ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Phosphorylation
  • American Association for the Advancement of Science (AAAS)  (22)
  • American Institute of Physics (AIP)
  • Institute of Physics
  • Oxford University Press
  • 1995-1999
  • 1990-1994  (22)
  • 1990  (22)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (22)
  • American Institute of Physics (AIP)
  • Institute of Physics
  • Oxford University Press
  • Springer  (2)
Years
  • 1995-1999
  • 1990-1994  (22)
Year
  • 1
    facet.materialart.
    Unknown
    Cell cycle control of DNA replication by a homologue from human cells of the p34cdc2 protein kinase (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-11-09
    Description: The regulation of DNA replication during the eukaryotic cell cycle was studied in a system where cell free replication of simian virus 40 (SV40) DNA was used as a model for chromosome replication. A factor, RF-S, was partially purified from human S phase cells based on its ability to activate DNA replication in extracts from G1 cells. RF-S contained a human homologue of the Schizosaccharomyces pombe p34cdc2 kinase, and this kinase was necessary for RF-S activity. The limiting step in activation of the p34 kinase at the G1 to S transition may be its association with a cyclin since addition of cyclin A to a G1 extract was sufficient to start DNA replication. These observations suggest that the role of p34cdc2 in controlling the start of DNA synthesis has been conserved in evolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉D'Urso, G -- Marraccino, R L -- Marshak, D R -- Roberts, J M -- New York, N.Y. -- Science. 1990 Nov 9;250(4982):786-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Basic Sciences, Fred Hutchinson Cancer Center, Seattle, WA 98104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2173140" target="_blank"〉PubMed〈/a〉
    Keywords: Burkitt Lymphoma ; CDC2 Protein Kinase/genetics/*physiology ; *Cell Cycle ; Cyclins/pharmacology ; *DNA Replication ; Humans ; Interphase ; Phosphorylation ; Schizosaccharomyces/enzymology ; Simian virus 40/*genetics/physiology ; Tumor Cells, Cultured ; *Virus Replication
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 2
    facet.materialart.
    Unknown
    Failure to phosphorylate the retinoblastoma gene product in senescent human fibroblasts (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-08-10
    Description: Heterokaryon studies suggest that senescent and quiescent human diploid fibroblasts (HDF) contain a common inhibitor of entry into S phase. DNA synthesis can be induced in senescent and quiescent HDF by fusing them with cells containing DNA viral oncogenes such as SV40 T antigen, adenovirus E1A, or human papillomavirus E7. Both senescent and quiescent HDF contained the unphosphorylated form (p110Rb) of the retinoblastoma protein, a putative inhibitor of proliferation. After serum stimulation, senescent HDF did not phosphorylate p110Rb and did not enter S phase, whereas quiescent HDF phosphorylated p110Rb and entered S phase. These findings, combined with the observations that T antigen, E1A, and E7 form complexes with, and presumably inactivate, unphosphorylated p110Rb, suggest that failure to phosphorylate p110Rb may be an immediate cause of failure to enter S phase in senescent HDF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stein, G H -- Beeson, M -- Gordon, L -- AG 00947/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1990 Aug 10;249(4969):666-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder 80309-0347.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2166342" target="_blank"〉PubMed〈/a〉
    Keywords: Adenovirus Early Proteins ; Antigens, Polyomavirus Transforming/genetics ; Cell Division ; Cell Line ; Fibroblasts/cytology/metabolism ; Humans ; Interphase ; Molecular Weight ; Nuclear Proteins/*metabolism ; Oncogene Proteins, Viral/metabolism ; Oncogenes ; Papillomaviridae/genetics ; Phosphoproteins/isolation & purification/*metabolism ; Phosphorylation ; Retinoblastoma Protein ; Simian virus 40/genetics/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 3
    facet.materialart.
    Unknown
    Autophosphorylation of protein kinase C at three separated regions of its primary sequence (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-07-27
    Description: The major autophosphorylation sites of the rat beta II isozyme of protein kinase C were identified. The modified threonine and serine residues were found in the amino-terminal peptide, the carboxyl-terminal tail, and the hinge region between the regulatory lipid-binding domain and the catalytic kinase domain. Because this autophosphorylation follows an intrapeptide mechanism, extraordinary flexibility of the protein is necessary to phosphorylate the three regions. Comparison of the sequences surrounding the modified residues showed no obvious recognition motif nor any similarity to substrate phosphorylation sites, suggesting that proximity to the active site may be the primary criterion for their phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flint, A J -- Paladini, R D -- Koshland, D E Jr -- DK09765/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1990 Jul 27;249(4967):408-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2377895" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Brain/enzymology ; Cloning, Molecular ; Isoenzymes/genetics/*metabolism ; Molecular Sequence Data ; Peptide Fragments/isolation & purification/metabolism ; Phosphorylation ; Protein Conformation ; Protein Kinase C/genetics/*metabolism ; Rats ; Recombinant Proteins/metabolism ; Signal Transduction ; Trypsin
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 4
    facet.materialart.
