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  • Kinetics  (375)
  • National Institutes of Health (U.S.)  (265)
  • American Association for the Advancement of Science (AAAS)  (640)
  • Annual Reviews
  • 1990-1994  (457)
  • 1980-1984  (183)
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  • 1
    Publication Date: 1990-08-10
    Description: The stimulation of phospholipase A2 by thrombin and type 2 (P2)-purinergic receptor agonists in Chinese hamster ovary cells is mediated by the G protein Gi. To delineate alpha chain regulatory regions responsible for control of phospholipase A2, chimeric cDNAs were constructed in which different lengths of the alpha subunit of Gs (alpha s) were replaced with the corresponding sequence of the Gi alpha subunit (alpha i2). When a carboxyl-terminal chimera alpha s-i(38), which has the last 38 amino acids of alpha s substituted with the last 36 residues of alpha i2, was expressed in Chinese hamster ovary cells, the receptor-stimulated phospholipase A2 activity was inhibited, although the chimera could still activate adenylyl cyclase. Thus, alpha s-i(38) is an active alpha s, but also a dominant negative alpha i molecule, indicating that the last 36 amino acids of alpha i2 are a critical domain for G protein regulation of phospholipase A2 activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gupta, S K -- Diez, E -- Heasley, L E -- Osawa, S -- Johnson, G L -- DK37871/DK/NIDDK NIH HHS/ -- GM30324/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Aug 10;249(4969):662-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Basic Sciences, National Jewish Center for Immunology and Respiratory Medicine, Denver, CO 80206.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2166341" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/pharmacology ; Animals ; Arachidonic Acid ; Arachidonic Acids/metabolism ; Cell Line ; Chlorides/pharmacology ; Enzyme Activation ; GTP-Binding Proteins/*genetics/metabolism ; Inositol Phosphates/metabolism ; Kinetics ; Lithium/pharmacology ; Lithium Chloride ; Macromolecular Substances ; *Mutation ; Phospholipases/*metabolism ; Phospholipases A/*metabolism ; Phospholipases A2 ; Receptors, Purinergic/drug effects/*physiology ; Restriction Mapping ; Thrombin/antagonists & inhibitors/*pharmacology ; Transfection
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  • 2
    Publication Date: 1990-08-17
    Description: The transcription factor C/EBP uses a bipartite structural motif to bind DNA. Two protein chains dimerize through a set of amphipathic alpha helices termed the leucine zipper. Highly basic polypeptide regions emerge from the zipper to form a linked set of DNA contact surfaces. In the recently proposed a "scissors grip" model, the paired set of basic regions begin DNA contact at a central point and track in opposite directions along the major groove, forming a molecular clamp around DNA. This model predicts that C/EBP must undertake significant changes in protein conformation as it binds and releases DNA. The basic region of ligand-free C/EBP is highly sensitive to protease digestion. Pronounced resistance to proteolysis occurred when C/EBP associated with its specific DNA substrate. Sequencing of discrete proteolytic fragments showed that prominent sites for proteolysis occur at two junction points predicted by the "scissors grip" model. One junction corresponds to the cleft where the basic regions emerge from the leucine zipper. The other corresponds to a localized nonhelical segment that has been hypothesized to contain an N-cap and facilitate the sharp angulation necessary for the basic region to track continuously in the major groove of DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shuman, J D -- Vinson, C R -- McKnight, S L -- New York, N.Y. -- Science. 1990 Aug 17;249(4970):771-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Research Laboratories, Department of Embryology, Baltimore, MD 21210.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2202050" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; CCAAT-Enhancer-Binding Proteins ; Chromatography, High Pressure Liquid ; DNA/*metabolism ; DNA-Binding Proteins/metabolism ; Kinetics ; Leucine ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Nuclear Proteins/*metabolism ; Peptide Fragments/metabolism ; Peptide Hydrolases/*metabolism ; Protein Conformation ; Transcription Factors/*metabolism ; Trypsin/metabolism
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-12-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pool, R -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1655-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2270476" target="_blank"〉PubMed〈/a〉
    Keywords: *Blood Substitutes/adverse effects ; Hemoglobins/*therapeutic use ; Humans ; National Institutes of Health (U.S.) ; United States ; United States Food and Drug Administration
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-04-06
    Description: The rate of release of guanine nucleotides from the ras proteins (Ras) is extremely slow in the presence of Mg2+. It seemed likely, therefore that a factor might exist to accelerate the release of guanosine diphosphate (GDP), and hence the exchange of GDP for guanosine triphosphate (GTP). Such a factor has now been discovered in rat brain cytosol. Brain cytosol was found to catalyze, by orders of magnitude, the release of guanine nucleotides from recombinant v-H-Ras protein bound with [alpha-32P]GDP. This effect occurred even in the presence of a large excess of Mg2+, but was destroyed by heat or by incubation of the cytosol for an hour at 37 degrees C in the absence of phosphatase inhibitors. The effect was observed with either v-H-Ras or c-H-Ras, but not with p25rab3A, a small G protein with about 30% similarity to Ras. The effect could not be mimicked by addition of recombinant Ras-GAP or purified GEF, a guanine nucleotide exchange factor involved in the regulation of eukaryotic protein synthesis. By gel filtration chromatography, the factor appears to possess a molecular size between 100,000 and 160,000 daltons. This protein (Ras-guanine nucleotide-releasing factor, or Ras-GRF) may be involved in the activation of p21ras.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wolfman, A -- Macara, I G -- CA 43551/CA/NCI NIH HHS/ -- ES 01247/ES/NIEHS NIH HHS/ -- GM 41220/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Apr 6;248(4951):67-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics, University of Rochester Medical Center, NY 14642.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2181667" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding, Competitive ; Brain/metabolism ; Cholic Acids ; Cytosol/*metabolism ; Guanine Nucleotides/*metabolism ; Guanosine 5'-O-(3-Thiotriphosphate) ; Guanosine Diphosphate/*metabolism ; Guanosine Triphosphate/analogs & derivatives/metabolism ; Hot Temperature ; Immunosorbent Techniques ; Kinetics ; Magnesium Chloride/pharmacology ; Molecular Weight ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins p21(ras) ; Rats ; Thionucleotides/metabolism
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-05-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wright, K -- New York, N.Y. -- Science. 1990 May 11;248(4956):682-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2333519" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*microbiology ; Animals ; HIV/isolation & purification/pathogenicity ; Humans ; Liver/microbiology ; Mycoplasma/*isolation & purification/pathogenicity ; National Institutes of Health (U.S.) ; Research/standards ; Research Design ; United States
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  • 6
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-09-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sinsheimer, R L -- New York, N.Y. -- Science. 1990 Sep 21;249(4975):1359.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2402630" target="_blank"〉PubMed〈/a〉
    Keywords: *Human Genome Project ; Humans ; National Institutes of Health (U.S.) ; United States
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-10-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pool, R -- New York, N.Y. -- Science. 1990 Oct 5;250(4977):23-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2218509" target="_blank"〉PubMed〈/a〉
    Keywords: *Electromagnetic Phenomena ; *Environmental Exposure ; Humans ; National Institutes of Health (U.S.) ; Neoplasms/*etiology ; United States ; United States Environmental Protection Agency
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-12-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1990 Dec 21;250(4988):1663.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2270479" target="_blank"〉PubMed〈/a〉
    Keywords: Cost Control ; DNA/*genetics ; Government Agencies ; Human Genome Project/*economics ; Humans ; National Institutes of Health (U.S.) ; United States
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-11-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1990 Nov 9;250(4982):756-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2237425" target="_blank"〉PubMed〈/a〉
    Keywords: Federal Government ; Government Agencies ; *Human Genome Project ; National Institutes of Health (U.S.) ; *Research Design ; Resource Allocation ; United States
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  • 10
    Publication Date: 1990-11-30
    Description: Conducting gramicidin channels form predominantly by the transmembrane association of monomers, one from each side of a lipid bilayer. In single-channel experiments in planar bilayers the two gramicidin analogs, [Val1]gramicidin A (gA) and [4,4,4-F3-Val1]gramicidin A (F3gA), form dimeric channels that are structurally equivalent and have characteristically different conductances. When these gramicidins were added asymmetrically, one to each side of a preformed bilayer, the predominant channel type was the hybrid channel, formed between two chemically dissimilar monomers. These channels formed by the association of monomers residing in each half of the membrane. These results also indicate that the hydrophobic gramicidins are surprisingly membrane impermeant, a conclusion that was confirmed in experiments in which gA was added asymmetrically and symmetrically to preformed bilayers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Connell, A M -- Koeppe, R E 2nd -- Andersen, O S -- GM21342/GM/NIGMS NIH HHS/ -- GM34968/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Nov 30;250(4985):1256-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, Cornell University Medical College, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1700867" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Membrane Permeability ; Chemistry, Physical ; Electric Conductivity ; Gramicidin/*chemistry/metabolism ; Ion Channels/*chemistry/physiology ; Kinetics ; Lipid Bilayers/*chemistry ; Macromolecular Substances ; Molecular Sequence Data ; Physicochemical Phenomena ; Protein Conformation
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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-08-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holden, C -- New York, N.Y. -- Science. 1990 Aug 31;249(4972):980-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2396100" target="_blank"〉PubMed〈/a〉
    Keywords: *Aversive Therapy ; Electroconvulsive Therapy ; Humans ; Intellectual Disability/*therapy ; National Institutes of Health (U.S.) ; Self Mutilation/prevention & control ; United States
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  • 12
    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
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  • 13
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-05-04
    Description: The amino acid sequences of three fragments of cyanogen bromide-digested human placental inositol 1,2-cyclic phosphate 2-phosphohydrolase, an enzyme of the phosphatidylinositol signaling pathway, are identical to sequences within lipocortin III, a member of a family of homologous calcium- and phospholipid-binding proteins that do not have defined physiological functions. Lipocortin III has also been previously identified as placental anticoagulant protein III (PAP III) and calcimedin 35 alpha. Antibodies to PAP III detected PAP III and inositol 1,2-cyclic phosphate 2-phosphohydrolase with identical reactivity on immunoblotting. In addition, inositol 1,2-cyclic phosphate 2-phosphohydrolase was stimulated by the same acidic phospholipids that bind lipocortins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ross, T S -- Tait, J F -- Majerus, P W -- HLBI 14147/HL/NHLBI NIH HHS/ -- HLBI 16634/HL/NHLBI NIH HHS/ -- HLBI 40801/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 May 4;248(4955):605-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, Washington University School of Medicine, St Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2159184" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Annexin A3 ; Annexins ; Calcium-Binding Proteins/*genetics ; Female ; Humans ; Immunoblotting ; Kinetics ; Molecular Sequence Data ; Phosphoric Diester Hydrolases/*genetics/isolation & purification/metabolism ; Placenta/*enzymology ; Pregnancy
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  • 14
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-06-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rubinstein, E -- New York, N.Y. -- Science. 1990 Jun 22;248(4962):1499-507.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2193399" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/history/*microbiology ; *Biomedical Research ; *Cell Line ; *Ethics ; Federal Government ; Government Regulation ; HIV/*isolation & purification ; History, 20th Century ; Humans ; *Information Dissemination ; National Institutes of Health (U.S.) ; United States
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  • 15
    Publication Date: 1990-09-28
