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  • Phosphorylation
  • American Association for the Advancement of Science (AAAS)  (12)
  • Springer  (4)
  • American Meteorological Society
  • MDPI Publishing
  • Protein Phosphorylation in Human Health
  • 1995-1999
  • 1985-1989  (16)
  • 1988  (16)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (12)
  • Springer  (4)
  • American Meteorological Society
  • MDPI Publishing
  • Protein Phosphorylation in Human Health
    • +
Years
  • 1995-1999
  • 1985-1989  (16)
Year
  • 1
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    Reconstitution and phosphorylation of chloride channels from airway epithelium membranes (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-12-09
    Description: Airway epithelial chloride secretion is controlled by the apical-membrane chloride permeability. Purified apical-membrane vesicles from bovine tracheal epithelium have now been shown to contain functional chloride channels by using the planar-bilayer technique. Three types of chloride channels were observed; a voltage-dependent, calcium-independent, 71-picoSiemen (in 150 mM NaCl) channel accounted for more than 80 percent of the vesicular chloride conductance and was under strict control of phosphorylation. The channel underwent a fast rundown in less than 2 to 3 minutes of recording, and reactivation required in situ exposure to a phosphorylating "cocktail" containing the catalytic subunit of the adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase. Mean open time and open probability were increased after phosphorylation, whereas slope conductance remained unchanged. Thus, metabolic control of tracheal chloride single channels can now be studied in vitro.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Valdivia, H H -- Dubinsky, W P -- Coronado, R -- DK 38518/DK/NIDDK NIH HHS/ -- GM 36852/GM/NIGMS NIH HHS/ -- HL 37044/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1988 Dec 9;242(4884):1441-4.〈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/2462280" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Cell Membrane/physiology ; Chloride Channels ; Chlorides/isolation & purification/metabolism/*physiology ; Electric Conductivity ; Ion Channels/*physiology ; Membrane Potentials ; Membrane Proteins/isolation & purification/metabolism/*physiology ; Phosphorylation ; Trachea/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Modulation of acetylcholine receptor desensitization by forskolin is independent of cAMP (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-06-17
    Description: Biochemical and electrophysiological studies suggest that adenosine 3',5'-monophosphate (cAMP)-dependent phosphorylation of the nicotinic acetylcholine receptor channel is functionally significant because it modifies the receptor's rate of desensitization to acetylcholine. In studies that support this conclusion researchers have used forskolin to stimulate cAMP-dependent phosphorylation in intact muscle. It is now shown that although forskolin facilitated desensitization in voltage-clamped rat muscle, this effect was not correlated with the abilities of forskolin and forskolin analogs to activate adenylate cyclase or phosphorylate the receptor. Furthermore, elevation of intracellular cAMP or addition of the catalytic subunit of A-kinase failed to alter desensitization. Therefore, in intact skeletal muscle, cAMP-dependent phosphorylation does not modulate desensitization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wagoner, P K -- Pallotta, B S -- GM32211/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 17;240(4859):1655-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Pharmacology, Glaxo Research Laboratories, Chapel Hill, NC 27599.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2454507" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Methyl-3-isobutylxanthine/pharmacology ; Acetylcholine/pharmacology ; Adenylyl Cyclases/metabolism ; Animals ; Bucladesine/pharmacology ; Colforsin/*pharmacology ; Cyclic AMP/analogs & derivatives/*pharmacology ; Electric Conductivity ; Enzyme Activation/drug effects ; Kinetics ; Muscles/*metabolism ; Phosphorylation ; Rats ; Receptors, Cholinergic/drug effects/*physiology ; Torpedo/metabolism
    Print ISSN: 0036-8075
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  • 3
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    Antiphosphotyrosine recovery of phospholipase C activity after EGF treatment of A-431 cells (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-08-19
