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  • Phosphorylation
  • American Association for the Advancement of Science (AAAS)  (34)
  • Springer Nature
  • American Chemical Society (ACS)
  • 1980-1984  (34)
Sammlung
Verlag/Herausgeber
  • American Association for the Advancement of Science (AAAS)  (34)
  • Springer Nature
  • American Chemical Society (ACS)
  • Springer  (6)
Erscheinungszeitraum
Jahr
  • 1
    Publikationsdatum: 1984-03-02
    Beschreibung: Mononuclear blood cells were obtained from a patient with type A insulin resistance. The cells showed a normal ability to bind iodine 125-labeled insulin. Analysis of solubilized insulin receptors from the patient's cells revealed a defect in insulin-stimulated tyrosine kinase activity, which is closely associated with the receptor itself. The enzyme failed to phosphorylate the insulin receptor and showed a markedly reduced ability to phosphorylate exogenously added substrates. It appears that receptors from this insulin-resistant patient have a defect distal to the insulin-binding site (the alpha subunit of the receptor). The defect could be located in the beta subunit, which has an adenosine triphosphate-binding site, or in another receptor component that transfers a signal of insulin binding into kinase activity. This dissociation between the normal binding and the defective protein kinase component of the insulin receptor represents the first biochemical defect of the receptor distal to ligand binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grunberger, G -- Zick, Y -- Gorden, P -- New York, N.Y. -- Science. 1984 Mar 2;223(4639):932-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6141638" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Caseins/metabolism ; Female ; Glutamates/metabolism ; Glutamic Acid ; Humans ; Insulin/blood/*metabolism ; *Insulin Resistance ; Monocytes/metabolism ; Phosphorylation ; Protein Kinases/*metabolism ; Receptor, Insulin/*metabolism ; Syndrome ; Tyrosine/metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1984-01-27
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1984 Jan 27;223(4634):385.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6318320" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenylyl Cyclases/*metabolism ; Animals ; Bufonidae/blood ; Cyclic AMP/metabolism ; Enzyme Activation ; Erythrocyte Membrane ; Membrane Fusion ; Phosphorylation ; Receptors, Adrenergic, beta/isolation & purification/*physiology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1984-09-21
    Beschreibung: Various extracellular informational signals such as those from a group of hormones and some neurotransmitters appear to be passed from the cell surface into the cell interior by two routes, protein kinase C activation and Ca2+ mobilization. Both routes usually become available as the result of an interaction of a single ligand and a receptor and act synergistically to evoke subsequent cellular responses such as release reactions. The signal-dependent breakdown of inositol phospholipids, particularly phosphatidylinositol bisphosphate, now appears to be a key event for initiating these processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nishizuka, Y -- New York, N.Y. -- Science. 1984 Sep 21;225(4668):1365-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6147898" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Brain/*physiology ; Calcium/metabolism ; Enzyme Activation ; Nerve Tissue Proteins/metabolism ; Neurotransmitter Agents/physiology ; Phosphatidylinositols/*metabolism ; Phosphoproteins/metabolism ; Phosphorylation ; Protein Kinase C ; Protein Kinases/metabolism ; Receptors, Cell Surface/physiology ; *Synaptic Transmission ; Tetradecanoylphorbol Acetate/pharmacology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1984-09-21
    Beschreibung: The presence of a great variety of neuron-specific phosphoproteins in nervous tissue supports the view that protein phosphorylation plays many roles in neuronal function. The physiological significance of several of these phosphoproteins has already been established. Some neuronal phosphoproteins have been detected throughout the entire nervous system, whereas the distribution of others is limited to one or a few neuronal cell types. These various neuron-specific phosphoproteins are proving of value in the study of the physiology, anatomy, developmental biology, and pathophysiology of the nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nestler, E J -- Walaas, S I -- Greengard, P -- MH-39327/MH/NIMH NIH HHS/ -- NS-21550/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1984 Sep 21;225(4668):1357-64.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6474180" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Basal Ganglia/physiology ; Brain/physiology ; Nerve Tissue Proteins/*physiology ; *Nervous System Physiological Phenomena ; Neurons/*physiology ; Phosphoproteins/isolation & purification/*physiology ; Phosphorylation ; Protein Kinases/*metabolism ; Tissue Distribution
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 5
    Publikationsdatum: 1984-05-04
