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A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates.

The Escherichia coli heat-shock protein DnaJ cooperates with the Hsp70 homolog DnaK in protein folding in vitro and in vivo. Little is known about the structural features of DnaJ that mediate its interaction with DnaK and unfolded polypeptide. DnaJ contains at least four blocks of sequence represent...

詳細記述

保存先:
書誌詳細
出版年:EMBO J
主要な著者: Szabo, A, Korszun, R, Hartl, F U, Flanagan, J
フォーマット: Artigo
言語:Inglês
出版事項: Nature Publishing Group 1996
主題:
オンライン・アクセス:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC449956/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8617216/
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