The Reduction Potential of the Active Site Disulfides of Human Protein Disulfide Isomerase Limits Oxidation of the Enzyme by Ero1α

Oxidative Activity of Yeast Ero1p on Protein Disulfide Isomerase and Related Oxidoreductases of the Endoplasmic Reticulum

(2010) Elvira Vitu et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins

(2009) C. E. Jessop et al.   JOURNAL OF CELL SCIENCE

A novel disulphide switch mechanism in Ero1α balances ER oxidation in human cells

(2008) Christian Appenzeller-Herzog et al.   EMBO JOURNAL

Low reduction potential of Ero1α regulatory disulphides ensures tight control of substrate oxidation

(2008) Karl M Baker et al.   EMBO JOURNAL

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

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

Ero1L, a thiol oxidase, is required for Notch signaling through cysteine bridge formation of the Lin12-Notch repeats inDrosophila melanogaster

(2008) An-Chi Tien et al.   JOURNAL OF CELL BIOLOGY

Alternative Conformations of the x Region of Human Protein Disulphide-Isomerase Modulate Exposure of the Substrate Binding b’ Domain

(2008) Van Dat Nguyen et al.   JOURNAL OF MOLECULAR BIOLOGY

In Vivo Reduction-Oxidation State of Protein Disulfide Isomerase: The Two Active Sites Independently Occur in the Reduced and Oxidized Forms

(2007) Christian Appenzeller-Herzog et al.   ANTIOXIDANTS & REDOX SIGNALING

Ero1 and redox homeostasis in the endoplasmic reticulum

(2007) Carolyn S. Sevier et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH