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  • Phosphorylation
  • American Association for the Advancement of Science (AAAS)  (43)
  • Springer  (5)
  • American Meteorological Society
  • MDPI Publishing
  • Protein Phosphorylation in Human Health
  • 1985-1989  (48)
Collection
Publisher
  • American Association for the Advancement of Science (AAAS)  (43)
  • Springer  (5)
  • American Meteorological Society
  • MDPI Publishing
  • Protein Phosphorylation in Human Health
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Years
Year
  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-07-28
    Description: The CD4 and CD8 T cell receptor accessory molecules can both be isolated from T lymphocytes in association with p56lck, a membrane-associated, cytoplasmic tyrosine protein kinase that is expressed exclusively in lymphoid cells. The enzymatic activity of p56lck may therefore be regulated by CD4 and CD8 and be important in antigen-induced T cell activation. Exposure of human T cells and some mouse T cells to the tumor promoter 12-O-tetradecanoyl phorbol-13-acetate (TPA), an activator of protein kinase C, caused the dissociation of p56lck and CD4. Activation of protein kinase C may therefore interrupt regulation of p56lck by CD4 and alter the ability of p56lck to interact with polypeptide substrates. In contrast, exposure of cells to TPA did not cause dissociation of p56lck and CD8. Regulation of p56lck by CD4 may therefore differ from regulation by CD8.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hurley, T R -- Luo, K -- Sefton, B M -- New York, N.Y. -- Science. 1989 Jul 28;245(4916):407-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology and Virology Laboratory, Salk Institute, San Diego, CA 92138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2787934" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Differentiation, T-Lymphocyte/*immunology ; Cell Line ; Enzyme Activation ; Humans ; Leukemia, T-Cell ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck) ; Phosphorylation ; Precipitin Tests ; Protein Kinase C/*metabolism ; Protein-Tyrosine Kinases/*metabolism ; T-Lymphocytes/*immunology ; Tetradecanoylphorbol Acetate/pharmacology ; Tumor Cells, Cultured
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  • 2
    Publication Date: 1989-07-28
    Description: A 47-kilodalton neutrophil cytosol factor (NCF-47k), required for activation of nicotinamide adenine dinucleotide phosphate (NADPH) oxidase superoxide (O2-.) production, is absent in most patients with autosomal recessive chronic granulomatous disease (AR-CGD). NCF-47k cDNAs were cloned from an expression library. The largest clone predicted a 41.9-kD protein that contained an arginine and serine-rich COOH-terminal domain with potential protein kinase C phosphorylation sites. A 33-amino acid segment of NCF-47k shared 49% identity with ras p21 guanosine triphosphatase activating protein. Recombinant NCF-47k restored O2-. -producing activity to AR-CGD neutrophil cytosol in a cell-free assay. Production of active recombinant NCF-47k will enable functional regions of this molecule to be mapped.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lomax, K J -- Leto, T L -- Nunoi, H -- Gallin, J I -- Malech, H L -- New York, N.Y. -- Science. 1989 Jul 28;245(4916):409-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Bacterial Diseases Section, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2547247" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Blotting, Northern ; Cloning, Molecular ; DNA/*genetics ; Granulomatous Disease, Chronic/enzymology/*genetics ; Humans ; Immunoblotting ; Molecular Sequence Data ; NADH, NADPH Oxidoreductases/*metabolism ; NADPH Oxidase ; Neutrophils/*metabolism ; Phosphoproteins/*genetics/metabolism ; Phosphorylation ; Recombinant Proteins/genetics/metabolism ; Superoxides/metabolism
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  • 3
    Publication Date: 1989-02-03
    Description: The nitrogen regulatory (NtrC) protein of enteric bacteria, which binds to sites that have the properties of transcriptional enhancers, is known to activate transcription by a form of RNA polymerase that contains the NtrA protein (sigma 54) as sigma factor (referred to as sigma 54-holoenzyme). In the presence of adenosine triphosphate, the NtrC protein catalyzes isomerization of closed recognition complexes between sigma 54-holoenzyme and the glnA promoter to open complexes in which DNA in the region of the transcription start site is locally denatured. NtrC is not required subsequently for maintenance of open complexes or initiation of transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Popham, D L -- Szeto, D -- Keener, J -- Kustu, S -- GM38361/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1989 Feb 3;243(4891):629-35.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of California, Berkley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2563595" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/analogs & derivatives/metabolism/pharmacology ; *Bacterial Proteins ; Base Sequence ; Binding Sites ; DNA, Bacterial/metabolism ; DNA-Binding Proteins/*metabolism ; DNA-Directed RNA Polymerases/metabolism ; Deoxyribonuclease I ; *Enhancer Elements, Genetic ; Glutamate-Ammonia Ligase/genetics ; Heparin/pharmacology ; Molecular Sequence Data ; Mutation ; PII Nitrogen Regulatory Proteins ; Phosphorylation ; Promoter Regions, Genetic ; Salmonella typhimurium/*genetics ; Sigma Factor/metabolism ; *Trans-Activators ; Transcription Factors ; *Transcription, Genetic