    Unknown
    beta-Arrestin: a protein that regulates beta-adrenergic receptor function (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-06-22
    Description: Homologous or agonist-specific desensitization of beta-adrenergic receptors is thought to be mediated by a specific kinase, the beta-adrenergic receptor kinase (beta ARK). However, recent data suggest that a cofactor is required for this kinase to inhibit receptor function. The complementary DNA for such a cofactor was cloned and found to encode a 418-amino acid protein homologous to the retinal protein arrestin. The protein, termed beta-arrestin, was expressed and partially purified. It inhibited the signaling function of beta ARK-phosphorylated beta-adrenergic receptors by more than 75 percent, but not that of rhodopsin. It is proposed that beta-arrestin in concert with beta ARK effects homologous desensitization of beta-adrenergic receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lohse, M J -- Benovic, J L -- Codina, J -- Caron, M G -- Lefkowitz, R J -- DK19318/DK/NIDDK NIH HHS/ -- HL16037/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 Jun 22;248(4962):1547-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Medicine, Biochemistry and Cell Biology, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2163110" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens/*genetics/isolation & purification/pharmacology ; Arrestin ; Blotting, Northern ; Chromatography, Ion Exchange ; Cloning, Molecular ; *Cyclic AMP-Dependent Protein Kinases ; DNA/genetics ; Eye Proteins/*genetics/isolation & purification/pharmacology ; Gene Expression Regulation ; Molecular Sequence Data ; Phosphodiesterase Inhibitors/*pharmacology ; Phosphorylation ; Protein Kinases/*pharmacology ; RNA, Messenger/analysis ; Receptors, Adrenergic, beta/*drug effects/physiology ; Transfection ; beta-Adrenergic Receptor Kinases
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 5
    facet.materialart.
    Unknown
    Direct interaction of a ligand for the erbB2 oncogene product with the EGF receptor and p185erbB2 (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-09-28
    Description: The erbB2 oncogene encodes a 185-kilodalton transmembrane protein whose sequence is similar to the epidermal growth factor receptor (EGFR). A 30-kilodalton factor (gp30) secreted from MDA-MB-231 human breast cancer cells was shown to be a ligand for p185erbB2. An antibody to EGFR abolished the tyrosine phosphorylation induced by EGF and transforming growth factor-alpha (TGF-alpha) but only partially blocked that produced by gp30 in SK-BR-3 breast cancer cells. In two cell lines that overexpress erbB2 but do not expresss EGFR (MDA-MB-453 breast cancer cells and a Chinese hamster ovary cell line that had been transfected with erbB2), phosphorylation of p185erbB2 was induced only by gp30. The gp30 specifically inhibited the growth of cells that overexpressed p185erbB2. An antibody to EGFR had no effect on the inhibition of SK-BR-3 cell colony formation obtained with gp30. Thus, it appeared that gp30 interacted directly with the EGFR and erbB2. Direct binding of gp30 to p185erbB2 was confirmed by binding competition experiments, where gp30 was found to displace the p185erbB2 binding of a specific antibody to p185erbB2. The evidence described here suggests that gp30 is a ligand for p185erbB2.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lupu, R -- Colomer, R -- Zugmaier, G -- Sarup, J -- Shepard, M -- Slamon, D -- Lippman, M E -- New York, N.Y. -- Science. 1990 Sep 28;249(4976):1552-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vincent T. Lombardi Cancer Research Center, Georgetown University Medical Center, Washington, DC 20007.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2218496" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Binding, Competitive ; Breast Neoplasms ; Cell Line ; Chromatography, Affinity ; Female ; Humans ; Kinetics ; Ligands ; Molecular Weight ; Phosphorylation ; Protein-Tyrosine Kinases/metabolism ; Proto-Oncogene Proteins/genetics/immunology/*metabolism ; Proto-Oncogenes ; Receptor, Epidermal Growth Factor/isolation & purification/*metabolism ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 6
    facet.materialart.
