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  • Population Dynamics  (61)
  • Signal Transduction  (57)
  • Binding Sites  (51)
  • American Association for the Advancement of Science (AAAS)  (168)
  • American Society of Hematology
  • EMBO Press
  • Essen : Verl. Glückauf
  • Krefeld : Geologischer Dienst Nordhein-Westfalen
  • 2005-2009  (168)
  • 2006  (168)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (168)
  • American Society of Hematology
  • EMBO Press
  • Essen : Verl. Glückauf
  • Krefeld : Geologischer Dienst Nordhein-Westfalen
Years
  • 2005-2009  (168)
Year
  • 1
    Publication Date: 2006-12-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pounds, J Alan -- Carnaval, Ana Carolina -- Puschendorf, Robert -- Haddad, Celio F B -- Masters, Karen L -- New York, N.Y. -- Science. 2006 Dec 8;314(5805):1541-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17158306" target="_blank"〉PubMed〈/a〉
    Keywords: *Amphibians ; Animals ; Biodiversity ; Chytridiomycota ; Conservation of Natural Resources ; *Ecosystem ; *Environment ; Greenhouse Effect ; Mycoses/veterinary ; Population Dynamics
    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: 2006-01-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steneck, Robert S -- New York, N.Y. -- Science. 2006 Jan 27;311(5760):480-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Marine Sciences, University of Maine, Darling Marine Center, Walpole, ME 04573, USA. steneck@maine.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16439653" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Anthozoa ; Caribbean Region ; Computer Simulation ; Conservation of Natural Resources ; *Ecosystem ; Fishes/growth & development/*physiology ; Larva/physiology ; Models, Biological ; Population Dynamics ; *Seawater ; *Swimming ; Water Movements
    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: 2006-08-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Crowder, L B -- Osherenko, G -- Young, O R -- Airame, S -- Norse, E A -- Baron, N -- Day, J C -- Douvere, F -- Ehler, C N -- Halpern, B S -- Langdon, S J -- McLeod, K L -- Ogden, J C -- Peach, R E -- Rosenberg, A A -- Wilson, J A -- New York, N.Y. -- Science. 2006 Aug 4;313(5787):617-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Marine Conservation, Nicholas School of the Environment and Earth Sciences, Duke University Marine Laboratory, Beaufort, NC 28516, USA. lcrowder@duke.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16888124" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biodiversity ; *Conservation of Natural Resources ; *Ecosystem ; Environment ; Fisheries ; Fishes ; *Government Regulation ; *Marine Biology ; Oceans and Seas ; Population Dynamics ; Seawater ; United States
    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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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-11-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stokstad, Erik -- New York, N.Y. -- Science. 2006 Nov 3;314(5800):745.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17082432" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; Biomass ; Conservation of Natural Resources ; *Ecosystem ; *Fisheries ; *Fishes ; Forecasting ; Oceans and Seas ; *Plants ; Population Dynamics ; Seafood ; Seawater ; Water Pollution
    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: 2006-10-21
    Description: Dey and Joshi (Reports, 21 April 2006, p. 434) studied replicate laboratory populations of Drosophila and reported that low migration led to asynchrony among subpopulations. We argue that this unexpected outcome may be due to variation in the initial size of the subpopulations and uncontrolled stochasticity in the experiments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ranta, Esa -- Kaitala, Veijo -- New York, N.Y. -- Science. 2006 Oct 20;314(5798):420; author reply 420.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Integrative Ecology Unit, Department of Biological and Environmental Sciences, P.O. Box 65 (Viikinkaari 1), FIN-00014 University of Helsinki, Finland. esa.ranta@helsinki.fi〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17053132" target="_blank"〉PubMed〈/a〉
    Keywords: *Animal Migration ; Animals ; Computer Simulation ; Drosophila melanogaster/*physiology ; Models, Biological ; Population Dynamics ; Population Growth ; Stochastic Processes
    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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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-12-13
    Description: Humans behave altruistically in natural settings and experiments. A possible explanation-that groups with more altruists survive when groups compete-has long been judged untenable on empirical grounds for most species. But there have been no empirical tests of this explanation for humans. My empirical estimates show that genetic differences between early human groups are likely to have been great enough so that lethal intergroup competition could account for the evolution of altruism. Crucial to this process were distinctive human practices such as sharing food beyond the immediate family, monogamy, and other forms of reproductive leveling. These culturally transmitted practices presuppose advanced cognitive and linguistic capacities, possibly accounting for the distinctive forms of altruism found in our species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bowles, Samuel -- New York, N.Y. -- Science. 2006 Dec 8;314(5805):1569-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Santa Fe Institute, 1399 Hyde Park Road, Santa Fe, NM 87501, USA, and Universita di Siena, 17 Piazza San Francesco, Siena, Italy. bowles@santafe.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17158320" target="_blank"〉PubMed〈/a〉
    Keywords: *Altruism ; Archaeology ; *Biological Evolution ; Climate ; *Competitive Behavior ; Cultural Evolution ; Genetic Variation ; Genetics, Population ; *Group Processes ; Humans ; Mathematics ; Models, Theoretical ; Population Dynamics ; *Reproduction ; Selection, Genetic ; Violence ; Warfare
    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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  • 7
    Publication Date: 2006-04-22
    Description: Given the considerable challenges to the rapid development of an effective vaccine against influenza, antiviral agents will play an important role as a first-line defense if a new pandemic occurs. The large-scale use of drugs for chemoprophylaxis and treatment will impose strong selection for the evolution of drug-resistant strains. The ensuing transmission of those strains could substantially limit the effectiveness of the drugs as a first-line defense. Summarizing recent data on the rate at which the treatment of influenza infection generates resistance de novo and on the transmission fitness of resistant virus, we discuss possible implications for the epidemiological spread of drug resistance in the context of an established population dynamic model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Regoes, Roland R -- Bonhoeffer, Sebastian -- New York, N.Y. -- Science. 2006 Apr 21;312(5772):389-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Integrative Biology, ETH Zurich, ETH Zentrum CHN K12.1, Universitatsstrasse 16, CH 8092 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16627735" target="_blank"〉PubMed〈/a〉
    Keywords: Acetamides/pharmacology/therapeutic use ; Amantadine/pharmacology/therapeutic use ; Antiviral Agents/*pharmacology/*therapeutic use ; Computer Simulation ; Disease Outbreaks ; *Drug Resistance, Viral/genetics ; Humans ; Influenza A virus/*drug effects/genetics/pathogenicity ; Influenza, Human/*drug therapy/epidemiology/*prevention & control/virology ; Mathematics ; Models, Biological ; Mutation ; Neuraminidase/antagonists & inhibitors ; Orthomyxoviridae/*drug effects/genetics/pathogenicity ; Oseltamivir ; Population Dynamics
    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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  • 8
    Publication Date: 2006-01-28
    Description: An ecological community's species diversity tends to erode through time as a result of stochastic extinction, competitive exclusion, and unstable host-enemy dynamics. This erosion of diversity can be prevented over the short term if recruits are highly diverse as a result of preferential recruitment of rare species or, alternatively, if rare species survive preferentially, which increases diversity as the ages of the individuals increase. Here, we present census data from seven New and Old World tropical forest dynamics plots that all show the latter pattern. Within local areas, the trees that survived were as a group more diverse than those that were recruited or those that died. The larger (and therefore on average older) survivors were more diverse within local areas than the smaller survivors. When species were rare in a local area, they had a higher survival rate than when they were common, resulting in enrichment for rare species and increasing diversity with age and size class in these complex ecosystems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wills, Christopher -- Harms, Kyle E -- Condit, Richard -- King, David -- Thompson, Jill -- He, Fangliang -- Muller-Landau, Helene C -- Ashton, Peter -- Losos, Elizabeth -- Comita, Liza -- Hubbell, Stephen -- Lafrankie, James -- Bunyavejchewin, Sarayudh -- Dattaraja, H S -- Davies, Stuart -- Esufali, Shameema -- Foster, Robin -- Gunatilleke, Nimal -- Gunatilleke, Savitri -- Hall, Pamela -- Itoh, Akira -- John, Robert -- Kiratiprayoon, Somboon -- de Lao, Suzanne Loo -- Massa, Marie -- Nath, Cheryl -- Noor, Md Nur Supardi -- Kassim, Abdul Rahman -- Sukumar, Raman -- Suresh, Hebbalalu Satyanarayana -- Sun, I-Fang -- Tan, Sylvester -- Yamakura, Takuo -- Zimmerman, Jess -- New York, N.Y. -- Science. 2006 Jan 27;311(5760):527-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biological Sciences, University of California, San Diego, La Jolla, CA 92093-0116, USA. cwills@ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16439661" target="_blank"〉PubMed〈/a〉
    Keywords: *Biodiversity ; *Ecosystem ; Population Density ; Population Dynamics ; *Trees/growth & development ; Tropical Climate
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-07-01
    Description: During embryogenesis, stem cells are set aside to fuel the postnatal hair cycle and repair the epidermis after injury. To define how hair follicle stem cells are specified and maintained in an undifferentiated state, we developed a strategy to isolate and transcriptionally profile embryonic hair progenitors in mice. We identified Lhx2 as a transcription factor positioned downstream of signals necessary to specify hair follicle stem cells, but upstream from signals required to drive activated stem cells to terminally differentiate. Using gain- and loss-of-function studies, we uncovered a role for Lhx2 in maintaining the growth and undifferentiated properties of hair follicle progenitors.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2405918/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2405918/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rhee, Horace -- Polak, Lisa -- Fuchs, Elaine -- R01 AR031737/AR/NIAMS NIH HHS/ -- R01 AR031737-24/AR/NIAMS NIH HHS/ -- R01 AR050452/AR/NIAMS NIH HHS/ -- R01 AR050452-04/AR/NIAMS NIH HHS/ -- R01-AR050452/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Jun 30;312(5782):1946-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Rockefeller University, 1230 York Avenue, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16809539" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Lineage ; Cell Proliferation ; Epidermis/cytology/embryology ; Female ; Gene Expression Profiling ; Gene Expression Regulation, Developmental ; Hair/embryology/growth & development ; Hair Follicle/*cytology/embryology/physiology ; Homeodomain Proteins/genetics/*physiology ; LIM-Homeodomain Proteins ; Male ; Mice ; Mice, Knockout ; Mice, Transgenic ; Morphogenesis ; Oligonucleotide Array Sequence Analysis ; Signal Transduction ; Skin Transplantation ; Stem Cells/*physiology ; Transcription Factors/genetics/*physiology ; Up-Regulation
    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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  • 10
    Publication Date: 2006-07-01
    Description: Although enzymes often incorporate molecular recognition elements to orient substrates selectively, such strategies are rarely achieved by synthetic catalysts. We combined molecular recognition through hydrogen bonding with C-H activation to obtain high-turnover catalytic regioselective functionalization of sp3 C-H bonds remote from the -COOH recognition group. The catalyst contains a Mn(mu-O)2Mn reactive center and a ligand based on Kemp's triacid that directs a -COOH group to anchor the carboxylic acid group of the substrate and thus modify the usual selectivity for oxidation. Control experiments supported the role of hydrogen bonding in orienting the substrate to achieve high selectivity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Das, Siddhartha -- Incarvito, Christopher D -- Crabtree, Robert H -- Brudvig, Gary W -- GM32715/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Jun 30;312(5782):1941-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Yale University, 225 Prospect Street, Post Office Box 208107, New Haven, CT 06520-8107, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16809537" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Carbon/*chemistry ; Carboxylic Acids/*chemistry ; *Catalysis ; Chemistry, Physical ; Hydrogen/*chemistry ; Hydrogen Bonding ; Ibuprofen/*chemistry ; Ligands ; Magnetic Resonance Spectroscopy ; Manganese/*chemistry ; Models, Chemical ; Models, Molecular ; Molecular Structure ; Organometallic Compounds/*chemistry ; Oxidation-Reduction ; Physicochemical Phenomena
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 11
    Publication Date: 2006-04-08
    Description: According to Darwinian theory, complexity evolves by a stepwise process of elaboration and optimization under natural selection. Biological systems composed of tightly integrated parts seem to challenge this view, because it is not obvious how any element's function can be selected for unless the partners with which it interacts are already present. Here we demonstrate how an integrated molecular system-the specific functional interaction between the steroid hormone aldosterone and its partner the mineralocorticoid receptor-evolved by a stepwise Darwinian process. Using ancestral gene resurrection, we show that, long before the hormone evolved, the receptor's affinity for aldosterone was present as a structural by-product of its partnership with chemically similar, more ancient ligands. Introducing two amino acid changes into the ancestral sequence recapitulates the evolution of present-day receptor specificity. Our results indicate that tight interactions can evolve by molecular exploitation-recruitment of an older molecule, previously constrained for a different role, into a new functional complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bridgham, Jamie T -- Carroll, Sean M -- Thornton, Joseph W -- F32-GM074398/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Apr 7;312(5770):97-101.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Ecology and Evolutionary Biology, University of Oregon, Eugene, OR 97403, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16601189" target="_blank"〉PubMed〈/a〉
    Keywords: Aldosterone/chemistry/*metabolism ; Amino Acid Substitution ; Animals ; Bayes Theorem ; Binding Sites ; Desoxycorticosterone/metabolism ; *Evolution, Molecular ; Gene Duplication ; Hagfishes ; Hydrocortisone/metabolism ; Lampreys ; Ligands ; Mutation ; Perciformes ; Phylogeny ; Rats ; Receptors, Glucocorticoid/chemistry/genetics/metabolism ; Receptors, Mineralocorticoid/chemistry/*genetics/*metabolism ; Receptors, Steroid/chemistry/*genetics/*metabolism ; Skates (Fish)
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  • 12
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-09-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mustelin, Tomas -- New York, N.Y. -- Science. 2006 Sep 29;313(5795):1902-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program on Inflammatory Disease Research, Infectious and Inflammatory Disease Center, and Program of Signal Transduction, Cancer Center, Burnham Institute for Medical Research, La Jolla, CA 92037, USA. tmustelin@burnham.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17008518" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigen Presentation ; Antigens, CD ; Antigens, CD28/metabolism ; Antigens, CD80/metabolism ; Antigens, CD86/metabolism ; Antigens, Differentiation/genetics/*physiology ; *Autoimmunity ; CTLA-4 Antigen ; Cell Adhesion ; Cell Movement ; Dendritic Cells/immunology ; Humans ; Integrins/physiology ; Ligands ; Lymph Nodes/*immunology ; Lymphocyte Activation ; Mice ; Receptors, Antigen, T-Cell/immunology/metabolism ; Signal Transduction ; T-Lymphocytes/immunology/*physiology
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 13
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-03-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Green, Rhys E -- New York, N.Y. -- Science. 2006 Mar 10;311(5766):1378.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16527954" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Domestic ; Anti-Inflammatory Agents, Non-Steroidal/poisoning ; Asia ; Diclofenac/*poisoning ; *Falconiformes ; Food Chain ; India ; Population Dynamics ; Thiazines/pharmacology ; Thiazoles/pharmacology
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  • 14
    Publication Date: 2006-03-11
    Description: Until recently, northern Bering Sea ecosystems were characterized by extensive seasonal sea ice cover, high water column and sediment carbon production, and tight pelagic-benthic coupling of organic production. Here, we show that these ecosystems are shifting away from these characteristics. Changes in biological communities are contemporaneous with shifts in regional atmospheric and hydrographic forcing. In the past decade, geographic displacement of marine mammal population distributions has coincided with a reduction of benthic prey populations, an increase in pelagic fish, a reduction in sea ice, and an increase in air and ocean temperatures. These changes now observed on the shallow shelf of the northern Bering Sea should be expected to affect a much broader portion of the Pacific-influenced sector of the Arctic Ocean.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grebmeier, Jacqueline M -- Overland, James E -- Moore, Sue E -- Farley, Ed V -- Carmack, Eddy C -- Cooper, Lee W -- Frey, Karen E -- Helle, John H -- McLaughlin, Fiona A -- McNutt, S Lyn -- New York, N.Y. -- Science. 2006 Mar 10;311(5766):1461-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Marine Biogeochemistry and Ecology Group, Department of Ecology and Evolutionary Biology, 10515 Research Drive, Building A, Suite 100, University of Tennessee, Knoxville, TN 37932, USA. jgrebmei@utk.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16527980" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arctic Regions ; Ducks ; *Ecosystem ; Fishes ; Geologic Sediments/chemistry ; *Ice Cover ; Oxygen/analysis ; Pacific Ocean ; Population Dynamics ; Temperature ; Walruses ; Whales
