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  • Articles  (22)
  • Extraterrestrial Environment  (14)
  • Binding Sites  (8)
  • 2000-2004  (22)
  • 1975-1979
  • 2004  (22)
  • Biology  (22)
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  • Articles  (22)
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  • 2000-2004  (22)
  • 1975-1979
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  • 1
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    Pancam multispectral imaging results from the Spirit Rover at Gusev Crater (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-07
    Description: Panoramic Camera images at Gusev crater reveal a rock-strewn surface interspersed with high- to moderate-albedo fine-grained deposits occurring in part as drifts or in small circular swales or hollows. Optically thick coatings of fine-grained ferric iron-rich dust dominate most bright soil and rock surfaces. Spectra of some darker rock surfaces and rock regions exposed by brushing or grinding show near-infrared spectral signatures consistent with the presence of mafic silicates such as pyroxene or olivine. Atmospheric observations show a steady decline in dust opacity during the mission, and astronomical observations captured solar transits by the martian moons, Phobos and Deimos, as well as a view of Earth from the martian surface.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bell, J F 3rd -- Squyres, S W -- Arvidson, R E -- Arneson, H M -- Bass, D -- Blaney, D -- Cabrol, N -- Calvin, W -- Farmer, J -- Farrand, W H -- Goetz, W -- Golombek, M -- Grant, J A -- Greeley, R -- Guinness, E -- Hayes, A G -- Hubbard, M Y H -- Herkenhoff, K E -- Johnson, M J -- Johnson, J R -- Joseph, J -- Kinch, K M -- Lemmon, M T -- Li, R -- Madsen, M B -- Maki, J N -- Malin, M -- McCartney, E -- McLennan, S -- McSween, H Y Jr -- Ming, D W -- Moersch, J E -- Morris, R V -- Dobrea, E Z Noe -- Parker, T J -- Proton, J -- Rice, J W Jr -- Seelos, F -- Soderblom, J -- Soderblom, L A -- Sohl-Dickstein, J N -- Sullivan, R J -- Wolff, M J -- Wang, A -- New York, N.Y. -- Science. 2004 Aug 6;305(5685):800-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cornell University, Ithaca, NY 14853-6801, USA. jfb8@cornell.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15297658" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere ; Evolution, Planetary ; Extraterrestrial Environment ; Ferric Compounds ; Geologic Sediments ; Iron Compounds ; *Mars ; Minerals ; Silicates ; Solar System ; Spectrum Analysis ; Water
    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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    Pancam multispectral imaging results from the Opportunity Rover at Meridiani Planum (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-04
    Description: Panoramic Camera (Pancam) images from Meridiani Planum reveal a low-albedo, generally flat, and relatively rock-free surface. Within and around impact craters and fractures, laminated outcrop rocks with higher albedo are observed. Fine-grained materials include dark sand, bright ferric iron-rich dust, angular rock clasts, and millimeter-size spheroidal granules that are eroding out of the laminated rocks. Spectra of sand, clasts, and one dark plains rock are consistent with mafic silicates such as pyroxene and olivine. Spectra of both the spherules and the laminated outcrop materials indicate the presence of crystalline ferric oxides or oxyhydroxides. Atmospheric observations show a steady decline in dust opacity during the mission. Astronomical observations captured solar transits by Phobos and Deimos and time-lapse observations of sunsets.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bell, J F 3rd -- Squyres, S W -- Arvidson, R E -- Arneson, H M -- Bass, D -- Calvin, W -- Farrand, W H -- Goetz, W -- Golombek, M -- Greeley, R -- Grotzinger, J -- Guinness, E -- Hayes, A G -- Hubbard, M Y H -- Herkenhoff, K E -- Johnson, M J -- Johnson, J R -- Joseph, J -- Kinch, K M -- Lemmon, M T -- Li, R -- Madsen, M B -- Maki, J N -- Malin, M -- McCartney, E -- McLennan, S -- McSween, H Y Jr -- Ming, D W -- Morris, R V -- Dobrea, E Z Noe -- Parker, T J -- Proton, J -- Rice, J W Jr -- Seelos, F -- Soderblom, J M -- Soderblom, L A -- Sohl-Dickstein, J N -- Sullivan, R J -- Weitz, C M -- Wolff, M J -- New York, N.Y. -- Science. 2004 Dec 3;306(5702):1703-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Astronomy, Cornell University, Ithaca NY 14853, USA. jfb8@cornell.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15576603" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere ; Extraterrestrial Environment ; Ferric Compounds ; Geologic Sediments ; Ice ; *Mars ; Silicates ; Spacecraft ; Spectrum Analysis ; Water
