Protein disulfide isomerase - PubMed (original) (raw)
Review
Protein disulfide isomerase
Bonney Wilkinson et al. Biochim Biophys Acta. 2004.
Abstract
During the maturation of extracellular proteins, disulfide bonds that chemically cross-link specific cysteines are often added to stabilize a protein or to join it covalently to other proteins. Disulfide formation, which requires a change in the covalent structure of the protein, occurs as the protein folds into its three-dimensional structure. In the eukaryotic endoplasmic reticulum and in the bacterial periplasm, an elaborate system of chaperones and folding catalysts ensure that disulfides connect the proper cysteines and that the folding protein does not make improper interactions. This review focuses specifically on one of these folding assistants, protein disulfide isomerase (PDI), an enzyme that catalyzes disulfide formation and isomerization and a chaperone that inhibits aggregation.
Similar articles
- Sulfhydryl oxidation, not disulfide isomerization, is the principal function of protein disulfide isomerase in yeast Saccharomyces cerevisiae.
Solovyov A, Xiao R, Gilbert HF. Solovyov A, et al. J Biol Chem. 2004 Aug 13;279(33):34095-100. doi: 10.1074/jbc.M405640200. Epub 2004 Jun 2. J Biol Chem. 2004. PMID: 15175335 - Catalysis of protein folding by protein disulfide isomerase and small-molecule mimics.
Kersteen EA, Raines RT. Kersteen EA, et al. Antioxid Redox Signal. 2003 Aug;5(4):413-24. doi: 10.1089/152308603768295159. Antioxid Redox Signal. 2003. PMID: 13678529 Free PMC article. Review. - Catalysis of protein disulfide bond isomerization in a homogeneous substrate.
Kersteen EA, Barrows SR, Raines RT. Kersteen EA, et al. Biochemistry. 2005 Sep 13;44(36):12168-78. doi: 10.1021/bi0507985. Biochemistry. 2005. PMID: 16142915 Free PMC article. - Enzymatic catalysis of disulfide formation.
Noiva R. Noiva R. Protein Expr Purif. 1994 Feb;5(1):1-13. doi: 10.1006/prep.1994.1001. Protein Expr Purif. 1994. PMID: 7909462 Review. - Chemical stress on protein disulfide isomerases and inhibition of their functions.
Imaoka S. Imaoka S. Int Rev Cell Mol Biol. 2011;290:121-66. doi: 10.1016/B978-0-12-386037-8.00003-X. Int Rev Cell Mol Biol. 2011. PMID: 21875564 Review.
Cited by
- Analysis of Punicalin and Punicalagin Interaction with PDIA3 and PDIA1.
Meschiari G, Minacori M, Fiorini S, Tedesco M, Eufemi M, Altieri F. Meschiari G, et al. Int J Mol Sci. 2024 Sep 30;25(19):10531. doi: 10.3390/ijms251910531. Int J Mol Sci. 2024. PMID: 39408858 Free PMC article. - Identification of the effects of hypoxia on the liver tissues of Nile tilapia Oreochromis Niloticus.
Li D, Yu J, Zhu J, Xiao W, Zou Z, Chen B, Wei C, Zhu J, Yang H. Li D, et al. BMC Genomics. 2024 Oct 8;25(1):946. doi: 10.1186/s12864-024-10700-9. BMC Genomics. 2024. PMID: 39379813 Free PMC article. - Post-Translational Modifications to Cysteine Residues in Plant Proteins and Their Impact on the Regulation of Metabolism and Signal Transduction.
Boutin C, Clément C, Rivoal J. Boutin C, et al. Int J Mol Sci. 2024 Sep 12;25(18):9845. doi: 10.3390/ijms25189845. Int J Mol Sci. 2024. PMID: 39337338 Free PMC article. Review. - Protein disulfide isomerase plays a crucial role in mediating chemically-induced, glutathione depletion-associated hepatocyte injury in vitro and in vivo.
Zhu YY, Zhang Q, Jia YC, Hou MJ, Zhu BT. Zhu YY, et al. Cell Commun Signal. 2024 Sep 6;22(1):431. doi: 10.1186/s12964-024-01798-1. Cell Commun Signal. 2024. PMID: 39243059 Free PMC article. - Protein disulfide isomerase-9 interacts with the lumenal region of the transmembrane endoplasmic reticulum stress sensor kinase, IRE1, to modulate the unfolded protein response in Arabidopsis.
Carrillo R, Iwai K, Albertson A, Dang G, Christopher DA. Carrillo R, et al. Front Plant Sci. 2024 May 16;15:1389658. doi: 10.3389/fpls.2024.1389658. eCollection 2024. Front Plant Sci. 2024. PMID: 38817940 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases