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  • Binding Sites
  • Phosphorylation
  • American Association for the Advancement of Science (AAAS)  (68)
  • American Institute of Physics (AIP)
  • 1980-1984  (68)
Collection
Publisher
  • American Association for the Advancement of Science (AAAS)  (68)
  • American Institute of Physics (AIP)
  • Springer  (6)
Years
Year
  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-05-25
    Description: The structure of this pleiotropic activator of gene transcription in bacteria and its interaction sites at promoter DNA's as well as the role of this protein in the RNA polymerase-promoter interactions are reviewed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Crombrugghe, B -- Busby, S -- Buc, H -- New York, N.Y. -- Science. 1984 May 25;224(4651):831-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6372090" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Crystallography ; DNA, Bacterial/metabolism ; DNA-Directed RNA Polymerases/metabolism ; Galactose/genetics ; *Gene Expression Regulation ; Lac Operon ; Operon ; Protein Conformation ; Receptors, Cyclic AMP/*physiology ; *Transcription, Genetic
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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-01-20
    Description: Peptide synthesis can be used for elucidating the roles of secondary structures in the specificity of hormones, antigens, and toxins. Intermediate sized peptides with these activities assume amphiphilic secondary structures in the presence of membranes. When models are designed to optimize the amphiphilicity of the secondary structure, stronger interactions can be observed with the synthetic peptides than with the naturally occurring analogs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, E T -- Kezdy, F J -- HL-18577/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1984 Jan 20;223(4633):249-55.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6322295" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Apolipoprotein A-I ; Apolipoproteins ; Binding Sites ; Calcitonin ; Chemical Phenomena ; Chemistry ; Corticotropin-Releasing Hormone ; Endorphins ; Glucagon ; Growth Hormone-Releasing Hormone ; *Hormones/pharmacology ; Lipoproteins, HDL ; Melitten ; Models, Structural ; *Peptides/chemical synthesis/metabolism/pharmacology ; Protein Conformation ; Structure-Activity Relationship ; beta-Endorphin
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  • 3
    Publication Date: 1984-03-02
    Description: 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〉
    Keywords: 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
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-01-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Light, K E -- New York, N.Y. -- Science. 1984 Jan 6;223(4631):76-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6546323" target="_blank"〉PubMed〈/a〉
    Keywords: Amphetamines/*metabolism ; Animals ; Binding Sites ; Brain Chemistry ; *Carrier Proteins ; Mathematics ; *Radioligand Assay ; Rats ; Receptors, Adrenergic/*metabolism ; Software
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-08-31
    Description: High-resolution carbon-13 nuclear magnetic resonance (NMR) spectra of enzyme-inhibitor and enzyme-substrate complexes provide detailed structural and stereochemical information on the mechanism of enzyme action. The proteases trypsin and papain are shown to form tetrahedrally coordinated complexes and acyl derivatives with a variety of compounds artificially enriched at the site or sites of interest. These results are compared with the structural information derived from x-ray diffraction. Detailed NMR studies have provided a clearer picture of the ionization state of the residues participating in enzyme-catalyzed processes than other more classical techniques. The dynamics of enzymic catalysis can be observed at sub-zero temperatures by a combination of cryoenzymology and carbon-13 NMR spectroscopy. With these powerful techniques, transient, covalently bound intermediates in enzyme-catalyzed reactions can be detected and their structures rigorously assigned.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mackenzie, N E -- Malthouse, J P -- Scott, A I -- New York, N.Y. -- Science. 1984 Aug 31;225(4665):883-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6433481" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Carbon Isotopes ; Carboxypeptidases/metabolism ; Carboxypeptidases A ; Catalysis ; Chemical Phenomena ; Chemistry ; Coenzymes/*metabolism ; Endopeptidases/metabolism ; Enzymes/*metabolism ; Freezing ; Fructose-Bisphosphate Aldolase/metabolism ; Magnetic Resonance Spectroscopy ; Papain/metabolism ; Pepsin A/metabolism ; Peptide Hydrolases/*metabolism ; Protease Inhibitors ; Pterins/metabolism ; Pyridoxal Phosphate/metabolism ; Serine Endopeptidases
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  • 6
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-01-27
    Description: 〈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〉
    Keywords: 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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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-09-21
    Description: 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〉
    Keywords: 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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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-09-21
    Description: 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〉
    Keywords: 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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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-09-21
