Hsp70 and Hsp90 of E. coli Directly Interact for Collaboration in Protein Remodeling.

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第一作者： Olivier,Genest

第一单位： Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.

作者： Olivier,Genest ^[1] ; Joel R,Hoskins ^[1] ; Andrea N,Kravats ^[1] ; Shannon M,Doyle ^[2] ; Sue,Wickner ^[3]

作者单位： Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA. ^[1] Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: doyles@mail.nih.gov. ^[2] Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: wickners@mail.nih.gov. ^[3]

关键词 CbpA DnaJ Hsp40 molecular chaperone protein remodeling

主题词氨基酸取代(Amino Acid Substitution);大肠杆菌(Escherichia coli);大肠杆菌蛋白质类(Escherichia coli Proteins);HSP70热休克蛋白质类(HSP70 Heat-Shock Proteins);HSP90热休克蛋白质类(HSP90 Heat-Shock Proteins);蛋白质结合(Protein Binding);蛋白质重折叠(Protein Refolding)

DOI 10.1016/j.jmb.2015.10.010

PMID 26482100

发布时间 2019-10-08

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