The endoplasmic reticulum and the unfolded protein response.

By J. Malhotra, R. Kaufman. Seminars in Cell and Developmental Biology, 2007

1,056 citations recorded by the source corpus.

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

Role of Oxidative Stress in Pathophysiology of Nonalcoholic Fatty Liver Disease (2018, background): “ER is involved in folding and assembling proteins to attain their final appropriate conformation, but under stress conditions, such as lipid overload, the unfolded and misfolded proteins accumulate in the ER lumen, activating a specific signaling pathway called the unfolded protein response (UPR), i”
Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities (2008, background): “Multiple disturbances can cause accumulation of unfolded proteins in the ER, triggering an evolutionarily conserved response termed the unfolded protein response (UPR”
PERK is required at the ER-mitochondrial contact sites to convey apoptosis after ROS-based ER stress (2012, background): “Alterations in the ER folding environment cause the accumulation of misfolded proteins in the ER lumen, leading to ER stress.(1)”
Calcium and ROS: A mutual interplay (2015, background): “ERO1α then uses a flavindependent reaction to transfer electrons from PDI to molecular oxygen, thereby oxidizing PDI.”