    Description: The nicotine receptor for the neurotransmitter acetylcholine is an allosteric protein composed of four different subunits assembled in a transmembrane pentamer alpha 2 beta gamma delta. The protein carries two acetylcholine sites at the level of the alpha subunits and contains the ion channel. The complete sequence of the four subunits is known. The membrane-bound protein undergoes conformational transitions that regulate the opening of the ion channel and are affected by various categories of pharmacologically active ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Changeux, J P -- Devillers-Thiery, A -- Chemouilli, P -- New York, N.Y. -- Science. 1984 Sep 21;225(4668):1335-45.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6382611" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Amino Acid Sequence ; Animals ; Binding Sites ; Cell Membrane/ultrastructure ; Cloning, Molecular ; DNA/analysis ; Electric Organ/metabolism ; Electrophorus ; Macromolecular Substances ; Protein Conformation ; *Receptors, Nicotinic/genetics/metabolism ; Torpedo
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  • 10
    Publication Date: 1984-05-04
    Description: 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〉
    Keywords: 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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  • 11
    Publication Date: 1984-03-30
    Description: 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〉
    Keywords: 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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  • 12
    Publication Date: 1984-02-10
    Description: 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〉
    Keywords: 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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  • 13
    Publication Date: 1984-11-16
    Description: Sequence-dependent variations in DNA revealed by x-ray crystallographic studies have suggested that certain DNA-reactive drugs may react preferentially with defined sequences in DNA. Drugs that wind around the helix and reside within one of the grooves of DNA have perhaps the greatest chance of recognizing sequence-dependent features of DNA. The antitumor antibiotic CC-1065 covalently binds through N-3 of adenine and resides within the minor groove of DNA. This drug overlaps with five base pairs for which a high sequence specificity exists.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hurley, L H -- Reynolds, V L -- Swenson, D H -- Petzold, G L -- Scahill, T A -- New York, N.Y. -- Science. 1984 Nov 16;226(4676):843-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6494915" target="_blank"〉PubMed〈/a〉
    Keywords: Antibiotics, Antineoplastic/*metabolism ; *Base Sequence ; Binding Sites ; Chemical Phenomena ; Chemistry ; DNA/*metabolism ; *Indoles ; Leucomycins/*metabolism ; Molecular Conformation ; X-Ray Diffraction
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  • 14
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-09-07
    Description: Several naturally occurring and synthetic flavones were found to inhibit the aromatization of androstenedione and testosterone to estrogens catalyzed by human placental and ovarian microsomes. These flavones include (in order of decreasing potency) 7,8-benzoflavone, chrysin, apigenin, flavone, flavanone, and quercetin; 5,6-benzoflavone was not inhibitory. 7,8-Benzoflavone and chrysin were potent competitive inhibitors and induced spectral changes in the aromatase cytochrome P-450 indicative of substrate displacement. Flavones may thus compete with steroids in their interaction with certain monooxygenases and thereby alter steroid hormone metabolism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kellis, J T Jr -- Vickery, L E -- AM1005/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1984 Sep 7;225(4666):1032-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6474163" target="_blank"〉PubMed〈/a〉
    Keywords: Androstenedione/*metabolism ; *Aromatase Inhibitors ; Benzoflavones/metabolism/pharmacology ; Binding Sites ; Binding, Competitive ; Female ; Flavonoids/metabolism/*pharmacology ; Humans ; Kinetics ; Microsomes/enzymology ; Ovary/*enzymology ; Oxidoreductases/*antagonists & inhibitors ; Placenta/*enzymology ; Pregnancy ; Testosterone/*metabolism ; beta-Naphthoflavone
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  • 15
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-09-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1984 Sep 28;225(4669):1460-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6433484" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine ; Animals ; Binding Sites ; Brain/drug effects/*enzymology/metabolism ; Haplorhini ; Humans ; Mice ; Monoamine Oxidase/*metabolism ; Oxidation-Reduction ; Parkinson Disease, Secondary/*chemically induced ; Pyridines/*metabolism/pharmacology/toxicity ; Rats
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  • 16
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-04-20
    Description: A replication-defective, acute transforming retrovirus (murine sarcoma virus 3611) was isolated from mouse and molecularly cloned. The nucleotide sequence of 1.5 kilobases encompassing the transforming gene (v-raf) was determined. This sequence, which predicts the amino acid sequence of a gag-raf fusion protein, terminates 180 nucleotides from the 3' end of the acquired cellular sequence. Comparison of the predicted amino acid sequence of v-raf with the predicted amino acid sequences of other oncogenes reveals significant homologies to the src family of oncogenes. There is a lack of homology within the sequence of the tyrosine acceptor domain described for the phosphotyrosine kinase members of the src family of transforming proteins. Phylogenetic arrangement of this family of oncogenes suggests that tyrosine-specific phosphorylation may be a recently acquired activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mark, G E -- Rapp, U R -- New York, N.Y. -- Science. 1984 Apr 20;224(4646):285-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6324342" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Biological Evolution ; Cell Transformation, Neoplastic ; Cell Transformation, Viral ; DNA Restriction Enzymes ; Gene Products, gag ; *Genes, Viral ; Mice ; *Oncogenes ; Protein Biosynthesis ; Protein Kinases/metabolism ; Protein-Tyrosine Kinases ; Sarcoma Viruses, Murine/*genetics ; Transcription, Genetic ; Tyrosine/metabolism ; Viral Proteins/analysis/*genetics