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Visfatin: a protein secreted by visceral fat that mimics the effects of insulin (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-18
    Description: Fat tissue produces a variety of secreted proteins (adipocytokines) with important roles in metabolism. We isolated a newly identified adipocytokine, visfatin, that is highly enriched in the visceral fat of both humans and mice and whose expression level in plasma increases during the development of obesity. Visfatin corresponds to a protein identified previously as pre-B cell colony-enhancing factor (PBEF), a 52-kilodalton cytokine expressed in lymphocytes. Visfatin exerted insulin-mimetic effects in cultured cells and lowered plasma glucose levels in mice. Mice heterozygous for a targeted mutation in the visfatin gene had modestly higher levels of plasma glucose relative to wild-type littermates. Surprisingly, visfatin binds to and activates the insulin receptor. Further study of visfatin's physiological role may lead to new insights into glucose homeostasis and/or new therapies for metabolic disorders such as diabetes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fukuhara, Atsunori -- Matsuda, Morihiro -- Nishizawa, Masako -- Segawa, Katsumori -- Tanaka, Masaki -- Kishimoto, Kae -- Matsuki, Yasushi -- Murakami, Mirei -- Ichisaka, Tomoko -- Murakami, Hiroko -- Watanabe, Eijiro -- Takagi, Toshiyuki -- Akiyoshi, Megumi -- Ohtsubo, Tsuguteru -- Kihara, Shinji -- Yamashita, Shizuya -- Makishima, Makoto -- Funahashi, Tohru -- Yamanaka, Shinya -- Hiramatsu, Ryuji -- Matsuzawa, Yuji -- Shimomura, Iichiro -- New York, N.Y. -- Science. 2005 Jan 21;307(5708):426-30. Epub 2004 Dec 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine and Pathophysiology, Graduate School of Medicine, and Department of Organismal Biosystems, Graduate School of Frontier Biosciences, Osaka University, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15604363" target="_blank"〉PubMed〈/a〉
    Keywords: Adipocytes/drug effects/metabolism ; Adipose Tissue/*metabolism ; Animals ; Binding Sites ; Blood Glucose/analysis ; Cell Line ; Cells, Cultured ; Cytokines/blood/genetics/*metabolism/pharmacology ; Diabetes Mellitus, Type 2/metabolism ; Dose-Response Relationship, Drug ; Female ; Gene Expression Profiling ; Gene Expression Regulation/drug effects ; Gene Targeting ; Humans ; Insulin/blood/*metabolism ; Insulin Resistance ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Obese ; Molecular Mimicry ; Muscle Cells/metabolism ; Nicotinamide Phosphoribosyltransferase ; Phosphorylation ; Receptor, Insulin/metabolism ; Recombinant Proteins/pharmacology ; Signal Transduction ; Subcutaneous Tissue ; Viscera
    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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    Jupiter's atmospheric composition from the Cassini thermal infrared spectroscopy experiment (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-21
    Description: The Composite Infrared Spectrometer observed Jupiter in the thermal infrared during the swing-by of the Cassini spacecraft. Results include the detection of two new stratospheric species, the methyl radical and diacetylene, gaseous species present in the north and south auroral infrared hot spots; determination of the variations with latitude of acetylene and ethane, the latter a tracer of atmospheric motion; observations of unexpected spatial distributions of carbon dioxide and hydrogen cyanide, both considered to be products of comet Shoemaker-Levy 9 impacts; characterization of the morphology of the auroral infrared hot spot acetylene emission; and a new evaluation of the energetics of the northern auroral infrared hot spot.