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The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone.

Data up to Jan 2025

Published1995
Citations247
References52

Total Citations Per Year

Abstract

References (52)

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1993 • 2,177 citations

MOLECULAR CHAPERONE FUNCTIONS OF HEAT-SHOCK PROTEINS

1993 • 1,591 citations

Speculations on the functions of the major heat shock and glucose-regulated proteins

1986 • 1,574 citations

Role of the Major Heat Shock Proteins as Molecular Chaperones

1993 • 1,096 citations

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1992 • 965 citations

Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK.

1991 • 835 citations

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

1993 • 593 citations

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1993 • 476 citations

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1993 • 473 citations

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1992 • 458 citations

Kinetics of Molecular Chaperone Action

1994 • 440 citations

The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner

1990 • 407 citations

Proteases and protein degradation inEscherichia coli

1992 • 387 citations

ATP-induced protein Hsp70 complex dissociation requires K+ but not ATP hydrolysis

1993 • 366 citations

Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock transcription factor σ32

1992 • 314 citations

Initiation of lambda DNA replication with purified host- and bacteriophage-encoded proteins: the role of the dnaK, dnaJ and grpE heat shock proteins.

1989 • 294 citations

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1990 • 275 citations

Hspl04 is a highly conserved protein with two essential nucleotide-binding sites

1991 • 268 citations

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1988 • 256 citations

The emergence of the chaperone machines

1992 • 249 citations

Isolation and characterization of ClpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli.

1993 • 247 citations

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

1991 • 245 citations

The Clp proteins: proteolysis regulators or molecular chaperones?

1992 • 216 citations

Function of DnaJ and DnaK as chaperones in origin-specific DNA binding by RepA

1991 • 204 citations

DnaA protein directs the binding of DnaB protein in initiation of DNA replication in Escherichia coli.

1994 • 204 citations

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

1992 • 199 citations

Role of the Escherichia coli DnaK and DnaJ heat shock proteins in the initiation of bacteriophage lambda DNA replication.

1988 • 194 citations

Sequence-specific DNA binding of the proto-oncoprotein ets-1 defines a transcriptional activator sequence within the long terminal repeat of the Moloney murine sarcoma virus.

1990 • 192 citations

Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes.

1994 • 181 citations

The heat-shock protein ClpB in Escherichia coli is a protein-activated ATPase.

1992 • 180 citations

Purification and properties of the dnaJ replication protein of Escherichia coli.

1985 • 178 citations

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

1992 • 178 citations

Processive degradation of proteins by the ATP-dependent Clp protease from Escherichia coli. Requirement for the multiple array of active sites in ClpP but not ATP hydrolysis.

1994 • 175 citations

Protease Ti, a new ATP-dependent protease in Escherichia coli, contains protein-activated ATPase and proteolytic functions in distinct subunits.

1988 • 172 citations

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1994 • 162 citations

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1987 • 160 citations

MecB of Bacillus subtilis, a member of the ClpC ATPase family, is a pleiotropic regulator controlling competence gene expression and growth at high temperature.

1994 • 154 citations

Purification and properties of the Escherichia coli dnaK replication protein.

1984 • 144 citations

Both the Escherichia coli chaperone systems, GroEL/GroES and DnaK/DnaJ/GrpE, can reactivate heat-treated RNA polymerase. Different mechanisms for the same activity.

1993 • 132 citations

A new component of bacteriophage Mu replicative transposition machinery: the Escherichia coli ClpX protein

1994 • 132 citations

Protease Ti from Escherichia coli Requires ATP Hydrolysis for Protein Breakdown but Not for Hydrolysis of Small Peptides

1989 • 126 citations

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1993 • 124 citations

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1985 • 122 citations

Aggregated dnaA protein is dissociated and activated for DNA replication by phospholipase or dnaK protein.

1990 • 119 citations

Purified bacteriophage λ O protein binds to four repeating sequences at the λ replication origin

1981 • 119 citations

The ClpP component of Clp protease is the sigma 32-dependent heat shock protein F21.5

1990 • 117 citations

Autoregulation of the Escherichia coli heat shock response by the DnaK and DnaJ heat shock proteins.

1993 • 116 citations

Reconstitution of a nine-protein system that initiates bacteriophage λ DNA replication

1989 • 98 citations

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1983 • 93 citations

Regulation of competence-specific gene expression by Mec-mediated protein-protein interaction in Bacillus subtilis.

1994 • 78 citations

Physical interactions between bacteriophage and Escherichia coli proteins required for initiation of lambda DNA replication.

1990 • 75 citations

Formation in vitro of complexes between an abnormal fusion protein and the heat shock proteins from Escherichia coli and yeast mitochondria

1991 • 34 citations

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The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity… (1995) – The EMBO Journal | Metascience Observatory Explorer