Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation

F Hatahet, LW Ruddock - Antioxidants & redox signaling, 2009 - liebertpub.com
Disulfide bond formation is probably involved in the biogenesis of approximately one third of
human proteins. A central player in this essential process is protein disulfide isomerase or …

[HTML][HTML] Ero1 and redox homeostasis in the endoplasmic reticulum

CS Sevier, CA Kaiser - Biochimica et Biophysica Acta (BBA)-Molecular Cell …, 2008 - Elsevier
Living cells must be able to respond to physiological and environmental fluctuations that
threaten cell function and viability. A cellular event prone to disruption by a wide variety of …

A guide to assessing endoplasmic reticulum homeostasis and stress in mammalian systems

D Sicari, A Delaunay‐Moisan, L Combettes… - The FEBS …, 2020 - Wiley Online Library
The endoplasmic reticulum (ER) is a multifunctional organelle that constitutes the entry into
the secretory pathway. The ER contributes to the maintenance of cellular calcium …

Ero1α Regulates Ca2+ Fluxes at the Endoplasmic Reticulum–Mitochondria Interface (MAM)

T Anelli, L Bergamelli, E Margittai… - Antioxidants & redox …, 2012 - liebertpub.com
Aims: The endoplasmic reticulum (ER) is involved in many functions, including protein
folding, redox homeostasis, and Ca2+ storage and signaling. To perform these multiple …

PDI-regulated disulfide bond formation in protein folding and biomolecular assembly

J Fu, J Gao, Z Liang, D Yang - Molecules, 2020 - mdpi.com
Disulfide bonds play a pivotal role in maintaining the natural structures of proteins to ensure
their performance of normal biological functions. Moreover, biological molecular assembly …

Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1

CS Sevier, H Qu, N Heldman, E Gross, D Fass… - Cell, 2007 - cell.com
Introduction of disulfide bonds into proteins entering the secretory pathway is catalyzed by
Ero1p, which generates disulfide bonds de novo, and Pdi1p, which transfers disulfides to …

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

C Appenzeller‐Herzog, J Riemer, B Christensen… - The EMBO …, 2008 - embopress.org
Oxidative maturation of secretory and membrane proteins in the endoplasmic reticulum (ER)
is powered by Ero1 oxidases. To prevent cellular hyperoxidation, Ero1 activity can be …

Glutathione peroxidase 7 utilizes hydrogen peroxide generated by Ero1α to promote oxidative protein folding

L Wang, L Zhang, Y Niu, R Sitia… - Antioxidants & redox …, 2014 - liebertpub.com
Aims: Ero1 flavoproteins catalyze oxidative folding in the endoplasmic reticulum (ER),
consuming oxygen and generating hydrogen peroxide (H2O2). The ER-localized …

FAT-switch-based quantitative S-nitrosoproteomics reveals a key role of GSNOR1 in regulating ER functions

G Qin, M Qu, B Jia, W Wang, Z Luo, CP Song… - Nature …, 2023 - nature.com
Reversible protein S-nitrosylation regulates a wide range of biological functions and
physiological activities in plants. However, it is challenging to quantitively determine the S …

Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI

K Inaba, S Masui, H Iida, S Vavassori, R Sitia… - The EMBO …, 2010 - embopress.org
In the endoplasmic reticulum (ER) of eukaryotic cells, Ero1 flavoenzymes promote oxidative
protein folding through protein disulphide isomerase (PDI), generating reactive oxygen …