    Description: Heparin-binding growth factor-1 (HBGF-1) is an angiogenic polypeptide mitogen for mesoderm- and neuroectoderm-derived cells in vitro and remains biologically active after truncation of the amino-terminal domain (HBGF-1 alpha) of the HBGF-1 beta precursor. Polymerase chain reaction mutagenesis and prokaryotic expression systems were used to prepare a mutant of HBGF-1 alpha lacking a putative nuclear translocation sequence (amino acid residues 21 to 27; HBGF-1U). Although HBGF-1U retains its ability to bind to heparin, HBGF-1U fails to induce DNA synthesis and cell proliferation at concentrations sufficient to induce intracellular receptor-mediated tyrosine phosphorylation and c-fos expression. Attachment of the nuclear translocation sequence from yeast histone 2B at the amino terminus of HBGF-1U yields a chimeric polypeptide (HBGF-1U2) with mitogenic activity in vitro and indicates that nuclear translocation is important for this biological response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Imamura, T -- Engleka, K -- Zhan, X -- Tokita, Y -- Forough, R -- Roeder, D -- Jackson, A -- Maier, J A -- Hla, T -- Maciag, T -- HL 32348/HL/NHLBI NIH HHS/ -- HL 35627/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 Sep 28;249(4976):1567-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, Jerome H. Holland Laboratory for the Biomedical Sciences, American Red Cross, Rockville, MD 20855.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1699274" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding, Competitive ; Cattle ; Cell Division/drug effects ; Cell Line ; Cell Nucleus/metabolism ; Cells, Cultured ; DNA Replication/drug effects ; Endothelium, Vascular/drug effects/metabolism ; Fibroblast Growth Factor 1/*genetics/metabolism/pharmacology ; Kinetics ; Mice ; Mitogens/pharmacology ; Molecular Sequence Data ; *Mutation ; Oligonucleotide Probes ; Receptors, Mitogen/metabolism ; Receptors, Vascular Endothelial Growth Factor ; Recombinant Proteins/metabolism/pharmacology ; Transcription, Genetic/drug effects
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  • 16
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-02-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abelson, P H -- New York, N.Y. -- Science. 1990 Feb 2;247(4942):513.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2300807" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antineoplastic Agents/pharmacology ; Drug Evaluation, Preclinical ; Drug Screening Assays, Antitumor ; Humans ; National Institutes of Health (U.S.) ; *Plants, Medicinal ; Tumor Cells, Cultured/drug effects ; United States
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  • 17
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-06-29
    Description: Soluble and hydrophobic lipid breakdown products have a variety of important signaling roles in cells. Here sphingoid bases derived in cells from sphingolipid breakdown are shown to have a potent and direct effect in mediating calcium release from intracellular stores. Sphingosine must be enzymically converted within the cell to a product believed to be sphingosine-1-phosphate, which thereafter effects calcium release from a pool including the inositol 1,4,5-trisphosphate-sensitive calcium pool. The sensitivity, molecular specificity, and reversibility of the effect on calcium movements closely parallel sphingoid base-mediated inhibition of protein kinase C. Generation of sphingoid bases in cells may activate a dual signaling pathway involving regulation of calcium and protein kinase C, comparable perhaps to the phosphatidylinositol and calcium signaling pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ghosh, T K -- Bian, J -- Gill, D L -- NS19304/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1990 Jun 29;248(4963):1653-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, University of Maryland School of Medicine, Baltimore 21201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2163543" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/pharmacology ; Animals ; Calcimycin/pharmacology ; Calcium/*metabolism ; Cell Line ; Kinetics ; Phosphoric Monoester Hydrolases/metabolism ; Phosphorylcholine/analogs & derivatives/pharmacology ; Protein Kinase C/metabolism ; Second Messenger Systems/drug effects ; Sphingosine/*analogs & derivatives/*pharmacology ; Thermodynamics
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  • 18
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-12-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1990 Dec 7;250(4986):1332.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2255903" target="_blank"〉PubMed〈/a〉
    Keywords: *Institute of Medicine (U.S.) ; National Institutes of Health (U.S.) ; *Research Support as Topic ; United States
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  • 19
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-11-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1990 Nov 30;250(4985):1196-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2244205" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*complications ; Health Policy ; Humans ; National Institutes of Health (U.S.) ; Periodicals as Topic ; Pneumonia, Pneumocystis/complications/*drug therapy ; Steroids/adverse effects/*therapeutic use ; United States
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  • 20
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-10-12
    Description: Voltage-dependent ion channels are responsible for electrical signaling in neurons and other cells. The main classes of voltage-dependent channels (sodium-, calcium-, and potassium-selective channels) have closely related molecular structures. For one member of this superfamily, the transiently voltage-activated Shaker H4 potassium channel, specific amino acid residues have now been identified that affect channel blockade by the small ion tetraethylammonium, as well as the conduction of ions through the pore. Furthermore, variation at one of these amino acid positions among naturally occurring potassium channels may account for most of their differences in sensitivity to tetraethylammonium.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉MacKinnon, R -- Yellen, G -- GM 43949/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Oct 12;250(4978):276-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Physiology, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2218530" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Electric Conductivity ; Kinetics ; Membrane Potentials/drug effects ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oligonucleotide Probes ; Potassium Channels/drug effects/genetics/*physiology ; Tetraethylammonium ; Tetraethylammonium Compounds/*pharmacology
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  • 21
    Publication Date: 1990-02-16
    Description: Sulfonylurea-sensitive adenosine triphosphate (ATP)-regulated potassium (KATP) channels are present in brain cells and play a role in neurosecretion at nerve terminals. KATP channels in substantia nigra, a brain region that shows high sulfonylurea binding, are inactivated by high glucose concentrations and by antidiabetic sulfonylureas and are activated by ATP depletion and anoxia. KATP channel inhibition leads to activation of gamma-aminobutyric acid (GABA) release, whereas KATP channel activation leads to inhibition of GABA release. These channels may be involved in the response of the brain to hyper- and hypoglycemia (in diabetes) and ischemia or anoxia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Amoroso, S -- Schmid-Antomarchi, H -- Fosset, M -- Lazdunski, M -- New York, N.Y. -- Science. 1990 Feb 16;247(4944):852-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Pharmacologie Moleculaire et Cellulaire, UPR 411 du CNRS, Valbonne, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2305257" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/*physiology ; Animals ; Cell Hypoxia ; Deoxyglucose/pharmacology ; Glucose/metabolism/*pharmacology ; Hypoglycemic Agents/*pharmacology ; In Vitro Techniques ; Kinetics ; Oligomycins/pharmacology ; Potassium/pharmacology ; Potassium Channels/drug effects/*physiology ; Rubidium/metabolism ; Structure-Activity Relationship ; Substantia Nigra/drug effects/*physiology ; gamma-Aminobutyric Acid/*metabolism
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  • 22
    Publication Date: 1990-05-04
    Description: Platelet-derived growth factor (PDGF) stimulates phospholipase C (PLC) activity and the phosphorylation of the gamma isozyme of PLC (PLC-gamma) in vitro and in living cells. The role of PLC-gamma in the phosphoinositide signaling pathway was addressed by examining the effect of overexpression of PLC-gamma on cellular responses to PDGF. Overexpression of PLC-gamma correlated with PDGF-induced tyrosine phosphorylation of PLC-gamma and with PDGF-induced breakdown of phosphatidylinositol 4,5-bisphosphate (PIP2). However, neither bradykinin- nor lysophosphatidic acid-induced phosphoinositide metabolism was enhanced in the transfected cells, suggesting that the G protein-coupled phosphoinositide responses to these ligands are mediated by other PLC isozymes. The enhanced PDGF-induced generation of inositol trisphosphate (IP3) did not enhance intracellular calcium signaling or influence PDGF-induced DNA synthesis. Thus, enzymes other than PLC-gamma may limit PDGF-induced calcium signaling and DNA synthesis. Alternatively, PDGF-induced calcium signaling and DNA synthesis may use biochemical pathways other than phosphoinositide metabolism for signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Margolis, B -- Zilberstein, A -- Franks, C -- Felder, S -- Kremer, S -- Ullrich, A -- Rhee, S G -- Skorecki, K -- Schlessinger, J -- New York, N.Y. -- Science. 1990 May 4;248(4955):607-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rorer Biotechnology, King of Prussia, PA 19406.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2333512" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/physiology ; Cattle ; Cell Division/*drug effects ; Cells, Cultured ; DNA Replication/drug effects ; Genetic Vectors ; Inositol Phosphates/metabolism ; Isoenzymes/biosynthesis/*genetics/metabolism ; Kinetics ; Mice ; Platelet-Derived Growth Factor/*pharmacology ; Second Messenger Systems/*drug effects ; Transfection ; Type C Phospholipases/biosynthesis/*genetics/metabolism
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  • 23
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-08-17
    Description: An antibody elicited to a distorted N-methyl porphyrin catalyzed metal ion chelation by the planar porphyrin. At fixed Zn2+ and Cu2+ concentrations, the antibody-catalyzed reaction showed saturation kinetics with respect to the substrate mesoporphyrin IX (2) and was inhibited by the hapten, N-methylmesoporphyrin IX (1). The turnover number of 80 hour-1 for antibody-catalyzed metallation of 2 with Zn2+ compares with an estimated value of 800 hour-1 for ferrochelatase. The antibody also catalyzed the insertion of Co2+ and Mn2+ into 2, but it did not catalyze the metallation of protoporphyrin IX (3) or deuteroporphyrin IX (4). The antibody has high affinity for several metalloporphyrins, suggesting an approach to developing antibody-heme catalysts for redox or electron transfer reactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cochran, A G -- Schultz, P G -- New York, N.Y. -- Science. 1990 Aug 17;249(4970):781-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2389144" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies/*metabolism ; Antigens/immunology ; Catalysis ; Cobalt/metabolism ; Copper/metabolism ; Ferrochelatase/metabolism ; Kinetics ; Manganese/metabolism ; Mesoporphyrins/immunology/metabolism ; Metals/*metabolism ; Porphyrins/*metabolism ; Zinc/metabolism
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  • 24
    Publication Date: 1991-08-23
    Description: The evolutionary significance of protein polymorphisms has long been debated. Exponents of the balanced theory advocate that selection operates to maintain polymorphisms, whereas the neoclassical school argues that most genetic variation is neutral. Some studies have suggested that protein polymorphisms are not neutral, but their significance has been questioned because one cannot eliminate the possibility that linked loci were responsible for the observed differences. Evidence is presented that an enzymatic phenotype can affect carbon flow through a metabolic pathway. Glucose flux differences between lactate dehydrogenase-B phenotypes of Fundulus heteroclitus were reversed by substituting the Ldh-B gene product of one homozygous genotype with that of another.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DiMichele, L -- Paynter, K T -- Powers, D A -- New York, N.Y. -- Science. 1991 Aug 23;253(5022):898-900.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Wildlife and Fisheries Sciences, Texas A&M University, College Station 77843.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1876847" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blastocyst/enzymology ; Genotype ; Glucose/metabolism ; Glycolysis ; Isoenzymes ; Killifishes/embryology/*genetics/metabolism ; Kinetics ; L-Lactate Dehydrogenase/*genetics/metabolism ; Lactates/metabolism ; Lactic Acid ; Microinjections ; Phenotype ; Swine
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  • 25
    Publication Date: 1991-09-20
    Description: CD45 is a leukocyte-specific, transmembrane protein tyrosine phosphatase (PTPase) required for T cell responsiveness. How the activity of PTPases is regulated in vivo is unclear. Treatment of murine thymocytes and a variety of murine T cell lines with the calcium ionophore ionomycin decreased CD45 PTPase activity. Ionomycin treatment also led to a decreased phosphorylation of serine residues in CD45. These results indicate that increased intracellular calcium modulates CD45 PTPase activity, demonstrating regulation of CD45 PTPase activity in vivo, and also implicate serine dephosphorylation as a possible mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ostergaard, H L -- Trowbridge, I S -- CA-17733/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Sep 20;253(5026):1423-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Biology, Salk Institute, San Diego, CA 92186.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1654595" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/*metabolism ; Antigens, CD45 ; Cell Line ; Histocompatibility Antigens/*metabolism ; Ionomycin/*pharmacology ; Kinetics ; Mice ; Mice, Inbred BALB C ; Phosphoprotein Phosphatases/*metabolism ; Protein Tyrosine Phosphatases ; Spleen/drug effects/enzymology/immunology ; T-Lymphocytes/drug effects/*enzymology/immunology ; Thymus Gland/immunology