    Beschreibung: A mouse monoclonal antibody that reacts with beta 2-microglobulin, the light chain of class I major histocompatibility antigens, inhibited the second wave of human platelet aggregation induced by adenosine diphosphate and epinephrine and blocked aggregation and platelet protein phosphorylation induced by sodium arachidonate. Thrombin-induced platelet aggregation was inhibited at threshold concentrations but not at higher concentrations. The antibody also inhibited aggregation and secretion in response to thromboxane A2 or the stable endoperoxide analog, U46619. These results suggest that beta 2-microglobulin in the histocompatibility complex is intimately associated with transmission of the endoperoxide-thromboxane signal at the platelet membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Curry, R A -- Messner, R P -- Johnson, G J -- AM 26696/AM/NIADDK NIH HHS/ -- HL 2807/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1984 May 4;224(4648):509-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6324346" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): 15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid ; Adenosine Triphosphate/blood ; *Antibodies, Monoclonal ; Antibody Specificity ; Arachidonic Acid ; Arachidonic Acids/pharmacology ; Blood Platelets/metabolism ; Blood Proteins/metabolism ; Cyclic AMP/blood ; HLA Antigens/*analysis ; Humans ; Phosphorylation ; *Platelet Aggregation/drug effects ; Prostaglandin Endoperoxides, Synthetic/pharmacology ; Receptors, Prostaglandin/metabolism ; Receptors, Thromboxane ; Thromboxane A2/pharmacology ; beta 2-Microglobulin/*immunology/physiology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 6
    Publikationsdatum: 1984-03-30
    Beschreibung: The role of cyclic adenosine monophosphate-mediated phosphorylation of myosin light chain kinase in relaxing smooth muscle was examined. The kinase was immunoprecipitated from tissue extracts and the phosphate content was determined. The addition of forskolin to resting or methacholine-contracted muscles resulted in an increase in myosin light chain kinase phosphorylation of myosin light chain kinase is one of the reactions in the process by which cyclic adenosine monophosphate causes relaxation of smooth muscle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Lanerolle, P -- Nishikawa, M -- Yost, D A -- Adelstein, R S -- New York, N.Y. -- Science. 1984 Mar 30;223(4643):1415-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6322302" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Cattle ; Colforsin ; Cyclic AMP/*physiology ; Diterpenes/pharmacology ; Muscle Relaxation ; Muscle, Smooth/drug effects/*metabolism/physiology ; Myosin-Light-Chain Kinase ; Phosphorylation ; Protein Kinases/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1984-02-10
    Beschreibung: Regression of the fetal rat Mullerian duct in vitro was stimulated by sodium fluoride in the absence of Mullerian inhibiting substance. The action of Mullerian inhibiting substance was inhibited by sodium vanadate, adenosine 5'-triphosphate, and several related nucleotides in the presence of manganese ions. Epidermal growth factor specifically inhibited the substance, but only with manganese ions present. Insulin, platelet-derived growth factor, and nerve growth factor had no effect. These results suggest that dephosphorylation of membrane proteins mediates the action of Mullerian inhibiting substance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hutson, J M -- Fallat, M E -- Kamagata, S -- Donahoe, P K -- Budzik, G P -- CA-17393/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1984 Feb 10;223(4636):586-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6607531" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Anti-Mullerian Hormone ; Cations, Divalent ; Dimethyl Sulfoxide/pharmacology ; Epidermal Growth Factor/pharmacology ; Female ; *Glycoproteins ; *Growth Inhibitors ; Kinetics ; Male ; Membrane Proteins/metabolism ; Mullerian Ducts/drug effects/*physiology ; Phosphorylation ; Pregnancy ; Rats ; Sodium Fluoride/pharmacology ; Testicular Hormones/*physiology ; Vanadates ; Vanadium/pharmacology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1984-04-20
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1984 Apr 20;224(4646):272.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6324341" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): 1-Phosphatidylinositol 4-Kinase ; Avian Sarcoma Viruses/*genetics ; *Cell Transformation, Neoplastic ; Diglycerides/metabolism ; Genes, Viral ; Inositol 1,4,5-Trisphosphate ; Inositol Phosphates/metabolism ; *Oncogenes ; Phosphatidylinositol Phosphates ; Phosphatidylinositols/*metabolism ; Phosphorylation ; Phosphotransferases/*genetics/metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1984-01-13
