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  • American Association for the Advancement of Science (AAAS)  (11)
  • Taylor & Francis
  • 1990-1994  (8)
  • 1980-1984  (3)
  • 1920-1924  (3)
  • 1
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    Membrane-mediated assembly of filamentous bacteriophage Pf1 coat protein (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-31
    Description: Filamentous bacteriophage Pf1 assembles by a membrane-mediated process during which the viral DNA is secreted through the membrane while being encapsulated by the major coat protein. Neutron diffraction studies showed that in the virus most of the coat protein consists of two alpha-helical segments arranged end-to-end with an intervening mobile surface loop. Nuclear magnetic resonance studies of the coat protein in the membrane-bound form have shown that the secondary structure is essentially identical to that in the intact virus. A comparison indicates that during membrane-mediated viral assembly, while the secondary structure of the coat protein is largely conserved, its tertiary structure changes substantially.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nambudripad, R -- Stark, W -- Opella, S J -- Makowski, L -- New York, N.Y. -- Science. 1991 May 31;252(5010):1305-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, Boston University, MA 02215.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925543" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophages/chemistry ; Capsid/*chemistry/metabolism ; *Capsid Proteins ; Cell Membrane/*metabolism ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Structure ; Neutrons ; Protein Conformation
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    A surface protease and the invasive character of plague (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-11-06
    Description: A 9.5-kilobase plasmid of Yersinia pestis, the causative agent of plague, is required for high virulence when mice are inoculated with the bacterium by subcutaneous injection. Inactivation of the plasmid gene pla, which encodes a surface protease, increased the median lethal dose of the bacteria for mice by a millionfold. Moreover, cloned pla was sufficient to restore segregants lacking the entire pla-bearing plasmid to full virulence. Both pla+ strains injected subcutaneously and pla- mutants injected intravenously reached high titers in liver and spleen of infected mice, whereas pla- mutants injected subcutaneously failed to do so even though they establish a sustained local infection at the injection site. More inflammatory cells accumulated in lesions caused by the pla- mutants than in lesions produced by the pla+ parent. The Pla protease was shown to be a plasminogen activator with unusual kinetic properties. It can also cleave complement C3 at a specific site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sodeinde, O A -- Subrahmanyam, Y V -- Stark, K -- Quan, T -- Bao, Y -- Goguen, J D -- AI22176/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1992 Nov 6;258(5084):1004-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester 01655.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1439793" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Bacterial Proteins ; Colony Count, Microbial ; Escherichia coli/enzymology ; Fibrinolysin/chemistry/metabolism ; Injections, Intravenous ; Kinetics ; Liver/microbiology ; Mice ; Molecular Sequence Data ; Mutation ; Plague/microbiology ; Plasmids ; Plasminogen Activators/genetics/*physiology ; Recombinant Proteins/metabolism ; Spleen/microbiology ; Tissue Plasminogen Activator/metabolism ; Urokinase-Type Plasminogen Activator/metabolism ; Yersinia pestis/*enzymology/isolation & purification/*pathogenicity
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  • 3
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    Regulation of the Amount of Starch in Plant Tissues by ADP Glucose Pyrophosphorylase (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-09
    Description: Starch, a major storage metabolite in plants, positively affects the agricultural yield of a number of crops. Its biosynthetic reactions use adenosine diphosphate glucose (ADPGlc) as a substrate; ADPGlc pyrophosphorylase, the enzyme involved in ADPGlc formation, is regulated by allosteric effectors. Evidence that this plastidial enzyme catalyzes a rate-limiting reaction in starch biosynthesis was derived by expression in plants of a gene that encodes a regulatory variant of this enzyme. Allosteric regulation was demonstrated to be the major physiological mechanism that controls starch biosynthesis. Thus, plant and bacterial systems for starch and glycogen biosynthesis are similar and distinct from yeast and mammalian systems, wherein glycogen synthase has been demonstrated to be the rate-limiting regulatory step.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stark, D M -- Timmerman, K P -- Barry, G F -- Preiss, J -- Kishore, G M -- New York, N.Y. -- Science. 1992 Oct 9;258(5080):287-92.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17835129" target="_blank"〉PubMed〈/a〉
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  • 4
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    Identification of a structural glycoprotein of an RNA virus as a ribonuclease (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-08-27