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  • 26
    Publication Date: 1991-05-03
    Description: A transition state analogue was used to produce a mouse antibody that catalyzes transesterification in water. The antibody behaves as a highly efficient catalyst with a covalent intermediate and the characteristic of induced fit. While some features of the catalytic pathway were programmed when the hapten was designed and reflect favorable substrate-antibody interactions, other features are a manifestation of the chemical potential of antibody diversity. The fact that antibodies recapitulate mechanisms and pathways previously thought to be a characteristic of highly evolved enzymes suggests that once an appropriate binding cavity is achieved, reaction pathways commensurate with the intrinsic chemical potential of proteins ensue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wirsching, P -- Ashley, J A -- Benkovic, S J -- Janda, K D -- Lerner, R A -- GM43858-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 3;252(5006):680-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2024120" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Alcohols/metabolism ; Animals ; Antibodies, Monoclonal/immunology/*metabolism ; Antibody Specificity ; Binding Sites, Antibody ; *Catalysis ; Enzymes/metabolism ; Esterification ; Haptens ; Kinetics ; Mice ; Water
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  • 27
    Publication Date: 1991-12-20
    Description: Rap1A is a low molecular weight guanosine triphosphate (GTP)-binding protein in human neutrophil membranes whose cellular function is unknown. Rap1A was found to form stoichiometric complexes with the cytochrome b558 component of the phagocyte nicotinamide adenine dinucleotide phosphate (NADPH) oxidase system. The (guanosine-5'-O-(3-thiotriphosphate) (GTP-gamma-S)-bound form of Rap1A bound more tightly to cytochrome b558 than did the guanosine diphosphate-bound form. No complex formation was observed between cytochrome b558 and H-Ras-GTP-gamma-S or Rap1A-GTP-gamma-S that had been heat-inactivated, nor between Rap1A-GTP-gamma-S and hydrophobic proteins serving as controls. Complex formation between Rap1A-GTP-gamma-S and cytochrome b558 was inhibited by phosphorylation of Rap1A with cyclic adenosine monophosphate (cAMP)-dependent protein kinase. These observations suggest that Rap1A may participate in the structure or regulation of the NADPH oxidase system and that this function of the Rap1A protein may be altered by phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bokoch, G M -- Quilliam, L A -- Bohl, B P -- Jesaitis, A J -- Quinn, M T -- 5RO126711/PHS HHS/ -- GM39434/GM/NIGMS NIH HHS/ -- GM44428/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1794-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1763330" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Chromatography, Gel ; Cytochrome b Group/isolation & purification/*metabolism ; GTP-Binding Proteins/antagonists & inhibitors/isolation & ; purification/*metabolism ; Guanosine 5'-O-(3-Thiotriphosphate)/metabolism ; Humans ; Kinetics ; Macromolecular Substances ; NADH, NADPH Oxidoreductases/*metabolism ; NADPH Oxidase ; Neutrophils/enzymology ; Phosphorylation ; Protein Binding ; Protein Kinase C/metabolism ; Proto-Oncogene Proteins/metabolism ; Recombinant Proteins/antagonists & inhibitors/isolation & purification/metabolism ; rap GTP-Binding Proteins
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  • 28
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-12-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1719-20.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1763320" target="_blank"〉PubMed〈/a〉
    Keywords: Breast Neoplasms/*economics/prevention & control/therapy ; Female ; Government Agencies ; Humans ; National Institutes of Health (U.S.) ; Research Support as Topic ; United States
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  • 29
    Publication Date: 1991-03-08
    Description: Engagement of the antigen-specific receptor (TCR) of CD4+ T lymphocytes without a second (costimulatory) signal prevents the subsequent production of interleukin-2 (IL-2) by these cells. Because IL-2 is a key immunoregulatory lymphokine and is also produced by a subset of CD8+ T cells that are able to kill target cells, the effect of engaging the TCR of one such clone in the absence of costimulatory signals was examined. The capacity for TCR-dependent IL-2 production was lost, indicating comparable costimulator-dependent signaling requirements for IL-2 production in CD4+ and CD8+ T cells. However, TCR-mediated cytotoxicity was not impaired, implying that costimulation is required for only certain TCR-dependent effector functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Otten, G R -- Germain, R N -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1228-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lymphocyte Biology Section, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1900952" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/immunology ; Antigen-Presenting Cells/immunology ; Antigens, CD8 ; Antigens, Differentiation, T-Lymphocyte/*immunology ; Female ; Interleukin-2/biosynthesis/*physiology ; Kinetics ; Lymphocyte Activation ; Mice ; Mice, Inbred Strains ; Ovalbumin/immunology ; Rats ; Receptors, Antigen, T-Cell/*immunology ; Spleen/immunology/radiation effects ; T-Lymphocytes/*immunology
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  • 30
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-06-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1991 Jun 7;252(5011):1369.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2047847" target="_blank"〉PubMed〈/a〉
    Keywords: *Hiv ; History, 20th Century ; Humans ; Male ; National Institutes of Health (U.S.) ; United States ; Virus Cultivation
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  • 31
    Publication Date: 1991-09-27
    Description: Dihydropyridine-sensitive voltage-dependent L-type calcium channels are critical to excitation-secretion and excitation-contraction coupling. The channel molecule is a complex of the main, pore-forming subunit alpha 1 and four additional subunits: alpha 2, delta, beta, and gamma (alpha 2 and delta are encoded by a single messenger RNA). The alpha 1 subunit messenger RNA alone directs expression of functional calcium channels in Xenopus oocytes, and coexpression of the alpha 2/delta and beta subunits enhances the amplitude of the current. The alpha 2, delta, and gamma subunits also have pronounced effects on its macroscopic characteristics, such as kinetics, voltage dependence of activation and inactivation, and enhancement by a dihydropyridine agonist. In some cases, specific modulatory functions can be assigned to individual subunits, whereas in other cases the different subunits appear to act in concert to modulate the properties of the channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Singer, D -- Biel, M -- Lotan, I -- Flockerzi, V -- Hofmann, F -- Dascal, N -- New York, N.Y. -- Science. 1991 Sep 27;253(5027):1553-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Pharmacology, Sackler School of Medicine, Tel Aviv University, Ramat Aviv, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1716787" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Pyridinecarboxylic acid, ; 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ; ester/pharmacology ; Animals ; Barium/pharmacology ; *Barium Compounds ; Cadmium/pharmacology ; Cadmium Chloride ; Calcium Channels/drug effects/genetics/*physiology ; *Chlorides ; Heart/physiology ; Kinetics ; Macromolecular Substances ; Membrane Potentials/drug effects ; Oocytes/physiology ; RNA, Messenger/genetics ; Xenopus
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  • 32
    Publication Date: 1991-02-01
    Description: Rhodopsin and the visual pigments are a distinct group within the family of G-protein-linked receptors in that they have a covalently bound ligand, the 11-cis-retinal chromophore, whereas all of the other receptors bind their agonists through noncovalent interactions. The retinal chromophore in rhodopsin is bound by means of a protonated Schiff base linkage to the epsilon-amino group of Lys-296. Two rhodopsin mutants have been constructed, K296G and K296A, in which the covalent linkage to the chromophore is removed. Both mutants form a pigment with an absorption spectrum close to that of the wild type when reconstituted with the Schiff base of an n-alkylamine and 11-cis-retinal. In addition, the pigment formed from K296G and the n-propylamine Schiff base of 11-cis-retinal was found to activate transducin in a light-dependent manner, with 30 to 40% of the specific activity measured for the wild-type protein. It appears that the covalent bond is not essential for binding of the chromophore or for catalytic activation of transducin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhukovsky, E A -- Robinson, P R -- Oprian, D D -- 5T32 GM07596-11/GM/NIGMS NIH HHS/ -- EY07965/EY/NEI NIH HHS/ -- R01 EY007965/EY/NEI NIH HHS/ -- S07 RR07044/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 1;251(4993):558-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate Department of Biochemistry, Brandeis University, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1990431" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Guanosine 5'-O-(3-Thiotriphosphate)/metabolism ; Kinetics ; Mutagenesis, Site-Directed ; Protein Binding ; Retinaldehyde/*metabolism ; Rhodopsin/genetics/*metabolism/radiation effects ; Schiff Bases ; Spectrophotometry ; Transducin/*metabolism/radiation effects
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  • 33
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-08-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hamilton, D P -- New York, N.Y. -- Science. 1991 Aug 16;253(5021):728-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1876829" target="_blank"〉PubMed〈/a〉
    Keywords: Hiv-1 ; History, 20th Century ; National Institutes of Health (U.S.) ; Patents as Topic ; *Scientific Misconduct ; United States
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  • 34
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-03-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1172.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2006406" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*economics ; Behavioral Research ; *Biomedical Research ; Federal Government ; Humans ; National Institutes of Health (U.S.) ; *Research Support as Topic ; *Resource Allocation ; United States
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  • 35
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-09-13
    Description: The phosphorylation of the cardiac sodium channel by adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase A leads to its inactivation. It was shown that extracellular cAMP can also modulate the sodium channel of rat, guinea pig, and frog ventricular myocytes in a rapid (less than 50 milliseconds), reversible, and dose-dependent manner. The decrease in the sodium current was accompanied by a 10- to 15-millivolt shift in the steady-state availability of the sodium channel toward more negative potentials and was inhibited by guanosine-5'-O-(2-thiodiphosphate) or pertussis toxin, suggesting that the extracellular modulation of the sodium channel by cAMP is mediated by a membrane-delimited mechanism that includes a pertussis toxin-sensitive G protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sorbera, L A -- Morad, M -- HL16152/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 Sep 13;253(5025):1286-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Pennsylvania, Philadelphia 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1653970" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cyclic AMP/*pharmacology ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Guanosine Diphosphate/analogs & derivatives/pharmacology ; Guinea Pigs ; Heart/drug effects/*physiology ; Isoproterenol/pharmacology ; Kinetics ; Membrane Potentials/drug effects ; Pertussis Toxin ; Rana pipiens ; Rats ; Receptors, Cyclic AMP/drug effects/*physiology ; Sodium Channels/drug effects/*physiology ; Thionucleotides/pharmacology ; Virulence Factors, Bordetella/pharmacology
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  • 36
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-10-25
    Description: The action of dopamine and other monoamine neurotransmitters at synapses is terminated predominantly by high-affinity reuptake into presynaptic terminals by specific sodium-dependent neurotransmitter transport proteins. A complementary DNA encoding a rat dopamine transporter has been isolated that exhibits high sequence similarity with the previously cloned norepinephrine and gamma-aminobutyric acid transporters. Transient expression of the complementary DNA in HeLa cells confirms the cocaine sensitivity of this transporter.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kilty, J E -- Lorang, D -- Amara, S G -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):578-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Yale University, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948035" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/drug effects/*genetics/metabolism ; Cloning, Molecular ; Cocaine/*pharmacology ; Dopamine/*metabolism ; Dopamine Plasma Membrane Transport Proteins ; Gene Expression ; HeLa Cells ; Humans ; Kinetics ; *Membrane Glycoproteins ; *Membrane Transport Proteins ; Molecular Sequence Data ; *Nerve Tissue Proteins ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction/methods ; Rats ; Sequence Homology, Nucleic Acid ; Transfection