    Description: A tenfold increase in phospholipase C activity specific for phosphatidylinositol 4,5-bisphosphate (PIP2) was immunopurified from extracts of A-431 epidermoid carcinoma cells stimulated with epidermal growth factor. This finding suggests a biochemical link between growth factor-stimulated tyrosine kinase activity and PIP2 hydrolysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wahl, M I -- Daniel, T O -- Carpenter, G -- CA 43720/CA/NCI NIH HHS/ -- DK 38517/DK/NIDDK NIH HHS/ -- GM 07347/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Aug 19;241(4868):968-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2457254" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies/immunology ; Carcinoma, Squamous Cell ; Chromatography, High Pressure Liquid ; Cytosol/enzymology ; Epidermal Growth Factor/*pharmacology ; Hydrolysis ; Inositol Phosphates/metabolism ; Phosphatidylinositol 4,5-Diphosphate ; Phosphatidylinositols/metabolism ; Phosphorylation ; Phosphotyrosine ; Protein-Tyrosine Kinases/metabolism ; Substrate Specificity ; Tumor Cells, Cultured ; Type C Phospholipases/*metabolism ; Tyrosine/*analogs & derivatives/immunology/metabolism
    Print ISSN: 0036-8075
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  • 4
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    Blocking of EGF-dependent cell proliferation by EGF receptor kinase inhibitors (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-11
    Description: A systematic series of low molecular weight protein tyrosine kinase inhibitors were synthesized; they had progressively increasing affinity over a 2500-fold range toward the substrate site of epidermal growth factor (EGF) receptor kinase domain. These compounds inhibited EGF receptor kinase activity up to three orders of magnitude more than they inhibited insulin receptor kinase, and they also effectively inhibited the EGF-dependent autophosphorylation of the receptor. The most potent compounds effectively inhibited the EGF-dependent proliferation of A431/clone 15 cells with little or no effect on the EGF-independent proliferation of these cells. The potential use of tyrosine protein kinase inhibitors as antiproliferative agents is demonstrated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yaish, P -- Gazit, A -- Gilon, C -- Levitzki, A -- New York, N.Y. -- Science. 1988 Nov 11;242(4880):933-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, Hebrew University of Jerusalem, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3263702" target="_blank"〉PubMed〈/a〉
    Keywords: Binding, Competitive ; Cell Division/drug effects ; Cell Line ; Epidermal Growth Factor/*pharmacology ; Molecular Structure ; Molecular Weight ; Phosphorylation ; Protein-Tyrosine Kinases/*antagonists & inhibitors ; Receptor, Epidermal Growth Factor/*metabolism ; Receptor, Insulin/metabolism ; Solubility ; Structure-Activity Relationship
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    GABAA-receptor function in hippocampal cells is maintained by phosphorylation factors (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-07-15
    Description: Gamma aminobutyric acid (GABA) mediates fast synaptic inhibition in the central nervous system by activating the chloride-permeable GABAA channel. The GABAA conductance progressively diminishes with time when the intracellular contents of hippocampal neurons are perfused with a minimal intracellular medium. This "run down" of the GABA-activated conductance can be prevented by the inclusion of magnesium adenosine triphosphate and calcium buffer in the intracellular medium. The amount of chloride conductance that can be activated by GABA is determined by competition between a calcium-dependent process that reduces the conductance and a phosphorylation process that maintains the conductance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stelzer, A -- Kay, A R -- Wong, R K -- NS 24519/NS/NINDS NIH HHS/ -- NS 24682/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jul 15;241(4863):339-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, College of Physicians and Surgeons, Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2455347" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/pharmacology ; Animals ; Calcium/physiology ; Chlorides/physiology ; Egtazic Acid/pharmacology ; Electric Conductivity ; Guinea Pigs ; Hippocampus/*physiology ; In Vitro Techniques ; Ion Channels/physiology ; Magnesium/pharmacology ; *Neural Inhibition ; Phosphorylation ; Receptors, GABA-A/*physiology ; gamma-Aminobutyric Acid/*physiology
    Print ISSN: 0036-8075
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  • 6
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    Effects of intracellular free magnesium on calcium current in isolated cardiac myocytes (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-02-12