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kunde, V G -- Flasar, F M -- Jennings, D E -- Bezard, B -- Strobel, D F -- Conrath, B J -- Nixon, C A -- Bjoraker, G L -- Romani, P N -- Achterberg, R K -- Simon-Miller, A A -- Irwin, P -- Brasunas, J C -- Pearl, J C -- Smith, M D -- Orton, G S -- Gierasch, P J -- Spilker, L J -- Carlson, R C -- Mamoutkine, A A -- Calcutt, S B -- Read, P L -- Taylor, F W -- Fouchet, T -- Parrish, P -- Barucci, A -- Courtin, R -- Coustenis, A -- Gautier, D -- Lellouch, E -- Marten, A -- Prange, R -- Biraud, Y -- Ferrari, C -- Owen, T C -- Abbas, M M -- Samuelson, R E -- Raulin, F -- Ade, P -- Cesarsky, C J -- Grossman, K U -- Coradini, A -- New York, N.Y. -- Science. 2004 Sep 10;305(5690):1582-6. Epub 2004 Aug 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Astronomy, University of Maryland, College Park, MD 20742, USA. Virgil.G.Kunde.1@gsfc.nasa.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15319491" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylene ; Atmosphere ; *Carbon Dioxide ; Ethane ; Extraterrestrial Environment ; *Hydrocarbons ; *Hydrogen Cyanide ; *Jupiter ; Spacecraft ; Spectrum Analysis ; Temperature
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    The structure and receptor binding properties of the 1918 influenza hemagglutinin (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-02-07
    Description: The 1918 influenza pandemic resulted in about 20 million deaths. This enormous impact, coupled with renewed interest in emerging infections, makes characterization of the virus involved a priority. Receptor binding, the initial event in virus infection, is a major determinant of virus transmissibility that, for influenza viruses, is mediated by the hemagglutinin (HA) membrane glycoprotein. We have determined the crystal structures of the HA from the 1918 virus and two closely related HAs in complex with receptor analogs. They explain how the 1918 HA, while retaining receptor binding site amino acids characteristic of an avian precursor HA, is able to bind human receptors and how, as a consequence, the virus was able to spread in the human population.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gamblin, S J -- Haire, L F -- Russell, R J -- Stevens, D J -- Xiao, B -- Ha, Y -- Vasisht, N -- Steinhauer, D A -- Daniels, R S -- Elliot, A -- Wiley, D C -- Skehel, J J -- AI-13654/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2004 Mar 19;303(5665):1838-42. Epub 2004 Feb 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council (MRC) National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14764886" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Birds ; Crystallography, X-Ray ; Hemagglutinin Glycoproteins, Influenza Virus/*chemistry/*metabolism ; History, 20th Century ; Humans ; Hydrogen Bonding ; Influenza A virus/*immunology/metabolism/pathogenicity ; Influenza, Human/epidemiology/history/*virology ; Membrane Glycoproteins/chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Tertiary ; Receptors, Virus/*metabolism ; Sequence Alignment ; Sialic Acids/metabolism ; Species Specificity ; Swine
    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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    In situ evidence for an ancient aqueous environment at Meridiani Planum, Mars (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-04
    Description: Sedimentary rocks at Eagle crater in Meridiani Planum are composed of fine-grained siliciclastic materials derived from weathering of basaltic rocks, sulfate minerals (including magnesium sulfate and jarosite) that constitute several tens of percent of the rock by weight, and hematite. Cross-stratification observed in rock outcrops indicates eolian and aqueous transport. Diagenetic features include hematite-rich concretions and crystal-mold vugs. We interpret the rocks to be a mixture of chemical and siliciclastic sediments with a complex diagenetic history. The environmental conditions that they record include episodic inundation by shallow surface water, evaporation, and desiccation. The geologic record at Meridiani Planum suggests that conditions were suitable for biological activity for a period of time in martian history.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Squyres, S W -- Grotzinger, J P -- Arvidson, R E -- Bell, J F 3rd -- Calvin, W -- Christensen, P R -- Clark, B C -- Crisp, J A -- Farrand, W H -- Herkenhoff, K E -- Johnson, J R -- Klingelhofer, G -- Knoll, A H -- McLennan, S M -- McSween, H Y Jr -- Morris, R V -- Rice, J W Jr -- Rieder, R -- Soderblom, L A -- New York, N.Y. -- Science. 2004 Dec 3;306(5702):1709-14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Astronomy, Cornell University, Ithaca, NY 14853, USA. squyres@astrosun.tn.cornell.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15576604" target="_blank"〉PubMed〈/a〉
