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  • Phosphorylation
  • American Association for the Advancement of Science (AAAS)  (7)
  • Springer  (1)
  • American Meteorological Society
  • MDPI Publishing
  • 1995-1999
  • 1985-1989  (8)
  • 1987  (8)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (7)
  • Springer  (1)
  • American Meteorological Society
  • MDPI Publishing
Years
  • 1995-1999
  • 1985-1989  (8)
Year
  • 1
    Electronic Resource
    Electronic Resource
    Inhibition of protein phosphorylation by chloroquine (1987)
    Springer
    Archives of microbiology 147 (1987), S. 235-239 
    Details
    ISSN: 1432-072X
    Keywords: Chloroquine ; Yeast ; Fructose-1,6-bisphosphatase ; Phosphorylation ; Protein kinase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The rapid phase of fructose-1,6-bisphosphatase (FBPase) inactivation following glucose addition to starved yeast cells [reported previously] is inhibited on addition of 10 mM chloroquine (CQ) at about pH 8. This inhibition of inactivation was shown to be due to the prevention of phosphorylation of the enzyme. CQ was also found to inhibit general protein phosphorylation in the yeast cells. Glycolysis, as observed by changes in intracellular glucose-6-phosphate and extracellular glucose and ethanol concentrations, was shown to be significantly inhibited in cells treated with CQ. Similarly, a decrease in ATP concentrations was observed. However, during the early stages of phosphorylation of FBPase, levels of ATP were similar in cells containing CQ as in those without CQ. Thus, decrease in ATP levels is not thought to be significantly responsible for the inhibition of protein phosphorylation. However, the phosphorylating activity of cyclic AMP-dependent protein kinases is inhibited in vitro by relatively low concentrations of CQ. Thus, prevention of protein phosphorylation by CQ is believed to be due to inhibition of protein kinases in yeast cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00463481
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  • 2
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    Characterization by tandem mass spectrometry of structural modifications in proteins (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-08-28
    Description: Tandem mass spectrometry can be used to solve a number of protein structural problems that are not amenable to conventional methods for amino acid sequencing. Typical problems that use this approach involve characterization of peptides with blocked amino termini or peptides that have been otherwise posttranslationally processed, such as, by phosphorylation or sulfation. The structure and homogeneity of synthetic peptides can also be evaluated. Since peptides can be selectively characterized in the presence of other peptides or contaminants, the need for extensive purification is reduced or eliminated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Biemann, K -- Scoble, H A -- GM05472/GM/NIGMS NIH HHS/ -- RR00317/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1987 Aug 28;237(4818):992-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3303336" target="_blank"〉PubMed〈/a〉
    Keywords: *Amino Acid Sequence ; Amino Acyl-tRNA Synthetases ; Escherichia coli ; Humans ; *Mass Spectrometry ; Phosphorylation ; Protein Processing, Post-Translational ; Proteins ; Saccharomyces cerevisiae
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    A chimeric, ligand-binding v-erbB/EGF receptor retains transforming potential (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-04-10
    Description: Comparison of amino acid sequences from human epidermal growth factor (EGF) receptor and avian erythroblastosis virus erbB oncogene product suggests that v-erbB represents a truncated avian EGF receptor gene product. Although both proteins are transmembrane tyrosine kinases, the v-erbB protein lacks most of the extracellular ligand-binding domain and a 32-amino acid cytoplasmic sequence present in the human EGF receptor. To test the validity of the proposed origin of v-erbB and to investigate the functional significance of the deleted extracellular sequences, a chimeric gene encoding the extracellular and the transmembrane domain of the human EGF receptor joined to sequences coding for the cytoplasmic domain of the avian erbB oncogene product was constructed. When expressed in Rat1 fibroblasts, this reconstituted gene product (HER-erbB) was transported to the cell surface and bound EGF. Its autophosphorylation activity was stimulated by interaction with the ligand. Expression of the HER-erbB chimera led to anchorage-independent cell growth in soft agar and EGF-induced focus formation in Rat1 monolayers. Thus, it appears that v-erbB protein sequences in the chimeric receptor retain their transforming activity under the influence of the human extracellular EGF-binding domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Riedel, H -- Schlessinger, J -- Ullrich, A -- New York, N.Y. -- Science. 