    Description: Magnesium ions play a fundamental role in cellular function, but the effects of changes in the concentration of intracellular ionized magnesium ([Mg2+]i) on cell physiology have only recently received experimental attention. Increasing [Mg2+]i from 0.3 to 3.0 mM in cardiac cells by internal perfusion has only small effects on the basal voltage-gated calcium current (ICa) or on ICa elevated by dihydropyridine calcium channel agonists. In contrast, ICa elevated by cyclic adenosine monophosphate (cAMP)-dependent phosphorylation decreases by more than 50 percent. The effect of [Mg2+]i is not due to changes in the concentration of cAMP or in the velocity of phosphorylation but rather appears to be a direct effect on the phosphorylated channel or on channel dephosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉White, R E -- Hartzell, H C -- HL21195/HL/NHLBI NIH HHS/ -- HL27385/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1988 Feb 12;239(4841 Pt 1):778-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Cell Biology, Emory University School of Medicine, Atlanta, GA 30322.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2448878" target="_blank"〉PubMed〈/a〉
    Keywords: 8-Bromo Cyclic Adenosine Monophosphate/pharmacology ; Animals ; Calcium/*metabolism/pharmacology ; Cyclic AMP/physiology ; Heart/drug effects/*physiology ; In Vitro Techniques ; Ion Channels/drug effects/*physiology ; Isoproterenol/pharmacology ; Magnesium/pharmacology/*physiology ; Membrane Potentials ; Phosphorylation ; Ranidae ; Ventricular Function
    Print ISSN: 0036-8075
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  • 7
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    T cell CD3-zeta eta heterodimer expression and coupling to phosphoinositide hydrolysis (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-10-28
    Description: The T cell antigen receptor consists of an antigen-binding heterodimer that is noncovalently associated with at least five CD3 subunits (gamma, delta, epsilon, zeta, and eta). The CD3-zeta chains are either disulfide-linked homodimers (CD3-zeta 2) or disulfide-linked heterodimers with eta (CD3-zeta eta). Variants of a murine antigen-specific T cell hybridoma that express normal amounts of CD3-zeta 2 but decreased amounts of CD3-zeta eta were isolated. When activated, the parental cell line increased both phosphatidylinositol hydrolysis and serine-specific protein kinase activity to a much greater extent than the variants. In contrast, the activation of a tyrosine-specific kinase after stimulation with a cross-linking antibody to CD3 was similar among these cells. There was a positive linear relation between the expression of CD3-zeta eta and phosphoinositide hydrolysis stimulated by the TCR, suggesting a differential coupling of the T cell alpha beta heterodimer to signal transduction mechanisms due to alpha beta association with either CD3-zeta 2 or CD3-zeta eta.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mercep, M -- Bonifacino, J S -- Garcia-Morales, P -- Samelson, L E -- Klausner, R D -- Ashwell, J D -- New York, N.Y. -- Science. 1988 Oct 28;242(4878):571-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biological Response Modifiers Program, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2845582" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens/immunology ; Antigens, CD3 ; Antigens, Differentiation, T-Lymphocyte/*physiology ; Cell Line ; Electrophoresis, Gel, Two-Dimensional ; Macromolecular Substances ; *Membrane Proteins ; Mice ; Phosphatidylinositols/*metabolism ; Phosphoproteins/metabolism ; Phosphorylation ; Precipitin Tests ; Protein Kinase C/physiology ; Receptors, Antigen, T-Cell/*physiology ; T-Lymphocytes/*physiology
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  • 8
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    The cellular src gene product regulates junctional cell-to-cell communication (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-01-22
    Description: Overexpression of the cellular src gene in NIH 3T3 cells causes reduction of cell-to-cell transmission of molecules in the 400- to 700-dalton range. This down-regulation of gap junctional communication correlates with the activity of the gene product, the protein tyrosine kinase pp60c-src. The down-regulation was enhanced by point mutation of Tyr527 (a site that is phosphorylated in pp60c-src and that inhibits kinase activity) or by substitution of the viral-src for the cellular-src carboxyl-terminal coding region. Mutation of Tyr416 (a site phosphorylated upon Tyr527 mutation) suppresses both the down-regulation of communication by Tyr527 mutation and that by gene overexpression. The regulation of communication by src may be important in the control of embryonic development and cellular growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Azarnia, R -- Reddy, S -- Kmiecik, T E -- Shalloway, D -- Loewenstein, W R -- CA-14464/CA/NCI NIH HHS/ -- CA-32317/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1988 Jan 22;239(4838):398-401.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, University of Miami School of Medicine, FL 33136.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2447651" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Communication ; Cell Line ; Cell Membrane Permeability ; Gene Expression Regulation ; *Intercellular Junctions ; Mice ; Mutation ; Phosphorylation ; Plasmids ; Protein-Tyrosine Kinases/*genetics ; Proto-Oncogene Proteins/genetics/*physiology ; Proto-Oncogene Proteins pp60(c-src) ; Structure-Activity Relationship ; Transcription, Genetic ; Transfection ; Tyrosine/metabolism