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  • 37
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-01-25
    Description: The higher order folding process of the catalytic RNA derived from the self-splicing intron of Tetrahymena thermophila was monitored with the use of Fe(II)-EDTA-induced free radical chemistry. The overall tertiary structure of the RNA molecule forms cooperatively with the uptake of at least three magnesium ions. Local folding transitions display different metal ion dependencies, suggesting that the RNA tertiary structure assembles through a specific folding intermediate before the catalytic core is formed. Enzymatic activity, assayed with an RNA substrate that is complementary to the catalytic RNA active site, coincides with the cooperative structural transition. The higher order RNA foldings produced by Mg(II), Ca(II), and Sr(II) are similar; however, only the Mg(II)-stabilized RNA is catalytically active. Thus, these results directly demonstrate that divalent metal ions participate in general folding of the ribozyme tertiary structure, and further indicate a more specific involvement of Mg(II) in catalysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Celander, D W -- Cech, T R -- New York, N.Y. -- Science. 1991 Jan 25;251(4992):401-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309-0215.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1989074" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Calcium/metabolism ; Densitometry ; Kinetics ; Magnesium/metabolism ; Magnesium Chloride/pharmacology ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA, Catalytic/*chemistry/drug effects/metabolism ; Strontium/metabolism ; Tetrahymena
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  • 38
    Publication Date: 1991-03-29
    Description: Cloned integrin alpha 2 subunit complementary DNA was expressed on human rhabdomyosarcoma (RD) cells to give a functional VLA-2 (alpha 2 beta 1) adhesion receptor. The VLA-2-positive RDA2 cells not only showed increased adhesion to collagen and laminin in vitro, but also formed substantially more metastatic tumor colonies in nude mice after either intravenous or subcutaneous injection. These results show that a specific adhesion receptor (VLA-2) can markedly enhance both experimental and spontaneous metastasis. In contrast to the metastasis results, there was no difference in either the in vitro growth rate or apparent in vivo tumorigenicity of RD and RDA2 cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, B M -- Matsuura, N -- Takada, Y -- Zetter, B R -- Hemler, M E -- CA 37393/CA/NCI NIH HHS/ -- GM 38903/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 29;251(5001):1600-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2011740" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Adhesion ; Cell Line ; Collagen ; Fibronectins ; Humans ; Kinetics ; Laminin ; Lung Neoplasms/pathology/secondary ; Mice ; Mice, Nude ; Neoplasm Metastasis ; Neoplasm Transplantation ; Receptors, Very Late Antigen/genetics/*physiology ; Rhabdomyosarcoma/*pathology ; Transplantation, Heterologous
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  • 39
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-05-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1991 May 24;252(5009):1046.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2031175" target="_blank"〉PubMed〈/a〉
    Keywords: Costs and Cost Analysis ; National Institutes of Health (U.S.) ; *Research Support as Topic ; United States
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  • 40
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-06-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koshland, D E Jr -- New York, N.Y. -- Science. 1991 May 31;252(5010):1229.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925529" target="_blank"〉PubMed〈/a〉
    Keywords: National Institutes of Health (U.S.) ; Research Support as Topic/*trends ; *Science ; United States
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  • 41
    Publication Date: 1991-08-02
    Description: Modulation of the activity of potassium and other ion channels is an essential feature of nervous system function. The open probability of a large conductance Ca(2+)-activated K+ channel from rat brain, incorporated into planar lipid bilayers, is increased by the addition of adenosine triphosphate (ATP) to the cytoplasmic side of the channel. This modulation takes place without the addition of protein kinase, requires Mg2+, and is mimicked by an ATP analog that serves as a substrate for protein kinases but not by a nonhydrolyzable ATP analog. Addition of protein phosphatase 1 reverses the modulation by MgATP. Thus, there may be an endogenous protein kinase activity firmly associated with this K+ channel. Some ion channels may exist in a complex that contains regulatory protein kinases and phosphatases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chung, S K -- Reinhart, P H -- Martin, B L -- Brautigan, D -- Levitan, I B -- DK31374/DK/NIDDK NIH HHS/ -- NS17910/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 2;253(5019):560-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate Department of Biochemistry, Brandeis University, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1857986" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/pharmacology ; Animals ; Brain/*physiology ; Calcium/*pharmacology ; Kinetics ; Lipid Bilayers ; Potassium Channels/drug effects/metabolism/*physiology ; Protein Kinases/*metabolism ; Rats
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  • 42
    Publication Date: 1991-02-22
    Description: Macrophage-like U-937 cells secrete a 22-kilodalton heparin-binding growth factor that is mitogenic for BALB-3T3 fibroblasts and smooth muscle cells, but not endothelial cells. The amino acid sequence predicted from complementary DNA clones indicates that the mitogen is a new member of the epidermal growth factor (EGF) family. This heparin-binding EGF-like growth factor (HB-EGF) binds to EGF receptors on A-431 epidermoid carcinoma cells and smooth muscle cells, but is a far more potent mitogen for smooth muscle cells than is EGF. HB-EGF is also expressed in cultured human macrophages and may be involved in macrophage-mediated cellular proliferation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Higashiyama, S -- Abraham, J A -- Miller, J -- Fiddes, J C -- Klagsbrun, M -- CA37392/CA/NCI NIH HHS/ -- CA45548/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 22;251(4996):936-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Surgical Research, Children's Hospital, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1840698" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Division/drug effects ; Cell Line ; Chromatography, Affinity ; Chromatography, High Pressure Liquid ; DNA Replication/drug effects ; Epidermal Growth Factor/genetics/isolation & ; purification/*metabolism/pharmacology ; Growth Substances/*metabolism ; Heparin/*metabolism ; Humans ; Kinetics ; Macrophages/*metabolism ; Molecular Sequence Data ; Protein Binding ; Receptor, Epidermal Growth Factor/metabolism ; Sequence Homology, Nucleic Acid
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  • 43
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-01-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rall, D P -- New York, N.Y. -- Science. 1991 Jan 4;251(4989):10-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1986406" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carcinogenicity Tests/standards ; Carcinogens/*toxicity ; Humans ; National Institutes of Health (U.S.) ; Neoplasms/*chemically induced ; *Toxicology ; United States
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  • 44
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-04-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1991 Apr 26;252(5005):490-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2020847" target="_blank"〉PubMed〈/a〉
    Keywords: Government Agencies ; National Institutes of Health (U.S.) ; *Research Support as Topic ; United States
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  • 45
    Publication Date: 1991-05-31
    Description: An identified neuron of the leech, a Retzius cell, has been attached to the open gate of a p-channel field-effect transistor. Action potentials, spontaneous or stimulated, modulate directly the source-drain current in silicon. The electronic signals match the shape of the action potential. The average voltage on the gate was up to 25 percent of the intracellular voltage change. Occasionally weak signals that resemble the first derivative of the action potential were observed. The junctions can be described by a model that includes capacitive coupling of the plasma membrane and the gate oxide and that accounts for variable resistance of the seal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fromherz, P -- Offenhausser, A -- Vetter, T -- Weis, J -- New York, N.Y. -- Science. 1991 May 31;252(5010):1290-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Abteilung Biophysik der Universitat Ulm, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925540" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Electric Conductivity ; Electrophysiology ; Kinetics ; Leeches/*physiology ; Microscopy, Electron, Scanning ; Neurons/*physiology/ultrastructure ; *Silicon ; Transistors, Electronic
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  • 46
    Publication Date: 1991-10-11
    Description: It is generally accepted that glutamate serves as the neurotransmitter at most excitatory synapses in the mammalian central nervous system (CNS). Synaptic release of glutamate may trigger a fast and a slow excitatory postsynaptic current (EPSC). The slow EPSC is mediated by N-methyl-D-aspartate (NMDA) receptor channels, whereas the fast EPSC is mediated by non-NMDA receptor channels. The nootropic agent aniracetam selectively and reversibly slows the desensitization kinetics of non-NMDA channels and lengthens their single-channel open times. Antiracetam also modulates the kinetics of the fast EPSC in a manner that mirrors its action on the kinetics of the non-NMDA channels. These results support the hypothesis that the properties of the non-NMDA glutamate channels rather than the rate of neurotransmitter clearance are the primary determinants of the kinetics of the fast EPSC in the mammalian CNS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tang, C M -- Shi, Q Y -- Katchman, A -- Lynch, G -- NS28158/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 11;254(5029):288-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, University of Pennsylvania, Philadelphia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1681589" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials/*drug effects ; Animals ; Glutamates/*physiology ; Glutamic Acid ; Kinetics ; Pyrrolidinones/*pharmacology ; Rats ; Receptors, Glutamate ; Receptors, N-Methyl-D-Aspartate/drug effects ; Receptors, Neurotransmitter/drug effects ; Synapses/*drug effects
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  • 47
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-10-25
    Description: SP-B is a protein in pulmonary surfactant that is, in greatest part, responsible for resistance to surface tension and prevention of collapse of pulmonary alveoli. Peptides of 21 residues, synthesized following the sequence of SP-B or resembling the hydrophobic and hydrophilic domains of SP-B (such as RLLLLRLLLLRLLLLRLLLLR, R, Arg, and L, Leu), enhanced the abilities of phospholipids to reduce surface tension both in vitro and in vivo. Intermittent positively charged residues were essential for this activity. The SP-B-like peptides were found by tryptophan fluorescence to partition within the phospholipid layer in contact with both polar head groups and acyl side chains. These data, together with findings that the SP-B-related peptides increase inter- and intramolecular order of the phospholipid layer, suggest that SP-B resists surface tension by increasing lateral stability of the phospholipid layer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cochrane, C G -- Revak, S D -- GM-37696/GM/NIGMS NIH HHS/ -- HL-23584/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):566-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948032" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Kinetics ; Molecular Sequence Data ; Peptides/*chemical synthesis/chemistry ; Phospholipids/metabolism ; Proteolipids/chemistry/*metabolism ; Pulmonary Surfactants/chemistry/*metabolism ; Structure-Activity Relationship ; Surface Tension
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  • 48
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-09-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moffat, A S -- New York, N.Y. -- Science. 1991 Sep 27;253(5027):1483.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1896855" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/prevention & control ; Adolescent ; Adult ; Female ; *Health Surveys ; Humans ; Male ; National Institutes of Health (U.S.) ; *Sexual Behavior ; Sexually Transmitted Diseases/prevention & control ; United States
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  • 49
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-11-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, J -- New York, N.Y. -- Science. 1991 Nov 1;254(5032):647.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948042" target="_blank"〉PubMed〈/a〉
    Keywords: *AIDS Vaccines ; Acquired Immunodeficiency Syndrome/prevention & control ; Animals ; Clinical Trials as Topic ; Humans ; National Institutes of Health (U.S.) ; United States
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  • 50