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  • 17
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-04-20
    Description: 〈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〉
    Keywords: 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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  • 18
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-01-13
    Description: 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〉
    Keywords: Animals ; Drosophila melanogaster/*metabolism ; Eye Proteins/*metabolism/radiation effects ; Isoelectric Point ; *Light ; Molecular Weight ; Phosphorylation ; Retina/metabolism
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  • 19
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-01-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maugh, T H 2nd -- New York, N.Y. -- Science. 1984 Jan 20;223(4633):269-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6608147" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Biochemistry/*methods ; Catalysis ; *Cloning, Molecular ; Enzymes/genetics/*metabolism ; Mutation ; Structure-Activity Relationship ; Substrate Specificity ; Tetrahydrofolate Dehydrogenase/metabolism ; Tyrosine-tRNA Ligase/metabolism ; beta-Lactamases/metabolism
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  • 20
    Publication Date: 1984-09-28
    Description: Tetanus-toxoid specific helper-inducer T-cell clones, which had been infected and transformed by human T-cell leukemia-lymphoma virus (HTLV-I), were obtained from an antigen-specific human T cell line by using a limiting dilution technique in the presence of the virus. These HTLV-I-infected T-cell clones proliferated specifically in response to soluble tetanus toxoid but, unlike normal T cells, they could do so in the absence of accessory cells. The HTLV-I-infected T-cell clones did not present the antigen to autologous antigen-specific T cells that were not infected with HTLV-I. The capacity of helper-inducer T cells to retain antigen-specific reactivity after infection by HTLV-I, while losing the normal T-cell requirement for accessory cells, has clinical and theoretical implications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mitsuya, H -- Guo, H G -- Cossman, J -- Megson, M -- Reitz, M S Jr -- Broder, S -- New York, N.Y. -- Science. 1984 Sep 28;225(4669):1484-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6206569" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, Surface/analysis ; Binding Sites ; Cell Line ; Cell Transformation, Viral ; Deltaretrovirus/genetics/*physiology ; Epitopes/metabolism ; Genes, Viral ; Humans ; *Lymphocyte Activation ; Phenotype ; T-Lymphocytes/*immunology/microbiology ; Tetanus Toxoid/immunology ; Viral Proteins/biosynthesis
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  • 21
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-04-27
    Description: Proteolytic enzymes have many physiological functions, ranging from generalized protein digestion to more specific regulated processes such as the activation of zymogens, blood coagulation and the lysis of fibrin clots, the release of hormones and pharmacologically active peptides from precursor proteins, and the transport of secretory proteins across membranes. They are present in all forms of living organisms. Comparisons of amino acid sequences, three-dimensional structures, and enzymatic reaction mechanisms of proteases indicate that there are distinct families of these proteins. Changes in molecular structure and function have accompanied the evolution of proteolytic enzymes and their inhibitors, each having relatively simple roles in primitive organisms and more diverse and more complex functions in higher organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neurath, H -- GM-15731/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Apr 27;224(4647):350-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6369538" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; *Biological Evolution ; Blood Coagulation ; Chemistry, Physical ; Enzyme Activation ; Enzyme Precursors/metabolism ; Genes ; Humans ; Mutation ; *Peptide Hydrolases/analysis/genetics/metabolism ; Peptides/metabolism ; Physicochemical Phenomena ; Protease Inhibitors/analysis/metabolism ; Protein Conformation ; Protein Sorting Signals ; Substrate Specificity
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  • 22
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-03-23
    Description: 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〉
    Keywords: 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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  • 23
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-09-14
