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  • American Association for the Advancement of Science (AAAS)  (7)
  • American Association of Petroleum Geologists (AAPG)
  • 2005-2009
  • 1990-1994  (7)
  • 1993  (7)
  • 1
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    SSZ-26 and SSZ-33: Two Molecular Sieves with Intersecting 10- and 12-Ring Pores (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-03
    Description: The framework structures of two closely related molecular sieves, SSZ-26 and SSZ-33, are described. These materials possess a previously missing but desired structural feature in a group of industrially significant zeolites. They contain a three-dimensional pore system that provides access to the crystal interior through both 10- and 12-rings. This property is a consequence of the organic structure-directing agents used in the synthesis of these materials. These materials are examples of the purposeful design of a micropore architecture. Both SSZ-26 and SSZ-33 contain the 4=4-1 building unit that had been previously found only in natural zeolites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lobo, R F -- Pan, M -- Chan, I -- Li, H X -- Medrud, R C -- Zones, S I -- Crozier, P A -- Davis, M E -- New York, N.Y. -- Science. 1993 Dec 3;262(5139):1543-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17829383" target="_blank"〉PubMed〈/a〉
    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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    Crystal structure of domains 3 and 4 of rat CD4: relation to the NH2-terminal domains (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-14
    Description: The CD4 antigen is a membrane glycoprotein of T lymphocytes that interacts with major histocompatibility complex class II antigens and is also a receptor for the human immunodeficiency virus. the extracellular portion of CD4 is predicted to fold into four immunoglobulin-like domains. The crystal structure of the third and fourth domains of rat CD4 was solved at 2.8 angstrom resolution and shows that both domains have immunoglobulin folds. Domain 3, however, lacks the disulfide between the beta sheets; this results in an expansion of the domain. There is a difference of 30 degrees in the orientation between domains 3 and 4 when compared with domains 1 and 2. The two CD4 fragment structures provide a basis from which models of the overall receptor can be proposed. These models suggest an extended structure comprising two rigid portions joined by a short and possibly flexible linker region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brady, R L -- Dodson, E J -- Dodson, G G -- Lange, G -- Davis, S J -- Williams, A F -- Barclay, A N -- New York, N.Y. -- Science. 1993 May 14;260(5110):979-83.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of York, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8493535" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD4/*chemistry ; Crystallization ; Humans ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Rats ; Sequence Alignment ; X-Ray Diffraction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Released form of CNTF receptor alpha component as a soluble mediator of CNTF responses (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-19
    Description: The alpha component of the receptor for ciliary neurotrophic factor (CNTF) differs from other known growth factor receptors in that it is anchored to cell membranes by a glycosylphosphatidylinositol linkage. One possible function of this type of linkage is to allow for the regulated release of this receptor component. Cell lines not normally responsive to CNTF responded to treatment with a combination of CNTF and a soluble form of the CNTF alpha receptor component. These findings not only demonstrate that the CNTF receptor alpha chain is a required component of the functional CNTF receptor complex but also reveal that it can function in soluble form as part of a heterodimeric ligand. Potential physiological roles for the soluble CNTF receptor are suggested by its presence in cerebrospinal fluid and by its release from skeletal muscle in response to peripheral nerve injury.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, S -- Aldrich, T H -- Ip, N Y -- Stahl, N -- Scherer, S -- Farruggella, T -- DiStefano, P S -- Curtis, R -- Panayotatos, N -- Gascan, H -- New York, N.Y. -- Science. 1993 Mar 19;259(5102):1736-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regeneron Pharmaceuticals, Inc., Tarrytown, NY 10591.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7681218" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation/drug effects ; Cell Division/drug effects ; Cell Membrane/metabolism ; Ciliary Neurotrophic Factor ; Cloning, Molecular ; Gene Expression ; Glycosylphosphatidylinositols/metabolism ; Growth Inhibitors/pharmacology ; Hematopoietic Stem Cells/cytology/drug effects ; Humans ; Interleukin-6/pharmacology ; Leukemia Inhibitory Factor ; Lymphokines/pharmacology ; Mice ; Muscle Denervation ; Muscles/innervation/metabolism ; Nerve Tissue Proteins/*pharmacology ; Phosphatidylinositol Diacylglycerol-Lyase ; Phosphoric Diester Hydrolases/metabolism ; Phosphotyrosine ; RNA, Messenger/genetics ; Rats ; Receptor, Ciliary Neurotrophic Factor ; Receptors, Cell Surface/chemistry/*physiology ; Signal Transduction/physiology ; Tumor Cells, Cultured ; Tyrosine/analogs & derivatives/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    LIFR beta and gp130 as heterodimerizing signal transducers of the tripartite CNTF receptor (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-06-18