    Unknown
    Regulation of an enzyme by phosphorylation at the active site (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-08-31
    Description: The isocitrate dehydrogenase of Escherichia coli is an example of a ubiquitous class of enzymes that are regulated by covalent modification. In the three-dimensional structure of the enzyme-substrate complex, isocitrate forms a hydrogen bond with Ser113, the site of regulatory phosphorylation. The structures of Asp113 and Glu113 mutants, which mimic the inactivation of the enzyme by phosphorylation, show minimal conformational changes from wild type, as in the phosphorylated enzyme. Calculations based on observed structures suggest that the change in electrostatic potential when a negative charge is introduced either by phosporylation or site-directed mutagenesis is sufficient to inactivate the enzyme. Thus, direct interaction at a ligand binding site is an alternative mechanism to induced conformational changes from an allosteric site in the regulation of protein activity by phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hurley, J H -- Dean, A M -- Sohl, J L -- Koshland, D E Jr -- Stroud, R M -- GM 24485/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Aug 31;249(4972):1012-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2204109" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Escherichia coli/*enzymology/genetics ; Homeostasis ; Isocitrate Dehydrogenase/genetics/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Phosphorylation ; Protein Conformation
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 7
    facet.materialart.
    Unknown
    In vivo receptor-mediated phosphorylation of a G protein in Dictyostelium (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-05-04
    Description: Extracellular adenosine 3',5'-monophosphate (cAMP) serves multiple roles in Dictyostelium development, acting as a chemoattractant, a cell-cell signaling molecule, and an inducer of differentiation. The Dictyostelium G-protein alpha subunit G alpha 2 appears to be the major transducer linking the surface cAMP receptor to these intracellular responses. On stimulation of cells with cAMP, G alpha 2 is phosphorylated on one or more serine residues, resulting in an alteration of its electrophoretic mobility. Phosphorylation of G alpha 2 is triggered by increased occupancy of the surface cAMP receptor and is rapid and transient, coinciding with the time course of activation of physiological responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gundersen, R E -- Devreotes, P N -- 28007/PHS HHS/ -- New York, N.Y. -- Science. 1990 May 4;248(4955):591-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2110382" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Membrane/metabolism ; Dictyostelium/*metabolism ; GTP-Binding Proteins/isolation & purification/*metabolism ; Macromolecular Substances ; Phosphates/metabolism ; Phosphorus Radioisotopes ; Phosphorylation ; Phosphoserine/analysis ; Receptors, Cyclic AMP/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 8
    facet.materialart.
    Unknown
    An insulin-stimulated protein kinase similar to yeast kinases involved in cell cycle control (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-07-06
    Description: A protein kinase characterized by its ability to phosphorylate microtubule-associated protein-2 (MAP2), is thought to be an early intermediate in an insulin-stimulated phosphorylation cascade and in a variety of other mammalian cell responses to extracellular signals. A complementary DNA that encodes this protein serine-threonine kinase has been cloned, and the protein designated extracellular signal-regulated kinase 1 (ERK1). ERK1 has striking similarity to two protein kinases, KSS1 and FUS3, from yeast. The yeast kinases function in an antagonistic manner to regulate the cell cycle in response to mating factors. Thus, ERK1 and the two yeast kinases constitute a family of evolutionarily conserved enzymes involved in regulating the response of eukaryotic cells to extracellular signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boulton, T G -- Yancopoulos, G D -- Gregory, J S -- Slaughter, C -- Moomaw, C -- Hsu, J -- Cobb, M H -- DK 01918/DK/NIDDK NIH HHS/ -- DK 34128/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1990 Jul 6;249(4964):64-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Texas Southwestern Graduate School of Biomedical Sciences, Dallas 75235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2164259" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Calcium-Calmodulin-Dependent Protein Kinases ; Cell Cycle/*physiology ; Cell Line ; Central Nervous System/*enzymology ; DNA/*genetics ; Fibroblasts/enzymology ; Humans ; Insulin/pharmacology ; Mitogen-Activated Protein Kinase 3 ; *Mitogen-Activated Protein Kinases ; Molecular Sequence Data ; Phosphorylation ; Protein Kinases/genetics/*metabolism ; Rats ; Receptor, Insulin/metabolism ; Yeasts/enzymology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 9
    facet.materialart.