    Publication Date: 1991-09-06
    Description: Calcium-induced calcium release (CICR) may function widely in calcium-mediated cell signaling, but has been most thoroughly characterized in muscle cells. In a homogenate of sea urchin eggs, which display transients in the intracellular free calcium concentration ([Ca2+]i) during fertilization and anaphase, addition of Ca2+ triggered CICR. Ca2+ release was also induced by the CICR modulators ryanodine and caffeine. Responses to both Ca2+ and CICR modulators (but not Ca2+ release mediated by inositol 1,4,5-trisphosphate) were inhibited by procaine and ruthenium red, inhibitors of CICR. Intact eggs also displayed transients of [Ca2+]i when microinjected with ryanodine. Cyclic ADP-ribose, a metabolite with potent Ca(2+)-releasing properties, appears to act by way of the CICR mechanism and may thus be an endogenous modulator of CICR. A CICR mechanism is present in these nonmuscle cells as is assumed in various models of intracellular Ca2+ wave propagation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Galione, A -- Lee, H C -- Busa, W B -- HD17484/HD/NICHD NIH HHS/ -- HD22879/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1991 Sep 6;253(5024):1143-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Johns Hopkins University, Baltimore, MD 21218.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1909457" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate Ribose/*pharmacology ; Adenosine Triphosphate/metabolism ; Animals ; Calcium/*metabolism/pharmacology ; Cyclic ADP-Ribose ; Egtazic Acid/pharmacology ; Kinetics ; Ovum/drug effects/*physiology ; Sea Urchins ; Spectrometry, Fluorescence ; Time Factors
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  • 51
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-11-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1991 Nov 22;254(5035):1104-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1957160" target="_blank"〉PubMed〈/a〉
    Keywords: Biotechnology ; *Dna ; *Human Genome Project ; Humans ; National Institutes of Health (U.S.) ; *Patents as Topic ; United States
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  • 52
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-09-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coles, P -- New York, N.Y. -- Science. 1991 Sep 27;253(5027):1479.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1896853" target="_blank"〉PubMed〈/a〉
    Keywords: *Acquired Immunodeficiency Syndrome ; France ; HIV/isolation & purification ; Humans ; National Institutes of Health (U.S.) ; *Publishing ; Scientific Misconduct ; United States
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  • 53
    Publication Date: 1991-05-24
    Description: The signal recognition particle (SRP) directs signal sequence specific targeting of ribosomes to the rough endoplasmic reticulum. Displacement of the SRP from the signal sequence of a nascent polypeptide is a guanosine triphosphate (GTP)-dependent reaction mediated by the membrane-bound SRP receptor. A nonhydrolyzable GTP analog can replace GTP in the signal sequence displacement reaction, but the SRP then fails to dissociate from the membrane. Complexes of the SRP with its receptor containing the nonhydrolyzable analog are incompetent for subsequent rounds of protein translocation. Thus, vectorial targeting of ribosomes to the endoplasmic reticulum is controlled by a GTP hydrolysis cycle that regulates the affinity between the SRP, signal sequences, and the SRP receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Connolly, T -- Rapiejko, P J -- Gilmore, R -- GM 35687/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 24;252(5009):1171-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester 01655.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1851576" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Centrifugation, Density Gradient ; Endoplasmic Reticulum/metabolism ; GTP-Binding Proteins/genetics/metabolism ; Guanosine Triphosphate/*metabolism ; Guanylyl Imidodiphosphate/pharmacology ; Hydrolysis ; Kinetics ; Macromolecular Substances ; Protein Binding ; Protein Biosynthesis ; Receptors, Cell Surface/isolation & purification/*metabolism ; *Receptors, Cytoplasmic and Nuclear ; *Receptors, Peptide ; Ribonucleoproteins/genetics/isolation & purification/*metabolism ; Ribosomes/metabolism ; Signal Recognition Particle ; Transcription, Genetic ; Vesicular stomatitis Indiana virus/genetics/metabolism
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-07-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1991 Jul 26;253(5018):376.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1862337" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Mapping ; Chromosomes, Human, Pair 19 ; *Human Genome Project ; Humans ; National Institutes of Health (U.S.) ; United States ; Universities
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  • 55
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-11-29
    Description: The N-end rule relates the in vivo half-life of a protein to the identity of its amino-terminal residue. Distinct versions of the N-end rule operate in all eukaryotes examined. It is shown that the bacterium Escherichia coli also has the N-end rule pathway. Amino-terminal arginine, lysine, leucine, phenylalanine, tyrosine, and tryptophan confer 2-minute half-lives on a test protein; the other amino-terminal residues confer greater than 10-hour half-lives on the same protein. Amino-terminal arginine and lysine are secondary destabilizing residues in E. coli because their activity depends on their conjugation to the primary destabilizing residues leucine or phenylalanine by leucine, phenylalanine-transfer RNA-protein transferase. The adenosine triphosphate-dependent protease Clp (Ti) is required for the degradation of N-end rule substrates in E. coli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tobias, J W -- Shrader, T E -- Rocap, G -- Varshavsky, A -- DK39520/DK/NIDDK NIH HHS/ -- GM31530/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1374-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1962196" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacteria/*metabolism ; Bacterial Proteins/*metabolism ; Escherichia coli/enzymology/metabolism ; Half-Life ; Kinetics ; Molecular Sequence Data ; Rabbits ; Reticulocytes/metabolism ; Saccharomyces cerevisiae/enzymology/metabolism ; Structure-Activity Relationship ; beta-Galactosidase/*metabolism
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-06-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Langreth, R -- New York, N.Y. -- Science. 1991 Jun 28;252(5014):1780.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1676541" target="_blank"〉PubMed〈/a〉
    Keywords: Alkaloids/*isolation & purification/therapeutic use ; Antineoplastic Agents, Phytogenic/*isolation & purification ; Environment ; Female ; Humans ; National Institutes of Health (U.S.) ; Neoplasms/*drug therapy ; Oregon ; Ovarian Neoplasms/drug therapy ; Paclitaxel ; Trees ; United States
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-11-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbons, A -- New York, N.Y. -- Science. 1991 Nov 15;254(5034):933.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948077" target="_blank"〉PubMed〈/a〉
    Keywords: Foundations ; National Institutes of Health (U.S.) ; *Research Support as Topic ; United States
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  • 58
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-08-23
    Description: The N-methyl-D-aspartate (NMDA) receptor, a subtype of glutamate receptors, plays a key role in synaptic plasticity in the nervous system. After NMDA receptor activation, calcium entry into the postsynaptic neuron is a critical initial event. However, the subsequent mechanisms by which the NMDA receptor signal is processed are incompletely understood. Stimulation of cultured rat hippocampal cells with glutamate resulted in the rapid and transient tyrosine phosphorylation of a 39-kilodalton protein (p39). Tyrosine phosphorylation of p39 was triggered by the NMDA receptor and required an influx of Ca2+ from the extracellular medium. Because p39 was found to be highly related or identical to the microtubule-associated protein 2 kinase, the NMDA receptor signal may be processed by a sequential activation of protein kinases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bading, H -- Greenberg, M E -- CA 43855/CA/NCI NIH HHS/ -- NS 28829/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 23;253(5022):912-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1715095" target="_blank"〉PubMed〈/a〉
    Keywords: 2-Amino-5-phosphonovalerate/pharmacology ; Animals ; Calcium/metabolism ; Calcium-Calmodulin-Dependent Protein Kinases ; Cells, Cultured ; Glutamates/pharmacology ; Glutamic Acid ; Hippocampus/drug effects/metabolism ; Immunoblotting ; Kinetics ; Phosphoproteins/*metabolism ; Phosphorylation ; Phosphotyrosine ; Protein Kinases/metabolism ; Rats ; Receptors, N-Methyl-D-Aspartate/*metabolism ; Tyrosine/*analogs & derivatives/metabolism
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-04-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1991 Apr 26;252(5005):500-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2020850" target="_blank"〉PubMed〈/a〉
    Keywords: California ; Human Genome Project/*organization & administration ; Humans ; National Institutes of Health (U.S.) ; United States
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  • 60
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-04-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1991 Apr 26;252(5005):498-501.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2020849" target="_blank"〉PubMed〈/a〉
    Keywords: Government Agencies ; Human Genome Project/*organization & administration ; Humans ; National Institutes of Health (U.S.) ; United States
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  • 61
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-04-19
    Description: A link is found between T wave alternans and vulnerability to ventricular fibrillation, and a new approach is provided for quantification of susceptibility to malignant arrhythmias. Complex demodulation reveals that alternation of the electrocardiogram is concentrated during the first half of the T wave, coinciding with the vulnerable period of the cardiac cycle. During myocardial ischemia and reperfusion, there are marked increases in the degree of T wave alternans that parallel the established time course of changes in vulnerability. The influence of the sympathetic nervous system in arrhythmogenesis is also accurately detected. Ultimately, complex demodulation of the electrocardiogram could provide a technique for identification and management of individuals at risk for sudden cardiac death.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nearing, B D -- Huang, A H -- Verrier, R L -- HL-33567/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 Apr 19;252(5004):437-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Georgetown University School of Medicine, Washington, DC 20007.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2017682" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Constriction ; Coronary Vessels ; Dogs ; Electric Stimulation ; *Electrocardiography ; Electrophysiology ; Female ; Heart Conduction System/*physiopathology ; Kinetics ; Male ; Mathematics ; Reperfusion ; Ventricular Fibrillation/*physiopathology
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  • 62
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-08-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rubinstein, E -- New York, N.Y. -- Science. 1991 Aug 16;253(5021):732.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1876831" target="_blank"〉PubMed〈/a〉
    Keywords: Hiv-1 ; History, 20th Century ; National Institutes of Health (U.S.) ; *Scientific Misconduct ; United States
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  • 63
    Publication Date: 1991-03-08
    Description: Epidermal growth factor and platelet-derived growth factor can stimulate the production of the second messenger inositol trisphosphate in responsive cells, but the biochemical pathway for these signaling events has been uncertain because the reactions have not been reconstituted with purified molecules in vitro. A reconstitution is described that requires not only the growth factor, its receptor with tyrosine kinase activity, and the soluble phospholipase C-gamma 1, but also the small soluble actin-binding protein profilin. Profilin binds to the substrate phosphatidylinositol 4,5-bisphosphate and inhibits its hydrolysis by unphosphorylated phospholipase C-gamma 1. Phosphorylation of phospholipase C-gamma 1 by the epidermal growth factor receptor tyrosine kinase overcomes the inhibitory effect of profilin and results in an effective activation of phospholipase C-gamma 1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldschmidt-Clermont, P J -- Kim, J W -- Machesky, L M -- Rhee, S G -- Pollard, T D -- GM-26338/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1231-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Anatomy, 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/1848725" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Contractile Proteins/metabolism ; Epidermal Growth Factor/*metabolism ; Inositol Phosphates/metabolism ; Isoenzymes/*metabolism ; Kinetics ; Microfilament Proteins/*metabolism ; Phosphatidylinositol 4,5-Diphosphate ; Phosphatidylinositols/metabolism ; Phosphorylation ; Profilins ; Protein-Tyrosine Kinases/*metabolism ; Receptor, Epidermal Growth Factor/*metabolism ; Signal Transduction ; Type C Phospholipases/*metabolism ; Tyrosine
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  • 64
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-09-13