    Beschreibung: A moderate light stimulus induced isoelectric point (pI) changes in three classes of retina-specific polypeptides (80, 49, and 39 kilodaltons) of Drosophila in vivo. When inorganic phosphate labeled with phosphorus-32 was fed to flies, the radioactive label was incorporated into these polypeptides during the pI changes, indicating light-induced phosphorylation of the polypeptides. A 1-millisecond flash induced a detectable amount of phosphorylation in the 80- and 49-kilodalton polypeptides within 3 seconds. These results, and our previous results with norpA mutants, suggest that phosphorylation of these two polypeptides may be involved in some early stages of photoreceptor excitation or its modulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matsumoto, H -- Pak, W L -- EY 00033/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1984 Jan 13;223(4632):184-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6419348" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Drosophila melanogaster/*metabolism ; Eye Proteins/*metabolism/radiation effects ; Isoelectric Point ; *Light ; Molecular Weight ; Phosphorylation ; Retina/metabolism
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1984-03-23
    Beschreibung: An antiserum to the insulin receptor mimicked insulin's acute actions on glucose transport, phosphorylation of integral membrane proteins, and internalization of the insulin receptor in isolated rat adipose cells. These insulinomimetic actions of the antiserum occurred without the equivalent increase in phosphorylation of the beta subunit of the insulin receptor observed with insulin. Thus, a role of receptor phosphorylation in acute insulin action is now questioned.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Simpson, I A -- Hedo, J A -- New York, N.Y. -- Science. 1984 Mar 23;223(4642):1301-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6367041" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): 3-O-Methylglucose ; Adipose Tissue/cytology ; Animals ; Biological Transport ; Cell Membrane/metabolism ; Immune Sera ; Insulin/metabolism/*pharmacology ; Membrane Proteins/metabolism ; Methylglucosides/metabolism ; Phosphorylation ; Rats ; Receptor, Insulin/immunology/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1984-10-12
    Beschreibung: Rhodopsin kinase, an enzyme involved in photochemical transduction in the retina, has been found in the mammalian pineal gland in amounts equal to those in the retina; other tissues had 7 percent of this amount, or less. This finding suggests that, in mammals, rhodopsin kinase functions in the pineal gland and other tissues to phosphorylate rhodopsin-like integral membrane receptors and is thereby involved in signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Somers, R L -- Klein, D C -- New York, N.Y. -- Science. 1984 Oct 12;226(4671):182-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6091271" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Brain/enzymology ; *Eye Proteins ; G-Protein-Coupled Receptor Kinase 1 ; Light ; Lung/enzymology ; Phosphorylation ; Pineal Gland/*enzymology ; Pituitary Gland/enzymology ; Protein Kinase Inhibitors ; Protein Kinases/*metabolism ; Rats ; Receptors, Adrenergic, beta/metabolism ; Retina/enzymology ; Tissue Distribution ; Zinc/pharmacology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 12
    Publikationsdatum: 1984-08-24
    Beschreibung: Long-term exposure of various cell types to beta-adrenergic agonists such as isoproterenol leads to an attenuated responsiveness ("desensitization") of the adenylate cyclase system to further challenge with these agonists. The turkey erythrocyte model system was used earlier to show that a covalent modification of the receptor (phosphorylation) is associated with this process. The functionality of the "desensitized" beta-adrenergic receptor was assessed by implanting purified beta-adrenergic receptor preparations from control and desensitized turkey erythrocytes into phospholipid mixtures and then fusing them with receptor-deficient cells (Xenopus laevis erythrocytes). Desensitized beta-adrenergic receptors showed a 40 to 50 percent reduction in their ability to couple to the heterologous adenylate cyclase system, comparable to the reduction in their functionality observed in their original membrane environment. These results demonstrate the utility of recently developed receptor reconstitution techniques for assessing the functionality of purified receptors and show a direct link between a covalent modification of a membrane-bound receptor and its impaired functionality in a reconstituted system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Strulovici, B -- Cerione, R A -- Kilpatrick, B F -- Caron, M G -- Lefkowitz, R J -- New York, N.Y. -- Science. 1984 Aug 24;225(4664):837-40.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6089331" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenylyl Cyclases/*metabolism ; Animals ; Epinephrine/pharmacology ; Erythrocyte Membrane/enzymology ; Erythrocytes ; Isoproterenol/*pharmacology ; Liposomes ; Membrane Fusion ; Norepinephrine/pharmacology ; Phosphorylation ; Receptors, Adrenergic, beta/drug effects/isolation & purification/*physiology ; Turkeys/blood ; Xenopus laevis/blood
    Print ISSN: 0036-8075
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 13
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1984-09-28
