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Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism.
Lavery, Laura A; Partridge, James R; Ramelot, Theresa A; Elnatan, Daniel; Kennedy, Michael A; Agard, David A.
Affiliation
  • Lavery LA; Howard Hughes Medical Institute and the Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA.
  • Partridge JR; Howard Hughes Medical Institute and the Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA.
  • Ramelot TA; Department of Chemistry and Biochemistry, Miami University Oxford, OH 45056, USA.
  • Elnatan D; Howard Hughes Medical Institute and the Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA.
  • Kennedy MA; Department of Chemistry and Biochemistry, Miami University Oxford, OH 45056, USA.
  • Agard DA; Howard Hughes Medical Institute and the Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA. Electronic address: agard@msg.ucsf.edu.
Mol Cell ; 53(2): 330-43, 2014 Jan 23.
Article in En | MEDLINE | ID: mdl-24462206
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Full text: 1 Database: MEDLINE Main subject: Adenosine Triphosphate / Zebrafish Proteins / TNF Receptor-Associated Factor 1 Language: En Year: 2014 Type: Article
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PubMed Links
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Full text: 1 Database: MEDLINE Main subject: Adenosine Triphosphate / Zebrafish Proteins / TNF Receptor-Associated Factor 1 Language: En Year: 2014 Type: Article