    Description: The preferred binding sites of echinomycin on DNA can be determined by a method called "footprinting." A 32P end-labeled restriction fragment from pBR322 DNA is protected by binding to echinomycin, and cleaved by a synthetic DNA cleaving reagent, methidiumpropyl--EDTA . Fe(II); the DNA cleavage products are then subjected to high-resolution gel analyses. This method reveals that echinomycin has a binding site size of four base pairs. The strong binding sites for echinomycin contain the central two-base-pair sequence 5'-CG-3'. From an analysis of 15 echinomycin sites on 210 base pairs of DNA, key recognition elements for echinomycin are contained in the sequences (5'-3') ACGT and TCGT (A, adenine; C, cytosine; G, guanine; T, thymine).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Van Dyke, M M -- Dervan, P B -- GM-07616/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Sep 14;225(4667):1122-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6089341" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; DNA/metabolism ; DNA Restriction Enzymes ; *Echinomycin/metabolism ; Electrophoresis ; Escherichia coli/genetics ; Plasmids ; *Quinoxalines/metabolism
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  • 24
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-10-12
    Description: 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〉
    Keywords: 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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  • 25
    Publication Date: 1984-08-24
    Description: 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〉
    Keywords: 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
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  • 26
    Publication Date: 1984-09-28
    Description: 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〉
    Keywords: 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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  • 27
    Publication Date: 1984-03-16
    Description: 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〉
    Keywords: 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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  • 28
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-01-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Siiteri, P K -- New York, N.Y. -- Science. 1984 Jan 13;223(4632):191-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6318319" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Female ; Hormones/*metabolism ; *Radioligand Assay ; Rats ; Rats, Inbred Strains ; Receptors, Cell Surface/*metabolism
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  • 29
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-07-22
    Description: 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〉
    Keywords: 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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  • 30
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-04-15
    Description: 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〉
    Keywords: 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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  • 31
    Publication Date: 1983-01-07
    Description: 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〉
    Keywords: 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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  • 32
    Publication Date: 1983-03-18
    Description: Several lines of evidence suggest that there might be immunologic cross-reactivity between the thyroid plasma membrane in humans and antigenic determinants in the enteric pathogen Yersinia enterocolitica. Studies were therefore performed to determine whether Y. enterocolitica, like the thyroid membrane, contains a thyrotropin binding site. A saturable binding site for bovine thyrotropin was indeed demonstrable, particularly in preparations of the organism that have been treated with ethylenediaminetetraacetate and lysozyme. Hormonal specificity of the binding site, as judged from the inhibition of binding of 125I-labeled bovine thyrotropin, was similar to that of the thyrotropin receptor in human thyroid tissue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weiss, M -- Ingbar, S H -- Winblad, S -- Kasper, D L -- AM 18416/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1983 Mar 18;219(4590):1331-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6298936" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Binding, Competitive ; Kinetics ; Receptors, Cell Surface/*metabolism ; Receptors, Thyrotropin ; Thyrotropin/*metabolism ; Yersinia enterocolitica/*metabolism
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  • 33
    Publication Date: 1983-05-13
    Description: Human alpha-thrombin is a potent chemoattractant for human monocytes, with optimum activity occurring at about 10 nanomoles per liter. A variety of thrombins that were chemically modified to alter procoagulant or esterolytic functions showed a similar optimum activity, but complexes of prothrombin or alpha-thrombin with either antithrombin III or hirudin did not. These findings indicate that the regions in thrombin responsible for monocyte chemotaxis are proximate to those involved in certain protein recognition interactions of alpha-thrombin (for example, hirudin binding) but are distinct from the catalytic site and from certain exosites required for clotting.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bar-Shavit, R -- Kahn, A -- Wilner, G D -- Fenton, J W 2nd -- DE-04629/DE/NIDCR NIH HHS/ -- HL-13160/HL/NHLBI NIH HHS/ -- HL-14147/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1983 May 13;220(4598):728-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6836310" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Chemotaxis, Leukocyte/*drug effects ; Hirudins/pharmacology ; Humans ; Monocytes/*drug effects ; Prothrombin/pharmacology ; Thrombin/*pharmacology
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  • 34
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-07-29
    Description: 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〉