1987 Apr 10;236(4798):197-200.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3494307" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Cycle ; Cell Line ; *Cell Transformation, Neoplastic ; DNA, Recombinant ; Epidermal Growth Factor/*physiology ; Humans ; *Oncogenes ; Phosphorylation ; Protein-Tyrosine Kinases/*genetics ; Rats ; Receptor, Epidermal Growth Factor/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Myosin rod phosphorylation and the catch state of molluscan muscles (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-01-16
    Description: "Catch" is a prolonged state of tension in molluscan smooth muscles shown by mechanical measurements to be associated with the level of protein phosphorylation. Myosin isolated from these muscles is unusual in being phosphorylated in the rod portion by an endogenous kinase, like certain nonmuscle myosins. These findings suggest that the myosin rod is a target for phosphorylation and that this reaction may control the transition from catch to relaxation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Castellani, L -- Cohen, C -- AM 17346/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1987 Jan 16;235(4786):334-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3026049" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/analogs & derivatives/pharmacology ; Animals ; Bivalvia/*physiology ; Calcium/*physiology ; Cyclic AMP/physiology ; Egtazic Acid/pharmacology ; In Vitro Techniques ; *Muscle Contraction ; Myosins/metabolism/*physiology ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation ; Protein Kinases/physiology ; Sodium Fluoride/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 5
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    Recombinant fragment of protein kinase inhibitor blocks cyclic AMP-dependent gene transcription (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-10-23
    Description: Transcriptional regulation by cyclic adenosine monophosphate (cAMP) in mammalian cells could be mediated by a phosphoprotein substrate of the cAMP-dependent protein kinase or, as in prokaryotes, by a cAMP-binding protein. Two synthetic genes that code for an active fragment of the protein inhibitor of this kinase and a mutant inactive fragment were constructed and used to distinguish these alternatives. Transient expression of the active peptide product specifically inhibited the cAMP-stimulated expression of a cotransfected reporter gene by more than 90 percent, whereas the expression of the inactive peptide did not alter cAMP-stimulated gene expression. The results indicate that an active kinase catalytic subunit is a necessary intermediate in the cAMP stimulation of gene transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grove, J R -- Price, D J -- Goodman, H M -- Avruch, J -- New York, N.Y. -- Science. 1987 Oct 23;238(4826):530-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02114.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2821622" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyltransferases/genetics ; Carrier Proteins/*pharmacology ; Chloramphenicol O-Acetyltransferase ; Cyanogen Bromide ; Cyclic AMP/*pharmacology ; DNA, Recombinant ; Escherichia coli/genetics ; *Intracellular Signaling Peptides and Proteins ; Nucleic Acid Hybridization ; Peptide Fragments/*pharmacology ; Phosphorylation ; Plasmids ; Protein Kinase Inhibitors ; Protein Kinases/metabolism ; RNA, Messenger/genetics ; Recombinant Proteins/*pharmacology ; Transcription, Genetic/*drug effects ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    After insulin binds (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-09-18
    Description: Three recent advances pertinent to the mechanism of insulin action include (i) the discovery that the insulin receptor is an insulin-dependent protein tyrosine kinase, functionally related to certain growth factor receptors and oncogene-encoded proteins, (ii) the molecular cloning of the insulin proreceptor complementary DNA, and (iii) evidence that the protein tyrosine kinase activity of the receptor is essential for insulin action. Efforts are now focusing on the physiological substrates for the receptor kinase. Experience to date suggests that they will be rare proteins whose phosphorylation in intact cells may be transient. The advantages of attempting to dissect the initial biochemical pathway of insulin action include the wealth of information about the metabolic consequences of insulin action and the potential for genetic analysis in Drosophila and in man.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rosen, O M -- New York, N.Y. -- Science. 1987 Sep 18;237(4821):1452-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2442814" target="_blank"〉PubMed〈/a〉
