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  • Articles  (2)
  • American Association for the Advancement of Science (AAAS)  (2)
  • Seismological Society of America (SSA)
  • Society of Exploration Geophysicists (SEG)
  • Computer Science  (2)
  • 1
    Publication Date: 2015-02-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McGarr, A -- Bekins, B -- Burkardt, N -- Dewey, J -- Earle, P -- Ellsworth, W -- Ge, S -- Hickman, S -- Holland, A -- Majer, E -- Rubinstein, J -- Sheehan, A -- New York, N.Y. -- Science. 2015 Feb 20;347(6224):830-1. doi: 10.1126/science.aaa0494.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉U.S. Geological Survey (USGS), Earthquake Science Center, Menlo Park, CA 94025, USA. mcgarr@usgs.gov. ; USGS, National Water Quality Assessment Program, Menlo Park, CA 94025, USA. ; USGS, Powell Center, Fort Collins, CO 80526, USA. ; USGS, Geologic Hazards Center, Golden, CO 80225, USA. ; U.S. Geological Survey (USGS), Earthquake Science Center, Menlo Park, CA 94025, USA. ; University of Colorado at Boulder, Boulder, CO 80302, USA. ; Oklahoma Geological Survey, Norman, OK 73069, USA. ; Lawrence Berkeley National Laboratory, Berkeley, CA, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25700505" target="_blank"〉PubMed〈/a〉
    Keywords: Disasters/*prevention & control/*statistics & numerical data ; Earthquakes/*statistics & numerical data ; Proportional Hazards Models ; Safety Management/methods ; United States ; Waste Disposal, Fluid/*methods
    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)
    In: Science
    Publication Date: 2017-11-17
    Description: Mitochondrial adenosine triphosphate (ATP) synthase produces the majority of ATP in eukaryotic cells, and its dimerization is necessary to create the inner membrane folds, or cristae, characteristic of mitochondria. Proton translocation through the membrane-embedded F O region turns the rotor that drives ATP synthesis in the soluble F 1 region. Although crystal structures of the F 1 region have illustrated how this rotation leads to ATP synthesis, understanding how proton translocation produces the rotation has been impeded by the lack of an experimental atomic model for the F O region. Using cryo–electron microscopy, we determined the structure of the dimeric F O complex from Saccharomyces cerevisiae at a resolution of 3.6 angstroms. The structure clarifies how the protons travel through the complex, how the complex dimerizes, and how the dimers bend the membrane to produce cristae.
    Keywords: Biochemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Geosciences , Computer Science , Medicine , Natural Sciences in General , Physics
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