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August 1, 1996Journal of Biological ChemistryOpen Access

Regulation of the Heat-shock Protein 70 Reaction Cycle by the Mammalian DnaJ Homolog, Hsp40

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Authors

YMYasufumi MinamiMaebashi Institute of TechnologyJHJörg HöhfeldUniversity of BonnKOKenzo OhtsukaChubu University

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Cite This Study

Minami et al. (1996) studied this question.

synapsesocial.com/papers/6a707da226770c2b8de090edhttps://doi.org/10.1074/jbc.271.32.19617
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1The Conserved G/F Motif of the DnaJ Chaperone Is Necessary for the Activation of the Substrate Binding Properties of the DnaK Chaperone1995 · 129 citations
  2. 2Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. The effect of lauryl maltoside.1986 · 129 citations
  3. 3MOLECULAR CHAPERONE FUNCTIONS OF HEAT-SHOCK PROTEINS1993 · 1,601 citations
  4. 4Effect of Nucleotide on the Binding of Peptides to 70-kDa Heat Shock Protein1995 · 89 citations
  5. 5Regulation of 70‐kDa Heat‐Shock‐Protein ATPase Activity and Substrate Binding by Human DnaJ‐Like Proteins, HSJ1a and HSJ1b1994 · 75 citations