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  • Humans  (4)
  • American Association for the Advancement of Science (AAAS)  (4)
  • 1
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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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  • 2
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-10-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stock, J -- New York, N.Y. -- Science. 1996 Oct 18;274(5286):370-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA. jstock@watson.princeton.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8927993" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartic Acid/metabolism ; Bacterial Proteins/chemistry/genetics/*metabolism ; Binding Sites ; Catalysis ; Chemoreceptor Cells ; Dimerization ; *Escherichia coli Proteins ; Humans ; Ligands ; Membrane Proteins/chemistry/genetics/*metabolism ; Protein Kinases/metabolism ; Receptors, Cell Surface/chemistry/*metabolism ; Receptors, Somatotropin/chemistry/metabolism ; Signal Transduction/*physiology
    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: 1993-02-12
    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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  • 4
    Publication Date: 2015-10-10
    Description: Characterizing genetic diversity in Africa is a crucial step for most analyses reconstructing the evolutionary history of anatomically modern humans. However, historic migrations from Eurasia into Africa have affected many contemporary populations, confounding inferences. Here, we present a 12.5x coverage ancient genome of an Ethiopian male ("Mota") who lived approximately 4500 years ago. We use this genome to demonstrate that the Eurasian backflow into Africa came from a population closely related to Early Neolithic farmers, who had colonized Europe 4000 years earlier. The extent of this backflow was much greater than previously reported, reaching all the way to Central, West, and Southern Africa, affecting even populations such as Yoruba and Mbuti, previously thought to be relatively unadmixed, who harbor 6 to 7% Eurasian ancestry.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gallego Llorente, M -- Jones, E R -- Eriksson, A -- Siska, V -- Arthur, K W -- Arthur, J W -- Curtis, M C -- Stock, J T -- Coltorti, M -- Pieruccini, P -- Stretton, S -- Brock, F -- Higham, T -- Park, Y -- Hofreiter, M -- Bradley, D G -- Bhak, J -- Pinhasi, R -- Manica, A -- Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2015 Nov 13;350(6262):820-2. doi: 10.1126/science.aad2879. Epub 2015 Oct 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Cambridge, Downing Street, Cambridge CB2 3EJ, UK. mg632@cam.ac.uk joneser@tcd.ie ron.pinhasi@ucd.ie am315@cam.ac.uk. ; Smurfit Institute of Genetics, Trinity College Dublin, Dublin, Ireland. mg632@cam.ac.uk joneser@tcd.ie ron.pinhasi@ucd.ie am315@cam.ac.uk. ; Department of Zoology, University of Cambridge, Downing Street, Cambridge CB2 3EJ, UK. Integrative Systems Biology Laboratory, Division of Biological and Environmental Sciences and Engineering, King Abdullah University of Science and Technology (KAUST), Thuwal 23955-6900, Kingdom of Saudi Arabia. ; Department of Zoology, University of Cambridge, Downing Street, Cambridge CB2 3EJ, UK. ; Department of Society, Culture, and Language, University of South Florida St. Petersburg, 140 7th Avenue South, St. Petersburg, FL 33701, USA. ; Department of Anthropology, Ventura College, 4667 Telegraph Road, Ventura, CA 93003, USA. Humanities and Social Sciences Program, UCLA Extension, University of California Los Angeles, 10995 Le Conte Avenue, Los Angeles, CA 90095, USA. ; Department of Archaeology and Anthropology, University of Cambridge, Pembroke Street, Cambridge CB2 3QG, UK. ; Department of Physical Sciences, Earth and Environment, University of Siena, Via di Laterina, 8-53100 Siena, Italy. ; Department of Anthropology, University of Illinois at Urbana-Champaign, Public Service Archaeology and Architecture Program, 109 Davenport Hall, 607 South Mathews Avenue, Urbana, IL 61801, USA. ; Oxford Radiocarbon Accelerator Unit, Research Laboratory for Archaeology and the History of Art, University of Oxford, Dyson Perrins Building, South Parks Road, Oxford OX1 3QY, UK. Cranfield Forensic Institute, Cranfield University, Defence Academy of the United Kingdom, Shrivenham, Oxon SN6 8LA, UK. ; Oxford Radiocarbon Accelerator Unit, Research Laboratory for Archaeology and the History of Art, University of Oxford, Dyson Perrins Building, South Parks Road, Oxford OX1 3QY, UK. ; Theragen BiO Institute, 2nd Floor B-dong, AICT bldg, Iui-dong, Youngtong-gu, Suwon 443-270, Republic of Korea. ; Institute for Biochemistry and Biology, Faculty for Mathematics and Natural Sciences, University of Potsdam, Karl-Liebknechtstrasse 24-25, 14476 Potsdam Golm, Germany. Department of Biology, University of York, Wentworth Way, Heslington, York YO10 5DD, UK. ; Smurfit Institute of Genetics, Trinity College Dublin, Dublin, Ireland. ; The Genomics Institute, Ulsan National Institute of Science and Technology, Ulsan 689-798, Republic of Korea. ; School of Archaeology and Earth Institute, University College Dublin, Dublin 4, Ireland. mg632@cam.ac.uk joneser@tcd.ie ron.pinhasi@ucd.ie am315@cam.ac.uk.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26449472" target="_blank"〉PubMed〈/a〉
    Keywords: African Continental Ancestry Group/*genetics ; Asia ; Biological Evolution ; Ethiopia ; Europe ; Genetic Variation ; *Genome, Human ; *Human Migration ; Humans ; Male
    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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