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  • American Association for the Advancement of Science (AAAS)  (5)
  • 1990-1994  (5)
  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-08-07
    Description: Lampreys and hagfishes (cyclostomes) traditionally were considered to be a natural (monophyletic) group. Recently, the consensus of opinion, based largely on morphological analyses, has shifted to a view that lampreys are more closely related to jawed vertebrates (gnathostomes) than to hagfishes. Phylogenetic comparisons of 18S ribosomal RNA sequences from two hagfishes, two lampreys, a tunicate, a lancelet, and a number of gnathostomes support the monophyly of the cyclostomes. These data force a reassessment of several features of early vertebrate evolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stock, D W -- Whitt, G S -- New York, N.Y. -- Science. 1992 Aug 7;257(5071):787-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ecology, Ethology, and Evolution, University of Illinois, Urbana 61801.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1496398" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA, Ribosomal/*genetics ; Genetic Variation ; Hagfishes/classification/*genetics ; Lampreys/classification/*genetics ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; *Phylogeny ; Polymerase Chain Reaction/methods ; RNA, Ribosomal, 18S/*genetics
    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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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-05-24
    Description: The probability that a residue in a protein is part of a coiled-coil structure was assessed by comparison of its flanking sequences with sequences of known coiled-coil proteins. This method was used to delineate coiled-coil domains in otherwise globular proteins, such as the leucine zipper domains in transcriptional regulators, and to predict regions of discontinuity within coiled-coil structures, such as the hinge region in myosin. More than 200 proteins that probably have coiled-coil domains were identified in GenBank, including alpha- and beta-tubulins, flagellins, G protein beta subunits, some bacterial transfer RNA synthetases, and members of the heat shock protein (Hsp70) family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lupas, A -- Van Dyke, M -- Stock, J -- AI20980/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1991 May 24;252(5009):1162-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Princeton University, NJ 08544.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2031185" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/chemistry ; Animals ; Databases, Factual ; Humans ; Probability ; *Protein Conformation ; Proteins/chemistry/*genetics
    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
    Publication Date: 1993-04-09
    Description: The Landers earthquake, which had a moment magnitude (M(w)) of 7.3, was the largest earthquake to strike the contiguous United States in 40 years. This earthquake resulted from the rupture of five major and many minor right-lateral faults near the southern end of the eastern California shear zone, just north of the San Andreas fault. Its M(w) 6.1 preshock and M(w) 6.2 aftershock had their own aftershocks and foreshocks. Surficial geological observations are consistent with local and far-field seismologic observations of the earthquake. Large surficial offsets (as great as 6 meters) and a relatively short rupture length (85 kilometers) are consistent with seismological calculations of a high stress drop (200 bars), which is in turn consistent with an apparently long recurrence interval for these faults.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sieh, K -- Jones, L -- Hauksson, E -- Hudnut, K -- Eberhart-Phillips, D -- Heaton, T -- Hough, S -- Hutton, K -- Kanamori, H -- Lilje, A -- Lindvall, S -- McGill, S F -- Mori, J -- Rubin, C -- Spotila, J A -- Stock, J -- Thio, H K -- Treiman, J -- Wernicke, B -- Zachariasen, J -- New York, N.Y. -- Science. 1993 Apr 9;260(5105):171-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17807175" 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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  • 4
    Publication Date: 1993-05-07
    Description: The fabrication of improved ceramic-matrix composites will require a better understanding of processing variables and how they control the development of the composite microstructure. Noninvasive, high-resolution methods of x-ray tomography have been used to measure the growth of silicon carbide in a woven Nicalon-fiber composite during chemical vapor infiltration. The high spatial resolution allows one to measure the densification within individual fiber tows and to follow the closure of macroscopic pores in situ. The experiments provide a direct test of a recently proposed model that describes how the surface area available for matrix deposition changes during infiltration. The measurements indicate that this surface area is independent of the fiber architecture and location within the preform and is dominated by large-scale macroporosity during the final stages of composite consolidation. The measured surface areas are in good agreement with the theoretical model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kinney, J H -- Breunig, T M -- Starr, T L -- Haupt, D -- Nichols, M C -- Stock, S R -- Butts, M D -- Saroyan, R A -- New York, N.Y. -- Science. 1993 May 7;260(5109):789-92.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17746112" 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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  • 5
    Publication Date: 1993-02-12
    Description: In human neutrophils, as in other cell types, Ras-related guanosine triphosphate-binding proteins are directed toward their regulatory targets in membranes by a series of posttranslational modifications that include methyl esterification of a carboxyl-terminal prenylcysteine residue. In intact cells and in a reconstituted in vitro system, the amount of carboxyl methylation of Ras-related proteins increased in response to the chemoattractant N-formyl-methionyl-leucyl-phenylalanine (FMLP). Activation of Ras-related proteins by guanosine-5'-O-(3-thiotriphosphate) had a similar effect and induced translocation of p22rac2 from cytosol to plasma membrane. Inhibitors of prenylcysteine carboxyl methylation effectively blocked neutrophil responses to FMLP. These findings suggest a direct link between receptor-mediated signal transduction and the carboxyl methylation of Ras-related proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Philips, M R -- Pillinger, M H -- Staud, R -- Volker, C -- Rosenfeld, M G -- Weissmann, G -- Stock, J B -- AR-07176-18/AR/NIAMS NIH HHS/ -- GM 20277/GM/NIGMS NIH HHS/ -- GM-8309/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1993 Feb 12;259(5097):977-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, New York University Medical Center, NY 10016.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8438158" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Membrane/metabolism ; Cytosol/metabolism ; GTP-Binding Proteins/*metabolism ; *Guanine Nucleotide Dissociation Inhibitors ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Guanosine Triphosphate/pharmacology ; Humans ; Methionine/analogs & derivatives/metabolism ; Methylation ; N-Formylmethionine Leucyl-Phenylalanine/pharmacology ; Neutrophils/*physiology ; Protein Methyltransferases/metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins p21(ras)/metabolism ; S-Adenosylmethionine/metabolism ; Signal Transduction/*physiology ; Tritium ; rap GTP-Binding Proteins ; rho-Specific Guanine Nucleotide Dissociation Inhibitors
    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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