    Beschreibung: Embryonic chicken brain tissue cultured in media containing 35S-labeled sulfate or 32P-labeled phosphate incorporated 35S or 32P into the neural cell adhesion molecule (N-CAM). The 35S label was located in asparagine-linked carbohydrates on both glycopeptides (molecular weights, 170,000 and 140,000) but not in the sialic acid. The 32P label was detected in phosphoamino acids in the carboxyl-terminal third of both polypeptides, but the ratio of phosphoserine to phosphothreonine differed in the two species. The sulfated saccharides and phosphoamino acids may provide additional sites for functional control of N-CAM.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sorkin, B C -- Hoffman, S -- Edelman, G M -- Cunningham, B A -- AI 11378/AI/NIAID NIH HHS/ -- HD 16550/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1984 Sep 28;225(4669):1476-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6474186" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Antigens, Surface/analysis/*metabolism ; Brain/*metabolism ; Cell Adhesion Molecules ; Chick Embryo ; Glycopeptides/analysis ; In Vitro Techniques ; Phosphates/analysis/*metabolism ; Phosphorylation ; Phosphoserine/analysis ; Phosphothreonine/analysis ; Sialic Acids/analysis ; Sulfates/analysis/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 14
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1984-03-16
    Beschreibung: 5-Amino-4-imidazolecarboxamide riboside triphosphate (ZTP) is thought to play a regulatory role in cellular metabolism. Unlike other nucleoside triphosphates, ZTP is synthesized in a one-step reaction in which the pyrophosphate group of 5-phosphoribosyl-l-pyrophosphate is transferred to the riboside monophosphate (ZMP) in a reaction catalyzed by 5-phosphoribosyl-l-pyrophosphate synthetase; reversal of this reaction leads to dephosphorylation of ZTP to ZMP. This unusual route of synthesis (and catabolism) of ZTP may be important in defining its metabolic effects in the cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sabina, R L -- Holmes, E W -- Becker, M A -- AM12413/AM/NIADDK NIH HHS/ -- AM28554/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1984 Mar 16;223(4641):1193-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6199843" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenosine Triphosphate/metabolism ; Aminoimidazole Carboxamide/analogs & derivatives/*biosynthesis/pharmacology ; Animals ; Cell Line ; Cricetinae ; Imidazoles/*biosynthesis ; Kinetics ; Phosphoribosyl Pyrophosphate/metabolism ; Phosphorylation ; Ribonucleosides/pharmacology ; Ribonucleotides/*biosynthesis ; Ribose-Phosphate Pyrophosphokinase/metabolism ; Substrate Specificity
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 15
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1983-07-22
    Beschreibung: Protein phosphorylation is a principal regulatory mechanism in the control of almost all cellular processes. The nature of the protein phosphatases that participate in these reactions has been a subject of controversy. Four enzymes, termed protein phosphatases 1, 2A, 2B, and 2C, account for virtually all of the phosphatase activity toward phosphoproteins involved in controlling glycogen metabolism, glycolysis, gluconeogenesis, fatty acid synthesis, cholesterol synthesis, and protein synthesis. The properties, physiological roles, and mechanisms for regulating the four protein phosphatases are reviewed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ingebritsen, T S -- Cohen, P -- New York, N.Y. -- Science. 1983 Jul 22;221(4608):331-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6306765" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Calcium/physiology ; Cyclic AMP/metabolism ; Glycogen/metabolism ; Liver/enzymology ; Muscles/enzymology ; Phosphoprotein Phosphatases/classification/*physiology ; Phosphoproteins/metabolism ; Phosphorylase Phosphatase/metabolism ; Phosphorylation ; Protein Biosynthesis ; Protein Kinases/physiology ; Rabbits ; Rats
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 16
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1983-04-15
    Beschreibung: Glucose given to the newborn human may result in hyperglycemia, suggesting that its utilization is impaired at this developmental stage. Galactose is thought to be a more appropriate carbohydrate source for the newborn. The enzymes involved in hexose phosphorylation may, in part, be responsible for these observations. A key regulatory enzyme of hepatic glucose assimilation, glucokinase, is diminished in newborns compared to adults, whereas galactokinase activity is increased. When newborn dogs were fasted and then fed either glucose or galactose, their plasma insulin responses to glucose were similar, but the pups fed galactose demonstrated an attenuated systemic appearance rate of glucose. Hexose incorporation into hepatic glycogen and net glycogen synthesis was augmented in the galactose-fed dogs. In vitro, liver from neonatal dogs showed enhanced galactokinase activity relative to that for hexokinase or glucokinase. Neonatal hexose assimilation may be independent of insulin action and, instead, be related to the developmental presence of hexose phosphorylating enzymes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kliegman, R M -- Miettinen, E L -- Morton, S -- HD05740/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1983 Apr 15;220(4594):302-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6836273" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adult ; Animals ; Animals, Newborn/metabolism ; *Carbohydrate Metabolism ; Dogs ; Galactokinase/*physiology ; Galactose/metabolism ; Galactosemias ; Glucose/metabolism ; Humans ; Infant, Newborn ; Liver/enzymology ; Liver Glycogen/biosynthesis ; Phosphorylation ; Rats