    Print ISSN: 0036-8075
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  • 9
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    A mutation in the catalytic subunit of cAMP-dependent protein kinase that disrupts regulation (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-04-01
    Description: A mutant catalytic subunit of adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase has been isolated from Saccharomyces cerevisiae that is no longer subject to regulation yet retains its catalytic activity. Biochemical analysis of the mutant subunit indicates a 100-fold decreased affinity for the regulatory subunit. The mutant catalytic subunit exhibits approximately a threefold increase in Michaelis constant for adenosine triphosphate and peptide cosubstrates, and is essentially unchanged in its catalytic rate. The nucleotide sequence of the mutant gene contains a single nucleotide change resulting in a threonine-to-alanine substitution at amino acid 241. This residue is conserved in other serine-threonine protein kinases. These results identify this threonine as an important contact between catalytic and regulatory subunits but only a minor contact in substrate recognition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levin, L R -- Kuret, J -- Johnson, K E -- Powers, S -- Cameron, S -- Michaeli, T -- Wigler, M -- Zoller, M J -- GM33986/GM/NIGMS NIH HHS/ -- R35 CA39829-02/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 1;240(4848):68-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, NY 11724.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2832943" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Catalysis ; Cyclic AMP/*pharmacology ; Genes, Fungal ; Kinetics ; Macromolecular Substances ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Protein Kinases/*genetics/metabolism ; Saccharomyces cerevisiae/enzymology/*genetics ; Structure-Activity Relationship ; Threonine
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  • 10
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    Autocrine stimulation of intracellular PDGF receptors in v-sis-transformed cells (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-02-19
    Description: Autocrine activation of platelet-derived growth factor (PDGF) receptors is the mechanism of transformation by the v-sis oncogene. Since the addition of PDGF does not transform normal cells, autocrine mechanisms may involve unique pathways of receptor activation. In this study autocrine stimulation of the PDGF receptor was observed in v-sis-transformed normal rat kidney (NRK) cells. In contrast to receptor activation in normal cells, autocrine activation of PDGF receptors in v-sis-transformed cells occurred in intracellular compartments, disrupting receptor processing and diverting receptors and their precursors to a chloroquine-sensitive degradation pathway. These findings show that intracellular activation of receptors by autocrine mechanisms may play a role in cell transformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keating, M T -- Williams, L T -- 5 K11 HL01556-02/HL/NHLBI NIH HHS/ -- R01 HL32898-04/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1988 Feb 19;239(4842):914-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, San Francisco, CA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2829358" target="_blank"〉PubMed〈/a〉
    Keywords: Ammonium Chloride/pharmacology ; Animals ; Cell Line, Transformed ; Cell Membrane/metabolism ; Chloroquine/pharmacology ; Half-Life ; Hexosaminidases/pharmacology ; Immunosorbent Techniques ; Molecular Weight ; *Oncogenes ; Phosphorylation ; Platelet-Derived Growth Factor/pharmacology ; Protein Precursors/metabolism ; Rats ; Receptors, Cell Surface/drug effects/*metabolism ; Receptors, Platelet-Derived Growth Factor ; Trypsin/metabolism
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  • 11
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    A common PDGF receptor is activated by homodimeric A and B forms of PDGF (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-06-10
