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  • Humans  (3)
  • Protein Structure, Secondary  (3)
  • American Association for the Advancement of Science (AAAS)  (6)
  • 1
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    Structure of yeast poly(A) polymerase alone and in complex with 3'-dATP (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-26
    Description: Polyadenylate [poly(A)] polymerase (PAP) catalyzes the addition of a polyadenosine tail to almost all eukaryotic messenger RNAs (mRNAs). The crystal structure of the PAP from Saccharomyces cerevisiae (Pap1) has been solved to 2.6 angstroms, both alone and in complex with 3'-deoxyadenosine triphosphate (3'-dATP). Like other nucleic acid polymerases, Pap1 is composed of three domains that encircle the active site. The arrangement of these domains, however, is quite different from that seen in polymerases that use a template to select and position their incoming nucleotides. The first two domains are functionally analogous to polymerase palm and fingers domains. The third domain is attached to the fingers domain and is known to interact with the single-stranded RNA primer. In the nucleotide complex, two molecules of 3'-dATP are bound to Pap1. One occupies the position of the incoming base, prior to its addition to the mRNA chain. The other is believed to occupy the position of the 3' end of the mRNA primer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bard, J -- Zhelkovsky, A M -- Helmling, S -- Earnest, T N -- Moore, C L -- Bohm, A -- R01 GM57218-01A2/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Aug 25;289(5483):1346-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10958780" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalytic Domain ; Crystallography, X-Ray ; Deoxyadenine Nucleotides/*chemistry/*metabolism ; Hydrogen Bonding ; Manganese/metabolism ; Models, Molecular ; Mutation ; Polynucleotide Adenylyltransferase/*chemistry/genetics/*metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA/metabolism ; RNA, Messenger/metabolism ; Ribosomal Protein S6 ; Ribosomal Proteins/chemistry/metabolism ; Saccharomyces cerevisiae/*enzymology
    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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    Three-dimensional structure of dimeric human recombinant macrophage colony-stimulating factor (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-11-20
    Description: Macrophage colony-stimulating factor (M-CSF) triggers the development of cells of the monocyte-macrophage lineage and has a variety of stimulatory effects on mature cells of this class. The biologically active form of M-CSF is a disulfide-linked dimer that activates an intrinsic tyrosine kinase activity on the M-CSF receptor by inducing dimerization of the receptor molecules. The structure of a recombinant human M-CSF dimer, determined at 2.5 angstroms by x-ray crystallography, contains two bundles of four alpha helices laid end-to-end, with an interchain disulfide bond. Individual monomers of M-CSF show a close structural similarity to the cytokines granulocyte-macrophage colony-stimulating factor and human growth hormone. Both of these cytokines are monomeric in their active form, and their specific receptors lack intrinsic tyrosine kinase activity. The similarity of these structures suggests that the receptor binding determinants for all three cytokines may be similar.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pandit, J -- Bohm, A -- Jancarik, J -- Halenbeck, R -- Koths, K -- Kim, S H -- New York, N.Y. -- Science. 1992 Nov 20;258(5086):1358-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Structural Biology Division, Lawrence Berkeley Laboratory, Berkeley, CA 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1455231" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallography ; Disulfides ; Granulocyte-Macrophage Colony-Stimulating Factor/ultrastructure ; Growth Hormone/chemistry ; Macrophage Colony-Stimulating Factor/*ultrastructure ; Models, Molecular ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins/ultrastructure ; Sequence Homology, Amino Acid ; X-Ray Diffraction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Measurements of energetic particle radiation in transit to Mars on the Mars Science Laboratory (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-06-01
    Description: The Mars Science Laboratory spacecraft, containing the Curiosity rover, was launched to Mars on 26 November 2011, and for most of the 253-day, 560-million-kilometer cruise to Mars, the Radiation Assessment Detector made detailed measurements of the energetic particle radiation environment inside the spacecraft. These data provide insights into the radiation hazards that would be associated with a human mission to Mars. We report measurements of the radiation dose, dose equivalent, and linear energy transfer spectra. The dose equivalent for even the shortest round-trip with current propulsion systems and comparable shielding is found to be 0.66 +/- 0.12 sievert.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zeitlin, C -- Hassler, D M -- Cucinotta, F A -- Ehresmann, B -- Wimmer-Schweingruber, R F -- Brinza, D E -- Kang, S -- Weigle, G -- Bottcher, S -- Bohm, E -- Burmeister, S -- Guo, J -- Kohler, J -- Martin, C -- Posner, A -- Rafkin, S -- Reitz, G -- New York, N.Y. -- Science. 2013 May 31;340(6136):1080-4. doi: 10.1126/science.1235989.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Southwest Research Institute, Boulder, CO, USA. zeitlin@boulder.swri.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23723233" target="_blank"〉PubMed〈/a〉
    Keywords: *Cosmic Radiation ; Humans ; *Mars ; *Radiation Dosage ; *Space Flight
    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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    Crystal structure of the DNA binding domain of the heat shock transcription factor (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-01-14
