx1, a Cdc25-regulatory kinase from Xenopus egg extracts (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-09-06
    Description: Cdc2, the cyclin-dependent kinase that controls mitosis, is negatively regulated by phosphorylation on its threonine-14 and tyrosine-15 residues. Cdc25, the phosphatase that dephosphorylates both of these residues, undergoes activation and phosphorylation by multiple kinases at mitosis. Plx1, a kinase that associates with and phosphorylates the amino-terminal domain of Cdc25, was purified extensively from Xenopus egg extracts. Cloning of its complementary DNA revealed that Plx1 is related to the Polo family of protein kinases. Recombinant Plx1 phosphorylated Cdc25 and stimulated its activity in a purified system. Cdc25 phosphorylated by Plx1 reacted strongly with MPM-2, a monoclonal antibody to mitotic phosphoproteins. These studies indicate that Plx1 may participate in control of mitotic progression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kumagai, A -- Dunphy, W G -- New York, N.Y. -- Science. 1996 Sep 6;273(5280):1377-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, 216-76, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703070" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; CDC2 Protein Kinase/metabolism ; Cell Cycle Proteins/chemistry/*metabolism ; Cloning, Molecular ; Cyclins/metabolism ; Enzyme Activation ; Molecular Sequence Data ; Mutation ; Oocytes/enzymology ; Peptide Mapping ; Phosphoprotein Phosphatases/chemistry/*metabolism ; Phosphorylation ; Phosphoserine/analysis ; Phosphothreonine/analysis ; Protein-Serine-Threonine Kinases/chemistry/genetics/*isolation & ; purification/metabolism ; Recombinant Proteins/metabolism ; Xenopus ; *Xenopus Proteins ; cdc25 Phosphatases
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    Neuronal gene expression in the waking state: a role for the locus coeruleus (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-15
    Description: Several transcription factors are expressed at higher levels in the waking than in the sleeping brain. In experiments with rats, the locus coeruleus, a noradrenergic nucleus with diffuse projections, was found to regulate such expression. In brain regions depleted of noradrenergic innervation, amounts of c-Fos and nerve growth factor-induced A after waking were as low as after sleep. Phosphorylation of cyclic adenosine monophosphate response element-binding protein was also reduced. In contrast, electroencephalographic activity was unchanged. The reduced activity of locus coeruleus neurons may explain why the induction of certain transcription factors, with potential effects on plasticity and learning, does not occur during sleep.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cirelli, C -- Pompeiano, M -- Tononi, G -- New York, N.Y. -- Science. 1996 Nov 15;274(5290):1211-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Neurosciences Institute, 10640 J. J. Hopkins Drive, San Diego, CA 92121, USA. tononi@nsi.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8895474" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenergic Fibers/drug effects/physiology ; Animals ; Benzylamines/pharmacology ; Brain/*metabolism ; Cerebral Cortex/metabolism ; Cyclic AMP Response Element-Binding Protein/metabolism ; DNA-Binding Proteins/genetics ; Early Growth Response Protein 1 ; Electroencephalography ; *Gene Expression Regulation ; *Genes, Immediate-Early ; Genes, fos ; Hippocampus/metabolism ; *Immediate-Early Proteins ; Locus Coeruleus/*physiology ; Neurons/*metabolism ; Norepinephrine/metabolism ; Oxidopamine/pharmacology ; Phosphorylation ; Rats ; Sleep ; Sleep Deprivation ; Sympathectomy, Chemical ; Transcription Factors/genetics ; *Wakefulness
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Binding of GSK3beta to the APC-beta-catenin complex and regulation of complex assembly (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-17
    Description: The adenomatous polyposis coli gene (APC) is mutated in most colon cancers. The APC protein binds to the cellular adhesion molecule beta-catenin, which is a mammalian homolog of ARMADILLO, a component of the WINGLESS signaling pathway in Drosophila development. Here it is shown that when beta-catenin is present in excess, APC binds to another component of the WINGLESS pathway, glycogen synthase kinase 3beta (GSK3beta), a mammalian homolog of Drosophila ZESTE WHITE 3. APC was a good substrate for GSK3 beta in vitro, and the phosphorylation sites were mapped to the central region of APC. Binding of beta-catenin to this region was dependent on phosphorylation by GSK3 beta.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rubinfeld, B -- Albert, I -- Porfiri, E -- Fiol, C -- Munemitsu, S -- Polakis, P -- New York, N.Y. -- Science. 1996 May 17;272(5264):1023-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Onyx Pharmaceuticals, Richmond, CA 94806, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638126" target="_blank"〉PubMed〈/a〉
