A Novel Reaction of Peroxiredoxin 4 towards Substrates in Oxidative Protein Folding

Glutathione Peroxidase 7 Utilizes Hydrogen Peroxide Generated by Ero1α to Promote Oxidative Protein Folding

(2013) Lei Wang et al.   ANTIOXIDANTS & REDOX SIGNALING

Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding

(2013) Yoshimi Sato et al.   Scientific Reports

Vitamin K epoxide reductase contributes to protein disulfide formation and redox homeostasis within the endoplasmic reticulum

(2012) Lori A. Rutkevich et al.   MOLECULAR BIOLOGY OF THE CELL

Endoplasmic Reticulum Thiol Oxidase Deficiency Leads to Ascorbic Acid Depletion and Noncanonical Scurvy in Mice

(2012) Ester Zito et al.   MOLECULAR CELL

Overexpression of the rhodanese PspE, a single cysteine-containing protein, restores disulphide bond formation to anEscherichia colistrain lacking DsbA

(2012) Shu-Sin Chng et al.   MOLECULAR MICROBIOLOGY

Peroxides and Peroxidases in the Endoplasmic Reticulum: Integrating Redox Homeostasis and Oxidative Folding

(2011) Taichi Kakihana et al.   ANTIOXIDANTS & REDOX SIGNALING

Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4

(2011) Xi Wang et al.   BIOCHEMICAL JOURNAL

Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking

(2011) Todd J Cohen et al.   EMBO JOURNAL

Human Protein-disulfide Isomerase Is a Redox-regulated Chaperone Activated by Oxidation of Domain a′

(2011) Chao Wang et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Two Endoplasmic Reticulum PDI Peroxidases Increase the Efficiency of the Use of Peroxide during Disulfide Bond Formation

(2011) Van Dat Nguyen et al.   JOURNAL OF MOLECULAR BIOLOGY

Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum

(2010) Timothy J Tavender et al.   EMBO JOURNAL

Disulphide production by Ero1α–PDI relay is rapid and effectively regulated

(2010) Christian Appenzeller-Herzog et al.   EMBO JOURNAL

Peroxiredoxin IV protects cells from oxidative stress by removing H2O2 produced during disulphide formation

(2010) T. J. Tavender et al.   JOURNAL OF CELL SCIENCE

Oxidative Protein Folding by an Endoplasmic Reticulum-Localized Peroxiredoxin

(2010) Ester Zito et al.   MOLECULAR CELL

Typical 2-Cys peroxiredoxins - structures, mechanisms and functions

(2009) Andrea Hall et al.   FEBS Journal

Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS

(2009) C. M. Karch et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells

(2008) Timothy J. Tavender et al.   BIOCHEMICAL JOURNAL

Reconstitution of Human Ero1-Lα/Protein-Disulfide Isomerase Oxidative Folding Pathwayin Vitro

(2008) Lei Wang et al.   JOURNAL OF BIOLOGICAL CHEMISTRY