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  • 15
    Publication Date: 2006-05-27
    Description: We describe a pathogenetic mechanism underlying a variant form of the inherited blood disorder alpha thalassemia. Association studies of affected individuals from Melanesia localized the disease trait to the telomeric region of human chromosome 16, which includes the alpha-globin gene cluster, but no molecular defects were detected by conventional approaches. After resequencing and using a combination of chromatin immunoprecipitation and expression analysis on a tiled oligonucleotide array, we identified a gain-of-function regulatory single-nucleotide polymorphism (rSNP) in a nongenic region between the alpha-globin genes and their upstream regulatory elements. The rSNP creates a new promoterlike element that interferes with normal activation of all downstream alpha-like globin genes. Thus, our work illustrates a strategy for distinguishing between neutral and functionally important rSNPs, and it also identifies a pathogenetic mechanism that could potentially underlie other genetic diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉De Gobbi, Marco -- Viprakasit, Vip -- Hughes, Jim R -- Fisher, Chris -- Buckle, Veronica J -- Ayyub, Helena -- Gibbons, Richard J -- Vernimmen, Douglas -- Yoshinaga, Yuko -- de Jong, Pieter -- Cheng, Jan-Fang -- Rubin, Edward M -- Wood, William G -- Bowden, Don -- Higgs, Douglas R -- MC_U137961143/Medical Research Council/United Kingdom -- MC_U137961145/Medical Research Council/United Kingdom -- MC_U137961147/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2006 May 26;312(5777):1215-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Molecular Haematology Unit, Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, OX3 9DS, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16728641" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cells, Cultured ; Chromatin Immunoprecipitation ; Chromosomes, Human, Pair 16/*genetics ; Erythroblasts ; GATA1 Transcription Factor/metabolism ; Gene Expression ; Gene Expression Profiling ; Globins/*genetics ; Haplotypes ; Humans ; Melanesia ; Minisatellite Repeats ; Multigene Family ; Oligonucleotide Array Sequence Analysis ; *Polymorphism, Single Nucleotide ; *Promoter Regions, Genetic ; Regulatory Elements, Transcriptional ; Transcription, Genetic ; alpha-Thalassemia/*genetics
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  • 16
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-08-12
    Description: Long-distance dispersal (LDD) of plants poses challenges to research because it involves rare events driven by complex and highly stochastic processes. The current surge of renewed interest in LDD, motivated by growing recognition of its critical importance for natural populations and communities and for humanity, promises an improved, quantitatively derived understanding of LDD. To gain deep insights into the patterns, mechanisms, causes, and consequences of LDD, we must look beyond the standard dispersal vectors and the mean trend of the distribution of dispersal distances. "Nonstandard" mechanisms such as extreme climatic events and generalized LDD vectors seem to hold the greatest explanatory power for the drastic deviations from the mean trend, deviations that make the nearly impossible LDD a reality.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nathan, Ran -- New York, N.Y. -- Science. 2006 Aug 11;313(5788):786-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Movement Ecology Laboratory, Department of Evolution, Systematics and Ecology, Alexander Silberman Institute of Life Sciences, Hebrew University of Jerusalem, Givat Ram, 91904 Jerusalem, Israel. rnathan@cc.huji.ac.il〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16902126" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; *Ecosystem ; *Environment ; Humans ; Models, Biological ; *Plants ; Pollen ; Population Dynamics ; Probability ; *Seeds ; Selection, Genetic ; Stochastic Processes ; Water Movements ; *Weather ; Wind
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  • 17
    Publication Date: 2006-06-10
    Description: Horizontal gene transfer plays a major role in microbial evolution. However, newly acquired sequences can decrease fitness unless integrated into preexisting regulatory networks. We found that the histone-like nucleoid structuring protein (H-NS) selectively silences horizontally acquired genes by targeting sequences with GC content lower than the resident genome. Mutations in hns are lethal in Salmonella unless accompanied by compensatory mutations in other regulatory loci. Thus, H-NS provides a previously unrecognized mechanism of bacterial defense against foreign DNA, enabling the acquisition of DNA from exogenous sources while avoiding detrimental consequences from unregulated expression of newly acquired genes. Characteristic GC/AT ratios of bacterial genomes may facilitate discrimination between a cell's own DNA and foreign DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Navarre, William Wiley -- Porwollik, Steffen -- Wang, Yipeng -- McClelland, Michael -- Rosen, Henry -- Libby, Stephen J -- Fang, Ferric C -- AI034829/AI/NIAID NIH HHS/ -- AI049417/AI/NIAID NIH HHS/ -- AI052237/AI/NIAID NIH HHS/ -- AI057733/AI/NIAID NIH HHS/ -- AI39557/AI/NIAID NIH HHS/ -- AI48622/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2006 Jul 14;313(5784):236-8. Epub 2006 Jun 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Laboratory Medicine, University of Washington, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16763111" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/genetics/*metabolism ; Base Composition ; Binding Sites ; Chromatin Immunoprecipitation ; DNA, Bacterial/*chemistry/*genetics ; DNA-Binding Proteins/genetics/*metabolism ; Gene Expression Regulation, Bacterial ; *Gene Silencing ; *Gene Transfer, Horizontal ; Genome, Bacterial ; Helicobacter pylori/genetics ; Models, Genetic ; Mutation ; Oligonucleotide Array Sequence Analysis ; Repressor Proteins/genetics/*metabolism ; Salmonella typhimurium/*genetics/physiology
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  • 18
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-06-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neels, Jaap G -- Olefsky, Jerrold M -- New York, N.Y. -- Science. 2006 Jun 23;312(5781):1756-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0673, USA. jolefsky@ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16794069" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyl-CoA Carboxylase/antagonists & inhibitors/*metabolism ; Adipocytes/metabolism ; Adipose Tissue/*metabolism ; Animals ; Cell Cycle Proteins/*metabolism ; Energy Intake ; Energy Metabolism ; Enzyme Activation ; Fasting ; Fatty Acids/metabolism ; Hepatocytes/metabolism ; Insulin/physiology ; Insulin Resistance ; *Lipid Metabolism ; Lipogenesis ; Liver/metabolism ; Malonyl Coenzyme A/metabolism ; Mice ; Models, Biological ; Nuclear Proteins/*metabolism ; Obesity/therapy ; Oxidation-Reduction ; Phosphorylation ; Proto-Oncogene Proteins c-akt/antagonists & inhibitors/metabolism ; Signal Transduction ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/*metabolism
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  • 19
    Publication Date: 2006-04-22
    Description: Very few experimental studies have examined how migration rate affects metapopulation dynamics and stability. We studied the dynamics of replicate laboratory metapopulations of Drosophila under different migration rates. Low migration stabilized metapopulation dynamics, while promoting unstable subpopulation dynamics, by inducing asynchrony among neighboring subpopulations. High migration synchronized subpopulation dynamics, thereby destabilizing the metapopulations. Contrary to some theoretical predictions, increased migration did not affect average population size. Simulations based on a simple non-species-specific population growth model captured most features of the data, which suggests that our results are generalizable.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dey, Sutirth -- Joshi, Amitabh -- New York, N.Y. -- Science. 2006 Apr 21;312(5772):434-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Evolutionary Biology Laboratory, Evolutionary & Organismal Biology Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Jakkur P.O., Bangalore 560 064, India.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16627743" target="_blank"〉PubMed〈/a〉
    Keywords: *Animal Migration ; Animals ; Computer Simulation ; Drosophila melanogaster/*physiology ; Models, Biological ; Population Density ; Population Dynamics ; Population Growth
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  • 20
    Publication Date: 2006-02-25
    Description: Sibly et al. (Reports, 22 July 2005, p. 607) recently estimated the relationship between population size and growth rate for 1780 time series of various species. I explain why some aspects of their analysis are questionable and, therefore, why their results and estimation procedure should be used with care.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ross, Joshua V -- New York, N.Y. -- Science. 2006 Feb 24;311(5764):1100; author reply 1100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Mathematics, University of Queensland, St. Lucia, QLD 4072, Australia. jvr@maths.uq.edu.au〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16497916" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Birds ; Conservation of Natural Resources ; Ecosystem ; *Fishes ; *Insects ; Logistic Models ; *Mammals ; Mathematics ; Models, Biological ; Population Density ; Population Dynamics ; Population Growth ; Regression Analysis
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  • 21
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-12-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Linden, Joel -- New York, N.Y. -- Science. 2006 Dec 15;314(5806):1689-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Virginia, Charlottesville, VA 22908, USA. jlinden@virginia.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17170280" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine/metabolism ; Adenosine Monophosphate/metabolism ; Adenosine Triphosphate/*metabolism ; Animals ; Apyrase/pharmacology ; *Autocrine Communication ; Blood Platelets/metabolism ; Cell Membrane/metabolism ; *Chemotaxis, Leukocyte/drug effects ; Endothelial Cells/metabolism ; Mice ; Models, Biological ; N-Formylmethionine Leucyl-Phenylalanine ; Neutrophils/drug effects/*metabolism/physiology ; Receptor, Adenosine A3/metabolism ; Receptors, Purinergic/*metabolism ; Receptors, Purinergic P2/metabolism ; Receptors, Purinergic P2Y2 ; Respiratory Burst/drug effects ; Signal Transduction
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  • 22
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-03-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, Richard -- New York, N.Y. -- Science. 2006 Mar 10;311(5766):1364-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16527940" target="_blank"〉PubMed〈/a〉
    Keywords: Archaeology ; Cambodia ; Cities/*history ; Conservation of Natural Resources ; Environment ; History, Medieval ; Population Dynamics ; Sanitary Engineering/history ; Trees ; Water Supply
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  • 23
    Publication Date: 2006-07-29
    Description: In flowering plants, the male germline begins with an asymmetric division, after which one of the resulting cells, the generative cell, divides symmetrically to produce two sperm cells. We show here that the male germline is initiated by transcriptional control. We identify GRSF, germline-restrictive silencing factor, from the lily. GRSF is ubiquitous in nongerm cells and is absent from male germ cells. GRSF recognizes silencer sequences in promoters of genes specific to the germline, stably repressing these genes in cells that are not destined to become germ cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haerizadeh, Farzad -- Singh, Mohan B -- Bhalla, Prem L -- New York, N.Y. -- Science. 2006 Jul 28;313(5786):496-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Plant Molecular Biology and Biotechnology Laboratory, Australian Research Council Centre of Excellence for Integrative Legume Research, Faculty of Land and Food Resources, University of Melbourne, Parkville, Victoria 3010, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16873660" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Arabidopsis/cytology/genetics/metabolism ; Binding Sites ; Cell Lineage ; Cell Nucleus/metabolism ; Chromatin Immunoprecipitation ; Conserved Sequence ; *Gene Expression Regulation, Plant ; Gene Silencing ; Genes, Plant ; Germ Cells/*cytology/metabolism ; Lilium/cytology/*genetics/metabolism ; Plant Proteins/chemistry/*genetics/metabolism ; Promoter Regions, Genetic ; Recombinant Fusion Proteins ; Repressor Proteins/chemistry/genetics/*metabolism ; *Silencer Elements, Transcriptional ; *Transcription, Genetic ; Transformation, Genetic
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  • 24
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-12-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yeates, Todd O -- Beeby, Morgan -- New York, N.Y. -- Science. 2006 Dec 22;314(5807):1882-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California Los Angeles, Los Angeles, CA90024-1569, USA. yeates@mbi.ucla.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17185587" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Evolution, Molecular ; Gene Duplication ; Gene Transfer, Horizontal ; *Metabolic Networks and Pathways ; Mutation ; Protein Binding ; *Protein Interaction Mapping ; Proteins/*chemistry/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/chemistry/metabolism
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  • 25
    Publication Date: 2006-04-08
    Description: Aortic aneurysm and dissection are manifestations of Marfan syndrome (MFS), a disorder caused by mutations in the gene that encodes fibrillin-1. Selected manifestations of MFS reflect excessive signaling by the transforming growth factor-beta (TGF-beta) family of cytokines. We show that aortic aneurysm in a mouse model of MFS is associated with increased TGF-beta signaling and can be prevented by TGF-beta antagonists such as TGF-beta-neutralizing antibody or the angiotensin II type 1 receptor (AT1) blocker, losartan. AT1 antagonism also partially reversed noncardiovascular manifestations of MFS, including impaired alveolar septation. These data suggest that losartan, a drug already in clinical use for hypertension, merits investigation as a therapeutic strategy for patients with MFS and has the potential to prevent the major life-threatening manifestation of this disorder.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1482474/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1482474/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Habashi, Jennifer P -- Judge, Daniel P -- Holm, Tammy M -- Cohn, Ronald D -- Loeys, Bart L -- Cooper, Timothy K -- Myers, Loretha -- Klein, Erin C -- Liu, Guosheng -- Calvi, Carla -- Podowski, Megan -- Neptune, Enid R -- Halushka, Marc K -- Bedja, Djahida -- Gabrielson, Kathleen -- Rifkin, Daniel B -- Carta, Luca -- Ramirez, Francesco -- Huso, David L -- Dietz, Harry C -- K08 HL067056/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2006 Apr 7;312(5770):117-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Pediatrics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16601194" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenergic beta-Antagonists/administration & dosage/therapeutic use ; Angiotensin II Type 1 Receptor Blockers/administration & dosage/*therapeutic use ; Animals ; Antibodies/immunology ; Aorta/pathology ; Aortic Aneurysm/etiology/*prevention & control ; *Disease Models, Animal ; Elastic Tissue/pathology ; Female ; Losartan/administration & dosage/*therapeutic use ; Lung/pathology ; Lung Diseases/drug therapy/pathology ; Marfan Syndrome/complications/*drug therapy/metabolism/pathology ; Mice ; Microfilament Proteins/genetics ; Mutation ; Neutralization Tests ; Pregnancy ; Pregnancy Complications/drug therapy ; Propranolol/administration & dosage/therapeutic use ; Pulmonary Alveoli/pathology ; Receptor, Angiotensin, Type 1/metabolism ; Signal Transduction ; Transforming Growth Factor beta/antagonists & inhibitors/immunology/*metabolism
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  • 26
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-03-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DiCicco-Bloom, Emanuel -- New York, N.Y. -- Science. 2006 Mar 17;311(5767):1560-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience and Cell Biology/Pediatrics (Neurology), University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA. diciccem@umdnj.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16543446" target="_blank"〉PubMed〈/a〉
    Keywords: Adherens Junctions/*physiology/ultrastructure ; Animals ; Brain/cytology/*embryology ; *Cell Adhesion ; Cell Count ; Cell Death ; Cell Differentiation ; Cell Movement ; Cell Proliferation ; Central Nervous System/cytology/embryology ; Cytoskeleton/physiology ; Hedgehog Proteins ; Hyperplasia ; Mice ; Mutation ; Neurons/cytology/*physiology ; Signal Transduction ; Stem Cells/cytology/physiology ; Trans-Activators/*metabolism ; alpha Catenin/genetics/*physiology
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  • 27
    Publication Date: 2006-12-16
    Description: Cells must amplify external signals to orient and migrate in chemotactic gradient fields. We find that human neutrophils release adenosine triphosphate (ATP) from the leading edge of the cell surface to amplify chemotactic signals and direct cell orientation by feedback through P2Y2 nucleotide receptors. Neutrophils rapidly hydrolyze released ATP to adenosine that then acts via A3-type adenosine receptors, which are recruited to the leading edge, to promote cell migration. Thus, ATP release and autocrine feedback through P2Y2 and A3 receptors provide signal amplification, controlling gradient sensing and migration of neutrophils.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Yu -- Corriden, Ross -- Inoue, Yoshiaki -- Yip, Linda -- Hashiguchi, Naoyuki -- Zinkernagel, Annelies -- Nizet, Victor -- Insel, Paul A -- Junger, Wolfgang G -- GM-60475/GM/NIGMS NIH HHS/ -- GM-66232/GM/NIGMS NIH HHS/ -- PR043034/PR/OCPHP CDC HHS/ -- R01 GM-51477/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Dec 15;314(5806):1792-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Surgery, University of California San Diego, San Diego, CA 92103, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17170310" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine/metabolism/pharmacology ; Adenosine A3 Receptor Agonists ; Adenosine A3 Receptor Antagonists ; Adenosine Triphosphate/analogs & derivatives/*metabolism/pharmacology ; Animals ; *Autocrine Communication ; Cell Membrane/metabolism ; *Chemotaxis, Leukocyte/drug effects ; Cytoplasmic Granules/metabolism ; HL-60 Cells ; Humans ; Hydrolysis ; Mice ; Mice, Knockout ; Neutrophils/drug effects/metabolism/*physiology ; Purinergic P2 Receptor Antagonists ; Receptor, Adenosine A3/*metabolism ; Receptors, Purinergic P2/*metabolism ; Receptors, Purinergic P2Y2 ; Signal Transduction ; Suramin/pharmacology