    Keywords: Adenomatous Polyposis Coli Protein ; Animals ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Line ; Cytoskeletal Proteins/*metabolism ; Glycogen Synthase Kinase 3 ; Glycogen Synthase Kinases ; Humans ; Mice ; Mutation ; Phosphorylation ; Protein Binding ; *Trans-Activators ; Tumor Cells, Cultured ; beta Catenin
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Activation of the budding yeast spindle assembly checkpoint without mitotic spindle disruption (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-08-16
    Description: The spindle assembly checkpoint keeps cells with defective spindles from initiating chromosome segregation. The protein kinase Mps1 phosphorylates the yeast protein Mad1p when this checkpoint is activated, and the overexpression of Mps1p induces modification of Mad1p and arrests wild-type yeast cells in mitosis with morphologically normal spindles. Spindle assembly checkpoint mutants overexpressing Mps1p pass through mitosis without delay and can produce viable progeny, which demonstrates that the arrest of wild-type cells results from inappropriate activation of the checkpoint in cells whose spindle is fully functional. Ectopic activation of cell-cycle checkpoints might be used to exploit the differences in checkpoint status between normal and tumor cells and thus improve the selectivity of chemotherapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hardwick, K G -- Weiss, E -- Luca, F C -- Winey, M -- Murray, A W -- New York, N.Y. -- Science. 1996 Aug 16;273(5277):953-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of California, San Francisco, CA 94143-0444, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8688079" target="_blank"〉PubMed〈/a〉
    Keywords: *Carrier Proteins ; Cell Cycle ; *Cell Cycle Proteins ; Fungal Proteins/*metabolism ; *Mitosis ; Nuclear Proteins/*metabolism ; Phosphoproteins/*metabolism ; Phosphorylation ; Protein Kinases ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Protein-Tyrosine Kinases/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Repressor Proteins ; Saccharomyces cerevisiae/cytology/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Spindle Apparatus/*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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  • 52
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    Role of beta-arrestin in mediating agonist-promoted G protein-coupled receptor internalization (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-01-19
    Description: beta-Arrestins are proteins that bind phosphorylated heterotrimeric GTP-binding protein (G protein)-coupled receptors (GPCRs) and contribute to the desensitization of GPCRs by uncoupling the signal transduction process. Resensitization of GPCR responsiveness involves agonist-mediated receptor sequestration. Overexpression of beta-arrestins in human embryonic kidney cells rescued the sequestration of beta 2-adrenergic receptor (beta 2AR) mutants defective in their ability to sequester, an effect enhanced by simultaneous overexpression of beta-adrenergic receptor kinase 1. Wild-type beta 2AR sequestration was inhibited by the overexpression of two beta-arrestin mutants. These findings suggest that beta-arrestins play an integral role in GPCR internalization and thus serve a dual role in the regulation of GPCR function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferguson, S S -- Downey, W E 3rd -- Colapietro, A M -- Barak, L S -- Menard, L -- Caron, M G -- NS 19576/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 19;271(5247):363-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute Laboratory, Duke University Medical Center, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8553074" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenergic beta-Agonists/*pharmacology ; Antigens/genetics/*physiology ; *Arrestins ; Cell Line ; Cyclic AMP-Dependent Protein Kinases/genetics/*metabolism ; DNA, Complementary ; Eye Proteins/genetics/*physiology ; GTP-Binding Proteins/*metabolism ; Humans ; Isoproterenol/pharmacology ; Mutation ; Phosphorylation ; Point Mutation ; Receptors, Adrenergic, beta-2/genetics/*metabolism ; Transfection ; beta-Adrenergic Receptor Kinases