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-05-05
    Description: Inositol phospholipid-specific phospholipase C is the enzyme that generates phosphoinositide-derived messenger molecules. Mammalian cells contain at least five immunologically distinct phospholipase C enzymes that appear to be separate gene products. Complete amino acid sequences of four of these isozymes have been established. The overall sequence similarity is surprisingly low for enzymes catalyzing the same chemical reaction: three of them show limited amino acid sequence similarity to each other in two narrow regions, and the fourth enzyme is completely different. The diversity in primary structure together with different regional and cellular expression of the isozymes suggests that each isozyme has a defined function in processing the physiological response of different cell types to a variety of external stimuli and that each is regulated differently.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rhee, S G -- Suh, P G -- Ryu, S H -- Lee, S Y -- New York, N.Y. -- Science. 1989 May 5;244(4904):546-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2541501" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Membrane/enzymology ; Cytosol/enzymology ; Isoenzymes/*metabolism ; Phosphatidylinositols/*metabolism ; Phosphoinositide Phospholipase C ; Phosphoric Diester Hydrolases/*metabolism ; Phosphorylation ; Second Messenger Systems ; Terminology as Topic
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  • 5
    Publication Date: 1989-09-08
    Description: Complementary DNAs for the beta subunit of the dihydropyridine-sensitive calcium channel of rabbit skeletal muscle were isolated on the basis of peptide sequences derived from the purified protein. The deduced primary structure is without homology to other known protein sequences and is consistent with the beta subunit being a peripheral membrane protein associated with the cytoplasmic aspect of the sarcolemma. The protein contains sites that might be expected to be preferentially phosphorylated by protein kinase C and guanosine 3',5'-monophosphate-dependent protein kinase. A messenger RNA for this protein appears to be expressed in brain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ruth, P -- Rohrkasten, A -- Biel, M -- Bosse, E -- Regulla, S -- Meyer, H E -- Flockerzi, V -- Hofmann, F -- New York, N.Y. -- Science. 1989 Sep 8;245(4922):1115-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Physiologische Chemie, Medizinische Fakultat, Homburg/Saar, Federal Republic of Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2549640" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Calcium Channel Blockers/*metabolism/pharmacology ; Calcium Channels/drug effects/*metabolism ; Dihydropyridines/*metabolism/pharmacology ; Molecular Sequence Data ; Muscles/*analysis ; Phosphorylation ; Protein Conformation ; RNA, Messenger/isolation & purification ; Rabbits ; Receptors, Nicotinic/drug effects/*isolation & purification/metabolism
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  • 6
    Publication Date: 1989-10-27
    Description: Activation of protein kinase C is thought to require association of the kinase with the cell membrane. It has been assumed that cellular substrates for the kinase must likewise be associated with membranes, and previous studies with membrane-associated myristoylated proteins have supported this view. It is now shown that a mutation that prevents the normal amino-terminal myristoylation of a prominent cellular substrate of protein kinase C, and appears to prevent its membrane association, does not prevent the normal phosphorylation of this protein in intact cells in response to phorbol esters. Thus, membrane association may not be required in order for protein kinase C substrates to undergo phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Graff, J M -- Gordon, J I -- Blackshear, P J -- 2T32-GM 07171/GM/NIGMS NIH HHS/ -- AI27179/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1989 Oct 27;246(4929):503-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute Laboratories, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2814478" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cells, Cultured ; Chickens ; Enzyme Activation ; *Intracellular Signaling Peptides and Proteins ; Membrane Proteins/metabolism ; Mutation ; Myristic Acid ; Myristic Acids ; Phosphorylation ; Protein Kinase C/*metabolism ; Proteins/*metabolism ; Substrate Specificity ; Transfection
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  • 7
    Publication Date: 1989-12-08
