Crystal structure of the nucleotide-binding domain of mortalin, the mitochondrial Hsp70 chaperone-Reference-Cited by-同舟云学术

Crystal structure of the nucleotide-binding domain of mortalin, the mitochondrial Hsp70 chaperone

Published:2014-04-17 Issue:6 Volume:23 Page:833-842
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Amick Joseph¹,Schlanger Simon E.¹,Wachnowsky Christine²,Moseng Mitchell A.³,Emerson Corey C.³,Dare Michelle¹,Luo Wen-I²,Ithychanda Sujay S.¹,Nix Jay C.⁴,Cowan J. A.²,Page Richard C.³,Misra Saurav¹

Affiliation:

1. Department of Molecular Cardiology; The Cleveland Clinic; Cleveland Ohio 44195

2. Department of Chemistry; The Ohio State University; Columbus Ohio 43210

3. Department of Chemistry and Biochemistry; Miami University; Oxford Ohio 45056

4. Molecular Biology Consortium, Advanced Light Source; Lawrence Berkeley National Laboratory; Berkeley California 94720

Funder

U.S. National Institutes of Health (S.M.)

National Institutes of Health (R.C.P.)

U.S. Department of Energy, Office of Basic Energy Sciences (The Advanced Light Source)

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.2466/fullpdf

Reference71 articles.

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3. Identification of a novel member of mouse hsp70 family;Wadhwa;Its association with cellular mortal phenotype. J Biol Chem,1993

4. Identification, characterization, and purification of two mammalian stress proteins present in mitochondria, grp 75, a member of the hsp 70 family and hsp 58, a homolog of the bacterial groEL protein;Mizzen;J Biol Chem,1989

5. Three faces of mortalin: a housekeeper, guardian and killer;Kaul;Exp Gerontol,2007

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