    Description: Interleukin-8 (IL-8) is an inflammatory cytokine that activates neutrophil chemotaxis, degranulation, and the respiratory burst. Neutrophils express receptors for IL-8 that are coupled to guanine nucleotide-binding proteins (G proteins); binding of IL-8 to its receptor induces the mobilization of intracellular calcium stores. A cDNA clone from HL-60 neutrophils, designated p2, has now been isolated that encodes a human IL-8 receptor. When p2 is expressed in oocytes from Xenopus laevis, the oocytes bind 125I-labeled IL-8 specifically and respond to IL-8 by mobilizing calcium stores with an EC50 of 20 nM. This IL-8 receptor has 77% amino acid identity with a second human neutrophil receptor isotype that binds IL-8 with higher affinity. It also exhibits 69% amino acid identity with a protein reported to be an N-formyl peptide receptor from rabbit neutrophils, but less than 30% identity with all other known G protein-coupled receptors, including the human N-formyl peptide receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murphy, P M -- Tiffany, H L -- New York, N.Y. -- Science. 1991 Sep 13;253(5025):1280-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Host Defenses, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1891716" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding, Competitive ; Cloning, Molecular/methods ; DNA/genetics ; Gene Library ; Humans ; Interleukin-8/*metabolism/pharmacology ; Kinetics ; Molecular Sequence Data ; Neutrophils/immunology ; Oocytes/drug effects/physiology ; Protein Biosynthesis ; Rabbits ; Receptors, Immunologic/drug effects/*genetics/physiology ; Receptors, Interleukin-8A ; Recombinant Proteins/metabolism ; Sequence Homology, Nucleic Acid ; Signal Transduction ; Transcription, Genetic ; Xenopus
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-02-01
    Description: In Virginia Morell's Research News article "New light on writing in the Americas" (18 Jan., p. 268), the illustrations on page 268 should have been credited to George Stuart of the National Geographic Society.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gorden, P -- New York, N.Y. -- Science. 1991 Feb 1;251(4993):500.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1990423" target="_blank"〉PubMed〈/a〉
    Keywords: *Cystic Fibrosis ; Humans ; National Institutes of Health (U.S.) ; *Research ; United States
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  • 66
    Publication Date: 1992-10-09
    Description: During early development of the mammalian cerebral cortex, young neurons migrate outward from the site of their final mitosis in the ventricular zone into the cortical plate, where they form the adult cortex. Time-lapse confocal microscopy was used to observe directly the dynamic behaviors of migrating cells in living slices of developing cortex. The majority of cells migrated along a radial pathway, consistent with the view that cortical neurons migrate along radial glial fibers. A fraction of cells, however, turned within the intermediate zone and migrated orthogonal to the radial fibers. This orthogonal migration may contribute to the tangential dispersion of clonally related cortical neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Rourke, N A -- Dailey, M E -- Smith, S J -- McConnell, S K -- EY06314/EY/NEI NIH HHS/ -- NS09027/NS/NINDS NIH HHS/ -- NS28587/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Oct 9;258(5080):299-302.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1411527" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Carbocyanines ; Cell Movement ; Cerebral Cortex/cytology/*growth & development ; Culture Techniques ; Ferrets ; Fluorescent Dyes ; Immunohistochemistry ; Kinetics ; Lasers ; Microscopy ; Neurons/*physiology ; Vimentin/immunology
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  • 67
    Publication Date: 1992-11-13
    Description: When glycine418 of Escherichia coli glutathione reductase, which is in a closely packed region of the dimer interface, is replaced with a bulky tryptophan residue, the enzyme becomes highly cooperative (Hill coefficient 1.76) for glutathione binding. The cooperativity is lost when the mutant subunit is hybridized with a wild-type subunit to create a heterodimer. The mutation appears to disrupt atomic packing at the dimer interface, which induces a change of kinetic mechanism. A single mutation in a region of the protein remote from the active site can thus act as a molecular switch to confer cooperativity on an enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scrutton, N S -- Deonarain, M P -- Berry, A -- Perham, R N -- New York, N.Y. -- Science. 1992 Nov 13;258(5085):1140-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Cambridge, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1439821" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Escherichia coli/*enzymology/genetics ; Genes, Bacterial ; Glutathione/metabolism ; Glutathione Reductase/*chemistry/genetics/metabolism ; Glycine/chemistry ; Kinetics ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; *Mutagenesis, Site-Directed ; NADP/metabolism ; Plasmids ; Protein Multimerization ; Tryptophan/chemistry
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-09-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1992 Sep 11;257(5076):1472-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1523403" target="_blank"〉PubMed〈/a〉
    Keywords: *AIDS Vaccines ; Acquired Immunodeficiency Syndrome/immunology/*prevention & control ; HIV/immunology ; Humans ; National Institutes of Health (U.S.) ; Recombinant Proteins ; Safety ; United States ; Vaccines, Synthetic
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  • 69
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-04-10
    Description: Diacylglycerols, which are generated during phospholipase-catalyzed hydrolysis of phospholipids, stimulated actin polymerization in the presence of highly purified plasma membranes from the cellular slime mold Dictyostelium discoideum. The increased rate of actin polymerization apparently resulted from de novo formation of actin nucleation sites rather than uncapping of existing filament ends, because the membranes lacked detectable endogenous actin. The increased actin nucleation was mediated by a peripheral membrane component other than protein kinase C, the classical target of diacylglycerol action. These results indicate that diacylglycerols increase actin nucleation at plasma membranes and suggest a mechanism whereby signal transduction pathways may control cytoskeletal assembly.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shariff, A -- Luna, E J -- GM-33048/GM/NIGMS NIH HHS/ -- R01 GM033048/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 10;256(5054):245-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology Group, Worcester Foundation for Experimental Biology, Shresbury, MA 01545.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1373523" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*metabolism ; Alkaloids/pharmacology ; Animals ; Calcium/pharmacology ; Cell Membrane/drug effects/*metabolism ; Dictyostelium/*metabolism ; Diglycerides/*pharmacology ; Kinetics ; Macromolecular Substances ; *Naphthalenes ; Polycyclic Compounds/pharmacology ; Protein Kinase C/antagonists & inhibitors ; Staurosporine ; Tetradecanoylphorbol Acetate/pharmacology ; Time Factors
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-04-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):24.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1566053" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Child ; Female ; *Health Promotion ; Humans ; Infant ; Infant Mortality ; Male ; Middle Aged ; *Minority Groups ; National Institutes of Health (U.S.) ; *Research Support as Topic ; United States
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  • 71
    Publication Date: 1992-05-01
    Description: A DNA-nicking activity was detected in the sera of patients with various autoimmune pathologies and was shown to be a property of autoantibodies. The DNA hydrolyzing activity, which was purified by affinity and high-performance liquid chromatography, corresponded in size to immunoglobulin M (IgM) and IgG and had a positive response to antibodies to human IgG. The DNA hydrolyzing autoantibodies were stable to acid shock and yielded a DNA degradation pattern that was different from that of deoxyribonuclease (DNase) I and blood DNase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shuster, A M -- Gololobov, G V -- Kvashuk, O A -- Bogomolova, A E -- Smirnov, I V -- Gabibov, A G -- New York, N.Y. -- Science. 1992 May 1;256(5057):665-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉V.A. Engelhardt Institute of Molecular Biology, Academy of Sciences of Russia, Moscow.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1585181" target="_blank"〉PubMed〈/a〉
    Keywords: Acetates/pharmacology ; Acetic Acid ; Autoantibodies/isolation & purification/*metabolism ; Autoimmune Diseases/*metabolism ; Chromatography, High Pressure Liquid ; DNA/*metabolism ; DNA Polymerase I/metabolism ; Deoxyribonuclease I/metabolism ; Electrophoresis, Agar Gel ; Humans ; Immunoglobulin G/isolation & purification/metabolism ; Immunoglobulin M/isolation & purification/metabolism ; Kinetics ; Lupus Erythematosus, Systemic/immunology ; Plasmids
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  • 72
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-05-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1992 May 15;256(5059):956-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1589774" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Mapping ; History, 20th Century ; Human Genome Project/economics/*organization & administration ; National Institutes of Health (U.S.) ; Research Support as Topic ; United States
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  • 73
    Publication Date: 1992-05-01
    Description: A membrane polypeptide involved in K+ transport in a higher plant was cloned by complementation of a yeast mutant defective in K+ uptake with a complementary DNA library from Arabidopsis thaliana. A 2.65-kilobase complementary DNA conferred ability to grow on media with K+ concentration in the micromolar range and to absorb K+ (or 86Rb+) at rates similar to those in wild-type yeast. The predicted amino acid sequence (838 amino acids) has three domains: a channel-forming region homologous to animal K+ channels, a cyclic nucleotide-binding site, and an ankyrin-like region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sentenac, H -- Bonneaud, N -- Minet, M -- Lacroute, F -- Salmon, J M -- Gaymard, F -- Grignon, C -- New York, N.Y. -- Science. 1992 May 1;256(5057):663-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biochimie et Physiologie Vegetales, ENSA-M/INRA/CNRS URA 573, Montpellier, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1585180" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Arabidopsis Proteins ; Biological Transport ; Blotting, Southern ; Carrier Proteins/chemistry/genetics ; *Cloning, Molecular ; DNA/genetics ; Deoxyribonuclease EcoRI ; Gene Expression ; Kinetics ; Molecular Sequence Data ; Plant Proteins/chemistry/*genetics ; Plants/*genetics ; Potassium/*metabolism ; Potassium Channels/chemistry/*genetics ; Saccharomyces cerevisiae/*genetics ; Sequence Homology, Nucleic Acid
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  • 74
    Publication Date: 1992-08-14
    Description: A pseudo--half-knot can be formed by binding an oligonucleotide asymmetrically to an RNA hairpin loop. This binding motif was used to target the human immunodeficiency virus TAR element, an important viral RNA structure that is the receptor for Tat, the major viral transactivator protein. Oligonucleotides complementary to different halves of the TAR structure bound with greater affinity than molecules designed to bind symmetrically around the hairpin. The pseudo--half-knot--forming oligonucleotides altered the TAR structure so that specific recognition and binding of a Tat-derived peptide was disrupted. This general binding motif may be used to disrupt the structure of regulatory RNA hairpins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ecker, D J -- Vickers, T A -- Bruice, T W -- Freier, S M -- Jenison, R D -- Manoharan, M -- Zounes, M -- New York, N.Y. -- Science. 1992 Aug 14;257(5072):958-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉ISIS Pharmaceuticals, Carlsbad, CA 92008.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1502560" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; DNA, Viral/metabolism ; Gene Products, tat/metabolism ; HIV/*genetics ; Kinetics ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Oligoribonucleotides/*chemistry ; RNA, Viral/*chemistry/genetics/metabolism ; tat Gene Products, Human Immunodeficiency Virus
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  • 75
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-05-22
    Description: The growth-inhibiting peptide hormone somatostatin stimulates phosphotyrosine phosphatase activity in the human pancreatic cell line MIA PaCa-2. This hormonal activation was mediated by a pertussis toxin-sensitive guanosine 5'-triphosphate-binding protein (G protein) in the membranes of these cells. Activation of this G protein by somatostatin stimulated the dephosphorylation of exogenous epidermal growth factor receptor prepared from A-431 cells in vitro. This pathway may mediate the antineoplastic action of somatostatin in these cells and in human tumors and could represent a general mechanism of G protein coupling that is utilized by normal cells in the hormonal control of cell growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pan, M G -- Florio, T -- Stork, P J -- New York, N.Y. -- Science. 1992 May 22;256(5060):1215-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute for Advanced Biomedical Research, Oregon Health Sciences University, Portland 97201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1350382" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Carcinoma, Squamous Cell ; Cell Line ; Cell Membrane/metabolism ; Dose-Response Relationship, Drug ; Enzyme Activation ; GTP-Binding Proteins/*metabolism ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Guanosine Diphosphate/analogs & derivatives/pharmacology ; Humans ; Kinetics ; Pancreatic Neoplasms ; Peptides/metabolism ; Pertussis Toxin ; Phosphorylation ; Protein Kinases/metabolism ; Protein Tyrosine Phosphatases/*metabolism ; Receptor, Epidermal Growth Factor/metabolism ; Somatostatin/*pharmacology ; Thionucleotides/pharmacology ; Virulence Factors, Bordetella/pharmacology