    Description: One of the three structural glycoproteins of classical swine fever virus (CSFV) is E0, a disulfide-bonded homodimer that induces virus-neutralizing antibodies and occurs in a virion-bound as well as a secreted form. E0 was shown to be similar to a family of fungal and plant ribonucleases. Purified E0 from CSFV-infected cells was a potent ribonuclease specific for uridine and inhibitable by zinc ions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schneider, R -- Unger, G -- Stark, R -- Schneider-Scherzer, E -- Thiel, H J -- New York, N.Y. -- Science. 1993 Aug 27;261(5125):1169-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Faculty of Natural Sciences, University of Innsbruck, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8356450" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Classical swine fever virus/*chemistry/enzymology/genetics ; Dithiothreitol/pharmacology ; Hydrogen-Ion Concentration ; Molecular Sequence Data ; Oxidation-Reduction ; RNA, Fungal/metabolism ; Ribonucleases/*chemistry/isolation & purification/metabolism ; Sequence Analysis ; Single-Chain Antibodies ; Substrate Specificity ; Temperature ; Uridine/metabolism ; Viral Structural Proteins/*chemistry/isolation & purification/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-03
    Description: Through the study of transcriptional activation in response to interferon alpha (IFN-alpha) and interferon gamma (IFN-gamma), a previously unrecognized direct signal transduction pathway to the nucleus has been uncovered: IFN-receptor interaction at the cell surface leads to the activation of kinases of the Jak family that then phosphorylate substrate proteins called STATs (signal transducers and activators of transcription). The phosphorylated STAT proteins move to the nucleus, bind specific DNA elements, and direct transcription. Recognition of the molecules involved in the IFN-alpha and IFN-gamma pathway has led to discoveries that a number of STAT family members exist and that other polypeptide ligands also use the Jak-STAT molecules in signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Darnell, J E Jr -- Kerr, I M -- Stark, G R -- New York, N.Y. -- Science. 1994 Jun 3;264(5164):1415-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Cell Biology, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8197455" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; DNA-Binding Proteins/*metabolism ; Genes ; Genetic Complementation Test ; Humans ; Interferon-Stimulated Gene Factor 3 ; Interferon-Stimulated Gene Factor 3, gamma Subunit ; Interferon-alpha/*pharmacology ; Interferon-gamma/*pharmacology ; Molecular Sequence Data ; Mutation ; Protein-Tyrosine Kinases/metabolism ; Regulatory Sequences, Nucleic Acid ; *Signal Transduction ; Transcription Factors/*metabolism ; *Transcriptional Activation
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  • 6
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    A single phosphotyrosine residue of Stat91 required for gene activation by interferon-gamma (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-09-24
    Description: Interferon-gamma (IFN-gamma) stimulates transcription of specific genes by inducing tyrosine phosphorylation of a 91-kilodalton cytoplasmic protein (termed STAT for signal transducer and activator of transcription). Stat91 was phosphorylated on a single site (Tyr701), and phosphorylation of this site was required for nuclear translocation, DNA binding, and gene activation. Stat84, a differentially spliced product of the same gene that lacks the 38 carboxyl-terminal amino acids of Stat91, did not activate transcription, although it was phosphorylated and translocated to the nucleus and bound DNA. Thus, Stat91 mediates activation of transcription in response to IFN-gamma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shuai, K -- Stark, G R -- Kerr, I M -- Darnell, J E Jr -- AI32489-02/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 24;261(5129):1744-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rockefeller University, Laboratory of Molecular Cell Biology, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7690989" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Line ; Cell Nucleus/metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; *Gene Expression Regulation ; Humans ; Interferon-gamma/*pharmacology ; Molecular Sequence Data ; Peptide Fragments/chemistry/metabolism ; Phosphotyrosine ; *Signal Transduction ; Transcription Factors/chemistry/*metabolism ; Transcriptional Activation ; Transfection ; Tyrosine/analogs & derivatives/chemistry
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  • 7
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    The transition state of the f + h2 reaction (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-17
