ERp57 and PDI: multifunctional protein disulfide isomerases with similar domain architectures but differing substrate–partner associationsThis paper is one of a selection of papers published in this Special Issue, entitled CSBMCB — Membrane Proteins in Health and Disease.
Author:
Affiliation:
1. Biochemistry Department, McGill University, 3655 Promenade Sir William Osler, Montréal, QC H3G 1Y6, Canada.
Abstract
Publisher
Canadian Science Publishing
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
http://www.nrcresearchpress.com/doi/pdf/10.1139/o06-186
Reference42 articles.
1. pH Dependence of the Peptide Thiol-Disulfide Oxidase Activity of Six Members of the Human Protein Disulfide Isomerase Family
2. Functional Characterization of ERp18, a New Endoplasmic Reticulum-located Thioredoxin Superfamily Member
3. Docking to single-domain and multiple-domain proteins: Old and new challenges
4. Identification of the protein disulfide isomerase family member PDIp in experimental Parkinson's disease and Lewy body pathology
5. Multiple epiphyseal dysplasia mutations inMATN3 cause misfolding of the A-domain and prevent secretion of mutant matrilin-3
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