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  • 28
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-04-29
    Description: Mutations in the nuclear structural protein lamin A cause the premature aging syndrome Hutchinson-Gilford progeria (HGPS). Whether lamin A plays any role in normal aging is unknown. We show that the same molecular mechanism responsible for HGPS is active in healthy cells. Cell nuclei from old individuals acquire defects similar to those of HGPS patient cells, including changes in histone modifications and increased DNA damage. Age-related nuclear defects are caused by sporadic use, in healthy individuals, of the same cryptic splice site in lamin A whose constitutive activation causes HGPS. Inhibition of this splice site reverses the nuclear defects associated with aging. These observations implicate lamin A in physiological aging.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1855250/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1855250/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scaffidi, Paola -- Misteli, Tom -- Z01 BC010309-07/BC/NCI NIH HHS/ -- Intramural NIH HHS/ -- New York, N.Y. -- Science. 2006 May 19;312(5776):1059-63. Epub 2006 Apr 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Cancer Institute (NCI), NIH, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16645051" target="_blank"〉PubMed〈/a〉
    Keywords: Aged, 80 and over ; Aging/*physiology ; Cell Line ; Cell Nucleus/pathology ; DNA Damage ; Exons ; Histones/metabolism ; Humans ; Lamin Type A/genetics/*physiology ; Progeria/genetics/pathology ; RNA Splicing/genetics ; Signal Transduction ; Tumor Suppressor Protein p53/genetics/metabolism
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  • 29
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-07-29
    Description: Fidelity of template-dependent nucleic acid synthesis is the main determinant of stable heredity and error-free gene expression. The mechanism (or mechanisms) ensuring fidelity of transcription by DNA-dependent RNA polymerases (RNAPs) is not fully understood. Here, we show that the 3' end-proximal nucleotide of the nascent transcript stimulates hydrolysis of the penultimate phosphodiester bond by providing active groups and coordination bonds to the RNAP active center. This stimulation is much higher in the case of misincorporated nucleotide. We show that during transcription elongation, the hydrolytic reaction stimulated by misincorporated nucleotides proofreads most of the misincorporation events and thus serves as an intrinsic mechanism of transcription fidelity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zenkin, Nikolay -- Yuzenkova, Yulia -- Severinov, Konstantin -- New York, N.Y. -- Science. 2006 Jul 28;313(5786):518-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Waksman Institute, Rutgers University, Piscataway, NJ 08854, USA. nicserzen@mail.ru〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16873663" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Monophosphate/metabolism ; Base Pairing ; Binding Sites ; Catalysis ; Cytidine Monophosphate/metabolism ; DNA/metabolism ; DNA-Directed RNA Polymerases/*metabolism ; Hydrogen Bonding ; Hydrolysis ; Kinetics ; Magnesium/metabolism ; Models, Genetic ; Nucleotides/metabolism ; RNA, Messenger/*metabolism ; Templates, Genetic ; Thermus/enzymology ; *Transcription, Genetic
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  • 30
    Publication Date: 2006-10-21
    Description: The tumor suppressor programmed cell death protein 4 (PDCD4) inhibits the translation initiation factor eIF4A, an RNA helicase that catalyzes the unwinding of secondary structure at the 5' untranslated region (5'UTR) of messenger RNAs (mRNAs). In response to mitogens, PDCD4 was rapidly phosphorylated on Ser67 by the protein kinase S6K1 and subsequently degraded via the ubiquitin ligase SCF(betaTRCP). Expression in cultured cells of a stable PDCD4 mutant that is unable to bind betaTRCP inhibited translation of an mRNA with a structured 5'UTR, resulted in smaller cell size, and slowed down cell cycle progression. We propose that regulated degradation of PDCD4 in response to mitogens allows efficient protein synthesis and consequently cell growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dorrello, N Valerio -- Peschiaroli, Angelo -- Guardavaccaro, Daniele -- Colburn, Nancy H -- Sherman, Nicholas E -- Pagano, Michele -- R01-CA76584/CA/NCI NIH HHS/ -- R01-GM57587/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Oct 20;314(5798):467-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, NYU Cancer Institute, New York University School of Medicine, 550 First Avenue, MSB 599, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17053147" target="_blank"〉PubMed〈/a〉
    Keywords: 5' Untranslated Regions ; Amino Acid Motifs ; Apoptosis Regulatory Proteins/chemistry/genetics/*metabolism ; Binding Sites ; Cell Line ; Cell Line, Tumor ; *Cell Proliferation ; Cell Size ; Eukaryotic Initiation Factor-4A/antagonists & inhibitors/metabolism ; Eukaryotic Initiation Factor-4F/metabolism ; Eukaryotic Initiation Factor-4G/metabolism ; Eukaryotic Initiation Factors/metabolism ; Humans ; Mitogens/pharmacology ; Phosphorylation ; *Protein Biosynthesis ; RNA, Small Interfering ; RNA-Binding Proteins/chemistry/genetics/*metabolism ; Ribosomal Protein S6 Kinases/metabolism ; SKP Cullin F-Box Protein Ligases/*metabolism ; Serine/metabolism ; Serum ; Signal Transduction ; beta-Transducin Repeat-Containing Proteins/genetics/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 31
    Publication Date: 2006-07-15
    Description: The electric fields produced in folded proteins influence nearly every aspect of protein function. We present a vibrational spectroscopy technique that measures changes in electric field at a specific site of a protein as shifts in frequency (Stark shifts) of a calibrated nitrile vibration. A nitrile-containing inhibitor is used to deliver a unique probe vibration to the active site of human aldose reductase, and the response of the nitrile stretch frequency is measured for a series of mutations in the enzyme active site. These shifts yield quantitative information on electric fields that can be directly compared with electrostatics calculations. We show that extensive molecular dynamics simulations and ensemble averaging are required to reproduce the observed changes in field.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Suydam, Ian T -- Snow, Christopher D -- Pande, Vijay S -- Boxer, Steven G -- New York, N.Y. -- Science. 2006 Jul 14;313(5784):200-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Stanford University, Stanford, CA 94305-5080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16840693" target="_blank"〉PubMed〈/a〉
    Keywords: Aldehyde Reductase/antagonists & inhibitors/*chemistry/genetics/metabolism ; Binding Sites ; Circular Dichroism ; Computer Simulation ; *Electricity ; Enzyme Inhibitors/metabolism/pharmacology ; Humans ; Models, Molecular ; Mutation ; Nitriles/metabolism/pharmacology ; Protein Conformation ; Protein Folding ; Protein Structure, Tertiary ; Spectrophotometry, Infrared ; Spectrum Analysis ; Static Electricity
    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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  • 32
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-05-13
    Description: The study of viruses has traditionally focused on their roles as infectious agents and as tools for understanding cell biology. Viruses are now finding a new expanded role as nanoplatforms with applications in materials science and medicine. Viruses form highly symmetrical monodisperse architectures and are ideal templates for engineering multifunctionality, including multivalent display of surface ligands and encapsulation of inorganic and organic materials. These developments assure that viruses will find applications as versatile nanoscale materials.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Douglas, Trevor -- Young, Mark -- R01EB000432/EB/NIBIB NIH HHS/ -- R01GM61340/GM/NIGMS NIH HHS/ -- R21EB005364/EB/NIBIB NIH HHS/ -- New York, N.Y. -- Science. 2006 May 12;312(5775):873-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Bio-Inspired Nanomaterials, Montana State University, Bozeman, MT 59717, USA. tdouglas@chemistry.montana.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16690856" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Biomimetics ; *Biotechnology ; *Capsid/chemistry/ultrastructure ; Genetic Vectors ; Inorganic Chemicals ; Ligands ; Metals/chemistry/metabolism ; *Nanostructures ; *Nanotechnology ; Organic Chemicals ; Peptide Library ; Surface Properties ; Virus Assembly ; *Viruses/chemistry/genetics/ultrastructure
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 33
    Publication Date: 2006-04-01
    Description: IRAK-4 is a protein kinase that is pivotal in mediating signals for innate immune responses. Here, we report that IRAK-4 signaling is also essential for eliciting adaptive immune responses. Thus, in the absence of IRAK-4, in vivo T cell responses were significantly impaired. Upon T cell receptor stimulation, IRAK-4 is recruited to T cell lipid rafts, where it induces downstream signals, including protein kinase C activation through the association with Zap70. This signaling pathway was found to be required for optimal activation of nuclear factor kappaB. Our findings suggest that T cells use this critical regulator of innate immunity for the development of acquired immunity, suggesting that IRAK-4 may be involved in direct signal cross talk between the two systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Suzuki, Nobutaka -- Suzuki, Shinobu -- Millar, Douglas G -- Unno, Midori -- Hara, Hiromitsu -- Calzascia, Thomas -- Yamasaki, Sho -- Yokosuka, Tadashi -- Chen, Nien-Jung -- Elford, Alisha R -- Suzuki, Jun-Ichiro -- Takeuchi, Arata -- Mirtsos, Christine -- Bouchard, Denis -- Ohashi, Pamela S -- Yeh, Wen-Chen -- Saito, Takashi -- New York, N.Y. -- Science. 2006 Mar 31;311(5769):1927-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Cell Signaling, RIKEN Research Center for Allergy and Immunology, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama City, Kanagawa 230-0045, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16574867" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Enzyme Activation ; Immunity, Innate ; Interleukin-1 Receptor-Associated Kinases ; Isoenzymes/metabolism ; *Lymphocyte Activation ; Membrane Microdomains/enzymology ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Mice, Transgenic ; NF-kappa B/metabolism ; Phosphotransferases (Alcohol Group Acceptor)/genetics/*metabolism ; Protein Kinase C/metabolism ; Receptors, Antigen, T-Cell/immunology ; Signal Transduction ; T-Lymphocytes/*immunology ; ZAP-70 Protein-Tyrosine Kinase/metabolism
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  • 34
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-10-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, Charles R -- New York, N.Y. -- Science. 2006 Oct 6;314(5796):66-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Organismic and Evolutionary Biology and Earth and Planetary Sciences, Harvard University, 26 Oxford Street Cambridge, MA 02138, USA. cmarshal@oeb.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17023640" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; *Biological Evolution ; *Bivalvia/anatomy & histology/classification ; *Fossils ; Geography ; Phylogeny ; Population Dynamics ; *Tropical Climate
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  • 35
    Publication Date: 2006-01-10
    Description: The pathophysiology of depression remains enigmatic, although abnormalities in serotonin signaling have been implicated. We have found that the serotonin 1B receptor [5-hydroxytryptamine (5-HT1B) receptor] interacts with p11. p11 increases localization of 5-HT1B receptors at the cell surface. p11 is increased in rodent brains by antidepressants or electroconvulsive therapy, but decreased in an animal model of depression and in brain tissue from depressed patients. Overexpression of p11 increases 5-HT1B receptor function in cells and recapitulates certain behaviors seen after antidepressant treatment in mice. p11 knockout mice exhibit a depression-like phenotype and have reduced responsiveness to 5-HT1B receptor agonists and reduced behavioral reactions to an antidepressant.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Svenningsson, Per -- Chergui, Karima -- Rachleff, Ilan -- Flajolet, Marc -- Zhang, Xiaoqun -- El Yacoubi, Malika -- Vaugeois, Jean-Marie -- Nomikos, George G -- Greengard, Paul -- DA10044/DA/NIDA NIH HHS/ -- MH40899/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2006 Jan 6;311(5757):77-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular and Cellular Neuroscience, Rockefeller University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16400147" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Animals ; Annexin A2/genetics/*metabolism ; Antidepressive Agents/pharmacology ; Behavior, Animal/drug effects ; Brain/drug effects/metabolism ; Cell Membrane/metabolism ; Depression/genetics/*metabolism ; Electroconvulsive Therapy ; Female ; Humans ; Male ; Mice ; Mice, Knockout ; Mice, Transgenic ; Middle Aged ; Neurons/metabolism ; Rats ; Receptor, Serotonin, 5-HT1B/*metabolism ; S100 Proteins/genetics/*metabolism ; Serotonin/metabolism/physiology ; Signal Transduction ; Two-Hybrid System Techniques
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  • 36
    Publication Date: 2006-10-28
    Description: The inflammatory bowel diseases Crohn's disease and ulcerative colitis are common, chronic disorders that cause abdominal pain, diarrhea, and gastrointestinal bleeding. To identify genetic factors that might contribute to these disorders, we performed a genome-wide association study. We found a highly significant association between Crohn's disease and the IL23R gene on chromosome 1p31, which encodes a subunit of the receptor for the proinflammatory cytokine interleukin-23. An uncommon coding variant (rs11209026, c.1142G〉A, p.Arg381Gln) confers strong protection against Crohn's disease, and additional noncoding IL23R variants are independently associated. Replication studies confirmed IL23R associations in independent cohorts of patients with Crohn's disease or ulcerative colitis. These results and previous studies on the proinflammatory role of IL-23 prioritize this signaling pathway as a therapeutic target in inflammatory bowel disease.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4410764/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4410764/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Duerr, Richard H -- Taylor, Kent D -- Brant, Steven R -- Rioux, John D -- Silverberg, Mark S -- Daly, Mark J -- Steinhart, A Hillary -- Abraham, Clara -- Regueiro, Miguel -- Griffiths, Anne -- Dassopoulos, Themistocles -- Bitton, Alain -- Yang, Huiying -- Targan, Stephan -- Datta, Lisa Wu -- Kistner, Emily O -- Schumm, L Philip -- Lee, Annette T -- Gregersen, Peter K -- Barmada, M Michael -- Rotter, Jerome I -- Nicolae, Dan L -- Cho, Judy H -- DK62413/DK/NIDDK NIH HHS/ -- DK62420/DK/NIDDK NIH HHS/ -- DK62422/DK/NIDDK NIH HHS/ -- DK62423/DK/NIDDK NIH HHS/ -- DK62429/DK/NIDDK NIH HHS/ -- DK62431/DK/NIDDK NIH HHS/ -- DK62432/DK/NIDDK NIH HHS/ -- P30 DK063491/DK/NIDDK NIH HHS/ -- P30 DK063491-019004/DK/NIDDK NIH HHS/ -- P30 DK063491-029004/DK/NIDDK NIH HHS/ -- P30 DK063491-039004/DK/NIDDK NIH HHS/ -- P30 DK063491-049004/DK/NIDDK NIH HHS/ -- U01 DK062420/DK/NIDDK NIH HHS/ -- U01 DK062422/DK/NIDDK NIH HHS/ -- U01 DK062423/DK/NIDDK NIH HHS/ -- U01 DK062429/DK/NIDDK NIH HHS/ -- U01 DK062432/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2006 Dec 1;314(5804):1461-3. Epub 2006 Oct 26.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Gastroenterology, Hepatology and Nutrition, Department of Medicine, School of Medicine, University of Pittsburgh, University of Pittsburgh Medical Center Presbyterian, Mezzanine Level, C-Wing, 200 Lothrop Street, Pittsburgh, PA 15213, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17068223" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Case-Control Studies ; Chromosomes, Human, Pair 1/genetics ; Cohort Studies ; Colitis, Ulcerative/genetics ; Crohn Disease/*genetics ; Genetic Markers ; Genetic Predisposition to Disease ; Genetic Testing ; Genome, Human ; Haplotypes ; Humans ; Interleukin-23/metabolism ; Jews/genetics ; Linkage Disequilibrium ; *Polymorphism, Single Nucleotide ; Receptors, Interleukin/*genetics/physiology ; Signal Transduction
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  • 37
    Publication Date: 2006-06-03
    Description: Checkpoints are evolutionarily conserved signaling mechanisms that arrest cell division and alter cellular stress resistance in response to DNA damage or stalled replication forks. To study the consequences of loss of checkpoint functions in whole animals, checkpoint genes were inactivated in the nematode C. elegans. We show that checkpoint proteins are not only essential for normal development but also determine adult somatic maintenance. Checkpoint proteins play a role in the survival of postmitotic adult cells.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2568993/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2568993/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Olsen, Anders -- Vantipalli, Maithili C -- Lithgow, Gordon J -- AG21069/AG/NIA NIH HHS/ -- AG22868/AG/NIA NIH HHS/ -- NS050789-01/NS/NINDS NIH HHS/ -- R01 AG021069/AG/NIA NIH HHS/ -- R01 AG021069-04/AG/NIA NIH HHS/ -- R01 AG022868/AG/NIA NIH HHS/ -- R01 AG022868-04/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2006 Jun 2;312(5778):1381-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Buck Institute, 8001 Redwood Boulevard, Novato, CA 94945, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16741121" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological/genetics/physiology ; Animals ; Caenorhabditis elegans/cytology/growth & development/*physiology ; Caenorhabditis elegans Proteins/genetics/*physiology ; Cell Cycle Proteins/genetics/*physiology ; Cell Survival ; Heat-Shock Proteins/biosynthesis/genetics ; Mitosis/genetics/*physiology ; Mutation ; Protein Kinases/metabolism ; Schizosaccharomyces pombe Proteins ; Signal Transduction ; Stem Cells/cytology
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  • 38
    Publication Date: 2006-02-18
