Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone.

No abstract is available for this paper.

• Publication year

  1998

• Venue

  Proceedings of the National Academy of Sciences of the United States of America

• Publication date

  1998-12-22

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1073/PNAS.95.26.15229PMID 9860951PMCID PMC28025
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• The Hsp70 and Hsp60 chaperone machines.

  1998cited by this paper
• Hsp70 chaperone systems: diversity of cellular functions and mechanism of action.

  1998cited by this paper
• Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ.

  1998cited by this paper
• Control of the DnaK Chaperone Cycle by Substoichiometric Concentrations of the Co-chaperones DnaJ and GrpE*

  1998cited by this paper
• Role of the J-domain in the cooperation of Hsp40 with Hsp70.

  1998cited by this paper
• Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK.

  1997cited by this paper
• Interaction of Hsp70 chaperones with substrates

  1997cited by this paper
• Regulatory region C of the E. coli heat shock transcription factor, sigma32, constitutes a DnaK binding site and is conserved among eubacteria.

  1996cited by this paper
• Molecular chaperones in cellular protein folding

  1996cited by this paper
• The second step of ATP binding to DnaK induces peptide release.

  1996cited by this paper
• A Bipartite Signaling Mechanism Involved in DnaJ-mediated Activation of the Escherichia coli DnaK Protein (*)

  1996cited by this paper
• Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK

  1996cited by this paper
• Divergent Effects of ATP on the Binding of the DnaK and DnaJ Chaperones to Each Other, or to Their Various Native and Denatured Protein Substrates (*)

  1995cited by this paper
• The Dissociation of ATP from hsp70 of Saccharomyces cerevisiae Is Stimulated by Both Ydj1p and Peptide Substrates (*)

  1995cited by this paper
• The role of ATP in the functional cycle of the DnaK chaperone system.

  1995cited by this paper
• Nucleotide-induced Conformational Changes in the ATPase and Substrate Binding Domains of the DnaK Chaperone Provide Evidence for Interdomain Communication (*)

  1995cited by this paper
• The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE.

  1994cited by this paper
• Kinetics of molecular chaperone action.

  1994cited by this paper
• A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE

  1994cited by this paper
• DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat‐induced protein damage.

  1993cited by this paper
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  1993cited by this paper
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  1993cited by this paper
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  1993cited by this paper
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  1991cited by this paper
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  1990cited by this paper
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  1990cited by this paper
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