    Unknown
    cdc2 gene expression at the G1 to S transition in human T lymphocytes (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-11-09
    Description: The product of the cdc2 gene, designated p34cdc2, is a serine-threonine protein kinase that controls entry of eukaryotic cells into mitosis. Freshly isolated human T lymphocytes (G0 phase) were found to have very low amounts of p34cdc2 and cdc2 messenger RNA. Expression of cdc2 increased 18 to 24 hours after exposure of T cells to phytohemagglutinin, coincident with the G1 to S transition. Antisense oligodeoxynucleotides could reduce the increase in cdc2 expression and inhibited DNA synthesis, but had no effect on several early and mid-G1 events, including blastogenesis and expression of interleukin-2 receptors, transferrin receptors, c-myb, and c-myc. Induction of cdc2 required prior induction of c-myb and c-myc. These results suggest that cdc2 induction is part of an orderly sequence of events that occurs at the G1 to S transition in T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Furukawa, Y -- Piwnica-Worms, H -- Ernst, T J -- Kanakura, Y -- Griffin, J D -- CA36167/CA/NCI NIH HHS/ -- CA47843/CA/NCI NIH HHS/ -- CA50767/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Nov 9;250(4982):805-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Tumor Immunology, Dana-Farber Cancer Institute, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2237430" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Blotting, Northern ; CDC2 Protein Kinase/biosynthesis/*genetics ; Cells, Cultured ; DNA/biosynthesis/genetics ; Flow Cytometry ; *G1 Phase ; *Gene Expression Regulation ; Genes, Retinoblastoma ; Genes, myc ; Humans ; Lymphocyte Activation ; Molecular Sequence Data ; Phosphorylation ; Polymerase Chain Reaction ; Proto-Oncogene Proteins/genetics ; Proto-Oncogene Proteins c-myb ; RNA, Messenger/biosynthesis/genetics ; *S Phase ; T-Lymphocytes/*cytology/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 10
    facet.materialart.
    Unknown
    Regulation of activity of a transcriptional anti-terminator in E. coli by phosphorylation in vivo (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-08-03
    Description: Expression of the bgl operon of Escherichia coli is regulated in vitro by phosphorylation and dephosphorylation of a positive regulatory protein, BglG, which functions in its nonphosphorylated state as a transcriptional antiterminator. The degree of phosphorylation of BglG in vivo was shown to be dependent on the cellular levels of BglF protein, which is both the BglG kinase and phosphatase. The degree of phosphorylation of BglG also depended on the presence or absence of a beta-glucoside, the inducer of operon expression. Addition of inducer to cells in growth medium resulted in rapid dephosphorylation of phosphorylated BglG. The bgl operon is thus regulated by a sensory system that modulates gene expression by protein phosphorylation and dephosphorylation in response to the external levels of inducer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Amster-Choder, O -- Wright, A -- New York, N.Y. -- Science. 1990 Aug 3;249(4968):540-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Microbiology, Tufts University Health Sciences Campus, Boston, MA 02111.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2200123" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/isolation & purification/*metabolism ; Escherichia coli/drug effects/*genetics ; *Gene Expression Regulation, Bacterial ; *Genes, Regulator ; Molecular Weight ; Operon ; Phosphorylation ; Plasmids ; *RNA-Binding Proteins ; Rifampin/pharmacology ; *Terminator Regions, Genetic ; *Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 11
    facet.materialart.
    Unknown
    Binding of transforming protein, P47gag-crk, to a broad range of phosphotyrosine-containing proteins (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-06-22
    Description: Although the oncogene product of CT10 virus, P47gag-crk, does not itself phosphorylate proteins at tyrosine residues, it elevates phosphotyrosine in transformed cells. The P47gag-crk oncoprotein contains SH2 and SH3 domains, which are conserved in several proteins involved in signal transduction, including nonreceptor tyrosine kinases. P47gag-crk bound in vitro to phosphotyrosine-containing proteins from crk-transformed cells and from cells transformed by oncogenic tyrosine kinases. The association between P47gag-crk and p60v-src, a phosphotyrosine-containing protein, was abolished by dephosphorylation of p60v-src. This suggests that the SH2 and SH3 regions function to regulate protein interactions in a phosphotyrosine-dependent manner.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matsuda, M -- Mayer, B J -- Fukui, Y -- Hanafusa, H -- AI 07233/AI/NIAID NIH HHS/ -- CA44356/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Jun 22;248(4962):1537-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1694307" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line, Transformed ; Cell Transformation, Viral ; Oncogene Protein v-crk ; Phosphorylation ; Phosphotyrosine ; Precipitin Tests ; Protein Binding ; Protein-Tyrosine Kinases/*metabolism ; Proto-Oncogene Proteins/*metabolism ; Retroviridae Proteins/*metabolism ; *Signal Transduction ; Tyrosine/*analogs & derivatives/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 12
    facet.materialart.