    Description: The human retinoblastoma gene (RB1) encodes a protein (Rb) of 105 kilodaltons that can be phosphorylated. Analysis of Rb metabolism has shown that the protein has a half-life of more than 10 hours and is synthesized at all phases of the cell cycle. Newly synthesized Rb is not extensively phosphorylated (it is "underphosphorylated") in cells in the G0 and G1 phases but is phosphorylated at multiple sites at the G1/S boundary and in S phase. HL-60 cells that were induced to terminally differentiate by various chemicals lost their ability to phosphorylate newly synthesized Rb at multiple sites when cell growth was arrested. These findings suggest that underphosphorylated Rb may restrict cell proliferation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mihara, K -- Cao, X R -- Yen, A -- Chandler, S -- Driscoll, B -- Murphree, A L -- T'Ang, A -- Fung, Y K -- 5P30CA14089/CA/NCI NIH HHS/ -- CA 44754/CA/NCI NIH HHS/ -- EY 07846/EY/NEI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1989 Dec 8;246(4935):1300-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Hematology/Oncology and Ophthalmology, Childrens Hospital of Los Angeles, CA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2588006" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Cycle/*genetics ; Cell Division/drug effects/genetics ; Eye Neoplasms/genetics ; *Gene Expression Regulation, Neoplastic ; Humans ; Interphase/genetics ; Neoplasm Proteins/genetics/*metabolism ; Phosphorylation ; Protein Processing, Post-Translational/drug effects/*genetics ; Retinoblastoma/*genetics ; Tretinoin/pharmacology ; Tumor Cells, Cultured
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  • 8
    Publication Date: 1989-10-13
    Description: The beta-adrenergic receptor kinase (beta-ARK), which specifically phosphorylates only the agonist-occupied form of the beta-adrenergic and closely related receptors, appears to be important in mediating rapid agonist-specific (homologous) desensitization. The structure of this enzyme was elucidated by isolating clones from a bovine brain complementary DNA library through the use of oligonucleotide probes derived from partial amino acid sequence. The beta-ARK cDNA codes for a protein of 689 amino acids (79.7 kilodaltons) with a protein kinase catalytic domain that bears greatest sequence similarity to protein kinase C and the cyclic adenosine monophosphate (cyclic AMP)--dependent protein kinase. When this clone was inserted into a mammalian expression vector and transfected into COS-7 cells, a protein that specifically phosphorylated the agonist-occupied form of the beta 2-adrenergic receptor and phosphorylated, much more weakly, the light-bleached form of rhodopsin was expressed. RNA blot analysis revealed a messenger RNA of four kilobases with highest amounts in brain and spleen. Genomic DNA blot analysis also suggests that beta-ARK may be the first sequenced member of a multigene family of receptor kinases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benovic, J L -- DeBlasi, A -- Stone, W C -- Caron, M G -- Lefkowitz, R J -- New York, N.Y. -- Science. 1989 Oct 13;246(4927):235-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Medicine, Duke University Medical Center, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2552582" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cattle ; Cloning, Molecular ; *Cyclic AMP-Dependent Protein Kinases ; Molecular Sequence Data ; Multigene Family/*genetics ; Organ Specificity ; Phosphorylation ; Protein Kinases/biosynthesis/*genetics/physiology ; Receptors, Adrenergic, beta/metabolism ; Sequence Homology, Nucleic Acid ; Substrate Specificity ; beta-Adrenergic Receptor Kinases
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-02-03
    Description: A defect in regulation of a chloride channel appears to be the molecular basis for cystic fibrosis (CF), a common lethal genetic disease. It is shown here that a chloride channel with kinetic and regulatory properties similar to those described for secretory epithelial cells is present in both T and B lymphocyte cell lines. The regulation of the channels by adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase in transformed B cells from CF patients is defective. Thus, lymphocytes may be an accessible source of CF tissue for study of this defect, for cloning of the chloride channel complex, and for diagnosis of the disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, J H -- Schulman, H -- Gardner, P -- New York, N.Y. -- Science. 1989 Feb 3;243(4891):657-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2464852" target="_blank"〉PubMed〈/a〉
    Keywords: 8-Bromo Cyclic Adenosine Monophosphate/pharmacology ; Adenosine Triphosphate/pharmacology ; B-Lymphocytes/metabolism ; Calcium/pharmacology ; Cell Line ; Cell Line, Transformed ; Chlorides/*metabolism ; Cyclic AMP/*pharmacology ; Cystic Fibrosis/*metabolism ; Electric Conductivity ; Epithelium/metabolism ; Herpesvirus 4, Human ; Humans ; Ion Channels/drug effects/*metabolism ; Membrane Potentials ; Phosphorylation ; Protein Kinases/metabolism ; T-Lymphocytes/metabolism
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-03-03
    Description: The molecules with which the platelet-derived growth factor (PDGF) receptor interacts to elicit the biochemical reactions responsible for cell proliferation have not been identified. Antisera directed against specific PDGF receptor peptides coprecipitated a phosphatidylinositol (PI) kinase and the PDGF receptor. Immunoprecipitates from PDGF-stimulated cells contained 10 to 50 times as much PI kinase as those from unstimulated cells. Mutation of the PDGF receptor by deletion of its kinase insert region resulted in a receptor markedly less effective than the wild type in eliciting cell proliferation and defective in PDGF-stimulated PI kinase, but still capable of PDGF-induced receptor autophosphorylation and phosphoinositide hydrolysis. These data show that the PDGF receptor is physically associated with a PDGF-sensitive PI kinase that is distinct from tyrosine kinase and is not required for PDGF-induced PI hydrolysis. The finding that the mutant PDGF receptor missing the kinase insert domain elicited known early biochemical responses to