    Keywords: Animals ; Anura ; Calcium/*physiology ; Muscle Contraction ; Muscle Relaxation ; Muscle, Smooth, Vascular/*metabolism/physiology ; Myosins/*metabolism/physiology ; Phosphorylation ; Swine
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  • 35
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-04-15
    Description: 〈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〉
    Keywords: 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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  • 36
    Publication Date: 1983-12-23
    Description: Steroid hormones, when complexed to their receptors, recognize and bind specific DNA sequences and subsequently induce increased levels of transcription. The mechanisms of steroid hormone action were analyzed by constructing chimeric DNA molecules from portions of mouse mammary tumor virus envelope and long terminal repeat (LTR) regions ligated to the thymidine kinase (tk) gene of herpes simplex virus. This construction allowed the tk gene to be expressed in a hormone-responsive fashion upon transfection into Ltk- cells. Comparison of transcription data with in vitro binding data showed that hormone-responsive transcription can be directly correlated to the presence of steroid hormone receptor binding sites on the DNA. There are at least two such receptor binding sites in the LTR region, one between -202 and -137 and another between -137 and -50 base pairs from the RNA cap site, as well as a site near the 5' end of the envelope region. These results strengthen the hypothesis that steroid-receptor complexes regulate genes primarily by binding to DNA sites near the promoter region and thereby modulate transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pfahl, M -- McGinnis, D -- Hendricks, M -- Groner, B -- Hynes, N E -- New York, N.Y. -- Science. 1983 Dec 23;222(4630):1341-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6318311" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Cell Line ; Chimera ; DNA, Viral/*metabolism ; Glucocorticoids/metabolism/*pharmacology ; Mammary Tumor Virus, Mouse/*analysis ; Mice ; Receptors, Glucocorticoid/*metabolism ; Receptors, Steroid/*metabolism ; Repetitive Sequences, Nucleic Acid ; Transcription, Genetic/*drug effects ; Transfection ; Triamcinolone Acetonide/metabolism
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  • 37
    Publication Date: 1983-07-29
    Description: 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〉
    Keywords: 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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  • 38
    Publication Date: 1983-06-10
    Description: 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〉
    Keywords: Animals ; Kinetics ; Mice ; Muscle Contraction ; Muscles/*metabolism/physiology ; Myosins/*metabolism/physiology ; Phosphorylation ; Rats
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  • 39
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-05-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Munson, P J -- Rodbard, D -- New York, N.Y. -- Science. 1983 May 27;220(4600):979-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6302842" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Ligands ; Mathematics ; Models, Biological ; Receptors, Cell Surface/*metabolism
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  • 40
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1982-05-14
    Description: 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〉
    Keywords: 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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  • 41
    Publication Date: 1982-12-24
    Description: 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〉
    Keywords: 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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  • 42
    Publication Date: 1982-10-15
    Description: The biotin-binding site on avidin has been labeled with biotin conjugated to undecagold, an organometallic cluster compound containing 11 gold atoms in a core angestroms in diameter. Examination of unstained specimens by scanning transmission electron microscopy reveals the labeled sites directly, without computational averaging or filtering of the images. This approach should be widely applicable for determining the locations of subunits and functional site in biological macromolecules at a resolution at a resolution in range of 15 angstroms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Safer, D -- Hainfeld, J -- Wall, J S -- Reardon, J E -- AM 28607/AM/NIADDK NIH HHS/ -- GM 12202/GM/NIGMS NIH HHS/ -- GM 28750/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1982 Oct 15;218(4569):290-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7123234" target="_blank"〉PubMed〈/a〉
    Keywords: Avidin/*metabolism ; Binding Sites ; Biotin/*metabolism ; Gold/*metabolism ; Organogold Compounds ; Organometallic Compounds/*metabolism ; Ovalbumin/*analogs & derivatives
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  • 43
    Publication Date: 1982-01-08
    Description: 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〉
    Keywords: 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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  • 44
    Publication Date: 1982-01-22
    Description: 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〉
    Keywords: 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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  • 45
    Publication Date: 1982-10-08
    Description: 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〉
    Keywords: 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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  • 46
    Publication Date: 1982-08-27