    Keywords: DNA/analysis ; Drosophila ; Humans ; Insulin/*metabolism ; Molecular Weight ; Oncogenes ; Phosphorylation ; Phosphoserine/metabolism ; Phosphothreonine/metabolism ; Phosphotyrosine ; Protein-Tyrosine Kinases/metabolism ; Receptor, Epidermal Growth Factor/physiology ; Receptor, Insulin/genetics/*physiology ; Receptors, Cell Surface/metabolism ; Substrate Specificity ; Tyrosine/analogs & derivatives/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Ribavirin antagonizes the effect of azidothymidine on HIV replication (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-03-13
    Description: Azidothymidine and ribavirin both inhibit replication of human immunodeficiency virus in vitro and show promise of clinical utility in patients infected with this virus. In this study, the possible interactions of these drugs were examined in vitro, and a reproducible antagonism between azidothymidine and ribavirin was found to occur under a variety of experimental conditions. The mechanism responsible for this antagonism appeared to be inhibition of azidothymidine phosphorylation by ribavirin. Because similar effects may occur in vivo, clinical trials of these two drugs in combination must be performed only under carefully controlled conditions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogt, M W -- Hartshorn, K L -- Furman, P A -- Chou, T C -- Fyfe, J A -- Coleman, L A -- Crumpacker, C -- Schooley, R T -- Hirsch, M S -- CA 09382-04/CA/NCI NIH HHS/ -- CA 12464/CA/NCI NIH HHS/ -- CA 27569/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Mar 13;235(4794):1376-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2435003" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; HIV/*drug effects/physiology ; Humans ; Lymphocytes/microbiology ; Monocytes/microbiology ; Phosphorylation ; Phytohemagglutinins/pharmacology ; RNA-Directed DNA Polymerase/metabolism ; Ribavirin/*pharmacology ; Ribonucleosides/*pharmacology ; Thymidine/*analogs & derivatives/antagonists & inhibitors/pharmacology ; Virus Replication/drug effects ; Zidovudine
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    A G protein directly regulates mammalian cardiac calcium channels (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-11-27
    Description: A possible direct effect of guanine nucleotide binding (G) proteins on calcium channels was examined in membrane patches excised from guinea pig cardiac myocytes and bovine cardiac sarcolemmal vesicles incorporated into planar lipid bilayers. The guanosine triphosphate analog, GTP gamma S, prolonged the survival of excised calcium channels independently of the presence of adenosine 3',5'-monophosphate (cAMP), adenosine triphosphate, cAMP-activated protein kinase, and the protein kinase C activator tetradecanoyl phorbol acetate. A specific G protein, activated Gs, or its alpha subunit, purified from the plasma membranes of human erythrocytes, prolonged the survival of excised channels and stimulated the activity of incorporated channels. Thus, in addition to regulating calcium channels indirectly through activation of cytoplasmic kinases, G proteins can regulate calcium channels directly. Since they also directly regulate a subset of potassium channels, G proteins are now known to directly gate two classes of membrane ion channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yatani, A -- Codina, J -- Imoto, Y -- Reeves, J P -- Birnbaumer, L -- Brown, A M -- HL-31154/HL/NHLBI NIH HHS/ -- HL-36930/HL/NHLBI NIH HHS/ -- HL-37044/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1987 Nov 27;238(4831):1288-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Molecular Biophysics, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2446390" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Pyridinecarboxylic acid, ; 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ; ester/pharmacology ; Animals ; Calcium/metabolism ; Colforsin/pharmacology ; GTP-Binding Proteins/*physiology ; Guanosine 5'-O-(3-Thiotriphosphate) ; Guanosine Triphosphate/analogs & derivatives/pharmacology ; Guinea Pigs ; Heart/*physiology ; Ion Channels/drug effects/*physiology ; Isoproterenol/pharmacology ; Leupeptins/pharmacology ; Membrane Potentials/drug effects ; Phosphorylation ; Thionucleotides/pharmacology ; Ventricular Function
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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