PDGF, but did not associate with or regulate PI kinase, suggests a novel role for the receptor-associated PI kinase in the transmission of mitogenic signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coughlin, S R -- Escobedo, J A -- Williams, L T -- HL 32898/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1989 Mar 3;243(4895):1191-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2466336" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Phosphatidylinositol 4-Kinase ; Animals ; Cell Line ; Chromatography ; Cricetinae ; Immunoassay ; Immunosorbent Techniques ; Mice ; Mice, Inbred BALB C ; Mutation ; Phosphatidylinositols/metabolism ; Phosphorylation ; Phosphotransferases/*metabolism ; Phosphotyrosine ; Platelet-Derived Growth Factor/pharmacology ; Protein-Tyrosine Kinases/metabolism ; Receptors, Cell Surface/genetics/*metabolism ; Receptors, Platelet-Derived Growth Factor ; *Signal Transduction ; Tyrosine/analogs & derivatives/metabolism
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  • 11
    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.
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  • 12
    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.
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  • 13
    Electronic Resource
    Electronic Resource
    Springer
    Protoplasma 145 (1988), S. 82-88 
    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.
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  • 14
    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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  • 15
    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
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  • 16
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    American Association for the Advancement of Science (AAAS)
    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
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  • 17
    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
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  • 18
    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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  • 19
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    American Association for the Advancement of Science (AAAS)
    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
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  • 20
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    American Association for the Advancement of Science (AAAS)
    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
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  • 21
    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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  • 22
    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
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  • 23
    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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  • 24
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    American Association for the Advancement of Science (AAAS)
    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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  • 25
    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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  • 26
    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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  • 27
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 147 (1987), S. 235-239 
    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.
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  • 28
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    American Association for the Advancement of Science (AAAS)
    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
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  • 29
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    American Association for the Advancement of Science (AAAS)
    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
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  • 30
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    American Association for the Advancement of Science (AAAS)
    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
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  • 31
    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
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  • 32
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    American Association for the Advancement of Science (AAAS)
    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
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  • 33
    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
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  • 34
    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
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  • 35
    Publication Date: 1986-12-12