    Description: The human platelet-derived growth factor (PDGF) receptor complementary DNA was cloned and expressed by transfection of Chinese hamster ovary (CHO) fibroblasts. The ability of CHO cells expressing the human receptor complementary DNA (CHO-HR5) to interact with different recombinant forms of PDGF (AA and BB homodimers) was tested. Both forms of PDGF bind to the transfected receptor, stimulate the receptor tyrosine kinase activity, and elicit a mitogenic response in a manner that was indistinguishable from the responses of Balb/c 3T3 cells to AA and BB forms of PDGF can be attributed to a single type of receptor and show that the AA form, like the BB form, is a true mitogen.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Escobedo, J A -- Navankasatussas, S -- Cousens, L S -- Coughlin, S R -- Bell, G I -- Williams, L T -- HL-32898/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 10;240(4858):1532-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Francisco.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2836953" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division/drug effects ; Cell Line ; Cells, Cultured ; DNA Replication/drug effects ; Enzyme Activation ; Humans ; Kinetics ; Macromolecular Substances ; Mice ; Phosphorylation ; Platelet-Derived Growth Factor/genetics/*metabolism/pharmacology ; Protein-Tyrosine Kinases/*metabolism ; Receptors, Cell Surface/genetics/*metabolism ; Receptors, Platelet-Derived Growth Factor ; Recombinant Proteins/pharmacology ; Transfection
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  • 12
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    Viroid-induced phosphorylation of a host protein related to a dsRNA-dependent protein kinase (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-07-22
    Description: Viroids are very small, unencapsidated RNAs that replicate and induce severe disease in plants without encoding for any proteins. The mechanisms by which the viroid RNA regulates these events and interacts with host factors are unknown. An Mr 68,000 host-encoded protein has been identified that is differentially phosphorylated in extracts from viroid-infected and mock-inoculated tissues. This phosphoprotein is immunologically related to a double-stranded (ds) RNA-dependent protein kinase from virus-infected, interferon-treated human cells. Further, nucleotide photoaffinity labeling indicates that the protein has an ATP binding site. This protein is similar to dsRNA-dependent protein kinases implicated in mammalian systems in the regulation of protein synthesis and virus replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hiddinga, H J -- Crum, C J -- Hu, J -- Roth, D A -- New York, N.Y. -- Science. 1988 Jul 22;241(4864):451-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant, Soil, and Insect Sciences, University of Wyoming, Laramie 82071.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3393910" target="_blank"〉PubMed〈/a〉
    Keywords: Molecular Weight ; Phosphoproteins/metabolism ; Phosphorylation ; Plant Proteins/*metabolism ; Plants/microbiology ; Protein Kinases/*physiology ; Viroids/*physiology ; eIF-2 Kinase
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  • 13
    Electronic Resource
    Electronic Resource
    Primary structure of the ribosomal protein gene S6 from Schizosaccharomyces pombe (1988)
    Springer
    Current genetics 13 (1988), S. 57-63 
    Details
    ISSN: 1432-0983
    Keywords: Fission yeast ; Ribosomal protein gene ; Phosphorylation ; Termination
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have determined the nucleotide sequence of a ribosomal protein gene which codes for the ribosomal protein S6 (rps6). The sequence analysis revealed that the gene comprises 239 amino acids, giving rise to a basic protein with a molecular weight of 27,502 Da. The product of this gene is the equivalent of the ribosomal protein S1O from Saccharomyces cerevisiae. Northern analyses and S1 mapping of both the 5′ and the 3′ end of the transcripts of this gene show that it is transcribed into three distinct transcripts with different sizes and heterogeneous termini. In the DNA region flanking the coding sequence, several conserved elements are present that may be involved in the transcription initiation and termination.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00365757
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  • 14
    Electronic Resource
    Electronic Resource
    The X-ray induced G2 arrest in mouse eggs: a maternal effect involving a lack of polypeptide phosphorylation (1988)
    Springer
    Development genes and evolution 197 (1988), S. 302-304 
    Details
    ISSN: 1432-041X
    Keywords: Mouse egg ; Maternal effect ; X irradiation ; Cell cycle ; Phosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In some strains of mice, eggs when X irradiated during the pronuclear stage, undergo a mitotic block in the G2 phase of the first cell cycle and cleave when the second division takes place in controls. The importance of this effect varies considerably with the strain and depends exclusively on the maternal genotype. In previous work, two-dimensional electrophoresis showed that eggs blocked at the one-cell stage after irradiation, undergo the same modifications in polypeptide synthesis as two-cell controls of the same age, except at the time of normal first mitosis, where three polypeptide sets of 30, 35 and 45 kDa appear only in cleaving controls. In the present study, we have found phosphorylations in dividing controls, on polypeptides of 30, 35 and 45 kDa. These phosphorylations are not seen in blocked irradiated eggs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00380025