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 17
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1983-01-07
    Beschreibung: Epidermal growth factor, a potent mitogen, stimulates phosphorylation of its 170,000-dalton plasma membrane receptor. Dimethyl sulfoxide selectively increased phosphorylation of the epidermal growth factor receptor in rat liver microsomal fraction. Maximal stimulation occurred at 15 to 25 percent dimethyl sulfoxide and resembled the effect of epidermal growth factor in magnitude and rapidity. Like epidermal growth factor, dimethyl sulfoxide selectively stimulated tyrosine residue phosphorylation of this protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rubin, R A -- Earp, H S -- 5T32 CA 90156/CA/NCI NIH HHS/ -- AM-30002/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1983 Jan 7;219(4580):60-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6294827" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Dimethyl Sulfoxide/*pharmacology ; In Vitro Techniques ; Microsomes, Liver/metabolism ; Phosphorylation ; Rats ; Receptor, Epidermal Growth Factor ; Receptors, Cell Surface/*metabolism ; Tyrosine/metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 18
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1983-07-29
    Beschreibung: Stress development depended on calcium-stimulated myosin phosphorylation in an arterial smooth muscle preparation in which the concentration of calcium was controlled. However, developed stress was maintained at a concentration of calcium that did not support phosphorylation. These results, in conjunction with other evidence, suggest that the interaction of two regulatory mechanisms with different calcium sensitivities regulate both stress and the rate and energetics of contraction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chatterjee, M -- Murphy, R A -- 5 PO1 HL 19242/HL/NHLBI NIH HHS/ -- 5T32 HL07355/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1983 Jul 29;221(4609):464-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6867722" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Anura ; Calcium/*physiology ; Muscle Contraction ; Muscle Relaxation ; Muscle, Smooth, Vascular/*metabolism/physiology ; Myosins/*metabolism/physiology ; Phosphorylation ; Swine
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 19
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1983-04-15
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolata, G -- New York, N.Y. -- Science. 1983 Apr 15;220(4594):291-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6220466" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Cell Differentiation/*drug effects ; Cell Division/drug effects ; Cell Transformation, Neoplastic/drug effects ; Humans ; Mice ; Phorbol Esters/*pharmacology ; Phorbols/*pharmacology ; Phosphorylation ; Protein Kinase C ; Protein Kinases/physiology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 20
    Publikationsdatum: 1983-07-29
    Beschreibung: Insulin directly inhibits protein phosphorylation in isolated rat liver nuclear envelopes. In the present studies, an antiserum to insulin receptor as well as the plant lectins concanavalin A and phytohemagglutinin mimicked insulin action in isolated nuclear envelopes. These studies suggest that insulin and agents that mimic it may directly regulate nuclear functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Purrello, F -- Burnham, D B -- Goldfine, I D -- AM 06659/AM/NIADDK NIH HHS/ -- AM 26667/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1983 Jul 29;221(4609):462-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6346487" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Concanavalin A/pharmacology ; Female ; Immune Sera ; Insulin/*pharmacology ; Lectins/*pharmacology ; Nuclear Envelope/*drug effects/metabolism ; Phosphorylation ; Phytohemagglutinins/pharmacology ; Rats ; Rats, Inbred Strains ; Receptor, Insulin/*immunology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 21
    Publikationsdatum: 1983-06-10