    Description: When isolated adult oligodendrocytes adhere to a substratum myelinogenesis occurs. Investigation of the mechanism by which this happens indicated that the oligodendrocyte-substratum interaction activated protein kinase C-dependent phosphorylation of myelin basic protein and promoted the synthesis of myelin basic protein. In addition, when agents that activate protein kinase C (second messenger diacylglycerol or a tumor-promoting phorbol ester) were added to nonattached oligodendrocytes, they mimicked the influence of the substratum by inducing phosphorylation of myelin basic protein; and reagents that increase cellular adenosine 3', 5'-monophosphate (cyclic AMP) inhibited phosphorylation of myelin basic protein. Thus, at least in vitro, the interaction between oligodendrocytes and the substratum may mediate myelinogenic events, and phosphorylation of myelin basic protein may be an early requirement in the sequence of steps that ultimately results in myelin formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vartanian, T -- Szuchet, S -- Dawson, G -- Campagnoni, A T -- GM-07183/GM/NIGMS NIH HHS/ -- HD-04583/HD/NICHD NIH HHS/ -- HD-06426/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Dec 12;234(4782):1395-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2431483" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Methyl-3-isobutylxanthine/pharmacology ; Adult ; Calcimycin/pharmacology ; Cell Adhesion ; Colforsin/pharmacology ; Cyclic AMP/metabolism ; Enzyme Activation ; Humans ; Myelin Basic Protein/*metabolism ; Neuroglia/*cytology ; Oligodendroglia/*cytology ; Phosphorylation ; Protein Kinase C/*metabolism ; Tetradecanoylphorbol Acetate/pharmacology
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  • 36
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-09-12
    Description: The SNF1 gene plays a central role in carbon catabolite repression in the yeast Saccharomyces cerevisiae, namely that SNF1 function is required for expression of glucose-repressible genes. The nucleotide sequence of the cloned SNF1 gene was determined, and the predicted amino acid sequence shows that SNF1 encodes a 72,040-dalton polypeptide that has significant homology to the conserved catalytic domain of mammalian protein kinases. Specific antisera were prepared and used to identify the SNF1 protein. The protein was shown to transfer phosphate from adenosine triphosphate to serine and threonine residues in an in vitro autophosphorylation reaction. These findings indicate that SNF1 encodes a protein kinase and suggest that protein phosphorylation plays a critical role in regulation by carbon catabolite repression in eukaryotic cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Celenza, J L -- Carlson, M -- GM34095/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Sep 12;233(4769):1175-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3526554" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Enzyme Repression ; Genes ; Glucose/*metabolism ; Phosphorylation ; Protein Kinases/biosynthesis/*genetics ; Saccharomyces cerevisiae/enzymology/*genetics
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  • 37
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-01-24
    Description: Saccharomyces cerevisiae was examined for tyrosine kinase activity in vitro because this organism offers molecular and genetic approaches for analyzing the role of tyrosine phosphorylation in cellular growth control that are unavailable in higher eukaryotes. Yeast extracts phosphorylated a random copolymer (glutamic acid:tyrosine, 80:20) at tyrosine in a reaction that was linear with respect to time and protein concentration. In the absence of added copolymer, phosphotyrosine was 0.1 percent of the total phosphoamino acids labeled with [gamma-32P]adenosine triphosphate in endogenous yeast proteins. However, specific activities of these reactions were low (approximately 1 percent of those in extracts of chick embryo fibroblasts). Lack of significant incorporation of label from [alpha-32P]adenosine triphosphate into the copolymer or endogenous yeast proteins demonstrated that nucleotide interconversion, adenylylation, and subsequent hydrolysis could not account for the generation of phosphotyrosine observed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schieven, G -- Thorner, J -- Martin, G S -- CA17546/CA/NCI NIH HHS/ -- ES07075/ES/NIEHS NIH HHS/ -- GM21841/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Jan 24;231(4736):390-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2417318" target="_blank"〉PubMed〈/a〉
    Keywords: Kinetics ; Peptides/metabolism ; Phosphorylation ; Phosphotyrosine ; Protein-Tyrosine Kinases/*metabolism ; Saccharomyces cerevisiae/*enzymology/metabolism ; Tyrosine/analogs & derivatives/metabolism
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  • 38
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-10-10
    Description: Polypeptide growth factors, regulatory peptides, and a variety of pharmacological agents acting alone or synergistically induce mitogenesis in cultured fibroblasts. The early signals in the membrane, cytosol, and nucleus promoted by these extracellular factors, together with their mitogenic effectiveness, are integrated in a unified hypothesis for the regulation of fibroblast growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rozengurt, E -- New York, N.Y. -- Science. 1986 Oct 10;234(4773):161-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3018928" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bombesin/pharmacology ; Cell Line ; Cell Membrane/metabolism ; Cell Nucleus/metabolism ; Cyclic AMP/metabolism ; Cytosol/metabolism ; DNA/biosynthesis ; Enzyme Activation ; Growth Substances/*pharmacology ; Interphase ; Ions/metabolism ; Mitogens/*pharmacology ; Mitosis ; Models, Biological ; Oncogenes ; Phosphorylation ; Platelet-Derived Growth Factor/*pharmacology ; Protein Kinase C/metabolism ; Receptor, Epidermal Growth Factor ; Receptors, Cell Surface/metabolism