    Description: 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〉
    Keywords: 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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  • 47
    Publication Date: 1982-10-29
    Description: The three-dimensional structure of a penicillin-sensitive D-alanyl-carboxypeptidase-transpeptidase has been determined by x-ray crystallography to a resolution of 2.8 angstroms. The site of binding of the beta-lactam antibiotics penicillin and cephalosporin has been located. These findings constitute direct observation of the interaction of beta-lactams with a transpeptidase enzyme and establish the feasibility of defining the molecular stereochemistry of this interaction for purposes of drug design.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kelly, J A -- Moews, P C -- Knox, J R -- Frere, J M -- Ghuysen, J M -- AI-13364-05/AI/NIAID NIH HHS/ -- AI-16702/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1982 Oct 29;218(4571):479-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7123246" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; *Carboxypeptidases ; *Cephalosporins ; Crystallography ; Models, Molecular ; *Muramoylpentapeptide Carboxypeptidase ; *Penicillins ; Protein Conformation ; X-Ray Diffraction
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  • 48
    Publication Date: 1981-07-31
    Description: 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〉
    Keywords: 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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  • 49
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1981-08-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Evans, C H -- Tew, W P -- New York, N.Y. -- Science. 1981 Aug 7;213(4508):653-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7256262" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cations ; *Erbium ; Kinetics ; *Magnetics
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  • 50
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1981-03-20
    Description: 〈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〉
    Keywords: 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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  • 51
    Publication Date: 1981-10-23
    Description: The complete nucleotide sequence of a mammalian transforming retrovirus. Moloney murine sarcoma virus, has been determined. MSV, recombinant virus derived of helper viral and cellular sequences, possesses termini resembling prokaryotic transposable elements. The viral genome has the coding capacity for the Moloney murine leukemia virus gag gene product and contains large deletions in pol and env genes. A large open reading frame encompassing its cell-derived sequences codes for its putative transforming protein. The nature of some of the important domains in the viral genome has been established, and their structure is discussed in relation to their function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reddy, E P -- Smith, M J -- Aaronson, S A -- New York, N.Y. -- Science. 1981 Oct 23;214(4519):445-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6170110" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, Viral/genetics ; Base Sequence ; Binding Sites ; Cell Transformation, Viral ; DNA, Viral/*genetics ; Defective Viruses/genetics ; Gene Products, gag ; *Genes, Viral ; Moloney murine leukemia virus/*genetics ; RNA, Transfer/genetics ; RNA-Directed DNA Polymerase/genetics ; Repetitive Sequences, Nucleic Acid ; Sarcoma Viruses, Murine/*genetics ; Transcription, Genetic ; Viral Proteins/genetics
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  • 52
    Publication Date: 1981-07-31
    Description: Membrane binding of ethanol, anesthetics, and hydrophobic molecules in brain synaptosomes and liver mitochondria from rats is conspicuously reduced after long-term consumption of ethanol. The membranes are resistant to structural disordering by both ethanol and halothane. Tolerance, cross-tolerance, and dependence in chronic alcoholics may in part result from membrane alterations that inhibit the binding of ethanol and other drugs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rottenberg, H -- Waring, A -- Rubin, E -- AA3442/AA/NIAAA NIH HHS/ -- GM 28173/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1981 Jul 31;213(4507):583-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6264608" target="_blank"〉PubMed〈/a〉
    Keywords: Alcoholism/*metabolism ; Binding Sites ; Brain/*metabolism ; Cell Membrane/drug effects/metabolism/ultrastructure ; Drug Tolerance ; Electron Spin Resonance Spectroscopy ; Ethanol/*pharmacology ; Halothane/pharmacology ; Humans ; Intracellular Membranes/drug effects/metabolism/ultrastructure ; Mitochondria, Liver/*metabolism ; Spin Labels ; Synaptosomes/*metabolism/ultrastructure
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  • 53
    Publication Date: 1981-01-30
    Description: 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〉
    Keywords: 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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  • 54
    Publication Date: 1981-10-23
    Description: 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〉
    Keywords: Animals ; Avoidance Learning/*physiology ; Brain/*enzymology ; Male ; Neuronal Plasticity ; Phosphoproteins/metabolism ; Phosphorylation ; Pyruvate Dehydrogenase Complex/*metabolism ; Rats
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  • 55
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1981-04-24
