Modulation of an Active-Site Cysteine pKa Allows PDI to Act as a Catalyst of both Disulfide Bond Formation and Isomerization-Reference-Cited by-同舟云学术

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Modulation of an Active-Site Cysteine pKa Allows PDI to Act as a Catalyst of both Disulfide Bond Formation and Isomerization

Published:2010-03 Issue:4 Volume:396 Page:883-892
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Karala Anna-Riikka,Lappi Anna-Kaisa,Ruddock Lloyd W.

Funder

Academy of Finland

Biocenter Oulu

University of Oulu

Oulu University Scholarship Foundation

Finnish Concordia Fund

Gustaf Komppa Foundation

Finnish Cultural Foundation,

Emil Aaltonen Foundation

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference25 articles.

1. Disulfide formation in the ER and mitochondria: two solutions to a common process;Riemer;Science,2009

2. Disulfide-linked protein folding pathways;Mamathambika;Annu. Rev. Cell Dev. Biol.,2008

3. Conservation and diversity of the cellular disulfide bond formation pathways;Sevier;Antioxid. Redox Signal.,2006

4. Oxidative protein folding in eukaryotes: mechanisms and consequences;Tu;J. Cell Biol.,2004

5. Protein disulphide isomerase: a critical evaluation of its function in disulphide bond formation;Hatahet;Antioxid. Redox Signal.,2009

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