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  • 39
    Publication Date: 1986-11-14
    Description: The expression of the cellular src gene product pp60c-src was examined in an embryonal carcinoma cell line that differentiates in vitro into neuronlike cells after being treated with retinoic acid. Quantitative and qualitative changes in c-src expression accompanied the events associated with neuronal differentiation. The levels of pp60c-src increased 8- to 20-fold during the period when the cells elaborated neuritic processes and expressed neuron-specific proteins. The electrophoretic mobility of pp60c-src induced in these cells was retarded in comparison with that in untreated cells or in treated cells before neurite elaboration. The shift in electrophoretic mobility was due to an alteration in the amino terminal 16,000 daltons of pp60c-src and similar to an alteration of c-src protein found in neural tissues and in pure primary cultures of neuronal cells. These results indicate that expression of pp60c-src induced by retinoic acid in these embryonal carcinoma cells mimics the expression of c-src in developing neurons. Therefore, this embryonal carcinoma cell line provides a model system to investigate the function of the src protein in neuronal differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lynch, S A -- Brugge, J S -- Levine, J M -- CA 28146/CA/NCI NIH HHS/ -- NS 21198/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1986 Nov 14;234(4778):873-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3095923" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Differentiation/drug effects ; Cell Line ; Embryonal Carcinoma Stem Cells ; Gene Expression Regulation ; Neoplastic Stem Cells/cytology/*metabolism ; Neurons/cytology ; Oncogene Protein pp60(v-src) ; Phosphorylation ; Protein-Tyrosine Kinases/metabolism ; Retroviridae Proteins/genetics/*metabolism ; Tretinoin/pharmacology
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  • 40
    Publication Date: 1986-06-27
    Description: Antibodies were raised against a synthetic peptide corresponding to 14 amino acid residues at the COOH-terminus of a protein deduced from the human c-erbB-2 nucleotide sequence. These antibodies immunoprecipitated a 185-kilodalton glycoprotein from MKN-7 adenocarcinoma cells. Incubation of the immunoprecipitates with (gamma-32P)ATP resulted in the phosphorylation of this protein on tyrosine residues. These results indicate that the human c-erbB-2 gene product is the 185-kilodalton glycoprotein that is associated with tyrosine kinase activity. Although the c-erbB-2 protein was predicted to encode a protein very similar to epidermal growth factor (EGF) receptor, EGF did not stimulate this kinase activity either in vivo or in vitro.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Akiyama, T -- Sudo, C -- Ogawara, H -- Toyoshima, K -- Yamamoto, T -- New York, N.Y. -- Science. 1986 Jun 27;232(4758):1644-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3012781" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Epidermal Growth Factor/metabolism ; *Genes ; Glycoproteins/genetics/isolation & purification/*metabolism ; HeLa Cells/metabolism ; Humans ; Molecular Weight ; Oncogenes ; Phosphorylation ; Protein-Tyrosine Kinases/*metabolism ; Receptor, Epidermal Growth Factor ; Receptors, Cell Surface/metabolism
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  • 41
    Publication Date: 1986-03-28
    Description: The gag-pol gene of HTLV-III (human T-lymphotropic virus), the virus linked to AIDS (acquired immune deficiency syndrome), was expressed in yeast, and processing of the gag precursor into proteins of the same size as those in the virion was observed. Processing of the gag gene in yeast cells mimics the process that naturally occurs in mammalian cells during maturation of virions. Therefore it was possible to perform mutational analysis of the virus genome to localize the gene that codes for the protease function to the amino terminal coding region of the pol gene. Since this region overlaps the gag gene, it is likely that ribosomal frameshifting occurs from gag to pol. Antibodies in all of the AIDS patients' sera tested recognized the yeast synthesized gag proteins, although the sera showed differences in relative reactivity to the individual gag proteins and the precursor. This yeast system should be valuable not only for production of viral proteins for diagnostic or vaccine purposes but also for analysis of the genetics and biochemistry of viral gene functions--parameters that are difficult to study otherwise with this virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kramer, R A -- Schaber, M D -- Skalka, A M -- Ganguly, K -- Wong-Staal, F -- Reddy, E P -- New York, N.Y. -- Science. 1986 Mar 28;231(4745):1580-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2420008" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/immunology ; Base Sequence ; Deltaretrovirus/enzymology/*genetics ; Gene Products, gag ; *Genes, Viral ; Humans ; Peptide Hydrolases/*genetics/metabolism ; Phosphorylation ; Protein Processing, Post-Translational ; RNA-Directed DNA Polymerase/genetics ; Retroviridae Proteins/genetics/immunology/*metabolism ; Saccharomyces cerevisiae/genetics
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  • 42
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-04-04
