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  • *Heat-Shock Proteins  (1)
  • *Radiation Dosage  (1)
  • American Association for the Advancement of Science (AAAS)  (2)
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  • American Association for the Advancement of Science (AAAS)  (2)
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  • 1
    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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  • 2
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    American Association for the Advancement of Science (AAAS)
    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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