    Description: Norepinephrine (NE) is widely implicated in opiate withdrawal, but much less is known about its role in opiate-induced locomotion and reward. In mice lacking dopamine beta-hydroxylase (DBH), an enzyme critical for NE synthesis, we found that NE was necessary for morphine-induced conditioned place preference (CPP; a measure of reward) and locomotion. These deficits were rescued by systemic NE restoration. Viral restoration of DBH expression in the nucleus tractus solitarius, but not in the locus coeruleus, restored CPP for morphine. Morphine-induced locomotion was partially restored by DBH expression in either brain region. These data suggest that NE signaling by the nucleus tractus solitarius is necessary for morphine reward.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Olson, Valerie G -- Heusner, Carrie L -- Bland, Ross J -- During, Matthew J -- Weinshenker, David -- Palmiter, Richard D -- New York, N.Y. -- Science. 2006 Feb 17;311(5763):1017-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16484499" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Behavior, Animal/drug effects ; Conditioning (Psychology) ; Dopamine beta-Hydroxylase/genetics/metabolism ; Droxidopa/pharmacology ; Locomotion/drug effects ; Locus Coeruleus/physiology ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Morphine/*pharmacology ; Motor Activity/drug effects ; Norepinephrine/*physiology ; *Reward ; Signal Transduction ; Solitary Nucleus/*physiology ; *Synaptic Transmission
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  • 39
    Publication Date: 2006-02-04
    Description: The aging of organisms is characterized by a gradual functional decline of all organ systems. Mammalian somatic cells in culture display a limited proliferative life span, at the end of which they undergo an irreversible cell cycle arrest known as replicative senescence. Whether cellular senescence contributes to organismal aging has been controversial. We investigated telomere dysfunction, a recently discovered biomarker of cellular senescence, and found that the number of senescent fibroblasts increases exponentially in the skin of aging baboons, reaching 〉15% of all cells in very old individuals. In addition, the same cells contain activated ataxia-telangiectasia mutated kinase and heterochromatinized nuclei, confirming their senescent status.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herbig, Utz -- Ferreira, Mark -- Condel, Laura -- Carey, Dee -- Sedivy, John M -- F32 CA099388/CA/NCI NIH HHS/ -- P01 HL028972/HL/NHLBI NIH HHS/ -- P20 RR015578/RR/NCRR NIH HHS/ -- P51 RR013986/RR/NCRR NIH HHS/ -- R01 AG016694/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2006 Mar 3;311(5765):1257. Epub 2006 Feb 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, RI 02903, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16456035" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/*physiology ; Animals ; Ataxia Telangiectasia Mutated Proteins ; Biomarkers ; Cell Aging/*physiology ; Cell Cycle Proteins/metabolism ; DNA Damage ; DNA Replication ; DNA-Binding Proteins/metabolism ; Dermis/cytology ; Female ; Fibroblasts/cytology/*physiology ; Heterochromatin/metabolism ; Male ; Oxidative Stress ; Papio/*physiology ; Protein-Serine-Threonine Kinases/metabolism ; Signal Transduction ; Telomere/physiology ; Tumor Suppressor Proteins/metabolism
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  • 40
    Publication Date: 2006-03-04
    Description: The homodimeric mammalian fatty acid synthase is one of the most complex cellular multienzymes, in that each 270-kilodalton polypeptide chain carries all seven functional domains required for fatty acid synthesis. We have calculated a 4.5 angstrom-resolution x-ray crystallographic map of porcine fatty acid synthase, highly homologous to the human multienzyme, and placed homologous template structures of all individual catalytic domains responsible for the cyclic elongation of fatty acid chains into the electron density. The positioning of domains reveals the complex architecture of the multienzyme forming an intertwined dimer with two lateral semicircular reaction chambers, each containing a full set of catalytic domains required for fatty acid elongation. Large distances between active sites and conformational differences between the reaction chambers demonstrate that mobility of the acyl carrier protein and general flexibility of the multienzyme must accompany handover of the reaction intermediates during the reaction cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maier, Timm -- Jenni, Simon -- Ban, Nenad -- New York, N.Y. -- Science. 2006 Mar 3;311(5765):1258-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology and Biophysics, Department of Biology, Swiss Federal Institute of Technology (ETH Zurich), 8093 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16513975" target="_blank"〉PubMed〈/a〉
    Keywords: Acyl Carrier Protein/chemistry/metabolism ; Animals ; Binding Sites ; Catalytic Domain ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Fatty Acid Synthases/*chemistry/isolation & purification/metabolism ; Fatty Acids/biosynthesis ; Mammary Glands, Animal/enzymology ; Models, Molecular ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Swine
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  • 41
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-09-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zuckerman, Ben -- New York, N.Y. -- Science. 2006 Sep 29;313(5795):1885-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17008509" target="_blank"〉PubMed〈/a〉
    Keywords: *Birth Rate ; *Conservation of Natural Resources ; *Developed Countries ; *Environment ; Humans ; Population Dynamics ; *Population Growth
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  • 42
    Publication Date: 2006-12-02
    Description: 〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4383235/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4383235/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maini, Philip K -- Baker, Ruth E -- Chuong, Cheng-Ming -- R01 AR042177/AR/NIAMS NIH HHS/ -- R01 AR042177-11/AR/NIAMS NIH HHS/ -- R01 AR042177-12/AR/NIAMS NIH HHS/ -- R01 AR047364/AR/NIAMS NIH HHS/ -- R01 AR047364-04/AR/NIAMS NIH HHS/ -- R01 AR047364-05/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Dec 1;314(5804):1397-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Mathematical Biology, University of Oxford, Oxford OX1 3LB, UK. maini@maths.ox.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17138885" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Body Patterning ; Diffusion ; Hair Follicle/*growth & development/metabolism ; Intercellular Signaling Peptides and Proteins/*metabolism ; Mathematics ; Mice ; *Models, Biological ; Signal Transduction ; Wnt Proteins/*metabolism
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  • 43
    Publication Date: 2006-08-12
    Description: Transient infection of eukaryotic cells with commensal and extraintestinal pathogenic Escherichia coli of phylogenetic group B2 blocks mitosis and induces megalocytosis. This trait is linked to a widely spread genomic island that encodes giant modular nonribosomal peptide and polyketide synthases. Contact with E. coli expressing this gene cluster causes DNA double-strand breaks and activation of the DNA damage checkpoint pathway, leading to cell cycle arrest and eventually to cell death. Discovery of hybrid peptide-polyketide genotoxins in E. coli will change our view on pathogenesis and commensalism and open new biotechnological applications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nougayrede, Jean-Philippe -- Homburg, Stefan -- Taieb, Frederic -- Boury, Michele -- Brzuszkiewicz, Elzbieta -- Gottschalk, Gerhard -- Buchrieser, Carmen -- Hacker, Jorg -- Dobrindt, Ulrich -- Oswald, Eric -- New York, N.Y. -- Science. 2006 Aug 11;313(5788):848-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉INRA, UMR1225, Ecole Nationale Veterinaire de Toulouse, Toulouse F-31076, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16902142" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Ataxia Telangiectasia Mutated Proteins ; Cell Cycle ; Cell Cycle Proteins/metabolism ; Cell Death ; Cell Line ; Cell Nucleus/chemistry ; Cytotoxins/*metabolism ; DNA/analysis ; *DNA Damage ; DNA-Binding Proteins/metabolism ; Escherichia coli/genetics/*pathogenicity/*physiology ; G2 Phase ; *Genomic Islands ; HeLa Cells ; Histones/metabolism ; Humans ; Intestinal Mucosa/cytology/microbiology ; Molecular Sequence Data ; Mutagenesis ; Mutagens/*metabolism ; Peptides/*metabolism ; Phosphorylation ; Polyketide Synthases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; Rats ; Signal Transduction ; Tumor Suppressor Proteins/metabolism
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  • 44
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-08-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dustin, Michael L -- New York, N.Y. -- Science. 2006 Aug 11;313(5788):767-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Progam in Molecular Pathogenesis, Skirball Institute, New York University Medical Center, 540 First Avenue, New York, NY 10016, USA. dustin@saturn.med.nyu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16902113" target="_blank"〉PubMed〈/a〉
    Keywords: Actin-Related Protein 2-3 Complex/antagonists & inhibitors/metabolism ; Actins/*metabolism ; Animals ; Apoptosis ; Binding Sites ; Cell Death ; Cell Movement ; *Chemotaxis, Leukocyte ; Homeostasis ; Intracellular Membranes/physiology ; Membrane Potentials ; Mice ; Microfilament Proteins/chemistry/*physiology ; Mitochondria/*physiology ; Protein Structure, Tertiary ; Receptors, Antigen, T-Cell/immunology ; T-Lymphocytes/immunology/*physiology ; Voltage-Dependent Anion Channels/metabolism
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  • 45
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-01-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tawfik, Dan S -- New York, N.Y. -- Science. 2006 Jan 27;311(5760):475-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel. tawfik@weizmann.ac.il〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16439649" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Catalytic Domain ; *Directed Molecular Evolution ; Evolution, Molecular ; *Protein Engineering ; Substrate Specificity ; Thiolester Hydrolases/*chemistry/*metabolism ; beta-Lactamases/chemistry/*metabolism ; beta-Lactams/metabolism
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  • 46
    Publication Date: 2006-08-12
    Description: Harvesting threatens many vertebrate species, yet few whole-system manipulations have been conducted to predict the consequences of vertebrate losses on ecosystem function. Here, we show that a harvested migratory detrital-feeding fish (Prochilodontidae: Prochilodus mariae) modulates carbon flow and ecosystem metabolism. Natural declines in and experimental removal of Prochilodus decreased downstream transport of organic carbon and increased primary production and respiration. Thus, besides its economic value, Prochilodus is a critical ecological component of South American rivers. Lack of functional redundancy for this species highlights the importance of individual species and, contrary to theory, suggests that losing one species from lower trophic levels can affect ecosystem functioning even in species-rich ecosystems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taylor, Brad W -- Flecker, Alexander S -- Hall, Robert O Jr -- New York, N.Y. -- Science. 2006 Aug 11;313(5788):833-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology and Physiology, University of Wyoming, Laramie, WY 82071, USA. brad.taylor@dartmouth.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16902137" target="_blank"〉PubMed〈/a〉
    Keywords: Animal Migration ; Animals ; Biofilms ; Biomass ; Body Size ; Carbon/*metabolism ; Conservation of Natural Resources ; *Ecosystem ; Feeding Behavior ; *Fisheries ; Fishes/anatomy & histology/*physiology ; Food Chain ; Population Dynamics ; *Rivers ; Seasons ; South America ; Tropical Climate
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  • 47
    Publication Date: 2006-02-14
    Description: Respiratory complex I plays a central role in cellular energy production in bacteria and mitochondria. Its dysfunction is implicated in many human neurodegenerative diseases, as well as in aging. The crystal structure of the hydrophilic domain (peripheral arm) of complex I from Thermus thermophilus has been solved at 3.3 angstrom resolution. This subcomplex consists of eight subunits and contains all the redox centers of the enzyme, including nine iron-sulfur clusters. The primary electron acceptor, flavin-mononucleotide, is within electron transfer distance of cluster N3, leading to the main redox pathway, and of the distal cluster N1a, a possible antioxidant. The structure reveals new aspects of the mechanism and evolution of the enzyme. The terminal cluster N2 is coordinated, uniquely, by two consecutive cysteines. The novel subunit Nqo15 has a similar fold to the mitochondrial iron chaperone frataxin, and it may be involved in iron-sulfur cluster regeneration in the complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sazanov, Leonid A -- Hinchliffe, Philip -- MC_U105674180/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2006 Mar 10;311(5766):1430-6. Epub 2006 Feb 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Dunn Human Nutrition Unit, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 2XY, U.K. sazanov@mrc-dunn.cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16469879" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins/*chemistry ; Binding Sites ; Crystallography, X-Ray ; Electron Transport Complex I/*chemistry ; Iron-Binding Proteins/chemistry ; Oxidation-Reduction ; Protein Conformation ; Protein Folding ; Protein Structure, Tertiary ; Protein Subunits ; Thermus thermophilus/*chemistry
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  • 48
    Publication Date: 2006-02-04
    Description: Until now, continental shelf environments have been monitored with highly localized line-transect methods from slow-moving research vessels. These methods significantly undersample fish populations in time and space, leaving an incomplete and ambiguous record of abundance and behavior. We show that fish populations in continental shelf environments can be instantaneously imaged over thousands of square kilometers and continuously monitored by a remote sensing technique in which the ocean acts as an acoustic waveguide. The technique has revealed the instantaneous horizontal structural characteristics and volatile short-term behavior of very large fish shoals, containing tens of millions of fish and stretching for many kilometers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Makris, Nicholas C -- Ratilal, Purnima -- Symonds, Deanelle T -- Jagannathan, Srinivasan -- Lee, Sunwoong -- Nero, Redwood W -- New York, N.Y. -- Science. 2006 Feb 3;311(5761):660-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Ocean Science and Engineering, Department of Mechanical Engineering, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA. makris@mit.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16456080" target="_blank"〉PubMed〈/a〉
    Keywords: Acoustics ; Animals ; Atlantic Ocean ; Behavior, Animal ; Ecosystem ; *Fishes ; Oceanography ; Population Density ; Population Dynamics ; *Seawater ; Time
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  • 49
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-11-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Enserink, Martin -- Vogel, Gretchen -- New York, N.Y. -- Science. 2006 Nov 3;314(5800):746-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17082433" target="_blank"〉PubMed〈/a〉
    Keywords: Animal Migration ; Animals ; Animals, Domestic ; *Animals, Wild ; Behavior, Animal ; *Carnivora/genetics/physiology ; *Conservation of Natural Resources ; Ecosystem ; Europe ; Humans ; Population Dynamics ; Public Opinion ; Ursidae
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  • 50
    Publication Date: 2006-04-15
    Description: We present an atomic-level description of the reaction chemistry of an enzyme-catalyzed reaction dominated by proton tunneling. By solving structures of reaction intermediates at near-atomic resolution, we have identified the reaction pathway for tryptamine oxidation by aromatic amine dehydrogenase. Combining experiment and computer simulation, we show proton transfer occurs predominantly to oxygen O2 of Asp(128)beta in a reaction dominated by tunneling over approximately 0.6 angstroms. The role of long-range coupled motions in promoting tunneling is controversial. We show that, in this enzyme system, tunneling is promoted by a short-range motion modulating proton-acceptor distance and no long-range coupled motion is required.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Masgrau, Laura -- Roujeinikova, Anna -- Johannissen, Linus O -- Hothi, Parvinder -- Basran, Jaswir -- Ranaghan, Kara E -- Mulholland, Adrian J -- Sutcliffe, Michael J -- Scrutton, Nigel S -- Leys, David -- New York, N.Y. -- Science. 2006 Apr 14;312(5771):237-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Manchester Interdisciplinary Biocentre, University of Manchester, Jackson's Mill, Post Office Box 88, Manchester M60 1QD, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16614214" target="_blank"〉PubMed〈/a〉
    Keywords: Alcaligenes faecalis/*enzymology ; Aspartic Acid/chemistry ; Binding Sites ; Catalysis ; Chemistry, Physical ; Computer Simulation ; Crystallography, X-Ray ; Kinetics ; Models, Chemical ; Motion ; Oxidation-Reduction ; Oxidoreductases Acting on CH-NH Group Donors/*chemistry/*metabolism ; Oxygen/chemistry ; Physicochemical Phenomena ; *Protons ; Temperature ; Thermodynamics ; Tryptamines/*metabolism ; Water/chemistry
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  • 51
    Publication Date: 2006-02-25
    Description: DNA glycosylases must interrogate millions of base pairs of undamaged DNA in order to locate and then excise one damaged nucleobase. The nature of this search process remains poorly understood. Here we report the use of disulfide cross-linking (DXL) technology to obtain structures of a bacterial DNA glycosylase, MutM, interrogating undamaged DNA. These structures, solved to 2.0 angstrom resolution, reveal the nature of the search process: The protein inserts a probe residue into the helical stack and severely buckles the target base pair, which remains intrahelical. MutM therefore actively interrogates the intact DNA helix while searching for damage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Banerjee, Anirban -- Santos, Webster L -- Verdine, Gregory L -- F32 GM067380/GM/NIGMS NIH HHS/ -- GM044853/GM/NIGMS NIH HHS/ -- R01 CA100742/CA/NCI NIH HHS/ -- R01 GM044853/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Feb 24;311(5764):1153-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16497933" target="_blank"〉PubMed〈/a〉
    Keywords: *Base Pairing ; Binding Sites ; Cross-Linking Reagents ; Crystallography, X-Ray ; DNA/*chemistry/metabolism ; *DNA Damage ; DNA Glycosylases/*chemistry/*metabolism ; Geobacillus stearothermophilus/*enzymology ; Guanine/*analogs & derivatives/analysis/metabolism ; Hydrogen Bonding ; Models, Molecular ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/chemistry/metabolism ; Protein Conformation ; Protein Structure, Secondary
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  • 52
    Publication Date: 2006-07-22
