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August 1, 1991Journal of Biological ChemistryOpen Access

The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein

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Authors

KLKrzysztof LiberekUniversity of GdańskDSDorota SkowyraNational Institutes of HealthMŻMaciej ŻyliczFoundation for Polish Science

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Cite This Study

Liberek et al. (1991) studied this question.

synapsesocial.com/papers/6a75ea04fbccc8f4fd162bd8https://doi.org/10.1016/s0021-9258(18)98713-2
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Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Heat Shock Protein-mediated Disassembly of Nucleoprotein Structures Is Required for the Initiation of Bacteriophage λ DNA Replication1989 · 164 citations
  2. 2A prepriming DNA replication enzyme of Escherichia coli. II. Actions of protein n': a sequence-specific, DNA-dependent ATPase.1980 · 114 citations
  3. 3Structural and functional studies of the dnaB protein using limited proteolysis. Characterization of domains for DNA-dependent ATP hydrolysis and for protein association in the primosome.1984 · 105 citations
  4. 4Purification of complexes of nuclear oncogene p53 with rat and Escherichia coli heat shock proteins: in vitro dissociation of hsc70 and dnaK from murine p53 by ATP.1988 · 105 citations