    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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    Regulation of T cell receptor signaling by tyrosine phosphatase SYP association with CTLA-4 (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-05-24
    Description: The absence of CTLA-4 results in uncontrolled T cell proliferation. The T cell receptor-specific kinases FYN, LCK, and ZAP-70 as well as the RAS pathway were found to be activated in T cells of Ctla-4-/- mutant mice. In addition, CTLA-4 specifically associated with the tyrosine phosphatase SYP, an interaction mediated by the SRC homology 2 (SH2) domains of SYP and the phosphotyrosine sequence Tyr-Val-Lys-Met within the CTLA-4 cytoplasmic tail. The CTLA-4-associated SYP had phosphatase activity toward the RAS regulator p52SHC. Thus, the RAS pathway and T cell activation through the T cell receptor are regulated by CTLA-4-associated SYP.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marengere, L E -- Waterhouse, P -- Duncan, G S -- Mittrucker, H W -- Feng, G S -- Mak, T W -- New York, N.Y. -- Science. 1996 May 24;272(5265):1170-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉AMGEN Institute, Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638161" target="_blank"〉PubMed〈/a〉
    Keywords: Abatacept ; *Adaptor Proteins, Signal Transducing ; *Adaptor Proteins, Vesicular Transport ; Amino Acid Sequence ; Animals ; Antigens, CD ; Antigens, CD3/metabolism ; Antigens, Differentiation/chemistry/*metabolism ; CTLA-4 Antigen ; GRB2 Adaptor Protein ; *Immunoconjugates ; Intracellular Signaling Peptides and Proteins ; Lymphocyte Activation ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Protein Tyrosine Phosphatase, Non-Receptor Type 11 ; Protein Tyrosine Phosphatase, Non-Receptor Type 6 ; Protein Tyrosine Phosphatases/*metabolism ; Protein-Tyrosine Kinases/metabolism ; Proteins/metabolism ; Receptors, Antigen, B-Cell/metabolism ; Receptors, Antigen, T-Cell/*metabolism ; Recombinant Fusion Proteins/metabolism ; SH2 Domain-Containing Protein Tyrosine Phosphatases ; Shc Signaling Adaptor Proteins ; *Signal Transduction ; T-Lymphocytes/immunology/*metabolism ; ras Proteins/metabolism ; src Homology Domains
    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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  • 54
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    Regulation of the inositol 1,4,5-trisphosphate receptor by tyrosine phosphorylation (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-07
    Description: Tyrosine kinases indirectly raise intracellular calcium concentration ([Ca2+]i) by activating phospholipases that generate inositol 1,4,5-trisphosphate (IP3). IP3 activates the IP3 receptor (IP3R), an intracellular calcium release channel on the endoplasmic reticulum. T cell receptor stimulation triggered a physical association between the nonreceptor protein tyrosine kinase Fyn and the IP3R, which induced tyrosine phosphorylation of the IP3R. Fyn activated an IP3-gated calcium channel in vitro, and tyrosine phosphorylation of the IP3R during T cell activation was reduced in thymocytes from fyn-/- mice. Thus, activation of the IP3R by tyrosine phosphorylation may play a role in regulating [Ca2+]i.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jayaraman, T -- Ondrias, K -- Ondriasova, E -- Marks, A R -- N529814/PHS HHS/ -- New York, N.Y. -- Science. 1996 Jun 7;272(5267):1492-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Molecular Cardiology, Department of Medicine, Mount Sinai School of Medicine, New York 10029, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8633244" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/metabolism ; Calcium/metabolism ; Calcium Channels/*metabolism ; Humans ; Inositol 1,4,5-Trisphosphate/*metabolism/pharmacology ; Inositol 1,4,5-Trisphosphate Receptors ; Lipid Bilayers ; Lymphocyte Activation ; Mice ; Phosphorylation ; Phosphotyrosine/*metabolism ; Protein-Tyrosine Kinases/metabolism ; Proto-Oncogene Proteins/metabolism/pharmacology ; Proto-Oncogene Proteins c-fyn ; Receptors, Cytoplasmic and Nuclear/*metabolism ; T-Lymphocytes/immunology/metabolism ; 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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    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
    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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