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The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins

Data up to Jan 2025

Published1998
Citations332
References31

Total Citations Per Year

Abstract

References (31)

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1994 • 718 citations

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The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency

1998 • 170 citations

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1996 • 148 citations

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1995 • 142 citations

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1966 • 139 citations

Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites.

1993 • 129 citations

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1995 • 128 citations

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1987 • 113 citations

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1991 • 87 citations

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1997 • 86 citations

Dissecting the Mechanism of Protein Disulfide Isomerase: Catalysis of Disulfide Bond Formation in a Model Peptide

1994 • 83 citations

The uncharged surface features surrounding the active site ofEscherichia coliDsbA are conserved and are implicated in peptide binding

1997 • 79 citations

Peptide binding by protein disulfide isomerase, a resident protein of the endoplasmic reticulum lumen.

1991 • 78 citations

A microsomal protein is involved in ATP-dependent transport of presecretory proteins into mammalian microsomes.

1991 • 77 citations

The unique hetero-oligomeric nature of the subunits in the catalytic cooperativity of the yeast Cct chaperonin complex

1997 • 75 citations

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1996 • 65 citations

Protein Disulphide Isomerase and a Lumenal Cyclophilin‐Type Peptidyl Prolyl Cis‐Trans Isomerase are in Transient Contact with Secretory Proteins During Late Stages of Translocation

1995 • 62 citations

Spinach Chloroplast cpn21 Co-chaperonin Possesses Two Functional Domains Fused Together in a Toroidal Structure and Exhibits Nucleotide-dependent Binding to Plastid Chaperonin 60

1995 • 62 citations

[38] Protein disulfide-isomerase

1995 • 52 citations

Nuclear magnetic resonance characterization of the N‐terminal thioredoxin‐like domain of protein disulfide isomerase

1995 • 45 citations

The membrane proteins TRAMp and sec61αp may be involved in post‐translational transport of presecretory proteins into mammalian microsomes

1994 • 22 citations

Protein Disulphide Isomerase and a Lumenal Cyclophilin-Type Peptidyl Prolyl Cis-Trans Isomerase are in Transient Contact with Secretory Proteins During Late Stages of Translocation

1995 • 8 citations

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The b' domain provides the principal peptide-binding site of protein disulfide isomerase… (1998) – The EMBO Journal | Metascience Observatory Explorer