    Description: Contraction and myosin light-chain phosphorylation were measured in electrically stimulated tracheal smooth muscle. Latencies for the onset of force, stiffness, and light-chain phosphorylation were 500 milliseconds. Myosin light chain was phosphorylated from 0.04 to 0.80 mole of phosphate per mole of light chain with a pseudo-first-order rate of 1.1 per second with no evidence of an ordered or negatively cooperative process. Following the period of latency, stiffness increased with phosphorylation and both increased more rapidly than isometric force. The linear relation between stiffness and phosphorylation during activation suggests independent attachment of each myosin head upon phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kamm, K E -- Stull, J T -- HL 26043/HL/NHLBI NIH HHS/ -- HL 32607/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1986 Apr 4;232(4746):80-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3754063" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carbachol/pharmacology ; Electric Stimulation ; In Vitro Techniques ; Kinetics ; *Muscle Contraction/drug effects ; Muscle, Smooth/*physiology ; Myosin-Light-Chain Kinase ; Myosins/*metabolism ; Phosphorylation ; Protein Kinases/metabolism ; Trachea/physiology
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  • 43
    Publication Date: 1986-03-21
    Description: The Rous sarcoma virus oncogene product, pp60v-src, transforms cultured fibroblasts but its corresponding proto-oncogene product, pp60c-src, does not. Both proteins are known to be protein-tyrosine kinases. Published results suggest that the kinase activity of pp60c-src is inhibited relative to that of pp60v-src, due perhaps to phosphorylation of a tyrosine in pp60c-src that is not phosphorylated in pp60v-src. In this study, it was observed that the tyrosine phosphorylated in pp60c-src is Tyr527, six residues from the COOH-terminus of the protein. The region of pp60c-src from residue 515 to the COOH-terminus, including Tyr527, has been replaced with a different sequence in pp60v-src. Thus, the increase in transforming ability and kinase activity that occurred in the genesis of pp60v-src may have resulted from the loss of a tyrosine involved in negative regulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cooper, J A -- Gould, K L -- Cartwright, C A -- Hunter, T -- CA-17096/CA/NCI NIH HHS/ -- CA-28151/CA/NCI NIH HHS/ -- CA-28458/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1986 Mar 21;231(4744):1431-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2420005" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avian Sarcoma Viruses/genetics ; Cell Transformation, Neoplastic/metabolism ; Chick Embryo ; Chickens ; Fibroblasts/metabolism ; Oncogene Protein pp60(v-src) ; Oncogenes ; Phosphorylation ; Protein Kinases/metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins pp60(c-src) ; Proto-Oncogenes ; Retroviridae Proteins/metabolism ; Tyrosine/*metabolism
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  • 44
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-11-15
    Description: Substantial evidence suggests that calcium has a pivotal role in regulating the initial events through which insulin alters plasma membrane metabolism. Because binding of insulin to its receptor represents the initial site of insulin action in the plasma membrane, studies were undertaken to determine whether the insulin receptor is a calmodulin-binding protein. Preparations enriched in the insulin receptor and calmodulin-binding proteins were isolated from detergent-solubilized rat adipocyte membranes by chromatography with wheat germ agglutinin agarose and calmodulin-conjugated Sepharose, respectively. Substantial purification of a manganese-dependent, insulin-sensitive phosphoprotein of 95K identified as the beta subunit of the insulin receptor was accomplished. Binding and photocovalent cross-linking of iodine-125-labeled calmodulin to these affinity-purified preparations and to isolated plasma membranes, followed by immunoadsorption with insulin receptor antibodies bound to protein A Sepharose, resulted in significant purification of a binding complex of 110K to 140K. These results indicate that the adipocyte insulin receptor or a polypeptide closely associated with the receptor is a calmodulin-binding protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Graves, C B -- Goewert, R R -- McDonald, J M -- AM-25897/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1985 Nov 15;230(4727):827-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3904001" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/cytology ; Animals ; Calmodulin/metabolism ; Calmodulin-Binding Proteins/isolation & purification/*metabolism ; Cell Membrane/metabolism ; Insulin/metabolism ; Phosphorylation ; Rats ; Receptor, Insulin/isolation & purification/*metabolism
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  • 45
    Publication Date: 1985-09-27