    Description: CorA family members are ubiquitously distributed transporters of divalent metal cations and are considered to be the primary Mg2+ transporter of Bacteria and Archaea. We have determined a 2.9 angstrom resolution structure of CorA from Thermotoga maritima that reveals a pentameric cone-shaped protein. Two potential regulatory metal binding sites are found in the N-terminal domain that bind both Mg2+ and Co2+. The structure of CorA supports an efflux system involving dehydration and rehydration of divalent metal ions potentially mediated by a ring of conserved aspartate residues at the cytoplasmic entrance and a carbonyl funnel at the periplasmic side of the pore.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eshaghi, Said -- Niegowski, Damian -- Kohl, Andreas -- Martinez Molina, Daniel -- Lesley, Scott A -- Nordlund, Par -- New York, N.Y. -- Science. 2006 Jul 21;313(5785):354-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biophysics, Department of Medical Biochemistry and Biophysics, Karolinska Institute, SE-171 77 Stockholm, Sweden. Said.Eshaghi@ki.se〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16857941" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Cation Transport Proteins/*chemistry/metabolism ; Chlorides/analysis/metabolism ; Cobalt/chemistry/*metabolism ; Crystallography, X-Ray ; Hydrophobic and Hydrophilic Interactions ; Magnesium/chemistry/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Sequence Alignment ; Thermotoga maritima/*chemistry ; Water/chemistry
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  • 53
    Publication Date: 2006-01-28
    Description: The postsynaptic density (PSD) is a complex assembly of proteins associated with the postsynaptic membrane that organizes neurotransmitter receptors, signaling pathways, and regulatory elements within a cytoskeletal matrix. Here we show that the sterile alpha motif domain of rat Shank3/ProSAP2, a master scaffolding protein located deep within the PSD, can form large sheets composed of helical fibers stacked side by side. Zn2+, which is found in high concentrations in the PSD, binds tightly to Shank3 and may regulate assembly. Sheets of the Shank protein could form a platform for the construction of the PSD complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baron, Marisa K -- Boeckers, Tobias M -- Vaida, Bianca -- Faham, Salem -- Gingery, Mari -- Sawaya, Michael R -- Salyer, Danielle -- Gundelfinger, Eckart D -- Bowie, James U -- R01 CA081000/CA/NCI NIH HHS/ -- R01 GM063919/GM/NIGMS NIH HHS/ -- R01 GM063919-07/GM/NIGMS NIH HHS/ -- R01 GM063919-08/GM/NIGMS NIH HHS/ -- R01 GM075922/GM/NIGMS NIH HHS/ -- R01 GM075922-04/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Jan 27;311(5760):531-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, Molecular Biology Institute, University of California, Los Angeles, 611 Charles E. Young Drive East, Los Angeles, CA 90095-1570, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16439662" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/analysis/*chemistry/genetics/metabolism ; Animals ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; Hippocampus/chemistry ; Microscopy, Electron ; Models, Molecular ; Mutation ; Nerve Tissue Proteins ; Neurons/chemistry ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Rats ; Recombinant Fusion Proteins/analysis ; Solubility ; Synapses/*chemistry ; Zinc/metabolism
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  • 54
    Publication Date: 2006-02-14
    Description: Plants may "eavesdrop" on volatile organic compounds (VOCs) released by herbivore-attacked neighbors to activate defenses before being attacked themselves. Transcriptome and signal cascade analyses of VOC-exposed plants suggest that plants eavesdrop to prime direct and indirect defenses and to hone competitive abilities. Advances in research on VOC biosynthesis and perception have facilitated the production of plants that are genetically "deaf" to particular VOCs or "mute" in elements of their volatile vocabulary. Such plants, together with advances in VOC analytical instrumentation, will allow researchers to determine whether fluency enhances the fitness of plants in natural communities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baldwin, Ian T -- Halitschke, Rayko -- Paschold, Anja -- von Dahl, Caroline C -- Preston, Catherine A -- New York, N.Y. -- Science. 2006 Feb 10;311(5762):812-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Ecology, Max Planck Institute for Chemical Ecology, Hans Knoll Strasse 8, Jena 07745, Germany. baldwin@ice.mpg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16469918" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptation, Physiological ; Diffusion ; Gene Expression Regulation, Plant ; Genomics ; Mutation ; Oligonucleotide Array Sequence Analysis ; Organic Chemicals/*metabolism ; Plant Leaves/metabolism ; *Plant Physiological Phenomena ; Plants/*genetics/metabolism ; Signal Transduction ; Volatilization
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  • 55
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-08-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holden, Constance -- New York, N.Y. -- Science. 2006 Aug 11;313(5788):779-82.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16902122" target="_blank"〉PubMed〈/a〉
    Keywords: *Animal Migration ; Animals ; Behavior, Animal ; Computer Simulation ; *Ecology ; Flight, Animal ; Humans ; Models, Biological ; *Movement ; Plant Physiological Phenomena ; Population Dynamics ; Wind
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  • 56
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-07-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balter, Michael -- New York, N.Y. -- Science. 2006 Jun 30;312(5782):1894-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16809522" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; *Birth Rate ; *Developed Countries ; Developing Countries ; Emigration and Immigration ; Family Characteristics ; Female ; Humans ; Male ; Parental Leave ; Population Dynamics ; *Population Growth ; Pregnancy ; Public Policy ; *Reproductive Behavior
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  • 57
    Publication Date: 2006-09-16
    Description: Liver regeneration is an orchestrated cellular response that coordinates cell activation, lipid metabolism, and cell division. We found that caveolin-1 gene-disrupted mice (cav1-/- mice) exhibited impaired liver regeneration and low survival after a partial hepatectomy. Hepatocytes showed dramatically reduced lipid droplet accumulation and did not advance through the cell division cycle. Treatment of cav1-/- mice with glucose (which is a predominant energy substrate when compared to lipids) drastically increased survival and reestablished progression of the cell cycle. Thus, caveolin-1 plays a crucial role in the mechanisms that coordinate lipid metabolism with the proliferative response occurring in the liver after cellular injury.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fernandez, Manuel A -- Albor, Cecilia -- Ingelmo-Torres, Mercedes -- Nixon, Susan J -- Ferguson, Charles -- Kurzchalia, Teymuras -- Tebar, Francesc -- Enrich, Carlos -- Parton, Robert G -- Pol, Albert -- New York, N.Y. -- Science. 2006 Sep 15;313(5793):1628-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departament de Biologia Cellular, Facultat de Medicina, Institut d'Investigacions Biomediques August Pi i Sunyer, Universitat de Barcelona, Casanova 143, 08036 Barcelona, Spain.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16973879" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caveolae/metabolism ; Caveolin 1/genetics/*physiology ; Cell Cycle ; Cell Division ; Fatty Acids/blood/metabolism ; Glucose/administration & dosage ; Hepatectomy ; Hepatocyte Growth Factor/metabolism ; Hepatocytes/cytology/*metabolism ; *Lipid Metabolism ; Lipids/blood ; Liver/metabolism/ultrastructure ; *Liver Regeneration ; Male ; Mice ; Phosphorylation ; RNA, Small Interfering ; STAT3 Transcription Factor/metabolism ; Signal Transduction ; Triglycerides/blood/metabolism
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  • 58
    Publication Date: 2006-01-10
    Description: It is currently unclear whether observed pelagic ecosystem responses to ocean warming, such as a mid-1970s change in the eastern North Pacific, depart from typical ocean variability. We report variations in planktonic foraminifera from varved sediments off southern California spanning the past 1400 years. Increasing abundances of tropical/subtropical species throughout the 20th century reflect a warming trend superimposed on decadal-scale fluctuations. Decreasing abundances of temperate/subpolar species in the late 20th century indicate a deep, penetrative warming not observed in previous centuries. These results imply that 20th-century warming, apparently anthropogenic, has already affected lower trophic levels of the California Current.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Field, David B -- Baumgartner, Timothy R -- Charles, Christopher D -- Ferreira-Bartrina, Vicente -- Ohman, Mark D -- New York, N.Y. -- Science. 2006 Jan 6;311(5757):63-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Scripps Institution of Oceanography, University of California, San Diego, La Jolla, CA 92093, USA. dfield@mbari.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16400144" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; California ; *Climate ; *Ecosystem ; Environment ; *Eukaryota/classification ; *Geologic Sediments ; Greenhouse Effect ; Population Density ; Population Dynamics ; Principal Component Analysis ; Seasons ; Temperature ; Time Factors ; *Zooplankton/classification
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  • 59
    Publication Date: 2006-08-12
    Description: The pattern of dispersal of biologically and behaviorally modern human populations from their African origins to the rest of the occupied world between approximately 60,000 and 40,000 years ago is at present a topic of lively debate, centering principally on the issue of single versus multiple dispersals. Here I argue that the archaeological and genetic evidence points to a single successful dispersal event, which took genetically and culturally modern populations fairly rapidly across southern and southeastern Asia into Australasia, and with only a secondary and later dispersal into Europe.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mellars, Paul -- New York, N.Y. -- Science. 2006 Aug 11;313(5788):796-800.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Archaeology, Cambridge University, Cambridge CB2 3DZ, UK. pam59@cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16902130" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; *Archaeology ; Asia ; Australia ; Chromosomes, Human, Y ; Continental Population Groups/genetics/*history ; DNA, Mitochondrial ; *Emigration and Immigration ; Europe ; Founder Effect ; Genetics, Population ; History, Ancient ; Humans ; Population Dynamics ; Time
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  • 60
    Publication Date: 2006-07-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mendelson, Joseph R 3rd -- Lips, Karen R -- Gagliardo, Ronald W -- Rabb, George B -- Collins, James P -- Diffendorfer, James E -- Daszak, Peter -- Ibanez D, Roberto -- Zippel, Kevin C -- Lawson, Dwight P -- Wright, Kevin M -- Stuart, Simon N -- Gascon, Claude -- da Silva, Helio R -- Burrowes, Patricia A -- Joglar, Rafael L -- La Marca, Enrique -- Lotters, Stefan -- du Preez, Louis H -- Weldon, Che -- Hyatt, Alex -- Rodriguez-Mahecha, Jose Vicente -- Hunt, Susan -- Robertson, Helen -- Lock, Brad -- Raxworthy, Christopher J -- Frost, Darrel R -- Lacy, Robert C -- Alford, Ross A -- Campbell, Jonathan A -- Parra-Olea, Gabriela -- Bolanos, Federico -- Domingo, Jose Joaquin Calvo -- Halliday, Tim -- Murphy, James B -- Wake, Marvalee H -- Coloma, Luis A -- Kuzmin, Sergius L -- Price, Mark Stanley -- Howell, Kim M -- Lau, Michael -- Pethiyagoda, Rohan -- Boone, Michelle -- Lannoo, Michael J -- Blaustein, Andrew R -- Dobson, Andy -- Griffiths, Richard A -- Crump, Martha L -- Wake, David B -- Brodie, Edmund D Jr -- New York, N.Y. -- Science. 2006 Jul 7;313(5783):48.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Zoo Atlanta, 800 Cherokee Avenue SE, Atlanta, GA 30315, USA. jmendelson@zooatlanta.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16825553" target="_blank"〉PubMed〈/a〉
    Keywords: *Amphibians ; Animals ; *Biodiversity ; Chytridiomycota ; Conservation of Natural Resources ; Ecosystem ; *International Agencies ; International Cooperation ; Mycoses/veterinary ; Population Dynamics
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  • 61
    Publication Date: 2006-10-14
    Description: The function of cyclin-dependent kinase 2 (CDK2) is often abolished after DNA damage. The inhibition of CDK2 plays a central role in DNA damage-induced cell cycle arrest and DNA repair. However, whether CDK2 also influences the survival of cells under genotoxic stress is unknown. Forkhead box O (FOXO) transcription factors are emerging as key regulators of cell survival. CDK2 specifically phosphorylated FOXO1 at serine-249 (Ser249) in vitro and in vivo. Phosphorylation of Ser249 resulted in cytoplasmic localization and inhibition of FOXO1. This phosphorylation was abrogated upon DNA damage through the cell cycle checkpoint pathway that is dependent on the protein kinases Chk1 and Chk2. Moreover, silencing of FOXO1 by small interfering RNA diminished DNA damage-induced death in both p53-deficient and p53-proficient cells. This effect was reversed by restored expression of FOXO1 in a manner depending on phosphorylation of Ser249. Functional interaction between CDK2 and FOXO1 provides a mechanism that regulates apoptotic cell death after DNA strand breakage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Haojie -- Regan, Kevin M -- Lou, Zhenkun -- Chen, Junjie -- Tindall, Donald J -- CA91956/CA/NCI NIH HHS/ -- DK60920/DK/NIDDK NIH HHS/ -- DK65236/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2006 Oct 13;314(5797):294-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Rochester, MN 55905, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17038621" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Camptothecin/pharmacology ; Cell Line, Tumor ; Cell Nucleus/metabolism ; Checkpoint Kinase 2 ; Cyclin-Dependent Kinase 2/antagonists & inhibitors/genetics/*metabolism ; Cytoplasm/metabolism ; *DNA Damage ; Forkhead Transcription Factors/antagonists & inhibitors/*metabolism ; Humans ; Mice ; Phosphorylation ; Phosphoserine/metabolism ; Protein Kinases/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; RNA, Small Interfering ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Transcription, Genetic ; Transfection ; Tumor Suppressor Protein p53/metabolism
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  • 62
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-10-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2006 Oct 13;314(5797):244-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17038601" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Brain/physiology ; Brain Chemistry ; Cognition ; Evolution, Molecular ; Gene Expression Profiling ; Humans ; Invertebrates/anatomy & histology/physiology ; Membrane Proteins/*analysis/genetics/metabolism ; Multiprotein Complexes/*analysis/genetics/metabolism ; Nerve Tissue Proteins/*analysis/genetics/metabolism ; Organ Size ; Receptors, Neurotransmitter/analysis/genetics/metabolism ; Signal Transduction ; Synaptic Membranes/*chemistry/physiology ; Synaptic Transmission ; Vertebrates/anatomy & histology/physiology
    Print ISSN: 0036-8075
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  • 63
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-04-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benkovic, Stephen J -- Hammes-Schiffer, Sharon -- GM24129/GM/NIGMS NIH HHS/ -- GM56207/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Apr 14;312(5771):208-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Pennsylvania State University, University Park, PA 16802, USA. sjb1@psu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16614206" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; Chemistry, Physical ; Computer Simulation ; Hydrogen/chemistry ; Kinetics ; Models, Chemical ; Motion ; Oxidation-Reduction ; Oxidoreductases Acting on CH-NH Group Donors/*chemistry/*metabolism ; Physicochemical Phenomena ; Protein Conformation ; *Protons ; Thermodynamics ; Tryptamines/*metabolism
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  • 64
    Publication Date: 2006-05-06
    Description: B cells recognize foreign antigens by virtue of cell surface immunoglobulin receptors and are most effectively activated by membrane-bound ligands. Here, we show that in the early stages of this process, B cells exhibit a two-phase response in which they first spread over the antigen-bearing membrane and then contract, thereby collecting bound antigen into a central aggregate. The extent of this response, which is both signaling- and actin-dependent, determines the quantity of antigen accumulated and hence the degree of B cell activation. Brownian dynamic simulations reproduce essential features of the antigen collection process and suggest a possible basis for affinity discrimination. We propose that dynamic spreading is an important step of the immune response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fleire, S J -- Goldman, J P -- Carrasco, Y R -- Weber, M -- Bray, D -- Batista, F D -- G64713/PHS HHS/ -- New York, N.Y. -- Science. 2006 May 5;312(5774):738-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lymphocyte Interaction Laboratory, London Research Institute, Cancer Research UK, 44 Lincoln's Inn Fields, London, WC2A 3PX, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16675699" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/physiology ; Algorithms ; Animals ; Antibody Affinity ; Antigen Presentation ; Antigens, Surface/*immunology ; B-Lymphocytes/*immunology/*physiology ; Cell Shape ; Computer Simulation ; Flow Cytometry ; Ligands ; Lipid Bilayers ; *Lymphocyte Activation ; Mice ; Mice, Transgenic ; Microscopy, Fluorescence ; Models, Immunological ; Muramidase/immunology ; Receptors, Antigen, B-Cell/*immunology/metabolism ; Recombinant Fusion Proteins/immunology ; Signal Transduction ; Stochastic Processes ; T-Lymphocytes/immunology
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  • 65
    Publication Date: 2006-04-08