    Description: The transition state region of the F + H(2) reaction has been studied by photoelectron spectroscopy of FH(2)(-). New para and normal FH(2)(-)photoelectron spectra have been measured in refined experiments and are compared here with exact three-dimensional quantum reactive scattering simulations that use an accurate new ab initio potential energy surface for F + H(2). The detailed agreement that is obtained between this fully ab initio theory and experiment is unprecedented for the F + H(2) reaction and suggests that the transition state region of the F + H(2) potential energy surface has finally been understood quantitatively.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Manolopoulos, D E -- Stark, K -- Werner, H J -- Arnold, D W -- Bradforth, S E -- Neumark, D M -- New York, N.Y. -- Science. 1993 Dec 17;262(5141):1852-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17829631" target="_blank"〉PubMed〈/a〉
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  • 8
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    Seismicity remotely triggered by the magnitude 7.3 landers, california, earthquake (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-06-11
    Description: The magnitude 7.3 Landers earthquake of 28 June 1992 triggered a remarkably sudden and widespread increase in earthquake activity across much of the western United States. The triggered earthquakes, which occurred at distances up to 1250 kilometers (17 source dimensions) from the Landers mainshock, were confined to areas of persistent seismicity and strike-slip to normal faulting. Many of the triggered areas also are sites of geothermal and recent volcanic activity. Static stress changes calculated for elastic models of the earthquake appear to be too small to have caused the triggering. The most promising explanations involve nonlinear interactions between large dynamic strains accompanying seismic waves from the mainshock and crustal fluids (perhaps including crustal magma).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hill, D P -- Reasenberg, P A -- Michael, A -- Arabaz, W J -- Beroza, G -- Brumbaugh, D -- Brune, J N -- Castro, R -- Davis, S -- Depolo, D -- Ellsworth, W L -- Gomberg, J -- Harmsen, S -- House, L -- Jackson, S M -- Johnston, M J -- Jones, L -- Keller, R -- Malone, S -- Munguia, L -- Nava, S -- Pechmann, J C -- Sanford, A -- Simpson, R W -- Smith, R B -- Stark, M -- Stickney, M -- Vidal, A -- Walter, S -- Wong, V -- Zollweg, J -- New York, N.Y. -- Science. 1993 Jun 11;260(5114):1617-23.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17810202" target="_blank"〉PubMed〈/a〉
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  • 9
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    Calcium regulation during stimulus-secretion coupling: continuous measurement of intracellular calcium activities (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-07-25
    Description: Accurate measurements of intracellular calcium activities in salivary gland epithelial cells of the insect Phormia regina were obtained with microelectrodes in which N,N'-di(11-ethoxycarbonyl)undecyl-N,N'-4,5-tetramethyl-3,6-dioxaoctane diacid diamide wsa incorporated in a liquid membrane system. When calibrated in solutions approximating the ionic concentration of the cell interior, these microelectrodes gave rapid stable responses that were linear functions of the logarithm of calcium activities and were not affected by potassium, sodium and magnesium. Continuous monitoring of calcium activities during serotonin-induced saliva release provided direct evidence of hormonal influence on transmembrane calcium movement and spontaneous regulation of intracellular calcium by stimulated cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Doherty, J -- Youmans, S J -- Armstrong, W M -- Stark, R J -- New York, N.Y. -- Science. 1980 Jul 25;209(4455):510-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7394518" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Transport/drug effects ; Calcium/*metabolism ; Diptera/*metabolism ; Epithelium/metabolism ; Kinetics ; Magnesium/pharmacology ; Microelectrodes ; Salivary Glands/drug effects/*metabolism ; Serotonin/pharmacology
    Print ISSN: 0036-8075
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  • 10
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    Lipofuscin: resolution of discrepant fluorescence data (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-05-14
    Description: Lipofuscin granules (age pigments) emit yellow light under ultraviolet excitation in the fluorescence microscope. The reported blue emission maximum of extracts of lipofuscin-laden cells may result from instrumental bias. The major fluorescent components that accumulate with age in these lysosomal residual bodies of human retinal pigment epithelium are yellow-emitting fluorophores. Different age-related fluorophores, which do emit blue light, are derived from other intracellular sources. A reevaluation of the connection between blue-emitting lipid peroxidation products and the age-related lipofuscin granules of classical pathology is necessary.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eldred, G E -- Miller, G V -- Stark, W S -- Feeney-Burns, L -- EY 03274/EY/NEI NIH HHS/ -- EY 03408/EY/NEI NIH HHS/ -- EY 05456/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1982 May 14;216(4547):757-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7079738" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Age Factors ; Cytoplasmic Granules ; Humans ; *Lipofuscin ; Lysosomes/analysis ; Pigment Epithelium of Eye/analysis/ultrastructure ; *Pigments, Biological ; Spectrometry, Fluorescence ; Spectrum Analysis
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