    Unknown
    T cell antigen receptor-mediated activation of phospholipase C requires tyrosine phosphorylation (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-03-30
    Description: Triggering of the antigen-specific T cell receptor-CD3 complex (TCR-CD3) stimulates a rapid phospholipase C-mediated hydrolysis of inositol phospholipids, resulting in the production of second messengers and in T cell activation and proliferation. The role of tyrosine phosphorylation in these events was investigated with a tyrosine protein kinase (TPK) inhibitor, genistein. At doses that inhibited TPK activity and tyrosine phosphorylation of the TCR zeta subunit, but not phospholipase C activity, genistein prevented TCR-CD3-mediated phospholipase C activation, interleukin-2 receptor expression, and T cell proliferation. These findings indicate that tyrosine phosphorylation is an early and critical event that most likely precedes, and is a prerequisite for, inositol phospholipid breakdown during receptor-mediated T cell activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mustelin, T -- Coggeshall, K M -- Isakov, N -- Altman, A -- AI28197/AI/NIAID NIH HHS/ -- CA35299/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Mar 30;247(4950):1584-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Scripps Clinic and Research Foundation, Immunology Department/IMM3, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2138816" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD3 ; Antigens, Differentiation, T-Lymphocyte/*metabolism ; Dose-Response Relationship, Drug ; Enzyme Activation ; Genistein ; Humans ; Hydrolysis ; Isoflavones/pharmacology ; Lymphocyte Activation/drug effects ; Ornithine Decarboxylase/metabolism ; Phospholipids/metabolism ; Phosphorylation ; Protein-Tyrosine Kinases/antagonists & inhibitors/*metabolism ; Receptors, Antigen, T-Cell/*metabolism ; Receptors, Interleukin-2/biosynthesis ; T-Lymphocytes/cytology/enzymology ; Type C Phospholipases/*metabolism ; Tyrosine/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 13
    facet.materialart.
    Unknown
    Phosphorylation of the polymeric immunoglobulin receptor required for its efficient transcytosis (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-05-11
    Description: The endosomal compartment of polarized epithelial cells is a major crossroads for membrane traffic. Proteins entering this compartment from the cell surface are sorted for transport to one of several destinations: recycling to the original cell surface, targeting to lysosomes for degradation, or transcytosis to the opposite surface. The polymeric immunoglobulin receptor (pIgR), which is normally transcytosed from the basolateral to the apical surface, was used as a model to dissect the signals that mediate this sorting event. When exogenous receptor was expressed in Madin-Darby Canine Kidney (MDCK) cells, it was shown that phosphorylation of pIgR at the serine residue at position 664 is required for efficient transcytosis. Replacement of this serine with alanine generated a receptor that is transcytosed only slowly, and appears to be recycled. Conversely, substitution with aspartic acid (which mimics the negative charge of the phosphate group) results in rapid transcytosis. It was concluded that phosphorylation is the signal that directs the pIgR from the endosome into the transcytotic pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Casanova, J E -- Breitfeld, P P -- Ross, S A -- Mostov, K E -- R01-AI-25144/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1990 May 11;248(4956):742-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2110383" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine ; Animals ; Aspartic Acid ; Cell Line ; Cell Membrane/immunology/metabolism ; Endocytosis ; Immunoglobulin A/metabolism ; Kinetics ; Ligands ; Membrane Glycoproteins/metabolism ; Molecular Weight ; Mutation ; Phosphorylation ; Rats ; Receptors, Immunologic ; Secretory Component/genetics/*metabolism ; Serine
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 14
    facet.materialart.
    Unknown
    Complementation of the mitotic activator, p80cdc25, by a human protein-tyrosine phosphatase (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-12-14
    Description: The onset of M phase requires the activation of the pp34 protein kinase in all eukaryotes thus far examined. In Schizosaccharomyces pombe, pp34 is phosphorylated on Tyr15, and dephosphorylation of this residue regulates the initiation of mitosis. In this study, it is shown that dephosphorylation of Tyr15 triggered activation of the pp34-cyclin complex from fission yeast, that a human protein-tyrosine phosphatase can catalyze this event both in vitro and in vivo, and that activation of fission yeast pp34 does not require threonine dephosphorylation. The complementary DNA that encoded the tyrosine phosphatase replaced the mitotic activator p80cdc25, closely associating the cdc25(+)-activating pathway with tyrosine dephosphorylation of pp34.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gould, K L -- Moreno, S -- Tonks, N K -- Nurse, P -- New York, N.Y. -- Science. 1990 Dec 14;250(4987):1573-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Oxford, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1703321" target="_blank"〉PubMed〈/a〉
    Keywords: *Cell Cycle Proteins ; Cyclins/metabolism ; Enzyme Activation ; Fungal Proteins/*metabolism ; Humans ; *Mitosis ; Mutation ; Phosphoprotein Phosphatases/genetics/*metabolism ; Phosphorylation ; Phosphotyrosine ; Protein Kinases/*metabolism ; Protein Tyrosine Phosphatases ; Schizosaccharomyces/genetics/*metabolism ; Transformation, Genetic ; Tyrosine/analogs & derivatives/metabolism ; *ras-GRF1
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 15
    facet.materialart.