    Beschreibung: An attempt was made to determine whether phosphorylation of the myosin light chain represents a thick filament-associated mechanism for modulating the rate of cross-bridge cycling in mouse skeletal muscle. When the degree of light chain phosphorylation was varied independently of tetanus duration, there was no correlation of phosphorylation with cross-bridge turnover rate, as measured by the shortening velocity of the muscle. It is concluded that in intact skeletal muscle phosphorylation of the myosin light chain does not in itself modulate cross-bridge cycling rate and that previously reported changes in cycling rate were due to other factors that may vary with tetanus duration.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Butler, T M -- Siegman, M J -- Mooers, S U -- Barsotti, R J -- AM 00973/AM/NIADDK NIH HHS/ -- HL 15835/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1983 Jun 10;220(4602):1167-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6857239" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Kinetics ; Mice ; Muscle Contraction ; Muscles/*metabolism/physiology ; Myosins/*metabolism/physiology ; Phosphorylation ; Rats
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 22
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1982-05-14
    Beschreibung: The influx of K+ into swollen mitochondria in the presence of valinomycin results in the synthesis of adenosine triphosphate in which approximately one H+ disappears per adenosine triphosphate synthesized. The synthesis is blocked by atractyloside but is insensitive to oligomycin and relatively insensitive to uncouplers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kinnally, K W -- Tedeschi, H -- GM27043/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1982 May 14;216(4547):742-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6281882" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenosine Triphosphate/*biosynthesis ; Animals ; Antimycin A/pharmacology ; Atractyloside/pharmacology ; Cyanides/pharmacology ; Ion Channels/physiology ; Mitochondria/*metabolism ; Mitochondrial Swelling ; Phosphorylation ; Potassium/*metabolism ; Rotenone/pharmacology ; Uncoupling Agents/pharmacology ; Valinomycin/pharmacology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 23
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1982-12-24
    Beschreibung: Cyclic adenosine monophosphate (AMP) analogs or agents that increase intracellular cyclic AMP rapidly stimulate transcription of the prolactin gene in a line of cultured rat pituitary cells. This effect is correlated with the phosphorylation of a chromatin-associated basic protein designated BPR. These data are consistent with the postulate that increased intracellular cyclic AMP concentrations induce rapid transcriptional effects on specific genes in eukaryotes, mediated by direct or indirect phosphorylation of a specific chromatin-associated protein or proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murdoch, G H -- Rosenfeld, M G -- New York, N.Y. -- Science. 1982 Dec 24;218(4579):1315-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6293056" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Cells, Cultured ; Chromatin/*metabolism ; Cyclic AMP/analogs & derivatives/*metabolism ; Nucleoproteins/metabolism ; Phosphorylation ; Pituitary Gland/metabolism ; Prolactin/genetics ; Rats ; *Transcription, Genetic
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 24
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1982-01-08
    Beschreibung: Cultured human lymphocytes and rat hepatoma cells were labeled with [32P]orthophosphate and the insulin receptor subunits identified by immunoprecipitation and sodium dodecyl sulfate-gel electrophoreses. In both cell types the 95,000-dalton (beta) subunit of the insulin receptor was selectively phosphorylated. Phosphorylation was specifically stimulated by insulin in a dose-dependent fashion after 1 and 15 minutes of hormone treatment, whereas human growth hormone was without effect. This phosphorylation may be a very early event in insulin action.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kasuga, M -- Karlsson, F A -- Kahn, C R -- New York, N.Y. -- Science. 1982 Jan 8;215(4529):185-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7031900" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Cells, Cultured ; Growth Hormone/pharmacology ; Humans ; Insulin/*pharmacology ; Liver Neoplasms, Experimental/metabolism ; Lymphocytes ; Macromolecular Substances ; Molecular Weight ; Phosphorylation ; Rats ; Receptor, Insulin/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 25
    Publikationsdatum: 1982-01-22
    Beschreibung: Polyamines putrescine, spermidine, and spermine specifically inhibit the PK 380--catalyzed phosphorylation of eukaryotic initiation factor 2 alpha (eIF-2 alpha). Since te PK 380--dependent phosphorylation of eIF-2 alpha inhibits the initiation or protein synthesis, the possibility exists that the polyamines enhance protein synthesis by inhibiting the phosphorylation of eIF-2 alpha by PK 380.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuroda, Y -- Merrick, W C -- Sharma, R K -- CA-16091/CA/NCI NIH HHS/ -- GM-26796/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1982 Jan 22;215(4531):415-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7058326" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adrenal Cortex/enzymology/*physiology ; Animals ; Cattle ; Cell-Free System ; Peptide Chain Initiation, Translational/drug effects ; Peptide Initiation Factors/*metabolism ; Phosphoproteins/metabolism ; Phosphorylation ; Polyamines/*pharmacology ; *Protein Kinase Inhibitors