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  • 76
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-08-14
    Description: In the past year, the National Institutes of Health (NIH) has filed patent applications on more than 2750 partial complementary DNA sequences of unknown function. The rationale for the filings--that patent protection may be necessary to ensure that private firms are willing to invest in developing related products--rests on two premises: first, that NIH may obtain patent rights that will offer effective product monopolies to licensee firms, and second, that unless NIH obtains these rights now, firms will be unable to obtain a comparable degree of exclusivity by other means, such as by obtaining patents on their own subsequent innovations. Neither premise is clearly wrong, although both are subject to doubt in view of statements from industry representatives that the NIH patenting strategy will deter rather than promote product development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eisenberg, R S -- New York, N.Y. -- Science. 1992 Aug 14;257(5072):903-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Michigan Law School, Ann Arbor 48109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1502556" target="_blank"〉PubMed〈/a〉
    Keywords: Biomedical Research ; Biotechnology ; DNA/*genetics ; *Federal Government ; *Genes ; Human Genome Project ; Humans ; National Institutes of Health (U.S.) ; *Patents as Topic ; United States
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  • 77
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-06-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1992 Jun 5;256(5062):1391.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1604312" target="_blank"〉PubMed〈/a〉
    Keywords: *Acquired Immunodeficiency Syndrome ; Ethics, Professional ; History, 20th Century ; Humans ; Jurisprudence ; National Institutes of Health (U.S.) ; Newspapers as Topic ; Paris ; Research/*standards ; Scientific Misconduct ; *Societies, Scientific ; United States
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  • 78
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-01-10
    Description: Many specific DNA-binding proteins bind to sites with dyad symmetry, and the bound form of the protein is a dimer. For some proteins, dimers form in solution and bind to DNA. LexA repressor of Escherichia coli has been used to test an alternative binding model in which two monomers bind sequentially. This model predicts that a repressor monomer should bind with high specificity to an isolated operator half-site. Monomer binding to a half-site was observed. A second monomer bound to an intact operator far more tightly than the first monomer; this cooperativity arose from protein-protein contacts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, B -- Little, J W -- GM24178/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jan 10;255(5041):203-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Arizona, Tucson 85721.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1553548" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*metabolism ; Base Sequence ; Binding Sites ; DNA, Bacterial/*metabolism ; DNA-Binding Proteins/*metabolism ; Deoxyribonucleases ; Escherichia coli/*metabolism ; Kinetics ; Macromolecular Substances ; Models, Structural ; Molecular Sequence Data ; Oligodeoxyribonucleotides/metabolism ; Operon ; Rec A Recombinases/genetics ; Repressor Proteins/metabolism ; *Serine Endopeptidases
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  • 79
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-03-06
    Description: Trypsin (Tr) and chymotrypsin (Ch) have similar tertiary structures, yet Tr cleaves peptides at arginine and lysine residues and Ch prefers large hydrophobic residues. Although replacement of the S1 binding site of Tr with the analogous residues of Ch is sufficient to transfer Ch specificity for ester hydrolysis, specificity for amide hydrolysis is not transferred. Trypsin is converted to a Ch-like protease when the binding pocket alterations are further modified by exchange of the Ch surface loops 185 through 188 and 221 through 225 for the analogous Tr loops. These loops are not structural components of either the S1 binding site or the extended substrate binding sites. This mutant enzyme is equivalent to Ch in its catalytic rate, but its substrate binding is impaired. Like Ch, this mutant utilizes extended substrate binding to accelerate catalysis, and substrate discrimination occurs during the acylation step rather than in substrate binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hedstrom, L -- Szilagyi, L -- Rutter, W J -- DK21344/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1992 Mar 6;255(5049):1249-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hormone Research Institute, University of California, San Francisco 94143-0534.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546324" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Amino Acid Sequence ; Base Sequence ; Binding Sites ; Chymotrypsin/*chemistry/metabolism ; Hydrolysis ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Mutagenesis, Site-Directed ; Protein Conformation ; Substrate Specificity ; Trypsin/*chemistry/genetics/metabolism
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  • 80
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-08-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, R -- New York, N.Y. -- Science. 1992 Aug 7;257(5071):739.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1496390" target="_blank"〉PubMed〈/a〉
    Keywords: Bioethics ; Body Height ; Child ; Growth Disorders/*drug therapy ; Growth Hormone/adverse effects/*therapeutic use ; Humans ; National Institutes of Health (U.S.) ; United States
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  • 81
    Publication Date: 1992-10-16
    Description: Double-strand breaks (DSBs) in Saccharomyces cerevisiae can be repaired by gene conversions or by deletions resulting from single-strand annealing between direct repeats of homologous sequences. Although rad1 mutants are resistant to x-rays and can complete DSB-mediated mating-type switching, they could not complete recombination when the ends of the break contained approximately 60 base pairs of nonhomology. Recombination was restored when the ends of the break were made homologous to donor sequences. Additionally, the absence of RAD1 led to the frequent appearance of a previously unobserved type of recombination product. These data suggest RAD1 is required to remove nonhomologous DNA from the 3' ends of recombining DNA, a process analogous to the excision of photodimers during repair of ultraviolet-damaged DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fishman-Lobell, J -- Haber, J E -- GM01722/GM/NIGMS NIH HHS/ -- GM20056/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Oct 16;258(5081):480-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1411547" target="_blank"〉PubMed〈/a〉
    Keywords: *DNA Repair ; DNA, Fungal/genetics ; Deoxyribonucleases, Type II Site-Specific/*metabolism ; Gene Conversion ; Kinetics ; *Recombination, Genetic ; Saccharomyces cerevisiae/*genetics ; Saccharomyces cerevisiae Proteins ; Sequence Deletion ; Ultraviolet Rays
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  • 82
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-05-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Culliton, B J -- New York, N.Y. -- Science. 1990 May 11;248(4956):676.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2333517" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*microbiology ; *Biotechnology ; Conflict (Psychology) ; Ethics, Professional ; *Hiv ; Humans ; National Institutes of Health (U.S.) ; *Research ; United States
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  • 83
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-03-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Culliton, B J -- New York, N.Y. -- Science. 1990 Mar 16;247(4948):1287.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2315696" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Deaminase/deficiency ; *Genetic Therapy ; Humans ; Immunologic Deficiency Syndromes/therapy ; National Institutes of Health (U.S.) ; United States
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  • 84
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-03-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Culliton, B J -- New York, N.Y. -- Science. 1990 Mar 30;247(4950):1532-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2181663" target="_blank"〉PubMed〈/a〉
    Keywords: France ; HIV/*isolation & purification ; History, 20th Century ; National Institutes of Health (U.S.) ; United States
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  • 85
    Publication Date: 1990-12-21
    Description: Human growth hormone (hGH) elicits a diverse set of biological activities including lactation that derives from binding to the prolactin (PRL) receptor. The binding affinity of hGH for the extracellular binding domain of the hPRL receptor (hPRLbp) was increased about 8000-fold by addition of 50 micromolar ZnCl2. Zinc was not required for binding of hGH to the hGH binding protein (hGHbp) or for binding of hPRL to the hPRLbp. Other divalent metal ions (Ca2+, Mg2+, Cu2+, Mn2+, and Co2+) at physiological concentrations did not support such strong binding. Scatchard analysis indicated a stoichiometry of one Zn2+ per hGH.hPRLbp complex. Mutational analysis showed that a cluster of three residues (His18, His21, and Glu174) in hGH and His188 from the hPRLbp (conserved in all PRL receptors but not GH receptors) are probable Zn2+ ligands. This polypeptide hormone.receptor "zinc sandwich" provides a molecular mechanism to explain why nonprimate GHs are not lactogenic and offers a molecular link between zinc deficiency and its association with altered functions of hGH.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cunningham, B C -- Bass, S -- Fuh, G -- Wells, J A -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1709-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Protein Engineering, Genentech, Inc., South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2270485" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Chlorides/*pharmacology ; Growth Hormone/*metabolism ; Humans ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oligonucleotide Probes ; Plasmids ; Protein Conformation ; Receptors, Prolactin/drug effects/genetics/*metabolism ; Restriction Mapping ; Zinc/metabolism/*pharmacology ; *Zinc Compounds
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  • 86
    Publication Date: 1990-11-23
    Description: Detailed kinetic investigations of a catalytic antibody that promotes the hydrolyses of an anilide and phenyl ester show that this catalyst uses a multistep kinetic sequence resembling that found in serine proteases to hydrolyze its substrates, although antibody was elicited to a single transition-state analog. Like the serine proteases the antibody catalyzes the hydrolysis reactions through a putative covalent intermediate, but unlike the enzymes it may use hydroxide ion to cleave the intermediates. Nevertheless, the antibody is a potent catalyst with turnover at higher pH values rivaling that of chymotrypsin. This analysis also reveals that turnover by the antibody is ultimately limited by product desorption, suggesting that improvements in catalytic efficiency may be achieved by judicious changes in the structure of the substrate, so that it is not superimposable on that of the eliciting hapten.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benkovic, S J -- Adams, J A -- Borders, C L Jr -- Janda, K D -- Lerner, R A -- GM4385801/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Nov 23;250(4984):1135-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pennsylvania State University, Department of Chemistry, University Park 16802.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2251500" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Aniline Compounds/metabolism ; Antibodies/*metabolism ; Catalysis ; Enzymes/*metabolism ; Hydrogen-Ion Concentration ; Hydrolysis ; Kinetics ; Nitrophenols/metabolism ; Spectrometry, Fluorescence ; Thermodynamics
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  • 87
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-05-11
    Description: Regulated expression of bacterial genes allows a pathogen to adapt to new environmental conditions within the host. The synthesis of over 30 Salmonella proteins is selectively induced during infection of macrophages. Two proteins induced by Salmonella are the heat shock proteins GroEL and DnaK. Two avirulent, macrophage-sensitive mutants of Salmonella synthesize GroEL and DnaK but fail to synthesize different subsets of proteins normally induced within the macrophage. Enhanced expression of selected Salmonella proteins contributes to bacterial survival within macrophages and may also contribute to the apparent immunodominance of heat shock proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Buchmeier, N A -- Heffron, F -- New York, N.Y. -- Science. 1990 May 11;248(4956):730-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1970672" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins/*biosynthesis/genetics/isolation & purification ; Cell Line ; Chaperonin 60 ; Electrophoresis, Gel, Two-Dimensional ; Electrophoresis, Polyacrylamide Gel ; *Escherichia coli Proteins ; *HSP70 Heat-Shock Proteins ; Heat-Shock Proteins/*biosynthesis/genetics/isolation & purification ; Kinetics ; Macrophages/*microbiology ; Molecular Weight ; Salmonella/*physiology