    Description: When vole cells that had been transformed by Rous sarcoma virus were treated with the tumor-promoting phorbol ester 12-O-tetradecanoyl-13-acetate (TPA), specific phosphorylation of pp60v-src was increased. Partial V8 protease mapping indicated that the increased phosphorylation occurred exclusively on serine residues located in the amino terminus of the molecule. Treatment of cells with dimethyl sulfoxide or 4 alpha-phorbol-12,13-didecanoate did not elicit this response. Two-dimensional tryptic phosphopeptide mapping of pp60v-src immunoprecipitated from untreated and TPA-treated cells indicated that a specific tryptic amino-terminal peptide was hyperphosphorylated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Purchio, A F -- Shoyab, M -- Gentry, L E -- New York, N.Y. -- Science. 1985 Sep 27;229(4720):1393-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2994221" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arvicolinae ; Carcinogens/*pharmacology ; Cell Transformation, Neoplastic/metabolism ; Cells, Cultured ; Dimethyl Sulfoxide/pharmacology ; Mice ; Mice, Inbred BALB C ; Oncogene Protein pp60(v-src) ; Phorbol Esters/pharmacology ; Phosphorylation ; Protein Kinase C ; Protein Kinases/metabolism ; Receptor, Epidermal Growth Factor ; Receptors, Cell Surface/metabolism ; Sarcoma, Avian/*genetics ; Tetradecanoylphorbol Acetate/pharmacology ; Viral Proteins/*metabolism
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  • 46
    Publication Date: 1985-06-14
    Description: The phosphorylation of 2-deoxyglucose by the mammalian brain is used as an index of the brain's energy metabolism. The results of phosphorus-31 nuclear magnetic resonance (31P NMR) monitoring of conscious animals in vivo showed rapid phosphorylation of 2-deoxyglucose by brain tissue. The rate of phosphorylation as determined by 31P NMR was consistent with results achieved by tracer methods using carbon-14-labeled 2-deoxyglucose. However, the disappearance of 2-deoxyglucose-6-phosphate was shown to be faster than that reported by tracer studies and occurred without alterations of intracellular pH and energy homeostasis. These results were confirmed by gas chromatography and mass spectroscopy. It is postulated that 2-deoxyglucose may be metabolized in several ways, including dephosphorylation by a hexose phosphatase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Deuel, R K -- Yue, G M -- Sherman, W R -- Schickner, D J -- Ackerman, J J -- AM-20579/AM/NIADDK NIH HHS/ -- GM-30331/GM/NIGMS NIH HHS/ -- RR 00954/RR/NCRR NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Jun 14;228(4705):1329-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4001946" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*metabolism ; Deoxy Sugars/*metabolism ; Deoxyglucose/*metabolism ; Kinetics ; Magnetic Resonance Spectroscopy ; Phosphorylation ; Rats ; Rats, Inbred Strains
    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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  • 47
    Publication Date: 1985-04-19
    Description: The c-fms proto-oncogene is a member of a gene family that has been implicated in tumorigenesis. Glycoproteins encoded by c-fms were identified in cat spleen cells by means of an immune-complex kinase assay performed with monoclonal antibodies to v-fms-coded epitopes. The major form of the normal cellular glycoprotein has an apparent molecular weight of 170,000 and, like the product of the viral oncogene, serves as a substrate for an associated tyrosine-specific protein kinase activity in vitro. The results suggest that the transforming glycoprotein specified by v-fms is a truncated form of a c-fms-coded growth factor receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rettenmier, C W -- Chen, J H -- Roussel, M F -- Sherr, C J -- 1 RO1 CA 38187/CA/NCI NIH HHS/ -- RR-05584-20/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1985 Apr 19;228(4697):320-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2580348" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/immunology ; Cats ; Glycoproteins/immunology/*metabolism ; Humans ; Mice ; Molecular Weight ; Neoplasm Proteins/immunology/*metabolism ; *Oncogenes ; Phosphorylation ; Protein Kinases/*metabolism ; Protein-Tyrosine Kinases ; RNA/metabolism ; Rats
    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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  • 48
    Publication Date: 1985-07-19
    Description: In experiments designed to study the mechanism by which peptide hormones binding to their plasma membrane receptors stimulate the expression of specific genes, the transcription of two neuroendocrine genes, prolactin and growth hormone, was analyzed in a rat pituitary cell line. The results showed that cyclic adenosine monophosphate (cyclic AMP) stimulates the transcription of discrete subsets of eukaryotic genes by at least two independent molecular mechanisms. Cyclic AMP stimulated growth hormone gene transcription and phosphorylation of a 19,000-dalton nuclear protein; this appears to reflect direct nuclear actions of the cyclic AMP-dependent protein kinase. In contrast, the stimulation by cyclic AMP of prolactin gene transcription appears to reflect activation of a discrete calcium-dependent event.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Waterman, M -- Murdoch, G H -- Evans, R M -- Rosenfeld, M G -- New York, N.Y. -- Science. 1985 Jul 19;229(4710):267-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990047" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cell Membrane/metabolism ; Cobalt/pharmacology ; Colforsin ; Cyclic AMP/*physiology ; Diterpenes/pharmacology ; Growth Hormone/biosynthesis/genetics ; Phosphorylation ; Pituitary Gland/cytology ; Prolactin/biosynthesis/genetics ; Protein Kinases/physiology ; Rats ; Thyrotropin-Releasing Hormone/pharmacology ; *Transcription, Genetic/drug effects
    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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