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Updated: May 15, 2026

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication
Published on: June 14, 2024
An involvement of oxidative stress in endoplasmic reticulum stress and its associated diseases
Bidur Bhandary1, Anu Marahatta, Hyung-Ryong Kim
1Department of Pharmacology, School of Medicine, Chonbuk National Univeristy, Jeonju 561-180, South Korea. hrkim@wonkwang.ac.kr.
Abstract:
The endoplasmic reticulum (ER) is the major site of calcium storage and protein folding. It has a unique oxidizing-folding environment due to the predominant disulfide bond formation during the process of protein folding. Alterations in the oxidative environment of the ER and also intra-ER Ca2+ cause the production of ER stress-induced reactive oxygen species (ROS). Protein disulfide isomerases, endoplasmic reticulum oxidoreductin-1, reduced glutathione and mitochondrial electron transport chain proteins also play crucial roles in ER stress-induced production of ROS. In this article, we discuss ER stress-associated ROS and related diseases, and the current understanding of the signaling transduction involved in ER stress.
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