    Unknown
    Binding of GAP to activated PDGF receptors (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-03-30
    Description: The ras proto-oncogene products appear to relay intracellular signals via the Ras guanosine triphosphatase (GTPase) activator protein, GAP. In dog epithelial cells expressing human platelet-derived growth factor (PDGF) receptors, binding of PDGF caused approximately one-tenth of the total GAP molecules to complex with the receptor. Studies with mutant PDGF receptors showed that maximum association required both receptor kinase activity and phosphorylatable tyrosine residues at both the identified sites of receptor autophosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kazlauskas, A -- Ellis, C -- Pawson, T -- Cooper, J A -- CA-28151/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Mar 30;247(4950):1578-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Fred Hutchinson Cancer Research Center, Seattle, WA 98104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2157284" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Electrophoresis, Gel, Two-Dimensional ; Electrophoresis, Polyacrylamide Gel ; GTP Phosphohydrolases/metabolism ; GTPase-Activating Proteins ; Humans ; Immunoblotting ; Oncogene Protein p21(ras)/metabolism ; Peptide Mapping ; Phosphopeptides/analysis ; Phosphorylation ; Platelet-Derived Growth Factor/*metabolism ; Precipitin Tests ; Protein Kinases/analysis ; Proteins/*metabolism ; Receptors, Cell Surface/*metabolism ; Receptors, Platelet-Derived Growth Factor ; Tyrosine/metabolism ; ras GTPase-Activating Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 16
    facet.materialart.
    Unknown
    Differential phosphorylation of c-Abl in cell cycle determined by cdc2 kinase and phosphatase activity (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-04-13
    Description: The product of the c-abl proto-oncogene (c-Abl) is phosphorylated on three sites during interphase and seven additional sites during mitosis. Two interphase and all mitotic c-Abl sites are phosphorylated by cdc2 kinase isolated from either interphase or mitotic cells, with the mitotic cdc2 having an 11-fold higher activity. Inhibition of phosphatases with okadaic acid in interphase cells leads to the phosphorylation of c-Abl mitotic sites, indicating that those sites are preferentially dephosphorylated during interphase. The differential phosphorylation of c-Abl in the cell cycle is therefore determined by an equilibrium between cdc2 kinase and protein phosphatase activities. Treatment of interphase cells with okadaic acid leads to a rounded morphology similar to that observed during mitosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kipreos, E T -- Wang, J Y -- CA43054/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Apr 13;248(4952):217-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, San Diego, La Jolla 92093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2183353" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; CDC2 Protein Kinase ; *Cell Cycle ; Cells, Cultured ; Ethers, Cyclic/pharmacology ; Interphase/drug effects ; Mice ; Mice, Inbred Strains ; Molecular Sequence Data ; Molecular Weight ; Okadaic Acid ; Peptide Fragments/isolation & purification ; Peptide Mapping ; Phosphoproteins/*metabolism ; Phosphorylation ; Protein-Tyrosine Kinases/*metabolism ; Proto-Oncogene Proteins/isolation & purification/*metabolism ; Proto-Oncogene Proteins c-abl
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 17
    facet.materialart.
    Unknown
    A 49-kilodalton phosphoprotein in the Drosophila photoreceptor is an arrestin homolog (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-04-27
    Description: The gene encoding the 49-kilodalton protein that undergoes light-induced phosphorylation in the Drosophila photoreceptor has been isolated and characterized. The encoded protein has 401 amino acid residues and a molecular mass of 44,972 daltons, and it shares approximately 42 percent amino acid sequence identity with arrestin (S-antigen), which has been proposed to quench the light-induced cascade of guanosine 3',5'-monophosphate hydrolysis in vertebrate photoreceptors. Unlike the 49-kilodalton protein, however, arrestin, which appears to bind to phosphorylated rhodopsin, has not itself been reported to undergo phosphorylation. In vitro, Ca2+ was the only agent found that would stimulate the phosphorylation of the 49-kilodalton protein. The phosphorylation of this arrestin-like protein in vivo may therefore be triggered by a Ca2+ signal that is likely to be regulated by light-activated phosphoinositide-specific phospholipase C.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamada, T -- Takeuchi, Y -- Komori, N -- Kobayashi, H -- Sakai, Y -- Hotta, Y -- Matsumoto, H -- EY06595/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1990 Apr 27;248(4954):483-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City 73190.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2158671" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Antigens ; Arrestin ; Binding Sites ; Calcium/pharmacology ; Cloning, Molecular ; Cyclic GMP/metabolism ; DNA/genetics ; Drosophila melanogaster/*genetics ; Enzyme Activation/drug effects ; *Eye Proteins ; Isoelectric Point ; Molecular Sequence Data ; Molecular Weight ; Mutation ; Phosphatidylinositol Diacylglycerol-Lyase ; *Phosphoproteins/genetics/metabolism ; Phosphoric Diester Hydrolases/metabolism ; Phosphorylation ; Photoreceptor Cells/*analysis ; Protein Biosynthesis ; Restriction Mapping ; Sequence Homology, Nucleic Acid
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 18
    facet.materialart.