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  • 15
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    Phosphorylation of neuronal microtubule proteins (1988)
    Springer
    Protoplasma 145 (1988), S. 82-88 
    Details
    ISSN: 1615-6102
    Keywords: Tubulin ; Microtubule-associated proteins ; Phosphorylation ; Neuronal differentiation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Phosphorylation of microtubule protein was tested during differentiation in neuroblastoma cells. Two microtubule proteins were modified, β-tubulin and MAP-1 B. In the first case less than one mol of phosphate was incorporated per mol of protein, whereas several residues were phosphorylated in MAP-1 B. The localization of the phosphorylated residue of β-tubulin indicated that it is present in an isoform, at its carboxy-terminal region, and probably correspond to the serine 444. When comparing thein vivo phosphorylation of tubulin with that produced by casein kinase IIin vitro, a similar pattern was obtained. A similar result was found upon the comparison of the phosphorylation pattern of MAP-1 B after phosphorylationin vivo andin vitro using casein kinase II. These results suggest a role for casein kinase II in the phosphorylation of microtubule proteins in neuroblastoma cells. A result similar to that found for neuroblastoma cells was found after injection of [32P]phosphate into the brain of seven-day-old rats; however, a more complex pattern was found for the phosphorylationin vivo in adult rats.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01349342
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  • 16
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    ATP formation onset lag and post-illumination phosphorylation initiated with single-turnover flashes. III. Characterization of the ATP formation onset lag and post-illumination phosphorylation for thylakoids exhibiting localized or bulk-phase delocalized energy coupling (1988)
    Springer
    Journal of bioenergetics and biomembranes 20 (1988), S. 129-154 
    Details
    ISSN: 1573-6881
    Keywords: Phosphorylation ; localized energy coupling ; delocalized energy coupling ; proton gradients
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract When 100 mM KCl replaced sucrose in a chloroplast thylakoid stock suspension buffer, the membranes were converted from a localized proton gradient to a delocalized proton gradient energy coupling mode. The KCl-suspended but not the sucrose-suspended thylakoids showed pyridine-dependent extensions of the ATP onset lag and pyridine effects on post-illumination phosphorylation. The ATP formation assays were performed in a medium of identical composition, using about a 200-fold dilution of the stock thylakoid suspension; hence the different responses were due to the pretreatment, and not the conditions present in the phosphorylation assay. Such permeable buffer effects on ATP formation provide a clear indicator of delocalized proton gradients as the driving force for phosphorylation. The pyridine-dependent increases in the onset lags (and effects on post-illumination phosphorylation) were not due to different ionic conductivities of the membranes (measured by the 515 nm electrochromic absorption change), H+/e − ratios, or electron transport capacities for the two thylakoid preparations. Thylakoid volumes and [ 14C]pyridine equilibration were similar with both preparations. The KCl-induced shift toward a bulk-phase delocalized energy coupling mode was reversed when the thylakoids were placed back in a low-salt medium. Proton uptake, at the ATP-formation energization threshold flash number, was much larger in the KCl-treated thylakoids and they also had a longer ATP formation onset lag, when no pyridine was present. These results are consistent with the salt treatment exposing additional endogenous buffering groups for interaction with the proton gradient. The concomitant appearance of the pyridine buffer effects implies that the additional endogenous buffering groups must be located on proteins directly exposed in the aqueous lumen phase. Kinetic analysis of the decay of the post-illumination phosphorylation in the two thylakoid preparations showed different apparent first-order rate constants, consistent with there being two different compartments contributing to the proton reservoirs that energize ATP formation. We suggest that the two compartments are a membrane-phase localized compartment operative in the sucrose-treated thylakoids and the bulk lumen phase into which protons readily equilibrate in the KCl-treated thylakoids.
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    URL: http://dx.doi.org/10.1007/BF00762141
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