    Description: A secondary structure model for 16S ribosomal RNA which is based on available chemical, enzymatic, and comparative sequence data shows good agreement between constraints dictated by the model and a wide variety of experimental observations. The four major structural domains created by the base-pairing scheme correspond closely to RNA fragments isolated after nuclease digestion in the presence of bound ribosomal proteins. Functionally important sites appear to be located in unpaired regions and are phylogenetically highly conserved.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Noller, H F -- Woese, C R -- GM 17129/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1981 Apr 24;212(4493):403-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6163215" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Biological Evolution ; Escherichia coli/ultrastructure ; Hydrogen Bonding ; Nucleic Acid Conformation ; Protein Binding ; *RNA, Bacterial ; *RNA, Ribosomal ; Ribonucleases/metabolism ; Ribosomal Proteins/metabolism ; Ribosomes/*ultrastructure ; Substrate Specificity
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  • 56
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1981-12-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ehrenstein, G -- Huang, L Y -- New York, N.Y. -- Science. 1981 Dec 18;214(4527):1365-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7313696" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Dose-Response Relationship, Drug ; Drug Synergism ; *Drug-Related Side Effects and Adverse Reactions ; Models, Biological ; Receptors, Drug/*drug effects
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  • 57
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1981-04-24
    Description: The affinity of the amino terminal tetrapeptide of the beta chain of fibrin, Gly-His-Arg-Pro, for fibrinogen dramatically increases in the presence of 2 millimolar calcium ion. In contrast, there is no significant increase in the affinity of peptides beginning with the amino terminal sequence of the fibrin alpha chain, Gly-Pro-Arg, in the presence of calcium ions, although the number of binding sites increases. In the latter case, the increased number of sites is due to the alpha chain analogs binding to the site ordinarily occupied by the beta chain analogs. These results indicate that structures at the amino terminus of the fibrin beta chain play a more important role in fibrin polymerization when calcium ions are present.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Laudano, A P -- Doolittle, R F -- AM-07233/AM/NIADDK NIH HHS/ -- HE-18, 576/PHS HHS/ -- New York, N.Y. -- Science. 1981 Apr 24;212(4493):457-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7209542" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Calcium/*pharmacology ; Fibrin/*metabolism ; Fibrinogen/*metabolism ; Humans ; Peptide Fragments/metabolism ; Protein Binding/drug effects
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  • 58
    Publication Date: 1981-09-18
    Description: 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〉
    Keywords: 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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 59
    Publication Date: 1981-05-01
    Description: By use of cadmium-113 nuclear magnetic resonance spectroscopy, a specific calcium ion binding site has been identified in the bovine two-zinc insulin hexamer. This site is composed of six glutamyl carboxylate groups clustered in the center of the hexamer, and is distinct from the normal zinc ion binding sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sudmeier, J L -- Bell, S J -- Storm, M C -- Dunn, M F -- 5S05RR 07010-09/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1981 May 1;212(4494):560-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7010607" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Cadmium ; Calcium/*metabolism ; Cattle ; *Insulin/metabolism ; Isotopes ; Ligands ; Macromolecular Substances ; Magnetic Resonance Spectroscopy ; Protein Conformation ; Zinc/*metabolism
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  • 60
    Publication Date: 1980-05-02
    Description: Amphibians of the family Bufonidae contain high levels of skin compounds that both inhibit Na+- and K+-dependent adenosinetriphosphatase and antagonize the binding of ouabain to the enzyme. In species of Bufo and Atelopus, these compounds are relatively nonpolar bufodienolides, whereas Dendrophryniscus and Melanophryniscus contain more polar compounds of unknown structure. Skin extracts from 30 of 48 species of frogs representing an additional eight families contained relatively low levels of compounds that inhibit binding of ouabain to Na+,K+-adenosinetriphosphatase. The widespread occurrence of low levels of inhibitory compounds is consonant with the role for these compounds as physiological regulators of Na+,K+-adenosinetriphosphatase in amphibian skin; high levels in the Bufonidae probably also serve as a defense against some predators.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flier, J -- Edwards, M W -- Daly, J W -- Myers, C W -- New York, N.Y. -- Science. 1980 May 2;208(4443):503-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6245447" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anura/*metabolism ; Binding Sites ; Bufanolides/pharmacology ; Ouabain/antagonists & inhibitors/*metabolism ; Skin/analysis/enzymology/*metabolism ; Sodium-Potassium-Exchanging ATPase/*metabolism ; Species Specificity ; Tissue Extracts/pharmacology
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  • 61
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1980-06-27