    Description: The structure of the DNA binding domain, determined at 1.8 angstrom resolution, contains a three-helix bundle that is capped by a four-stranded antiparallel beta sheet. This structure is a variant of the helix-turn-helix motif, typified by catabolite activator protein. In the heat shock transcription factor, the first helix of the motif (alpha 2) has an alpha-helical bulge and a proline-induced kink. The angle between the two helices of the motif (alpha 2 and alpha 3) is about 20 degrees smaller than the average for canonical helix-turn-helix proteins. Nevertheless, the relative positions of the first and third helices of the bundle (alpha 1 and alpha 3) are conserved. It is proposed here that the first helix of the three-helix bundle be considered a component of the helix-turn-helix motif.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harrison, C J -- Bohm, A A -- Nelson, H C -- GM08295/GM/NIGMS NIH HHS/ -- GM44086/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Jan 14;263(5144):224-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8284672" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Crystallography, X-Ray ; DNA/*metabolism ; DNA-Binding Proteins/*chemistry/metabolism ; *Heat-Shock Proteins ; *Helix-Loop-Helix Motifs ; Models, Molecular ; Molecular Sequence Data ; Protein Structure, Secondary ; Transcription Factors/*chemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Long-acting integrase inhibitor protects macaques from intrarectal simian/human immunodeficiency virus (2014)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2014-03-07
    Description: GSK1265744 (GSK744) is an integrase strand-transfer inhibitor that has been formulated as a long-acting (LA) injectable suitable for monthly to quarterly clinical administration. GSK744 LA was administered at two time points 4 weeks apart beginning 1 week before virus administration, and macaques were challenged weekly for 8 weeks. GSK744 LA, at plasma concentrations achievable with quarterly injections in humans, protected all animals against repeated low-dose challenges. In a second experiment, macaques were given GSK744 LA 1 week before virus administration and challenged repeatedly until infection occurred. Protection decreased over time and correlated with the plasma drug levels. With a quarterly dosing schedule in humans, our results suggest that GSK744 LA could potentially decrease adherence problems associated with daily preexposure prophylaxis (PrEP).〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4308974/" 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/PMC4308974/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Andrews, Chasity D -- Spreen, William R -- Mohri, Hiroshi -- Moss, Lee -- Ford, Susan -- Gettie, Agegnehu -- Russell-Lodrigue, Kasi -- Bohm, Rudolf P -- Cheng-Mayer, Cecilia -- Hong, Zhi -- Markowitz, Martin -- Ho, David D -- 1DP1-DA033263/DA/NIDA NIH HHS/ -- 2P51-OD11104-52/OD/NIH HHS/ -- P51 OD011104/OD/NIH HHS/ -- R0-AI100724/AI/NIAID NIH HHS/ -- R01 AI100724/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2014 Mar 7;343(6175):1151-4. doi: 10.1126/science.1248707. Epub 2014 Mar 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Aaron Diamond AIDS Research Center, Rockefeller University, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24594934" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Delayed-Action Preparations/administration & dosage/pharmacokinetics ; HIV Infections/*prevention & control ; HIV Integrase Inhibitors/*administration & dosage/blood/pharmacokinetics ; HIV-1/*drug effects ; Humans ; Macaca mulatta ; Molecular Sequence Data ; Pyridones/*administration & dosage ; Rectum/virology ; Simian Acquired Immunodeficiency Syndrome/*prevention & control ; Simian Immunodeficiency Virus/*drug effects
    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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    Mars' surface radiation environment measured with the Mars Science Laboratory's Curiosity rover (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-12-11
    Description: The Radiation Assessment Detector (RAD) on the Mars Science Laboratory's Curiosity rover began making detailed measurements of the cosmic ray and energetic particle radiation environment on the surface of Mars on 7 August 2012. We report and discuss measurements of the absorbed dose and dose equivalent from galactic cosmic rays and solar energetic particles on the martian surface for ~300 days of observations during the current solar maximum. These measurements provide insight into the radiation hazards associated with a human mission to the surface of Mars and provide an anchor point with which to model the subsurface radiation environment, with implications for microbial survival times of any possible extant or past life, as well as for the preservation of potential organic biosignatures of the ancient martian environment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hassler, Donald M -- Zeitlin, Cary -- Wimmer-Schweingruber, Robert F -- Ehresmann, Bent -- Rafkin, Scot -- Eigenbrode, Jennifer L -- Brinza, David E -- Weigle, Gerald -- Bottcher, Stephan -- Bohm, Eckart -- Burmeister, Soenke -- Guo, Jingnan -- Kohler, Jan -- Martin, Cesar -- Reitz, Guenther -- Cucinotta, Francis A -- Kim, Myung-Hee -- Grinspoon, David -- Bullock, Mark A -- Posner, Arik -- Gomez-Elvira, Javier -- Vasavada, Ashwin -- Grotzinger, John P -- MSL Science Team -- New York, N.Y. -- Science. 2014 Jan 24;343(6169):1244797. doi: 10.1126/science.1244797. Epub 2013 Dec 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Southwest Research Institute, Boulder, CO 80302, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24324275" target="_blank"〉PubMed〈/a〉
    Keywords: *Cosmic Radiation ; Deinococcus/physiology/radiation effects ; *Exobiology ; *Extraterrestrial Environment ; Humans ; *Mars ; Organic Chemicals/analysis ; Radiation Dosage ; Space Flight ; Surface Properties/radiation effects
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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