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DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.

Data up to Jan 2025

Published1993
Citations593
References50
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Total Citations Per Year

Abstract

References (50)

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Chaperonin-facilitated refolding of ribulose bisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are potassium dependent

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Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism

1989 • 234 citations

DnaK as a thermometer: threonine-199 is site of autophosphorylation and is critical for ATPase activity.

1991 • 218 citations

Escherichia coli heat shock gene mutants are defective in proteolysis.

1988 • 205 citations

Involvement of the chaperonin dnaK in the rapid degradation of a mutant protein in Escherichia coli.

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The DnaK chaperone modulates the heat shock response of Escherichia coli by binding to the sigma 32 transcription factor.

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Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone.

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The heat-shock-regulated grpE gene of Escherichia coli is required for bacterial growth at all temperatures but is dispensable in certain mutant backgrounds

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Purification 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 • 28 citations

Antibody to sigma 32 cross-reacts with DnaK: association of DnaK protein with Escherichia coli RNA polymerase.

1988 • 23 citations

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DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced… (1993) – The EMBO Journal | Metascience Observatory Explorer