    Unknown
    Regulation of progesterone receptor-mediated transcription by phosphorylation (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-12-21
    Description: The progesterone receptor (PR) in the chicken oviduct is a phosphoprotein that regulates gene transcription in the presence of progesterone. Treatment with progesterone in vivo stimulates phosphorylation of the progesterone receptor. With transient transfection assays, the present work has tested whether phosphorylation participates in the regulation of PR-mediated transcription. Treatment with 8-bromo-cyclic adenosine monophosphate (8-Br cAMP), a stimulator of cAMP-dependent protein kinase [protein kinase A (PKA)], mimicked progesterone-dependent, receptor-mediated transcription in the absence of progesterone. Inhibition of PKA blocked hormone action. Treatment with okadaic acid, an inhibitor of protein phosphatases 1 and 2A, stimulated transcription in a manner similar to that of progesterone. These observations suggest that phosphorylation of the PR or other proteins in the transcription complex can modulate PR-mediated transcription in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Denner, L A -- Weigel, N L -- Maxwell, B L -- Schrader, W T -- O'Malley, B W -- HD-07857/HD/NICHD NIH HHS/ -- HD-22061/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1740-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2176746" target="_blank"〉PubMed〈/a〉
    Keywords: 8-Bromo Cyclic Adenosine Monophosphate/pharmacology ; Animals ; Cell Line ; Chickens ; Female ; Gene Expression Regulation ; Kinetics ; Oviducts/metabolism ; Phosphoprotein Phosphatases/antagonists & inhibitors ; Phosphorylation ; Progesterone/*pharmacology ; Receptors, Progesterone/*metabolism ; *Transcription, Genetic/drug effects ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 19
    facet.materialart.
    Unknown
    Increase of the catalytic activity of phospholipase C-gamma 1 by tyrosine phosphorylation (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-11-30
    Description: Phospholipase C-gamma 1 (PLC-gamma 1), an isozyme of the phosphoinositide-specific phospholipase C family, which occupies a central role in hormonal signal transduction pathways, is an excellent substrate for the epidermal growth factor (EGF) receptor tyrosine kinase. Epidermal growth factor elicits tyrosine phosphorylation of PLC-gamma 1 and phosphatidylinositol 4,5-bisphosphate hydrolysis in various cell lines. The ability of tyrosine phosphorylation to activate the catalytic activity of PLC-gamma 1 was tested. Tyrosine phosphorylation in intact cells or in vitro increased the catalytic activity of PLC-gamma 1. Also, treatment of EGF-activated PLC-gamma 1 with a tyrosine-specific phosphatase substantially decreased the catalytic activity of PLC-gamma 1. These results suggest that the EGF-stimulated formation of inositol 1,4,5-trisphosphate and diacylglycerol in intact cells results, at least in part, from catalytic activation of PLC-gamma 1 through tyrosine phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nishibe, S -- Wahl, M I -- Hernandez-Sotomayor, S M -- Tonks, N K -- Rhee, S G -- Carpenter, G -- CA43720/CA/NCI NIH HHS/ -- GMO7347/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Nov 30;250(4985):1253-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1700866" target="_blank"〉PubMed〈/a〉
    Keywords: Catalysis ; Diglycerides/metabolism ; Enzyme Activation/drug effects ; Epidermal Growth Factor/pharmacology ; Immunosorbent Techniques ; Inositol 1,4,5-Trisphosphate/metabolism ; Isoenzymes/*metabolism ; Kinetics ; Phosphatidylinositol 4,5-Diphosphate ; Phosphatidylinositol Diacylglycerol-Lyase ; Phosphatidylinositols/metabolism ; Phosphoric Diester Hydrolases/*metabolism ; Phosphorylation ; Phosphotyrosine ; Protein-Tyrosine Kinases/metabolism ; Receptor, Epidermal Growth Factor ; Signal Transduction ; Tyrosine/*analogs & derivatives/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 20
    facet.materialart.