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  • 88
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-01-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1990 Jan 26;247(4941):404-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2300803" target="_blank"〉PubMed〈/a〉
    Keywords: *Budgets ; Financing, Government/*legislation & jurisprudence ; National Institutes of Health (U.S.) ; Research Support as Topic/*legislation & jurisprudence ; United States
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  • 89
    Publication Date: 1990-07-20
    Description: Infection by human immunodeficiency virus type-1 (HIV-1) is initiated when its envelope protein, gp120, binds to its receptor, the cell surface glycoprotein CD4. Small molecules, termed N-carbomethoxycarbonyl-prolyl-phenylalanyl benzyl esters (CPFs), blocked this binding. CPFs interacted with gp120 and did not interfere with the binding of CD4 to class II major histocompatibility complex molecules. One CPF isomer, CPF(DD), preserved CD4-dependent T cell function while inhibiting HIV-1 infection of H9 tumor cells and human T cells. Although the production of viral proteins in infected T cells is unaltered by CPF(DD), this compound prevents the spread of infection in an in vitro model system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Finberg, R W -- Diamond, D C -- Mitchell, D B -- Rosenstein, Y -- Soman, G -- Norman, T C -- Schreiber, S L -- Burakoff, S J -- New York, N.Y. -- Science. 1990 Jul 20;249(4966):287-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute, Department of Medicine, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2115689" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD4/*immunology ; Antiviral Agents/*pharmacology ; Benzyl Compounds/pharmacology ; Cell Line ; Genes, MHC Class II ; HIV Envelope Protein gp120/*immunology ; HIV-1/drug effects/immunology/*physiology ; Humans ; Kinetics ; T-Lymphocytes/immunology
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  • 90
    Publication Date: 1990-07-20
    Description: Epidermal growth factor (EGF) treatment of A-431 epidermoid carcinoma cells elicited a redistribution of phospholipase C-gamma 1 (PLC-gamma 1) from a predominantly cytosolic localization to membrane fractions. The temporal coincidence of this redistribution with EGF stimulation of inositol phosphate formation and EGF increased phosphorylation of PLC-gamma 1 suggests that the membrane association of PLC-gamma 1 is a significant event in second messenger transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Todderud, G -- Wahl, M I -- Rhee, S G -- Carpenter, G -- CA24071/CA/NCI NIH HHS/ -- GM07347/GM/NIGMS NIH HHS/ -- T32 AM07491/AM/NIADDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Jul 20;249(4966):296-8.〈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/2374928" target="_blank"〉PubMed〈/a〉
    Keywords: Carcinoma, Squamous Cell ; Cell Line ; Cell Membrane/drug effects/enzymology ; Cytosol/enzymology ; Epidermal Growth Factor/*pharmacology ; Humans ; Isoenzymes/*metabolism ; Kinetics ; Phosphopeptides/isolation & purification ; Protein Binding ; Trypsin ; Type C Phospholipases/*metabolism
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  • 91
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-04-06
    Description: The Human Genome Project is under way. The Department of Energy and the National Institutes of Health are cooperating effectively to develop organizational structures and scientific priorities that should keep the project on schedule and within its budget.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cantor, C R -- CA 39782/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Apr 6;248(4951):49-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Human Genome Center, Lawrence Berkeley Laboratory, Berkeley, CA 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2181666" target="_blank"〉PubMed〈/a〉
    Keywords: Budgets ; Federal Government ; Genomic Library ; Human Genome Project/economics/*organization & administration ; Humans ; Information Systems ; Interinstitutional Relations ; National Institutes of Health (U.S.) ; United States
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 92
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-08-31
    Description: The sodium- and potassium-dependent adenosine triphosphatase (Na+,K(+)-ATPase) maintains the transmembrane Na+ gradient to which is coupled all active cellular transport systems. The R and S alleles of the gene encoding the Na+,K(+)-ATPase alpha 1 subunit isoform were identified in Dahl salt-resistant (DR) and Dahl salt-sensitive (DS) rats, respectively. Characterization of the S allele-specific Na+,K(+)-ATPase alpha 1 complementary DNA identified a leucine substitution of glutamine at position 276. This mutation alters the hydropathy profile of a region in proximity to T3(Na), the trypsin-sensitive site that is only detected in the presence of Na+. This mutation causes a decrease in the rubidium-86 influx of S allele-specific sodium pumps, thus marking a domain in the Na+,K(+)-ATPase alpha subunit important for K+ transport, and supporting the hypothesis of a putative role of these pumps in hypertension.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herrera, V L -- Ruiz-Opazo, N -- HL 01967/HL/NHLBI NIH HHS/ -- HL 18318/HL/NHLBI NIH HHS/ -- HL 39267/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 Aug 31;249(4972):1023-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Molecular Genetics, Whitaker Cardiovascular Institute, Boston University School of Medicine, MA 02118.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1975705" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Membrane/enzymology ; Kidney/enzymology ; Kinetics ; Molecular Sequence Data ; *Mutation ; Polymorphism, Restriction Fragment Length ; Protein Conformation ; Rats ; Rats, Inbred Strains ; Rubidium/*metabolism ; Rubidium Radioisotopes ; Sodium-Potassium-Exchanging ATPase/*genetics/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 93
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-10-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Norman, C -- New York, N.Y. -- Science. 1990 Oct 5;250(4977):22.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2218508" target="_blank"〉PubMed〈/a〉
    Keywords: Budgets ; Institute of Medicine (U.S.) ; National Institutes of Health (U.S.) ; *Research Support as Topic ; *Training Support ; United States
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  • 94
    Publication Date: 1990-09-28
    Description: The proliferative potential of human diploid endothelial cells is finite, and cellular senescence in vitro is accompanied by the failure of the endothelial cell to respond to exogenous growth factors. Senescent human endothelial cells were shown to contain high amounts of the transcript for the cytokine interleukin-1 alpha (IL-1 alpha), a potent inhibitor of endothelial cell proliferation in vitro. In contrast, transformed human endothelial cells did not contain detectable IL-1 alpha messenger RNA. Treatment of human endothelial cell populations with an antisense oligodeoxynucleotide to the human IL-1 alpha transcript prevented cell senescence and extended the proliferative life-span of the cells in vitro. Removal of the IL-1 alpha antisense oligomer resulted in the generation of the senescent phenotype and loss of proliferative potential. These data suggest that human endothelial cell senescence in vitro is a dynamic process regulated by the potential intracellular activity of IL-1 alpha.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maier, J A -- Voulalas, P -- Roeder, D -- Maciag, T -- AG07450/AG/NIA NIH HHS/ -- HL32348/HL/NHLBI NIH HHS/ -- HL35627/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 Sep 28;249(4976):1570-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, Jerome H. Holland, Laboratory for the Biomedical Sciences, American Red Cross, Rockville, MD 20855.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2218499" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Division ; Cell Survival ; Cells, Cultured ; Endothelium, Vascular/*cytology/physiology ; Humans ; Interleukin-1/*genetics ; Kinetics ; Molecular Sequence Data ; Oligonucleotide Probes ; RNA, Antisense/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 95
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-04-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1990 Apr 6;248(4951):20-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2321022" target="_blank"〉PubMed〈/a〉
    Keywords: Coal ; Europe, Eastern/epidemiology ; Humans ; *International Cooperation ; Kidney Diseases/epidemiology ; National Institutes of Health (U.S.) ; *Research Support as Topic ; United States
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  • 96
    Publication Date: 1990-09-21
    Description: Calmodulin is a calcium-binding protein that participates in the transduction of calcium signals. The electric phenotypes of calmodulin mutants of Paramecium have suggested that the protein may regulate some calcium-dependent ion channels. Calcium-dependent sodium single channels in excised patches of the plasma membrane from Paramecium were identified, and their activity was shown to decrease after brief exposure to submicromolar concentrations of calcium. Channel activity was restored to these inactivated patches by adding calmodulin that was isolated from Paramecium to the cytoplasmic surface. This restoration of channel activity did not require adenosine triphosphate and therefore, probably resulted from direct binding of calmodulin, either to the sodium channel itself or to a channel regulator that was associated with the patch membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saimi, Y -- Ling, K Y -- GM22714/GM/NIGMS NIH HHS/ -- GM36386/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Sep 21;249(4975):1441-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, University of Wisconsin-Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2169650" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*pharmacology ; Calmodulin/genetics/*pharmacology/physiology ; Cell Membrane/physiology ; Kinetics ; Models, Biological ; Paramecium/*physiology ; Sodium Channels/drug effects/*physiology
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  • 97
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-08-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1990 Aug 17;249(4970):734.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2202049" target="_blank"〉PubMed〈/a〉
    Keywords: History, 20th Century ; National Institutes of Health (U.S.) ; Research Support as Topic ; Scientific Misconduct/*legislation & jurisprudence ; United States
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  • 98
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-01-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1990 Jan 5;247(4938):19.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2403693" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/history ; HIV/*isolation & purification ; History, 20th Century ; National Institutes of Health (U.S.) ; United States
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 99
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-04-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1990 Apr 13;248(4952):152, 154-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2326628" target="_blank"〉PubMed〈/a〉
    Keywords: *Biomedical Research ; Economics ; Editorial Policies ; Ethics, Professional ; Federal Government ; Humans ; *Industry ; National Institutes of Health (U.S.) ; *Science ; United States
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  • 100
    Publication Date: 1991-11-01
    Description: Voltage-dependent ion channels respond to changes in the membrane potential by means of charged voltage sensors intrinsic to the channel protein. Changes in transmembrane potential cause movement of these charged residues, which results in conformational changes in the channel. Movements of the charged sensors can be detected as currents known as gating currents. Measurement of the gating currents of the Drosophila Shaker potassium channel indicates that the charge on the voltage sensor of the channels is progressively immobilized by prolonged depolarizations. The charge is not immobilized in a mutant of the channel that lacks inactivation. These results show that the region of the molecule responsible for inactivation interacts, directly or indirectly, with the voltage sensor to prevent the return of the charge to its original position. The gating transitions between closed states of the channel appear not to be independent, suggesting that the channel subunits interact during activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bezanilla, F -- Perozo, E -- Papazian, D M -- Stefani, E -- GM30376/GM/NIGMS NIH HHS/ -- GM43459/GM/NIGMS NIH HHS/ -- HL37044/HL/NHLBI NIH HHS/ -- R01 GM043459/GM/NIGMS NIH HHS/ -- R01 GM043459-09/GM/NIGMS NIH HHS/ -- R01 GM043459-10/GM/NIGMS NIH HHS/ -- R01 GM043459-11/GM/NIGMS NIH HHS/ -- R01 GM043459-12/GM/NIGMS NIH HHS/ -- R01 GM043459-13/GM/NIGMS NIH HHS/ -- R01 GM043459-14/GM/NIGMS NIH HHS/ -- R01 GM043459-15/GM/NIGMS NIH HHS/ -- R01 GM043459-15S1/GM/NIGMS NIH HHS/ -- R01 GM043459-16/GM/NIGMS NIH HHS/ -- R01 GM043459-17/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Nov 1;254(5032):679-83.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, UCLA School of Medicine 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948047" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Drosophila/physiology ; *Ion Channel Gating/drug effects ; Kinetics ; Mutagenesis, Site-Directed ; Oocytes/drug effects/physiology ; Potassium Channels/drug effects/genetics/*physiology ; Tetraethylammonium ; Tetraethylammonium Compounds/pharmacology ; Xenopus
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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