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ATP Binding and Hydrolysis by the Multifunctional Protein Disulfide Isomerase

Data up to Jan 2025

Published1996
Citations37
References27

Total Citations Per Year

Abstract

References (27)

Protein folding in the cell

1992 • 4,138 citations

Protein disulphide isomerase: building bridges in protein folding

1994 • 718 citations

Kinetics of Molecular Chaperone Action

1994 • 440 citations

Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer

1991 • 408 citations

The Role of ATP in the Functional Cycle of the DnaK Chaperone System

1995 • 388 citations

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

1993 • 366 citations

Protein disulfide isomerase. A multifunctional protein resident in the lumen of the endoplasmic reticulum.

1992 • 318 citations

Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum

1992 • 286 citations

A set of endoplasmic reticulum proteins possessing properties of molecular chaperones includes Ca(2+)-binding proteins and members of the thioredoxin superfamily.

1994 • 279 citations

Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds.

1994 • 268 citations

Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme.

1994 • 267 citations

The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity

1993 • 201 citations

Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli. This multifunctional polypeptide has two independently acting catalytic sites for the isomerase activity.

1992 • 144 citations

Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange

1992 • 132 citations

Translocation of ATP into the lumen of rough endoplasmic reticulum-derived vesicles and its binding to luminal proteins including BiP (GRP 78) and GRP 94.

1992 • 131 citations

Effects of the chaperonin GroE on the refolding of tryptophanase from Escherichia coli. Refolding is enhanced in the presence of ADP.

1992 • 115 citations

Heat shock in Escherichia coli alters the protein-binding properties of the chaperonin groEL by inducing its phosphorylation

1992 • 105 citations

Kinetics and specificity of homogeneous protein disulphide-isomerase in protein disulphide isomerization and in thiol-protein-disulphide oxidoreduction

1983 • 102 citations

Effect of protein and peptide inhibitors on the activity of protein disulfide-isomerase

1991 • 87 citations

Enzymatic Catalysis of Disulfide Formation

1994 • 77 citations

Folding in vitro of bovine pancreatic trypsin inhibitor in the presence of proteins of the endoplasmic reticulum

1992 • 65 citations

An ATP transporter is required for protein translocation into the yeast endoplasmic reticulum.

1993 • 65 citations

Role of accessory proteins in protein folding

1993 • 56 citations

A major phosphoprotein of the endoplasmic reticulum is protein disulfide isomerase.

1994 • 56 citations

Fluorescence detection of conformational changes in GroEL induced by thermal switching and nucleotide binding.

1994 • 26 citations

Association and dissociation of protein disulfide isomerase

1994 • 23 citations

A pleîotropic acid phosphatase-deficient mutant of Escherichia coli shows premature termination in the dsbA gene. Use of dsbA :: phoA furions to localize a structurally important domain in DsbA

1994 • 13 citations

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ATP Binding and Hydrolysis by the Multifunctional Protein Disulfide Isomerase (1996) – Journal of Biological Chemistry | Metascience Observatory Explorer