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 26
    Publikationsdatum: 1982-10-08
    Beschreibung: Protein phosphorylation in cerebral cell-free preparations from neonate rabbits was inhibited by bilirubin and promoted by aminophylline when these substances had been administered intravenously. In animals given both compounds, the bilirubin-induced inhibition of phosphorylation was partly reversed by aminophylline. Adenosine 3',5'-monophosphate added in vitro during the assays also increased protein phosphorylation. These data introduce new concepts in the pathogenesis of kernicterus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morphis, L -- Constantopoulos, A -- Matsaniotis, N -- Papaphilis, A -- New York, N.Y. -- Science. 1982 Oct 8;218(4568):156-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7123226" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Aminophylline/pharmacology ; Animals ; Animals, Newborn ; Bilirubin/metabolism/*pharmacology ; Brain/drug effects/*metabolism ; Kinetics ; Nerve Tissue Proteins/*metabolism ; Phosphorylation ; Protein Kinases/*metabolism ; Rabbits
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 27
    Publikationsdatum: 1982-08-27
    Beschreibung: Phosphorylation of the 18,000-dalton light chains of the fast-twitch myosin in mouse extensor digitorum longus muscles was correlated with reduction in the rate of the actomyosin adenosinetriphosphatase in vivo, but neither of these changes occurred in the soleus muscle. These results suggest that actomyosin interactions can be down-regulated by a reversible covalent modification of myosin light chains, that a mechanism for thick-filament regulation occurs in vertebrate skeletal muscle, and that the expression of this regulation may be limited to a specific fiber type.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Crow, M T -- Kushmerick, M J -- New York, N.Y. -- Science. 1982 Aug 27;217(4562):835-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6285472" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Actomyosin/metabolism ; Adenosine Triphosphatases/metabolism ; Animals ; Energy Metabolism ; Kinetics ; Mice ; Muscle Contraction ; Muscle, Smooth/metabolism ; Muscles/*metabolism ; Myosin-Light-Chain Phosphatase ; Myosins/*metabolism ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 28
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1981-07-31
    Beschreibung: Benzodiazepines inhibit Ca2+-calmodulin-stimulated membrane protein phosphorylation. The effects of the benzodiazepines on protein phosphorylation are stereospecific and produced by membrane-bound benzodiazepine. The potency of benzodiazepine kinase inhibition is correlated with the ability of the benzodiazepines to inhibit electric shock-induced convulsions. These findings provide evidence that some of the anticonvulsant and neuronal stabilizing effects of benzodiazepines may be modulated by the Ca2+-calmodulin protein kinase system and indicate that this calmodulin-kinase system represents an identifiable benzodiazepine receptor in brain that is distinquishable by several criteria from the previously described high affinity benzodiazepine receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DeLorenzo, R J -- Burdette, S -- Holderness, J -- NS 1352/NS/NINDS NIH HHS/ -- NSI-EA-1-K04-NS245/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1981 Jul 31;213(4507):546-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6264605" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Benzodiazepines/metabolism ; Brain/*enzymology ; Calcium/*pharmacology ; Calcium-Binding Proteins/*pharmacology ; Calmodulin/*pharmacology ; Cell Membrane/enzymology ; Chlordiazepoxide/*pharmacology ; Diazepam/*pharmacology ; Enzyme Activation ; Kinetics ; Molecular Weight ; Phosphorylation ; Protein Kinases/*metabolism ; Rats ; Receptors, Drug/metabolism ; Receptors, GABA-A
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 29
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1981-03-20
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1981 Mar 20;211(4488):1336-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6259729" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Abelson murine leukemia virus/enzymology ; Alpharetrovirus/enzymology ; Animals ; Avian Sarcoma Viruses/enzymology ; Cell Adhesion ; *Cell Transformation, Viral ; Glycolysis ; Humans ; Oncogene Protein pp60(v-src) ; Oncogenic Viruses/*enzymology ; Phosphoproteins/physiology ; Phosphorylation ; Protein Kinases/*physiology ; Tumor Virus Infections/*enzymology ; Tyrosine/metabolism ; Viral Proteins/*physiology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 30
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1981-01-30