    Description: Biological responses to histone methylation critically depend on the faithful readout and transduction of the methyl-lysine signal by "effector" proteins, yet our understanding of methyl-lysine recognition has so far been limited to the study of histone binding by chromodomain and WD40-repeat proteins. The double tudor domain of JMJD2A, a Jmjc domain-containing histone demethylase, binds methylated histone H3-K4 and H4-K20. We found that the double tudor domain has an interdigitated structure, and the unusual fold is required for its ability to bind methylated histone tails. The cocrystal structure of the JMJD2A double tudor domain with a trimethylated H3-K4 peptide reveals that the trimethyl-K4 is bound in a cage of three aromatic residues, two of which are from the tudor-2 motif, whereas the binding specificity is determined by side-chain interactions involving amino acids from the tudor-1 motif. Our study provides mechanistic insights into recognition of methylated histone tails by tudor domains and reveals the structural intricacy of methyl-lysine recognition by two closely spaced effector domains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Ying -- Fang, Jia -- Bedford, Mark T -- Zhang, Yi -- Xu, Rui-Ming -- DK62248/DK/NIDDK NIH HHS/ -- GM 63718/GM/NIGMS NIH HHS/ -- GM68804/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 May 5;312(5774):748-51. Epub 2006 Apr 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉W. M. Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16601153" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; DNA-Binding Proteins/*chemistry/genetics/*metabolism ; Histones/*chemistry/*metabolism ; Humans ; Hydrogen Bonding ; Jumonji Domain-Containing Histone Demethylases ; Lysine/metabolism ; Methylation ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Oxidoreductases, N-Demethylating ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Tertiary ; Static Electricity ; Transcription Factors/*chemistry/genetics/*metabolism
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  • 66
    Publication Date: 2006-09-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koenig, Robert -- New York, N.Y. -- Science. 2006 Sep 22;313(5794):1724-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16990528" target="_blank"〉PubMed〈/a〉
    Keywords: Africa, Eastern/epidemiology ; Animals ; *Animals, Wild ; Bacterial Toxins/analysis/toxicity ; Behavior, Animal ; Bird Diseases/*epidemiology ; *Birds ; *Conservation of Natural Resources ; Cyanobacteria ; *Ecosystem ; Feeding Behavior ; Fresh Water ; Hydrogen-Ion Concentration ; Population Density ; Population Dynamics ; Temperature
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  • 67
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-07-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2006 Jul 14;313(5784):156.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16840668" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Beak/*anatomy & histology ; *Biological Evolution ; Competitive Behavior ; Diet ; Disasters ; Ecosystem ; Ecuador ; Feeding Behavior ; *Finches/anatomy & histology/physiology ; *Food ; Population Dynamics ; *Seeds ; *Selection, Genetic
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  • 68
    Publication Date: 2006-04-15
    Description: Protein dynamics plays an important role in protein function. Many functionally important motions occur on the microsecond and low millisecond time scale and can be characterized by nuclear magnetic resonance relaxation experiments. We describe the different states of a peptidyl carrier protein (PCP) that play a crucial role in its function as a peptide shuttle in the nonribosomal peptide synthetases of the tyrocidine A system. Both apo-PCP (without the bound 4'-phosphopantetheine cofactor) and holo-PCP exist in two different stable conformations. We show that one of the apo conformations and one of the holo conformations are identical, whereas the two remaining conformations are only detectable by nuclear magnetic resonance spectroscopy in either the apo or holo form. We further demonstrate that this conformational diversity is an essential prerequisite for the directed movement of the 4'-PP cofactor and its interaction with externally acting proteins such as thioesterases and 4'-PP transferase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koglin, Alexander -- Mofid, Mohammad R -- Lohr, Frank -- Schafer, Birgit -- Rogov, Vladimir V -- Blum, Marc-Michael -- Mittag, Tanja -- Marahiel, Mohamed A -- Bernhard, Frank -- Dotsch, Volker -- New York, N.Y. -- Science. 2006 Apr 14;312(5771):273-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Biophysical Chemistry, Centre for Biomolecular Magnetic Resonance (BMRZ), J.W. Goethe University of Frankfurt, Marie-Curie-Strasse, D-60439 Frankfurt/Main, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16614225" target="_blank"〉PubMed〈/a〉
    Keywords: Apoproteins/chemistry/metabolism ; Bacterial Proteins/chemistry/metabolism ; Binding Sites ; Carrier Proteins/*chemistry/*metabolism ; Crystallography, X-Ray ; Fatty Acid Synthases/metabolism ; Holoenzymes/chemistry/metabolism ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; Pantetheine/analogs & derivatives/metabolism ; Peptide Synthases/*chemistry/*metabolism ; *Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Thiolester Hydrolases/metabolism ; Transferases/metabolism
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  • 69
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-03-11
    Description: Easter Island (Rapa Nui) provides a model of human-induced environmental degradation. A reliable chronology is central to understanding the cultural, ecological, and demographic processes involved. Radiocarbon dates for the earliest stratigraphic layers at Anakena, Easter Island, and analysis of previous radiocarbon dates imply that the island was colonized late, about 1200 A.D. Substantial ecological impacts and major cultural investments in monumental architecture and statuary thus began soon after initial settlement.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hunt, Terry L -- Lipo, Carl P -- New York, N.Y. -- Science. 2006 Mar 17;311(5767):1603-6. Epub 2006 Mar 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anthropology, University of Hawai'i Manoa, 2424 Maile Way, Honolulu, HI 96822, USA. thunt@hawaii.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16527931" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Anthropology ; Anthropology, Cultural ; Conservation of Natural Resources ; Ecosystem ; Emigration and Immigration/*history ; *Environment ; History, Ancient ; Humans ; Plants ; Polynesia ; Population Density ; Population Dynamics ; Population Growth
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  • 70
    Publication Date: 2006-08-12
    Description: Dispersal is often risky to the individual, yet the long-term survival of populations depends on having a sufficient number of individuals that move, find each other, and locate suitable breeding habitats. This tension has consequences that rarely meet our conservation or management goals. This is particularly true in changing environments, which makes the study of dispersal urgently topical in a world plagued with habitat loss, climate change, and species introductions. Despite the difficulty of tracking mobile individuals over potentially vast ranges, recent research has revealed a multitude of ways in which dispersal evolution can either constrain, or accelerate, species' responses to environmental changes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kokko, Hanna -- Lopez-Sepulcre, Andres -- New York, N.Y. -- Science. 2006 Aug 11;313(5788):789-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Ecological and Evolutionary Dynamics, Department of Biological and Environmental Science, University of Helsinki, Post Office Box 65 (Viikinkaari 1), FIN-00014 Helsinki, Finland. hanna.kokko@helsinki.fi〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16902127" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; *Animal Migration ; Animals ; Behavior, Animal ; Biological Evolution ; Cues ; *Ecosystem ; *Environment ; Genes ; Homing Behavior ; Humans ; *Movement ; Population Dynamics ; Reproduction ; Selection, Genetic
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  • 71
    Publication Date: 2006-12-16
    Description: Fisheries have removed at least 50 million tons of tuna and other top-level predators from the Pacific Ocean pelagic ecosystem since 1950, leading to concerns about a catastrophic reduction in population biomass and the collapse of oceanic food chains. We analyzed all available data from Pacific tuna fisheries for 1950-2004 to provide comprehensive estimates of fishery impacts on population biomass and size structure. Current biomass ranges among species from 36 to 91% of the biomass predicted in the absence of fishing, a level consistent with or higher than standard fisheries management targets. Fish larger than 175 centimeters fork length have decreased from 5% to approximately 1% of the total population. The trophic level of the catch has decreased slightly, but there is no detectable decrease in the trophic level of the population. These results indicate substantial, though not catastrophic, impacts of fisheries on these top-level predators and minor impacts on the ecosystem in the Pacific Ocean.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sibert, John -- Hampton, John -- Kleiber, Pierre -- Maunder, Mark -- New York, N.Y. -- Science. 2006 Dec 15;314(5806):1773-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Joint Institute for Marine and Atmospheric Research, University of Hawaii, Honolulu, HI 96822, USA. sibert@hawaii.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17170304" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biomass ; Body Size ; Conservation of Natural Resources ; *Ecosystem ; *Fisheries ; *Food Chain ; Pacific Ocean ; Perciformes/anatomy & histology/physiology ; Population Density ; Population Dynamics ; Predatory Behavior ; *Sharks/anatomy & histology/physiology ; *Tuna/anatomy & histology/physiology
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  • 72
    Publication Date: 2006-08-12
    Description: The Arabidopsis CLAVATA3 (CLV3) gene encodes a stem cell-specific protein presumed to be a precursor of a secreted peptide hormone. Matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry (MALDI-TOF MS) applied to in situ Arabidopsis tissues determined the structure of a modified 12-amino acid peptide (MCLV3), which was derived from a conserved motif in the CLV3 sequence. Synthetic MCLV3 induced shoot and root meristem consumption as cells differentiated into other organs, displaying the typical phenotype of transgenic plants overexpressing CLV3. These results suggest that the functional peptide of CLV3 is MCLV3.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kondo, Tatsuhiko -- Sawa, Shinichiro -- Kinoshita, Atsuko -- Mizuno, Satoko -- Kakimoto, Tatsuo -- Fukuda, Hiroo -- Sakagami, Youji -- New York, N.Y. -- Science. 2006 Aug 11;313(5788):845-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate School of Bio-Agricultural Sciences, Nagoya University, Chikusa, Nagoya, 464-8601, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16902141" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Arabidopsis/*cytology/genetics/metabolism ; Arabidopsis Proteins/*chemistry/genetics/*metabolism/pharmacology ; Cell Differentiation ; Cells, Cultured ; Hydroxyproline/chemistry ; Meristem/*cytology/drug effects/metabolism ; Molecular Sequence Data ; Oligopeptides/chemistry/*metabolism/pharmacology ; Plant Roots/growth & development ; Plants, Genetically Modified ; Signal Transduction ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Stem Cells/cytology
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  • 73
    Publication Date: 2006-06-17
    Description: Inflammation and trauma lead to enhanced pain sensitivity (hyperalgesia), which is in part due to altered sensory processing in the spinal cord. The synaptic hypothesis of hyperalgesia, which postulates that hyperalgesia is induced by the activity-dependent long-term potentiation (LTP) in the spinal cord, has been challenged, because in previous studies of pain pathways, LTP was experimentally induced by nerve stimulation at high frequencies ( approximately 100 hertz). This does not, however, resemble the real low-frequency afferent barrage that occurs during inflammation. We identified a synaptic amplifier at the origin of an ascending pain pathway that is switched-on by low-level activity in nociceptive nerve fibers. This model integrates known signal transduction pathways of hyperalgesia without contradiction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ikeda, Hiroshi -- Stark, Johanna -- Fischer, Harald -- Wagner, Matthias -- Drdla, Ruth -- Jager, Tino -- Sandkuhler, Jurgen -- P 18129/Austrian Science Fund FWF/Austria -- New York, N.Y. -- Science. 2006 Jun 16;312(5780):1659-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurophysiology, Center for Brain Research, Medical University of Vienna, Vienna, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16778058" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Electric Stimulation ; Excitatory Postsynaptic Potentials ; Hyperalgesia/*physiopathology ; Inflammation/*physiopathology ; Long-Term Potentiation ; Nerve Fibers, Unmyelinated/*physiology ; Neuronal Plasticity ; Nitric Oxide/physiology ; Pain/*physiopathology ; Patch-Clamp Techniques ; Periaqueductal Gray/physiology ; Posterior Horn Cells/*physiopathology ; Rats ; Rats, Sprague-Dawley ; Signal Transduction ; Spinal Cord/physiopathology ; Synapses/physiology ; *Synaptic Transmission
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  • 74
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-05-27
    Description: Ciona is an emerging model system for elucidating gene networks in development. Comprehensive in situ hybridization assays have identified 76 regulatory genes with localized expression patterns in the early embryo, at the time when naive blastomeres are determined to follow specific cell fates. Systematic gene disruption assays provided more than 3000 combinations of gene expression profiles in mutant backgrounds. Deduced gene circuit diagrams describing the formation of larval tissues were computationally visualized. These diagrams constitute a blueprint for the Ciona embryo and provide a foundation for understanding the evolutionary origins of the chordate body plan.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Imai, Kaoru S -- Levine, Michael -- Satoh, Nori -- Satou, Yutaka -- New York, N.Y. -- Science. 2006 May 26;312(5777):1183-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto, 606-8502, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16728634" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Blastomeres/cytology/physiology ; Body Patterning/genetics ; Cell Differentiation/genetics ; Cell Lineage ; Ciona intestinalis/*embryology/*genetics ; Computational Biology ; Embryo, Nonmammalian/*physiology ; Embryonic Development/*genetics ; Epidermis/cytology ; Gastrula/cytology/physiology ; Gene Expression Profiling ; *Gene Expression Regulation, Developmental ; Genes, Regulator ; In Situ Hybridization ; Intracellular Signaling Peptides and Proteins/*genetics/physiology ; Neurons/cytology ; Nodal Protein ; Notochord/embryology ; Reverse Transcriptase Polymerase Chain Reaction ; Signal Transduction ; Transcription Factors/*genetics/physiology ; Transcription, Genetic ; Transforming Growth Factor beta/genetics/physiology
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  • 75
    Publication Date: 2006-02-25
    Description: Sibly et al. (Reports, 22 July 2005, p. 607) concluded that density dependence acts far below the carrying capacity in most animal populations. We argue that the authors confused discrete and continuous models, that their best-fit models cannot explain observed oscillations, and that their estimation procedures appear biased. They also neglected trophic and migratory processes, which we demonstrate could underlie their empirical findings.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Getz, Wayne M -- Lloyd-Smith, James O -- New York, N.Y. -- Science. 2006 Feb 24;311(5764):1100; author reply 1100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Environmental Sciences, Policy, and Management, University of California at Berkeley, CA 94720-3114, USA. getz@nature.berkeley.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16497915" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Birds ; Conservation of Natural Resources ; Databases, Factual ; Ecosystem ; *Fishes ; *Insects ; Logistic Models ; *Mammals ; Mathematics ; Models, Biological ; Population Density ; Population Dynamics ; Population Growth ; Regression Analysis
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  • 76
    Publication Date: 2006-08-19
    Description: Mutations in gld-1 cause lethal germline tumors in the nematode Caenorhabditis elegans. We find that a wide variety of mutations that extend C. elegans' life span confer resistance to these tumors. The long life spans of daf-2/insulin-receptor mutants were not shortened at all by gld-1 mutations; we attribute this finding to decreased cell division and increased DAF-16/p53-dependent apoptosis within the tumors. Mutations that increase life span by restricting food intake or inhibiting respiration did not affect apoptosis but reduced tumor cell division. Unexpectedly, none of these longevity mutations affected mitosis in normal germlines; this finding suggests that cellular changes that lead to longevity preferentially antagonize tumor cell growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pinkston, Julie M -- Garigan, Delia -- Hansen, Malene -- Kenyon, Cynthia -- AG000278/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2006 Aug 18;313(5789):971-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94158, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16917064" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Caenorhabditis elegans/*genetics/physiology ; Caenorhabditis elegans Proteins/*genetics/physiology ; Caloric Restriction ; Cell Proliferation ; Forkhead Transcription Factors ; Genes, Helminth ; Germ Cells/cytology ; Insulin/metabolism ; Insulin-Like Growth Factor I/metabolism ; Longevity/*genetics ; Mitochondria/metabolism ; Models, Animal ; *Mutation ; Neoplasms/genetics/*pathology ; Oogenesis ; Receptor, Insulin/*genetics/physiology ; Reproduction ; Signal Transduction ; Transcription Factors/genetics/physiology
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  • 77
    Publication Date: 2006-07-22
    Description: Radiocarbon data from 150 archaeological excavations in the now hyper-arid Eastern Sahara of Egypt, Sudan, Libya, and Chad reveal close links between climatic variations and prehistoric occupation during the past 12,000 years. Synoptic multiple-indicator views for major time slices demonstrate the transition from initial settlement after the sudden onset of humid conditions at 8500 B.C.E. to the exodus resulting from gradual desiccation since 5300 B.C.E. Southward shifting of the desert margin helped trigger the emergence of pharaonic civilization along the Nile, influenced the spread of pastoralism throughout the continent, and affects sub-Saharan Africa to the present day.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuper, Rudolph -- Kropelin, Stefan -- New York, N.Y. -- Science. 2006 Aug 11;313(5788):803-7. Epub 2006 Jul 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Collaborative Research Center 389 (ACACIA), University of Cologne, Institute of Prehistoric Archaeology, Africa Research Unit, Jennerstrasse 8, 50823 Koln, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16857900" target="_blank"〉PubMed〈/a〉
    Keywords: Agriculture/history ; Animal Husbandry/history ; Archaeology ; Chad ; Civilization/*history ; *Climate ; *Cultural Evolution ; Desert Climate ; Egypt ; Emigration and Immigration ; Environment ; History, Ancient ; Humans ; Humidity ; Libya ; Population Dynamics ; Rain ; Sudan
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  • 78