    Description: A discussion of drug-receptor theory is used to show that the three-dimensional structure, or shape, of molecules is important for biological activity. The computer-assisted molecular modeling system at Merck is described, and it is shown that this system is useful for generating and storing molecular structures, determining preferred conformation, comparing molecular shapes, and computing molecular properties. Applications of the system to the study of anti-inflammatory drugs, somatostatin-like compounds, and dihydrofolate reductase inhibitors are summarized.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gund, P -- Andose, J D -- Rhodes, J B -- Smith, G M -- New York, N.Y. -- Science. 1980 Jun 27;208(4451):1425-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6104357" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arachidonic Acids ; Binding Sites ; Computers ; Cyclooxygenase Inhibitors ; Humans ; Indomethacin ; *Models, Molecular ; *Models, Structural ; *Molecular Conformation ; *Pharmaceutical Preparations ; Receptors, Drug/metabolism ; Somatostatin/analogs & derivatives ; Structure-Activity Relationship
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 62
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1980-07-11
    Description: Synthetic metal complexes can closely approach the properties of metal ions in proteins and yield useful information concerning biological structure and function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ibers, J A -- Holm, R H -- New York, N.Y. -- Science. 1980 Jul 11;209(4453):223-35.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7384796" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Electron Transport ; Humans ; Iron-Sulfur Proteins ; *Metalloproteins ; *Metals ; Molecular Conformation ; Myoglobin ; Oxygen/blood ; Oxyhemoglobins ; Protein Binding ; Protein Conformation
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  • 63
    Publication Date: 1980-09-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mardian, J K -- Paton, A E -- Bunick, G J -- Olins, D E -- GM 19334/GM/NIGMS NIH HHS/ -- GM 7438/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1980 Sep 26;209(4464):1534-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7433974" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Chickens ; Chromosomal Proteins, Non-Histone/*metabolism ; Erythrocytes/ultrastructure ; Nucleosomes/*metabolism/ultrastructure ; Poly dA-dT/metabolism ; Protein Binding
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  • 64
    Publication Date: 1980-12-05
    Description: 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〉
    Keywords: 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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  • 65
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1980-10-17
    Description: The crystal and molecular structure of folic acid dihydrate has been determined by x-ray diffraction. Folic acid is in an extended conformation with the pteridine ring in the keto form. The C(4) oxygen and N(10) atoms are on the same side of the molecule, hydrogen-bonded to the same water. This conformation has the pteridine rotated approximately 180 degrees away from the orientation of the pteridine ring of methotrexate bound to dihydrofolate reductase. The folic acid pteridine and phenyl rings interact in a stacking manner which is suggestive of the type of associations these groups could form in a complex of folate, dihydrofolate reductase, and reduced nicotinamide adenine dinucleotide phosphate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mastropaolo, D -- Camerman, A -- Camerman, N -- CA-15879/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1980 Oct 17;210(4467):334-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7423195" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Crystallography ; *Folic Acid ; Molecular Conformation ; Protein Conformation ; Tetrahydrofolate Dehydrogenase ; X-Ray Diffraction
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  • 66
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1980-01-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1980 Jan 11;207(4427):164-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7350651" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Cells/*metabolism ; Cytoplasmic Granules/metabolism ; Endoplasmic Reticulum/metabolism ; Glycoproteins/biosynthesis/metabolism ; Golgi Apparatus/metabolism ; Humans ; Lysosomes/metabolism ; Protein Precursors/metabolism ; Proteins/*metabolism
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  • 67
    Publication Date: 1980-09-19
    Description: In vitro genetic techniques were used to study the sequence requirements for the initiation of specific transcription. Deletion mutants were constructed around the putative promoter of the adenovirus-2 major late and chicken conalbumin genes. Specific transcription in vitro by RNA polymerase B together with a HeLa cell cytoplasmic extract was used as the test for promoter function. With this approach sequences which are essential for the initiation of specific transcription in vitro, were shown to be located between 12 and 32 base pairs upstream from the 5' end of these genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Corden, J -- Wasylyk, B -- Buchwalder, A -- Sassone-Corsi, P -- Kedinger, C -- Chambon, P -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1406-14.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6251548" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; *Cell Physiological Phenomena ; DNA/genetics ; DNA Restriction Enzymes ; DNA, Recombinant ; DNA-Directed RNA Polymerases/*metabolism ; Eukaryotic Cells/*physiology ; *Operon ; RNA Polymerase II/*metabolism ; RNA, Messenger/genetics ; *Transcription, Genetic
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  • 68
    Publication Date: 1980-01-04
    Description: 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〉
    Keywords: 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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