    Description: The ciliary neurotrophic factor (CNTF) receptor complex is shown here to include the CNTF binding protein (CNTFR alpha) as well as the components of the leukemia inhibitory factor (LIF) receptor, LIFR beta (the LIF binding protein) and gp130 [the signal transducer of interleukin-6 (IL-6)]. Thus, the conversion of a bipartite LIF receptor into a tripartite CNTF receptor apparently occurs by the addition of the specificity-conferring element CNTFR alpha. Both CNTF and LIF trigger the association of initially separate receptor components, which in turn results in tyrosine phosphorylation of receptor subunits. Unlike the IL-6 receptor complex in which homodimerization of gp130 appears to be critical for signal initiation, signaling by the CNTF and LIF receptor complexes depends on the heterodimerization of gp130 with LIFR beta. Ligand-induced dimerization of signal-transducing receptor components, also seen with receptor tyrosine kinases, may provide a general mechanism for the transmission of a signal across the cell membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, S -- Aldrich, T H -- Stahl, N -- Pan, L -- Taga, T -- Kishimoto, T -- Ip, N Y -- Yancopoulos, G D -- New York, N.Y. -- Science. 1993 Jun 18;260(5115):1805-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regeneron Pharmaceuticals, Inc., Tarrytown, NY 10591.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8390097" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigens, CD ; Cell Line ; Cytokine Receptor gp130 ; Growth Inhibitors/pharmacology ; Interleukin-6/pharmacology ; Leukemia Inhibitory Factor ; Lymphokines/pharmacology ; Macromolecular Substances ; Membrane Glycoproteins/chemistry/*metabolism ; Models, Biological ; Nerve Growth Factors ; Nerve Tissue Proteins/pharmacology ; Phosphorylation ; Receptor, Ciliary Neurotrophic Factor ; Receptors, Cell Surface/chemistry/*metabolism ; *Receptors, Cytokine ; Receptors, Immunologic/chemistry/*metabolism ; Receptors, Interleukin-6 ; Receptors, OSM-LIF ; *Signal Transduction ; Tumor Cells, Cultured ; Tyrosine/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Women in biomedicine (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, L I -- White, A M -- New York, N.Y. -- Science. 1993 Dec 24;262(5142):1954-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17794946" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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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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  • 7
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    PAC-1: a mitogen-induced nuclear protein tyrosine phosphatase (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-19
    Description: Tyrosine phosphorylation of proteins is required for signal transduction in cells and for growth regulation. A mitogen-induced gene (PAC-1) has been cloned from human T cells and encodes a 32-kilodalton protein that contains a sequence that defines the enzymatic site of known protein phosphotyrosine phosphatases (PTPases). Other than this sequence, PAC-1 is different from several other known related PTPases exemplified by PTP-1b. PAC-1 is similar to a phosphatase induced by mitogens or heat shock in fibroblasts, a yeast gene, and a vaccinia virus-encoded serine-tyrosine phosphatase (VH1). PAC-1 was predominantly expressed in hematopoietic tissues and localized to the nucleus in transfected COS-7 cells and in mitogen-stimulated T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rohan, P J -- Davis, P -- Moskaluk, C A -- Kearns, M -- Krutzsch, H -- Siebenlist, U -- Kelly, K -- New York, N.Y. -- Science. 1993 Mar 19;259(5102):1763-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Pathology, National Cancer Institute, NIH, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7681221" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Blotting, Northern ; Cell Line ; Cell Nucleus/enzymology ; Conserved Sequence ; Cytoplasm/enzymology ; Dual Specificity Phosphatase 2 ; Fluorescent Antibody Technique ; Humans ; Immunosorbent Techniques ; Mice ; Mitogens/*pharmacology ; Molecular Sequence Data ; Organ Specificity ; Protein Phosphatase 2 ; Protein Tyrosine Phosphatases/chemistry/*genetics ; RNA/analysis ; Sequence Homology, Amino Acid ; Signal Transduction/physiology ; T-Lymphocytes/enzymology ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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