    Publication Date: 2006-01-28
    Description: Directly transmitted parasites often provide substantial information about the temporal and spatial characteristics of host-to-host contact. Here, we demonstrate that a fast-evolving virus (feline immunodeficiency virus, FIV) can reveal details of the contemporary population structure and recent demographic history of its natural wildlife host (Puma concolor) that were not apparent from host genetic data and would be impossible to obtain by other means. We suggest that rapidly evolving pathogens may provide a complementary tool for studying population dynamics of their hosts in "shallow" time.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Biek, Roman -- Drummond, Alexei J -- Poss, Mary -- New York, N.Y. -- Science. 2006 Jan 27;311(5760):538-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wildlife Biology Program, University of Montana, Missoula, MT 59812, USA. rbiek@emory.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16439664" target="_blank"〉PubMed〈/a〉
    Keywords: Alberta/epidemiology ; Animals ; Bayes Theorem ; British Columbia/epidemiology ; Ecosystem ; *Evolution, Molecular ; Genes, env ; Genes, pol ; Geography ; Immunodeficiency Virus, Feline/*classification/*genetics ; Lentivirus Infections/epidemiology/*veterinary/virology ; Microsatellite Repeats ; Molecular Sequence Data ; Montana/epidemiology ; Phylogeny ; Population Dynamics ; *Puma/genetics/virology ; Time Factors ; Wyoming/epidemiology
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  • 79
    Publication Date: 2006-03-25
    Description: Innate immunity against bacterial and fungal pathogens is mediated by Toll and immune deficiency (Imd) pathways, but little is known about the antiviral response in Drosophila. Here, we demonstrate that an RNA interference pathway protects adult flies from infection by two evolutionarily diverse viruses. Our work also describes a molecular framework for the viral immunity, in which viral double-stranded RNA produced during infection acts as the pathogen trigger whereas Drosophila Dicer-2 and Argonaute-2 act as host sensor and effector, respectively. These findings establish a Drosophila model for studying the innate immunity against viruses in animals.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1509097/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1509097/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Xiao-Hong -- Aliyari, Roghiyh -- Li, Wan-Xiang -- Li, Hong-Wei -- Kim, Kevin -- Carthew, Richard -- Atkinson, Peter -- Ding, Shou-Wei -- AI052447/AI/NIAID NIH HHS/ -- R01 AI052447/AI/NIAID NIH HHS/ -- R01 GM068743/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Apr 21;312(5772):452-4. Epub 2006 Mar 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate Program for Microbiology, University of California, Riverside, CA 92521, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16556799" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Argonaute Proteins ; Cell Line ; Drosophila Proteins/genetics/metabolism/physiology ; Drosophila melanogaster/embryology/genetics/*immunology/*virology ; Embryo, Nonmammalian/immunology/virology ; Escherichia coli/physiology ; *Immunity, Innate ; Insect Viruses/genetics/*physiology ; Micrococcus luteus/physiology ; Mutation ; Nodaviridae/*physiology ; RNA Helicases/genetics/metabolism ; *RNA Interference ; RNA Viruses/genetics/physiology ; RNA, Double-Stranded/metabolism ; RNA, Small Interfering/metabolism ; RNA, Viral/genetics/metabolism ; RNA-Binding Proteins/genetics/physiology ; RNA-Induced Silencing Complex/genetics/physiology ; Ribonuclease III ; Signal Transduction ; Toll-Like Receptors/physiology ; Transfection ; Virus Replication
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  • 80
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-09-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2006 Sep 1;313(5791):1230-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16946049" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/*growth & development/metabolism ; Arabidopsis Proteins/chemistry/*metabolism ; Bacteria/metabolism ; Bacterial Physiological Phenomena ; Computer Simulation ; F-Box Proteins/chemistry/*metabolism ; Gene Expression Regulation, Plant ; Indoleacetic Acids/*metabolism ; MicroRNAs/metabolism ; Models, Biological ; *Plant Development ; Plant Growth Regulators/*metabolism ; Plant Proteins/*metabolism ; Plants/genetics/metabolism/microbiology ; RNA Interference ; RNA, Plant/metabolism ; Receptors, Cell Surface/chemistry/*metabolism ; Signal Transduction
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  • 81
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-10-21
    Description: The role of constraint in adaptive evolution is an open question. Directed evolution of an engineered beta-isopropylmalate dehydrogenase (IMDH), with coenzyme specificity switched from nicotinamide adenine dinucleotide (NAD) to nicotinamide adenine dinucleotide phosphate (NADP), always produces mutants with lower affinities for NADP. This result is the correlated response to selection for relief from inhibition by NADPH (the reduced form of NADP) expected of an adaptive landscape subject to three enzymatic constraints: an upper limit to the rate of maximum turnover (kcat), a correlation in NADP and NADPH affinities, and a trade-off between NAD and NADP usage. Two additional constraints, high intracellular NADPH abundance and the cost of compensatory protein synthesis, have ensured the conserved use of NAD by IMDH throughout evolution. Our results show that selective mechanisms and evolutionary constraints are to be understood in terms of underlying adaptive landscapes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, Stephen P -- Lunzer, Mark -- Dean, Antony M -- GM060611/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Oct 20;314(5798):458-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉BioTechnology Institute, University of Minnesota, St. Paul, MN 55108, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17053145" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Isopropylmalate Dehydrogenase/antagonists & ; inhibitors/chemistry/genetics/*metabolism ; *Adaptation, Physiological ; Amino Acid Substitution ; Binding Sites ; Codon ; *Directed Molecular Evolution ; Escherichia coli/*enzymology/growth & development/physiology ; *Evolution, Molecular ; Kinetics ; Mutation ; NAD/metabolism ; NADP/metabolism ; Phenotype ; Selection, Genetic
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  • 82
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-07-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cramer, Patrick -- New York, N.Y. -- Science. 2006 Jul 28;313(5786):447-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gene Center Munich, Department of Chemistry and Biochemistry, Ludwig-Maximilians-Universitat Munchen, Feodor-Lynen-Strasse 25, 81377 Munich, Germany. cramer@lmb.uni-muenchen.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16873631" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; DNA-Directed DNA Polymerase/metabolism ; DNA-Directed RNA Polymerases/*metabolism ; Evolution, Molecular ; Magnesium/metabolism ; RNA, Messenger/*metabolism ; *Transcription, Genetic
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  • 83
    Publication Date: 2006-04-22
    Description: G protein betagamma subunits have potential as a target for therapeutic treatment of a number of diseases. We performed virtual docking of a small-molecule library to a site on Gbetagamma subunits that mediates protein interactions. We hypothesized that differential targeting of this surface could allow for selective modulation of Gbetagamma subunit functions. Several compounds bound to Gbetagamma subunits with affinities from 0.1 to 60 muM and selectively modulated functional Gbetagamma-protein-protein interactions in vitro, chemotactic peptide signaling pathways in HL-60 leukocytes, and opioid receptor-dependent analgesia in vivo. These data demonstrate an approach for modulation of G protein-coupled receptor signaling that may represent an important therapeutic strategy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bonacci, Tabetha M -- Mathews, Jennifer L -- Yuan, Chujun -- Lehmann, David M -- Malik, Sundeep -- Wu, Dianqing -- Font, Jose L -- Bidlack, Jean M -- Smrcka, Alan V -- GM60286/GM/NIGMS NIH HHS/ -- HL-T3207949/HL/NHLBI NIH HHS/ -- HL080706/HL/NHLBI NIH HHS/ -- K05-DA00360/DA/NIDA NIH HHS/ -- R01 CA132317/CA/NCI NIH HHS/ -- R01 GM054597/GM/NIGMS NIH HHS/ -- R01 GM054597-09/GM/NIGMS NIH HHS/ -- R01 HL080706/HL/NHLBI NIH HHS/ -- R01 HL080706-10/HL/NHLBI NIH HHS/ -- R01 HL080706-11/HL/NHLBI NIH HHS/ -- T32DA07232/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 2006 Apr 21;312(5772):443-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology and Physiology, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16627746" target="_blank"〉PubMed〈/a〉
    Keywords: Analgesics/pharmacology ; Animals ; Binding Sites ; Binding, Competitive ; Cell Line ; Computer Simulation ; Cyclohexanes/chemistry/*metabolism/*pharmacology ; Drug Evaluation, Preclinical/*methods ; Enzyme-Linked Immunosorbent Assay ; G-Protein-Coupled Receptor Kinase 2 ; GTP-Binding Protein alpha Subunits/metabolism ; GTP-Binding Protein beta Subunits/chemistry/*metabolism ; GTP-Binding Protein gamma Subunits/chemistry/*metabolism ; HL-60 Cells ; Humans ; Isoenzymes/metabolism ; Mice ; Mice, Inbred ICR ; Mitogen-Activated Protein Kinases/metabolism ; Molecular Structure ; Morphine/pharmacology ; N-Formylmethionine Leucyl-Phenylalanine/metabolism ; Peptide Library ; Peptides/*metabolism ; Phosphatidylinositol 3-Kinases/metabolism ; Phospholipase C beta ; Protein Binding ; Protein Interaction Mapping ; *Signal Transduction ; Software ; Structure-Activity Relationship ; Type C Phospholipases/metabolism ; Xanthenes/chemistry/*metabolism/*pharmacology ; beta-Adrenergic Receptor Kinases/metabolism
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  • 84
    Publication Date: 2006-10-07
    Description: The evolutionary dynamics underlying the latitudinal gradient in biodiversity have been controversial for over a century. Using a spatially explicit approach that incorporates not only origination and extinction but immigration, a global analysis of genera and subgenera of marine bivalves over the past 11 million years supports an "out of the tropics" model, in which taxa preferentially originate in the tropics and expand toward the poles without losing their tropical presence. The tropics are thus both a cradle and a museum of biodiversity, contrary to the conceptual dichotomy dominant since 1974; a tropical diversity crisis would thus have profound evolutionary effects at all latitudes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jablonski, David -- Roy, Kaustuv -- Valentine, James W -- New York, N.Y. -- Science. 2006 Oct 6;314(5796):102-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Geophysical Sciences, University of Chicago, 5734 South Ellis Avenue, Chicago, IL 60637, USA. djablons@uchicago.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17023653" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; *Biological Evolution ; *Bivalvia/classification ; *Fossils ; Geography ; Models, Biological ; Phylogeny ; Population Dynamics ; *Tropical Climate
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  • 85
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-05-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lemaire, Patrick -- New York, N.Y. -- Science. 2006 May 26;312(5777):1145-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Biologie du Developpement de Marseille Luminy, UMR6216 CNRS-Universite de la Mediterranee, Campus de Luminy, F-13288 Marseille cedex 9, France. lemaire@ibdm.univ-mrs.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16728621" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Body Patterning/genetics ; Cell Differentiation/genetics ; Ciona intestinalis/*embryology/*genetics ; Embryo, Nonmammalian/physiology ; Embryonic Development/*genetics ; Gene Expression Profiling ; *Gene Expression Regulation, Developmental ; Genes, Regulator ; In Situ Hybridization ; Intracellular Signaling Peptides and Proteins/*genetics/physiology ; Ligands ; Polymerase Chain Reaction ; Signal Transduction ; Transcription Factors/*genetics/physiology ; Transcription, Genetic
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  • 86
    Publication Date: 2006-08-05
    Description: Assembly of the soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) syntaxin 1, SNAP-25, and synaptobrevin 2 is thought to be the driving force for the exocytosis of synaptic vesicles. However, whereas exocytosis is triggered at a millisecond time scale, the SNARE-mediated fusion of liposomes requires hours for completion, which challenges the idea of a key role for SNAREs in the final steps of exocytosis. We found that liposome fusion was dramatically accelerated when a stabilized syntaxin/SNAP-25 acceptor complex was used. Thus, SNAREs do have the capacity to execute fusion at a speed required for neuronal secretion, demonstrating that the maintenance of acceptor complexes is a critical step in biological fusion reactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pobbati, Ajaybabu V -- Stein, Alexander -- Fasshauer, Dirk -- P01 GM072694/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Aug 4;313(5787):673-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16888141" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Circular Dichroism ; Dimerization ; Exocytosis ; Liposomes/*chemistry ; *Membrane Fusion ; Molecular Sequence Data ; Peptide Fragments/chemistry/metabolism ; Protein Binding ; Protein Folding ; Protein Structure, Secondary ; Qa-SNARE Proteins/chemistry/*metabolism ; R-SNARE Proteins/chemistry/metabolism ; Rats ; Synaptosomal-Associated Protein 25/chemistry/*metabolism
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  • 87
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-11-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2006 Nov 3;314(5800):749.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17082434" target="_blank"〉PubMed〈/a〉
    Keywords: *Breeding ; *Conservation of Natural Resources ; Ecosystem ; Europe ; Humans ; *Lynx/physiology ; Population Density ; Population Dynamics
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  • 88
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-03-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krajick, Kevin -- New York, N.Y. -- Science. 2006 Mar 3;311(5765):1230-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16513956" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Zoo ; Biodiversity ; *Bufonidae/physiology ; Cell Line ; *Conservation of Natural Resources ; Developed Countries ; *Ecosystem ; Environment ; Population Dynamics ; Rivers ; Tanzania ; Water Movements
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  • 89
    Publication Date: 2006-09-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Laviano, Alessandro -- Meguid, Michael M -- Inui, Akio -- Rossi-Fanelli, Filippo -- New York, N.Y. -- Science. 2006 Sep 1;313(5791):1236-8; author reply 1236-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16946053" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Appetite ; Brain/metabolism ; *Eating ; Humans ; Leucine/*administration & dosage/*physiology ; *Protein Biosynthesis ; Protein Kinases/metabolism ; Rats ; Signal Transduction ; TOR Serine-Threonine Kinases
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  • 90
    Publication Date: 2006-11-25
    Description: Canonical cap-dependent translation initiation requires a large number of protein factors that act in a stepwise assembly process. In contrast, internal ribosomal entry sites (IRESs) are cis-acting RNAs that in some cases completely supplant these factors by recruiting and activating the ribosome using a single structured RNA. Here we present the crystal structures of the ribosome-binding domain from a Dicistroviridae intergenic region IRES at 3.1 angstrom resolution, providing a view of the prefolded architecture of an all-RNA translation initiation apparatus. Docking of the structure into cryo-electron microscopy reconstructions of an IRES-ribosome complex suggests a model for ribosome manipulation by a dynamic IRES RNA.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2669756/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2669756/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pfingsten, Jennifer S -- Costantino, David A -- Kieft, Jeffrey S -- R01 GM072560/GM/NIGMS NIH HHS/ -- R01 GM072560-01/GM/NIGMS NIH HHS/ -- R01 GM072560-02/GM/NIGMS NIH HHS/ -- R01 GM072560-03/GM/NIGMS NIH HHS/ -- R01 GM072560-04/GM/NIGMS NIH HHS/ -- R01 GM072560-05/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Dec 1;314(5804):1450-4. Epub 2006 Nov 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Genetics, University of Colorado at Denver and Health Sciences Center, Mail Stop 8101, Post Office Box 6511, Aurora, CO 80045, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17124290" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cryoelectron Microscopy ; Crystallization ; Crystallography, X-Ray ; Models, Molecular ; Mutation ; Nucleic Acid Conformation ; *Protein Biosynthesis ; RNA Viruses/*genetics ; RNA, Viral/*chemistry/genetics/metabolism ; *Regulatory Sequences, Ribonucleic Acid/genetics ; Ribosomes/*metabolism
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  • 91
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-11-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fujita, Takashi -- New York, N.Y. -- Science. 2006 Nov 10;314(5801):935-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Genetics, Institute for Virus Research, Kyoto University, Kyoto 606- 8507, Japan. tfujita@virus.kyoto-u.ac.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17095686" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cytoplasm/metabolism/virology ; DEAD-box RNA Helicases/chemistry/*metabolism ; Humans ; Immunity, Innate ; Interferons/biosynthesis ; Nucleic Acid Conformation ; Phosphates/metabolism ; Phosphorylation ; RNA Caps/metabolism ; RNA, Double-Stranded/chemistry/metabolism ; RNA, Viral/chemistry/*metabolism ; Signal Transduction ; Toll-Like Receptors/metabolism ; Viral Nonstructural Proteins/metabolism ; Virus Diseases/immunology
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  • 92
    Publication Date: 2006-05-27