    Keywords: Exobiology ; Extraterrestrial Environment ; Ferric Compounds ; Geologic Sediments ; Life ; *Mars ; Minerals ; Silicates ; Spacecraft ; Spectrum Analysis ; Sulfates ; Sulfur ; *Water
    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
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    The galactic habitable zone and the age distribution of complex life in the Milky Way (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-06
    Description: We modeled the evolution of the Milky Way Galaxy to trace the distribution in space and time of four prerequisites for complex life: the presence of a host star, enough heavy elements to form terrestrial planets, sufficient time for biological evolution, and an environment free of life-extinguishing supernovae. We identified the Galactic habitable zone (GHZ) as an annular region between 7 and 9 kiloparsecs from the Galactic center that widens with time and is composed of stars that formed between 8 and 4 billion years ago. This GHZ yields an age distribution for the complex life that may inhabit our Galaxy. We found that 75% of the stars in the GHZ are older than the Sun.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lineweaver, Charles H -- Fenner, Yeshe -- Gibson, Brad K -- New York, N.Y. -- Science. 2004 Jan 2;303(5654):59-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Astrophysics, University of New South Wales (NSW), Sydney, NSW 2052, Australia. charley@bat.phys.unsw.edu.au〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14704421" target="_blank"〉PubMed〈/a〉
    Keywords: Astronomical Phenomena ; *Astronomy ; Computer Simulation ; Evolution, Chemical ; Evolution, Planetary ; *Exobiology ; Extraterrestrial Environment ; Models, Theoretical ; Probability ; Time
    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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  • 8
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    Mechanism of ammonia transport by Amt/MEP/Rh: structure of AmtB at 1.35 A (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-09-14
    Description: The first structure of an ammonia channel from the Amt/MEP/Rh protein superfamily, determined to 1.35 angstrom resolution, shows it to be a channel that spans the membrane 11 times. Two structurally similar halves span the membrane with opposite polarity. Structures with and without ammonia or methyl ammonia show a vestibule that recruits NH4+/NH3, a binding site for NH4+, and a 20 angstrom-long hydrophobic channel that lowers the NH4+ pKa to below 6 and conducts NH3. Favorable interactions for NH3 are seen within the channel and use conserved histidines. Reconstitution of AmtB into vesicles shows that AmtB conducts uncharged NH3.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Khademi, Shahram -- O'Connell, Joseph 3rd -- Remis, Jonathan -- Robles-Colmenares, Yaneth -- Miercke, Larry J W -- Stroud, Robert M -- GM24485/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Sep 10;305(5690):1587-94.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, S412C Genentech Hall, University of California-San Francisco, 600 16th Street, San Francisco, CA 94143-2240, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15361618" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Ammonia/*metabolism ; Binding Sites ; Biological Transport ; Cation Transport Proteins/*chemistry/genetics/metabolism ; Cell Membrane/chemistry ; Crystallization ; Crystallography, X-Ray ; Escherichia coli/*chemistry/metabolism ; Escherichia coli Proteins/*chemistry/genetics/metabolism ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Hydrophobic and Hydrophilic Interactions ; Liposomes ; Membrane Potentials ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Quaternary Ammonium Compounds/metabolism ; Rh-Hr Blood-Group System/chemistry/metabolism ; Sequence Alignment ; Water/chemistry/metabolism
