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  • 1
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    Geophysics. Coping with earthquakes induced by fluid injection (2015)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Cryo-EM studies of the structure and dynamics of vacuolar-type ATPases (2016)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2016-07-24
    Description: Electron cryomicroscopy (cryo-EM) has significantly advanced our understanding of molecular structure in biology. Recent innovations in both hardware and software have made cryo-EM a viable alternative for targets that are not amenable to x-ray crystallography or nuclear magnetic resonance (NMR) spectroscopy. Cryo-EM has even become the method of choice in some situations where x-ray crystallography and NMR spectroscopy are possible but where cryo-EM can determine structures at higher resolution or with less time or effort. Rotary adenosine triphosphatases (ATPases) are crucial to the maintenance of cellular homeostasis. These enzymes couple the synthesis or hydrolysis of adenosine triphosphate to the use or production of a transmembrane electrochemical ion gradient, respectively. However, the membrane-embedded nature and conformational heterogeneity of intact rotary ATPases have prevented their high-resolution structural analysis to date. Recent application of cryo-EM methods to the different types of rotary ATPase has led to sudden advances in understanding the structure and function of these enzymes, revealing significant conformational heterogeneity and characteristic transmembrane α helices that are highly tilted with respect to the membrane. In this Review, we will discuss what has been learned recently about rotary ATPase structure and function, with a particular focus on the vacuolar-type ATPases.
    Electronic ISSN: 2375-2548
    Topics: Natural Sciences in General
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Atomic model for the dimeric FO region of mitochondrial ATP synthase (2017)
    American Association for the Advancement of Science (AAAS)
    In: Science
    Details
    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
    Published by American Association for the Advancement of Science (AAAS)
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