    Description: Yersinia species use a variety of type III effector proteins to target eukaryotic signaling systems. The effector YopJ inhibits mitogen-activated protein kinase (MAPK) and the nuclear factor kappaB (NFkappaB) signaling pathways used in innate immune response by preventing activation of the family of MAPK kinases (MAPKK). We show that YopJ acted as an acetyltransferase, using acetyl-coenzyme A (CoA) to modify the critical serine and threonine residues in the activation loop of MAPKK6 and thereby blocking phosphorylation. The acetylation on MAPKK6 directly competed with phosphorylation, preventing activation of the modified protein. This covalent modification may be used as a general regulatory mechanism in biological signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mukherjee, Sohini -- Keitany, Gladys -- Li, Yan -- Wang, Yong -- Ball, Haydn L -- Goldsmith, Elizabeth J -- Orth, Kim -- R01-AI056404/AI/NIAID NIH HHS/ -- R21-DK072134/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2006 May 26;312(5777):1211-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16728640" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyl Coenzyme A/metabolism ; Acetylation ; Acetyltransferases/metabolism ; Bacterial Proteins/*metabolism ; Catalytic Domain ; Cell Line ; Cell-Free System ; Electrophoresis, Polyacrylamide Gel ; Enzyme Activation ; Extracellular Signal-Regulated MAP Kinases/metabolism ; Humans ; I-kappa B Kinase/*metabolism ; MAP Kinase Kinase 6/chemistry/*metabolism ; MAP Kinase Signaling System ; NF-kappa B/metabolism ; Phosphorylation ; Recombinant Proteins/metabolism ; Serine/metabolism ; Signal Transduction ; Threonine/metabolism ; Yersinia/*metabolism/pathogenicity
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 93
    Publication Date: 2006-07-22
    Description: Despite widespread concern about declines in pollination services, little is known about the patterns of change in most pollinator assemblages. By studying bee and hoverfly assemblages in Britain and the Netherlands, we found evidence of declines (pre-versus post-1980) in local bee diversity in both countries; however, divergent trends were observed in hoverflies. Depending on the assemblage and location, pollinator declines were most frequent in habitat and flower specialists, in univoltine species, and/or in nonmigrants. In conjunction with this evidence, outcrossing plant species that are reliant on the declining pollinators have themselves declined relative to other plant species. Taken together, these findings strongly suggest a causal connection between local extinctions of functionally linked plant and pollinator species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Biesmeijer, J C -- Roberts, S P M -- Reemer, M -- Ohlemuller, R -- Edwards, M -- Peeters, T -- Schaffers, A P -- Potts, S G -- Kleukers, R -- Thomas, C D -- Settele, J -- Kunin, W E -- New York, N.Y. -- Science. 2006 Jul 21;313(5785):351-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Integrative and Comparative Biology and Earth and Biosphere Institute, University of Leeds, Leeds, LS2 9JT, UK. j.c.biesmeijer@leeds.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16857940" target="_blank"〉PubMed〈/a〉
    Keywords: Animal Migration ; Animals ; *Bees ; *Biodiversity ; *Diptera ; *Ecosystem ; Environment ; Flowers ; Great Britain ; Netherlands ; *Plants ; *Pollen ; Population Dynamics
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  • 94
    Publication Date: 2006-03-04
    Description: All steps of fatty acid synthesis in fungi are catalyzed by the fatty acid synthase, which forms a 2.6-megadalton alpha6beta6 complex. We have determined the molecular architecture of this multienzyme by fitting the structures of homologous enzymes that catalyze the individual steps of the reaction pathway into a 5 angstrom x-ray crystallographic electron density map. The huge assembly contains two separated reaction chambers, each equipped with three sets of active sites separated by distances up to approximately 130 angstroms, across which acyl carrier protein shuttles substrates during the reaction cycle. Regions of the electron density arising from well-defined structural features outside the catalytic domains separate the two reaction chambers and serve as a matrix in which domains carrying the various active sites are embedded. The structure rationalizes the compartmentalization of fatty acid synthesis, and the spatial arrangement of the active sites has specific implications for our understanding of the reaction cycle mechanism and of the architecture of multienzymes in general.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jenni, Simon -- Leibundgut, Marc -- Maier, Timm -- Ban, Nenad -- New York, N.Y. -- Science. 2006 Mar 3;311(5765):1263-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology and Biophysics, Department of Biology, Swiss Federal Institute of Technology (ETH Zurich), 8093 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16513976" target="_blank"〉PubMed〈/a〉
    Keywords: Acyl Carrier Protein/chemistry/metabolism ; Ascomycota/*enzymology ; Binding Sites ; Catalytic Domain ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Fatty Acid Synthases/*chemistry/isolation & purification/metabolism ; Fatty Acids/biosynthesis ; Models, Molecular ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Sequence Homology, Amino Acid
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  • 95
    Publication Date: 2006-05-13
    Description: The interface between an infectious agent and its host represents the ultimate battleground for survival: The microbe must secure a niche for replication, whereas the host must limit the pathogen's advance. Among the host's arsenal of antimicrobial factors, the type 1 interferons (IFNs) induce potent defense mechanisms against viruses and are key in the host-virus standoff. Viruses have evolved multiple tricks to avoid the immediate antiviral effects of IFNs and, in turn, hosts have adapted use of this innate cytokine system to galvanize multiple additional layers of immune defense. The plasticity that exists in these interactions provides us with a lesson in detente.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Garcia-Sastre, Adolfo -- Biron, Christine A -- P01AI52106/AI/NIAID NIH HHS/ -- P01AI58113/AI/NIAID NIH HHS/ -- R01AI46954/AI/NIAID NIH HHS/ -- R01AI55677/AI/NIAID NIH HHS/ -- R01CA41268/CA/NCI NIH HHS/ -- U19AI62623/AI/NIAID NIH HHS/ -- U54AI57158/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2006 May 12;312(5775):879-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Mount Sinai School of Medicine, New York, NY 10029, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16690858" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cytokines/physiology ; *Immunity, Innate ; Interferon Regulatory Factors/physiology ; Interferon Type I/biosynthesis/genetics/*physiology ; Models, Biological ; RNA Helicases/metabolism ; Signal Transduction ; Toll-Like Receptors/physiology ; Viral Proteins/metabolism ; *Virus Physiological Phenomena ; Viruses/*immunology
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  • 96
    Publication Date: 2006-12-23
    Description: Iron regulatory protein 1 (IRP1) binds iron-responsive elements (IREs) in messenger RNAs (mRNAs), to repress translation or degradation, or binds an iron-sulfur cluster, to become a cytosolic aconitase enzyme. The 2.8 angstrom resolution crystal structure of the IRP1:ferritin H IRE complex shows an open protein conformation compared with that of cytosolic aconitase. The extended, L-shaped IRP1 molecule embraces the IRE stem-loop through interactions at two sites separated by approximately 30 angstroms, each involving about a dozen protein:RNA bonds. Extensive conformational changes related to binding the IRE or an iron-sulfur cluster explain the alternate functions of IRP1 as an mRNA regulator or enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walden, William E -- Selezneva, Anna I -- Dupuy, Jerome -- Volbeda, Anne -- Fontecilla-Camps, Juan C -- Theil, Elizabeth C -- Volz, Karl -- DK20251/DK/NIDDK NIH HHS/ -- DK47281/DK/NIDDK NIH HHS/ -- GM47522/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Dec 22;314(5807):1903-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of Illinois at Chicago, Chicago, IL 60612-7344, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17185597" target="_blank"〉PubMed〈/a〉
    Keywords: Apoferritins/*genetics ; Binding Sites ; Crystallography, X-Ray ; Hydrogen Bonding ; Iron/metabolism ; Iron Regulatory Protein 1/*chemistry/*metabolism ; Models, Molecular ; Nucleic Acid Conformation ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA, Messenger/chemistry/genetics/metabolism ; *Regulatory Sequences, Ribonucleic Acid ; *Response Elements ; Sulfur/metabolism ; Untranslated Regions/*chemistry/*metabolism
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  • 97
    Publication Date: 2006-11-11
    Description: We report the sequence and analysis of the 814-megabase genome of the sea urchin Strongylocentrotus purpuratus, a model for developmental and systems biology. The sequencing strategy combined whole-genome shotgun and bacterial artificial chromosome (BAC) sequences. This use of BAC clones, aided by a pooling strategy, overcame difficulties associated with high heterozygosity of the genome. The genome encodes about 23,300 genes, including many previously thought to be vertebrate innovations or known only outside the deuterostomes. This echinoderm genome provides an evolutionary outgroup for the chordates and yields insights into the evolution of deuterostomes.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3159423/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3159423/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sea Urchin Genome Sequencing Consortium -- Sodergren, Erica -- Weinstock, George M -- Davidson, Eric H -- Cameron, R Andrew -- Gibbs, Richard A -- Angerer, Robert C -- Angerer, Lynne M -- Arnone, Maria Ina -- Burgess, David R -- Burke, Robert D -- Coffman, James A -- Dean, Michael -- Elphick, Maurice R -- Ettensohn, Charles A -- Foltz, Kathy R -- Hamdoun, Amro -- Hynes, Richard O -- Klein, William H -- Marzluff, William -- McClay, David R -- Morris, Robert L -- Mushegian, Arcady -- Rast, Jonathan P -- Smith, L Courtney -- Thorndyke, Michael C -- Vacquier, Victor D -- Wessel, Gary M -- Wray, Greg -- Zhang, Lan -- Elsik, Christine G -- Ermolaeva, Olga -- Hlavina, Wratko -- Hofmann, Gretchen -- Kitts, Paul -- Landrum, Melissa J -- Mackey, Aaron J -- Maglott, Donna -- Panopoulou, Georgia -- Poustka, Albert J -- Pruitt, Kim -- Sapojnikov, Victor -- Song, Xingzhi -- Souvorov, Alexandre -- Solovyev, Victor -- Wei, Zheng -- Whittaker, Charles A -- Worley, Kim -- Durbin, K James -- Shen, Yufeng -- Fedrigo, Olivier -- Garfield, David -- Haygood, Ralph -- Primus, Alexander -- Satija, Rahul -- Severson, Tonya -- Gonzalez-Garay, Manuel L -- Jackson, Andrew R -- Milosavljevic, Aleksandar -- Tong, Mark -- Killian, Christopher E -- Livingston, Brian T -- Wilt, Fred H -- Adams, Nikki -- Belle, Robert -- Carbonneau, Seth -- Cheung, Rocky -- Cormier, Patrick -- Cosson, Bertrand -- Croce, Jenifer -- Fernandez-Guerra, Antonio -- Geneviere, Anne-Marie -- Goel, Manisha -- Kelkar, Hemant -- Morales, Julia -- Mulner-Lorillon, Odile -- Robertson, Anthony J -- Goldstone, Jared V -- Cole, Bryan -- Epel, David -- Gold, Bert -- Hahn, Mark E -- Howard-Ashby, Meredith -- Scally, Mark -- Stegeman, John J -- Allgood, Erin L -- Cool, Jonah -- Judkins, Kyle M -- McCafferty, Shawn S -- Musante, Ashlan M -- Obar, Robert A -- Rawson, Amanda P -- Rossetti, Blair J -- Gibbons, Ian R -- Hoffman, Matthew P -- Leone, Andrew -- Istrail, Sorin -- Materna, Stefan C -- Samanta, Manoj P -- Stolc, Viktor -- Tongprasit, Waraporn -- Tu, Qiang -- Bergeron, Karl-Frederik -- Brandhorst, Bruce P -- Whittle, James -- Berney, Kevin -- Bottjer, David J -- Calestani, Cristina -- Peterson, Kevin -- Chow, Elly -- Yuan, Qiu Autumn -- Elhaik, Eran -- Graur, Dan -- Reese, Justin T -- Bosdet, Ian -- Heesun, Shin -- Marra, Marco A -- Schein, Jacqueline -- Anderson, Michele K -- Brockton, Virginia -- Buckley, Katherine M -- Cohen, Avis H -- Fugmann, Sebastian D -- Hibino, Taku -- Loza-Coll, Mariano -- Majeske, Audrey J -- Messier, Cynthia -- Nair, Sham V -- Pancer, Zeev -- Terwilliger, David P -- Agca, Cavit -- Arboleda, Enrique -- Chen, Nansheng -- Churcher, Allison M -- Hallbook, F -- Humphrey, Glen W -- Idris, Mohammed M -- Kiyama, Takae -- Liang, Shuguang -- Mellott, Dan -- Mu, Xiuqian -- Murray, Greg -- Olinski, Robert P -- Raible, Florian -- Rowe, Matthew -- Taylor, John S -- Tessmar-Raible, Kristin -- Wang, D -- Wilson, Karen H -- Yaguchi, Shunsuke -- Gaasterland, Terry -- Galindo, Blanca E -- Gunaratne, Herath J -- Juliano, Celina -- Kinukawa, Masashi -- Moy, Gary W -- Neill, Anna T -- Nomura, Mamoru -- Raisch, Michael -- Reade, Anna -- Roux, Michelle M -- Song, Jia L -- Su, Yi-Hsien -- Townley, Ian K -- Voronina, Ekaterina -- Wong, Julian L -- Amore, Gabriele -- Branno, Margherita -- Brown, Euan R -- Cavalieri, Vincenzo -- Duboc, Veronique -- Duloquin, Louise -- Flytzanis, Constantin -- Gache, Christian -- Lapraz, Francois -- Lepage, Thierry -- Locascio, Annamaria -- Martinez, Pedro -- Matassi, Giorgio -- Matranga, Valeria -- Range, Ryan -- Rizzo, Francesca -- Rottinger, Eric -- Beane, Wendy -- Bradham, Cynthia -- Byrum, Christine -- Glenn, Tom -- Hussain, Sofia -- Manning, Gerard -- Miranda, Esther -- Thomason, Rebecca -- Walton, Katherine -- Wikramanayke, Athula -- Wu, Shu-Yu -- Xu, Ronghui -- Brown, C Titus -- Chen, Lili -- Gray, Rachel F -- Lee, Pei Yun -- Nam, Jongmin -- Oliveri, Paola -- Smith, Joel -- Muzny, Donna -- Bell, Stephanie -- Chacko, Joseph -- Cree, Andrew -- Curry, Stacey -- Davis, Clay -- Dinh, Huyen -- Dugan-Rocha, Shannon -- Fowler, Jerry -- Gill, Rachel -- Hamilton, Cerrissa -- Hernandez, Judith -- Hines, Sandra -- Hume, Jennifer -- Jackson, Laronda -- Jolivet, Angela -- Kovar, Christie -- Lee, Sandra -- Lewis, Lora -- Miner, George -- Morgan, Margaret -- Nazareth, Lynne V -- Okwuonu, Geoffrey -- Parker, David -- Pu, Ling-Ling -- Thorn, Rachel -- Wright, Rita -- 2P42 ESO7381/PHS HHS/ -- 5 U54 HG003273/HG/NHGRI NIH HHS/ -- EY11930/EY/NEI NIH HHS/ -- F32 ESO12794/PHS HHS/ -- F32 HD047136/HD/NICHD NIH HHS/ -- F32 HD047136-02/HD/NICHD NIH HHS/ -- F32 HD047136-03/HD/NICHD NIH HHS/ -- F32-HD47136/HD/NICHD NIH HHS/ -- GM058231/GM/NIGMS NIH HHS/ -- GM070840/GM/NIGMS NIH HHS/ -- GM61005/GM/NIGMS NIH HHS/ -- GM61464/GM/NIGMS NIH HHS/ -- HD-37105/HD/NICHD NIH HHS/ -- HD039948/HD/NICHD NIH HHS/ -- HD14483/HD/NICHD NIH HHS/ -- HD66219/HD/NICHD NIH HHS/ -- P30-CA14051/CA/NCI NIH HHS/ -- R01 ES006272/ES/NIEHS NIH HHS/ -- R01 ES006272-13/ES/NIEHS NIH HHS/ -- R01 GM070840/GM/NIGMS NIH HHS/ -- R01 HD028152/HD/NICHD NIH HHS/ -- R01ES006272/ES/NIEHS NIH HHS/ -- R37-HD12896/HD/NICHD NIH HHS/ -- RR-15044/RR/NCRR NIH HHS/ -- S19916/Biotechnology and Biological Sciences Research Council/United Kingdom -- T32 GM007601/GM/NIGMS NIH HHS/ -- U54 HG003273/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2006 Nov 10;314(5801):941-52.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17095691" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcification, Physiologic ; Cell Adhesion Molecules/genetics/physiology ; Complement Activation/genetics ; Computational Biology ; Embryonic Development/genetics ; Evolution, Molecular ; Gene Expression Regulation, Developmental ; Genes ; *Genome ; Immunity, Innate/genetics ; Immunologic Factors/genetics/physiology ; Male ; Nervous System Physiological Phenomena ; Proteins/genetics/physiology ; *Sequence Analysis, DNA ; Signal Transduction ; Strongylocentrotus purpuratus/embryology/*genetics/immunology/physiology ; Transcription Factors/genetics
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  • 98
    Publication Date: 2006-05-27
    Description: Genetic mutations that disrupt osteoblast function can result in skeletal dysmorphogenesis or, more rarely, in increased postnatal bone formation. Here we show that Schnurri-3 (Shn3), a mammalian homolog of the Drosophila zinc finger adapter protein Shn, is an essential regulator of adult bone formation. Mice lacking Shn3 display adult-onset osteosclerosis with increased bone mass due to augmented osteoblast activity. Shn3 was found to control protein levels of Runx2, the principal transcriptional regulator of osteoblast differentiation, by promoting its degradation through recruitment of the E3 ubiquitin ligase WWP1 to Runx2. By this means, Runx2-mediated extracellular matrix mineralization was antagonized, revealing an essential role for Shn3 as a central regulator of postnatal bone mass.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jones, Dallas C -- Wein, Marc N -- Oukka, Mohamed -- Hofstaetter, Jochen G -- Glimcher, Melvin J -- Glimcher, Laurie H -- AI29673/AI/NIAID NIH HHS/ -- AR46983/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 2006 May 26;312(5777):1223-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16728642" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; *Bone Density ; Bone and Bones/*anatomy & histology/chemistry/physiology ; Cell Line ; Cells, Cultured ; Core Binding Factor Alpha 1 Subunit/genetics/metabolism ; DNA-Binding Proteins/analysis/genetics/*metabolism ; Gene Expression Regulation ; Immunoprecipitation ; Mice ; Osteoblasts/chemistry/physiology ; Osteoclasts/physiology ; Osteogenesis ; Protein Binding ; Protein Structure, Tertiary ; RNA Interference ; RNA, Messenger/genetics/metabolism ; Transcriptional Activation ; Transfection ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/chemistry/metabolism ; Zinc Fingers
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  • 99
    Publication Date: 2006-09-16
    Description: We used nuclear magnetic resonance relaxation dispersion to characterize higher energy conformational substates of Escherichia coli dihydrofolate reductase. Each intermediate in the catalytic cycle samples low-lying excited states whose conformations resemble the ground-state structures of preceding and following intermediates. Substrate and cofactor exchange occurs through these excited substates. The maximum hydride transfer and steady-state turnover rates are governed by the dynamics of transitions between ground and excited states of the intermediates. Thus, the modulation of the energy landscape by the bound ligands funnels the enzyme through its reaction cycle along a preferred kinetic path.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boehr, David D -- McElheny, Dan -- Dyson, H Jane -- Wright, Peter E -- GM56879/GM/NIGMS NIH HHS/ -- GM75995/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Sep 15;313(5793):1638-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Skaggs Institute for Chemical Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16973882" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; Escherichia coli/*enzymology ; Kinetics ; Ligands ; Models, Molecular ; NADP/metabolism ; Nuclear Magnetic Resonance, Biomolecular ; Protein Binding ; *Protein Conformation ; Tetrahydrofolate Dehydrogenase/*chemistry/*metabolism ; Tetrahydrofolates/metabolism ; Thermodynamics
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  • 100
    Publication Date: 2006-06-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mora, Camilo -- Andrefouet, Serge -- Costello, Mark J -- Kranenburg, Christine -- Rollo, Audrey -- Veron, John -- Gaston, Kevin J -- Myers, Ransom A -- New York, N.Y. -- Science. 2006 Jun 23;312(5781):1750-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Leigh Marine Laboratory, University of Auckland, Post Office Box 349, Warkworth, New Zealand. moracamilo@hotmail.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16794065" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Anthozoa ; *Biodiversity ; *Conservation of Natural Resources ; Databases, Factual ; *Ecosystem ; *Fishes ; Homing Behavior ; Marine Biology ; Population Dynamics
    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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