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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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    Semaphorin 3E and plexin-D1 control vascular pattern independently of neuropilins (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-11-20
    Description: The development of a patterned vasculature is essential for normal organogenesis. We found that signaling by semaphorin 3E (Sema3E) and its receptor plexin-D1 controls endothelial cell positioning and the patterning of the developing vasculature in the mouse. Sema3E is highly expressed in developing somites, where it acts as a repulsive cue for plexin-D1-expressing endothelial cells of adjacent intersomitic vessels. Sema3E-plexin-D1 signaling did not require neuropilins, which were previously presumed to be obligate Sema3 coreceptors. Moreover, genetic ablation of Sema3E or plexin-D1 but not neuropilin-mediated Sema3 signaling disrupted vascular patterning. These findings reveal an unexpected semaphorin signaling pathway and define a mechanism for controlling vascular patterning.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gu, Chenghua -- Yoshida, Yutaka -- Livet, Jean -- Reimert, Dorothy V -- Mann, Fanny -- Merte, Janna -- Henderson, Christopher E -- Jessell, Thomas M -- Kolodkin, Alex L -- Ginty, David D -- CA23767-24/CA/NCI NIH HHS/ -- MH59199-06/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2005 Jan 14;307(5707):265-8. Epub 2004 Nov 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205-2185, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15550623" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Blood Vessels/*embryology/metabolism ; Body Patterning ; COS Cells ; Cercopithecus aethiops ; Chick Embryo ; Endothelial Cells/cytology/physiology ; Endothelium, Vascular/cytology/embryology ; Glycoproteins/*metabolism ; In Situ Hybridization ; Ligands ; Membrane Glycoproteins/*metabolism ; Membrane Proteins/*metabolism ; Mice ; Morphogenesis ; Mutation ; Nerve Tissue Proteins/*metabolism ; Neuropilin-1/metabolism ; Neuropilin-2/metabolism ; Phenotype ; Protein Binding ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Somites/*metabolism ; Transfection
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  • 10
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    Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-06
    Description: The crystal structure of biotin synthase from Escherichia coli in complex with S-adenosyl-L-methionine and dethiobiotin has been determined to 3.4 angstrom resolution. This structure addresses how "AdoMet radical" or "radical SAM" enzymes use Fe4S4 clusters and S-adenosyl-L-methionine to generate organic radicals. Biotin synthase catalyzes the radical-mediated insertion of sulfur into dethiobiotin to form biotin. The structure places the substrates between the Fe4S4 cluster, essential for radical generation, and the Fe2S2 cluster, postulated to be the source of sulfur, with both clusters in unprecedented coordination environments.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1456065/" 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/PMC1456065/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berkovitch, Frederick -- Nicolet, Yvain -- Wan, Jason T -- Jarrett, Joseph T -- Drennan, Catherine L -- NSLS X25/NS/NINDS NIH HHS/ -- R01 GM059175/GM/NIGMS NIH HHS/ -- R01-GM59175/GM/NIGMS NIH HHS/ -- R01-GM65337/GM/NIGMS NIH HHS/ -- T32-GM07229/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Jan 2;303(5654):76-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14704425" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Binding Sites ; Biotin/*analogs & derivatives/*chemistry/metabolism ; Catalysis ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Escherichia coli/*enzymology ; Escherichia coli Proteins/*chemistry/*metabolism ; Hydrogen/chemistry ; Hydrogen Bonding ; Iron/chemistry ; Ligands ; Models, Molecular ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; S-Adenosylmethionine/*chemistry/metabolism ; Sulfur/chemistry ; Sulfurtransferases/*chemistry/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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