    Unknown
    PDGF-induced activation of phospholipase C is not required for induction of DNA synthesis (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-06-29
    Description: Platelet-derived growth factor (PDGF) induction of DNA synthesis is believed to involve activation of phospholipase C (PLC) and subsequent accumulation of inositol 1,4,5-triphosphate [I(1,4,5)P3], increase in intracellular Ca2+, activation of protein kinase C (PKC), and receptor down regulation. Generation of these events is triggered by the tyrosine protein kinase (TPK) activity of the PDGF receptor. The TPK inhibitor genistein blocked PDGF induction of these events, including DNA synthesis, with the exception of receptor down regulation. PDGF-induced phosphotyrosine phosphorylations, including receptor autophosphorylation, were inhibited by genistein. Removal of genistein and PDGF resulted in DNA synthesis without the occurrence of PLC activation. These findings indicate that these early events, with the exception of receptor down regulation, are not necessary for PDGF-induced DNA synthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hill, T D -- Dean, N M -- Mordan, L J -- Lau, A F -- Kanemitsu, M Y -- Boynton, A L -- CA 2942/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Jun 29;248(4963):1660-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Research Center of Hawaii, University of Hawaii, Honolulu 96813.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2163545" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Cells, Cultured ; Chlorides/pharmacology ; DNA Replication/*drug effects ; Dimethyl Sulfoxide/pharmacology ; Enzyme Activation ; Genistein ; Inositol Phosphates/metabolism ; Isoflavones/pharmacology ; Kinetics ; Lithium/pharmacology ; Lithium Chloride ; Mice ; Phosphatidylinositol 4,5-Diphosphate ; Phosphatidylinositols/metabolism ; Phosphorylation ; Platelet-Derived Growth Factor/*pharmacology ; Protein Kinase C/metabolism ; Protein-Tyrosine Kinases/metabolism ; Type C Phospholipases/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 21
    facet.materialart.
    Unknown
    Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-11-16
    Description: Phospholipase C gamma 1 (PLC gamma 1) and p21ras guanosine triphosphatase (GTPase) activating protein (GAP) bind to and are phosphorylated by activated growth factor receptors. Both PLC gamma 1 and GAP contain two adjacent copies of the noncatalytic Src homology 2 (SH2) domain. The SH2 domains of PLC gamma 1 synthesized individually in bacteria formed high affinity complexes with the epidermal growth factor (EGF)- or platelet derived growth factor (PDGF)-receptors in cell lysates, and bound synergistically to activated receptors when expressed together as one bacterial protein. In vitro complex formation was dependent on prior growth factor stimulation and was competed by intracellular PLC gamma 1. Similar results were obtained for binding of GAP SH2 domains to the PDGF-receptor. The isolated SH2 domains of other signaling proteins, such as p60src and Crk, also bound activated PDGF-receptors in vitro. SH2 domains, therefore, provide a common mechanism by which enzymatically diverse regulatory proteins can physically associate with the same activated receptors and thereby couple growth factor stimulation to intracellular signal transduction pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anderson, D -- Koch, C A -- Grey, L -- Ellis, C -- Moran, M F -- Pawson, T -- New York, N.Y. -- Science. 1990 Nov 16;250(4983):979-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular and Developmental Biology, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2173144" target="_blank"〉PubMed〈/a〉
    Keywords: GTPase-Activating Proteins ; Genes, src/*genetics ; Phosphorylation ; Proteins/genetics/*metabolism ; Receptor, Epidermal Growth Factor/genetics/*metabolism ; Receptors, Cell Surface/genetics/*metabolism ; Receptors, Platelet-Derived Growth Factor ; Sequence Homology, Nucleic Acid ; Type C Phospholipases/genetics/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 22
    facet.materialart.
    Unknown
    Growth factors induce phosphorylation of the Na+/H+ antiporter, glycoprotein of 110 kD (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-02-09
    Description: The Na+/H+ antiporter, which regulates intracellular pH in virtually all cells, is one of the best examples of a mitogen- and oncogene-activated membrane target whose activity rapidly changes on stimulation. The activating mechanism is unknown. A Na+/H+ antiporter complementary DNA fragment was expressed in Escherichia coli as a beta-galactosidase fusion protein, and a specific antibody to the fusion protein was prepared. Use of this antibody revealed that the Na+/H+ antiporter is a 110-kilodalton glycoprotein that is phosphorylated in growing cells. Mitogenic activation of resting hamster fibroblasts and A431 human epidermoid cells with epidermal growth factor, thrombin, phorbol esters, or serum, stimulated phosphorylation of the Na+/H+ antiporter with a time course similar to that of the rise in intracellular pH.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sardet, C -- Counillon, L -- Franchi, A -- Pouyssegur, J -- New York, N.Y. -- Science. 1990 Feb 9;247(4943):723-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre de Biochimie-CNRS, Nice, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2154036" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood ; Carrier Proteins/genetics/*metabolism ; Cell Line ; Cricetinae ; DNA/genetics ; Epidermal Growth Factor/pharmacology ; Escherichia coli/genetics ; Fibroblasts/metabolism ; Glycosylation ; Growth Substances/*pharmacology ; Humans ; Immunoblotting ; Mammary Tumor Virus, Mouse/genetics ; Molecular Weight ; Phosphorylation ; Promoter Regions, Genetic ; Recombinant Fusion Proteins/metabolism ; Sodium-Hydrogen Antiporter ; Thrombin/pharmacology ; Transfection ; beta-Galactosidase/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...