Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

0
3
0

Year Published

2019
2019
2022
2022

Publication Types

Select...
3

Relationship

0
3

Authors

Journals

citations
Cited by 3 publications
(3 citation statements)
references
References 7 publications
(9 reference statements)
0
3
0
Order By: Relevance
“…Several adverse conditions, such as hypodermic hypoxia, accumulation of reactive oxygen species, lack of ATP, nutrient deprivation, and mutations in specific proteins may lead to the accumulation of misfolded proteins in the ER. To keep the cell working normally and not harming other cells, the ER tends to stimulate an unfolded protein response (UPR) [3]. ER-triggered UPR affects the problem of misfolded and unfolded proteins, mainly through four mechanisms.…”
Section: Introductionmentioning
confidence: 99%
“…Several adverse conditions, such as hypodermic hypoxia, accumulation of reactive oxygen species, lack of ATP, nutrient deprivation, and mutations in specific proteins may lead to the accumulation of misfolded proteins in the ER. To keep the cell working normally and not harming other cells, the ER tends to stimulate an unfolded protein response (UPR) [3]. ER-triggered UPR affects the problem of misfolded and unfolded proteins, mainly through four mechanisms.…”
Section: Introductionmentioning
confidence: 99%
“…Endoplasmic reticulum is the most important organelle for protein synthesis and intracellular calcium storages, which is also involved in the regulation of multiple cellular signaling pathways (Tsai and Weissman, 2010;Schwarz and Blower, 2016). Upon the induction of intracellular and extracellular stress, the accumulation of unfolded or misfolded proteins can activate the unfolded protein response (UPR) to restore the homeostasis of ER (Namba, 2015). The PERK/ATF4/CHOP, IRE-1/XBP1, and ATF6 signaling pathways have an essential role in regulating ER stress-induced physiological responses in cells (Lee, 2005;Luo and Lee, 2013).…”
Section: Discussionmentioning
confidence: 99%
“…The UPR maintains and restores ER homeostasis by inducing ER chaperone proteins, thereby increasing the secretory function of the ER. 147 In the presence of excess unfolded proteins, Grp78, which acts as a molecular chaperone, is removed from its interaction with PERK, ATF6, and IRE-1. This allows ATF6, PERK and IRE-1 to dimerize and become active.…”
Section: Atf6mentioning
confidence: 99%