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Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates

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第一作者： Mattoo,R.U.H.

作者： Mattoo,R.U.H. ^[1] ; Sharma,S.K. ; Priya,S. ; Finka,A. ; Goloubinoff,P.

作者单位： Department of Plant Molecular Biology, Faculty of Biology and Medicine, University of Lausanne ^[1]

发布时间 2014-01-21

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The Journal of biological chemistry

2013年288卷29期

21399-21411页

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The Journal of biological chemistry

2013年288卷29期

21399-21411页

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Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates

The Journal of biological chemistry

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Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates

The Journal of biological chemistry

相似文献

同项目论文

The Journal of biological chemistry

相关期刊

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