    Beschreibung: Phosphorylation of the 20,000-dalton light chain of myosin is closely correlated with cross-bridge cycling in arterial smooth muscle. Evidence is presented that dephosphorylation can produce an attached, noncycling cross-bridge (latch-bridge) which is responsible for the high economy of force maintenance in this tissue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dillon, P F -- Aksoy, M O -- Driska, S P -- Murphy, R A -- New York, N.Y. -- Science. 1981 Jan 30;211(4481):495-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6893872" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Actins/*metabolism ; Animals ; Calcium/physiology ; Carotid Arteries/*physiology ; Macromolecular Substances ; *Muscle Contraction ; Muscle, Smooth/*physiology ; Myosins/*metabolism ; Phosphorylation ; Protein Kinases/metabolism ; Swine
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 31
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1981-10-23
    Beschreibung: The active portion of the alpha subunit of pyruvate dehydrogenase in rat frontal cortex was elevated after a training experience. No change in total pyruvate dehydrogenase activity was observed. The phosphorylation in vitro of pyruvate dehydrogenase (band F-2) was also elevated after training. Since activation of pyruvate dehydrogenase requires its dephosphorylation, the following sequence is proposed. Training alters frontal cortex and reduces the phosphate content of pyruvate dehydrogenase in vivo; this leads to enzyme activation; and an increase in back-titration of sites available for phosphorylation in vitro.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morgan, D G -- Routtenberg, A -- MH25281/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1981 Oct 23;214(4519):470-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7291989" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Avoidance Learning/*physiology ; Brain/*enzymology ; Male ; Neuronal Plasticity ; Phosphoproteins/metabolism ; Phosphorylation ; Pyruvate Dehydrogenase Complex/*metabolism ; Rats
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 32
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1981-09-18
    Beschreibung: The relationship between the actin-activated adenosinetriphosphatase activity of smooth muscle myosin and the extent of myosin light chain phosphorylation is nonlinear. It is suggested that the phosphorylation of the two heads of smooth muscle myosin is an ordered process and that the two heads are influenced by cooperative interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Persechini, A -- Hartshorne, D J -- HL 23615/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1981 Sep 18;213(4514):1383-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6455737" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Actins/pharmacology ; Adenosine Triphosphatases/metabolism ; Allosteric Regulation ; Animals ; Chickens ; Enzyme Activation/drug effects ; Gizzard ; Macromolecular Substances ; Muscle, Smooth/*metabolism ; Myosin-Light-Chain Kinase ; Myosins/*metabolism ; Phosphorylation ; Protein Kinases/metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 33
    Publikationsdatum: 1980-12-05
    Beschreibung: An endogenous polysomal cyclic AMP-dependent protein kinase specifically phosphorylates a 150,000-dalton peptide bound to an adrenocortical polyadenylated messenger ribonucleoprotein complex. There is a possibility that this protein is a physiological substrate of cyclic AMP-dependent protein kinase and that the phosphorylation and dephosphorylation of this substrate may be important in the translation control of adrenal polyadenylated messenger RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moore, R E -- Sharma, R K -- New York, N.Y. -- Science. 1980 Dec 5;210(4474):1137-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6255561" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adrenal Cortex/*metabolism ; Animals ; Cattle ; Cyclic AMP/metabolism ; Molecular Weight ; Nucleoproteins/*metabolism ; Phosphorylation ; Polyribosomes/metabolism ; Protein Kinases/*metabolism ; RNA, Messenger/*metabolism ; Ribonucleoproteins/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 34
    Publikationsdatum: 1980-01-04
    Beschreibung: Cromolyn inhibited histamine release from mast cells that was induced by a classic secretagogue and correspondingly increased incorporation of radioactive phosphate into a 78,000-dalton protein. These effects on histamine secretion and on protein phosphorylation were rapid in onset and both showed tachyphylaxis. Cromolyn may therefore act by altering the phosphorylation of a protein involved in the regulation of secretion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Theoharides, T C -- Sieghart, W -- Greengard, P -- Douglas, W W -- New York, N.Y. -- Science. 1980 Jan 4;207(4426):80-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6153130" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Calcium/physiology ; Cromolyn Sodium/*pharmacology ; Histamine Release/*drug effects ; Kinetics ; Mast Cells/*drug effects/immunology/metabolism ; Molecular Weight ; Phosphoproteins/*metabolism ; Phosphorylation ; Rats ; p-Methoxy-N-methylphenethylamine/antagonists & inhibitors
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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