ER stress and diseases

@article{Yoshida2007ERSA,
  title={ER stress and diseases},
  author={Hiderou Yoshida},
  journal={The FEBS Journal},
  year={2007},
  volume={274}
}
  • H. Yoshida
  • Published 1 February 2007
  • Chemistry, Medicine
  • The FEBS Journal
Proteins synthesized in the endoplasmic reticulum (ER) are properly folded with the assistance of ER chaperones. Malfolded proteins are disposed of by ER‐associated protein degradation (ERAD). When the amount of unfolded protein exceeds the folding capacity of the ER, human cells activate a defense mechanism called the ER stress response, which induces expression of ER chaperones and ERAD components and transiently attenuates protein synthesis to decrease the burden on the ER. It has been… 
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References

SHOWING 1-10 OF 330 REFERENCES
ER stress and neurodegenerative diseases
TLDR
The possible role of ER stress in neurodegenerative diseases is discussed, and current knowledge in this field that may reveal novel insight into disease mechanisms and help to design better therapies for these disorders are highlighted.
Endoplasmic reticulum stress response and neurodegeneration.
TLDR
New observations suggesting that impairment of ER functioning may be a common denominator of pathological processes resulting in neuronal cell injury in acute disorders and degenerative diseases of the brain are summarized.
Roles of CHOP/GADD153 in endoplasmic reticulum stress
TLDR
The current understanding of the roles of C/EBP homologous protein (CHOP) and GADD153 in ER stress-mediated apoptosis and in diseases including diabetes, brain ischemia and neurodegenerative disease are summarized.
Survival and apoptosis signals in ER stress: the role of protein kinases
TLDR
Current knowledge about the protein kinases involved in ER stress, and their involvement in the pathogenesis of neurodegenerative disorders, is summarized.
Endoplasmic reticulum stress and diabetes mellitus.
TLDR
A comprehensive understanding of the impact of the ER stress pathway in beta-cells and how it relates to the development of diabetes may contribute to provide new targets for the prevention and treatment of this disease.
ER stress and the unfolded protein response.
TLDR
A model in which the activity of UPR signaling pathways reflects the biosynthetic activity of the ER is proposed, which shows that this information is integrated into control of cellular events, which were previously not considered to be under control of ER signaling pathways.
ER signaling in unfolded protein response.
TLDR
It is suggested that HRD1 and SEL1 are up-regulated by the UPR and contribute to protection against the ER stress-induced cell death by degrading unfolded proteins accumulated in the ER.
Endoplasmic reticulum stress and the development of diabetes: a review.
TLDR
The role of ER stress in the development of more common forms of the disease is considered and mutations associated with the Wolcott-Rallison syndrome of infantile diabetes and mutations that prevent the alpha-subunit of eIF2 from being phosphorylated by PERK are reviewed.
Endoplasmic Reticulum Stress Features Are Prominent in Alzheimer Disease but Not in Prion Diseases In Vivo
TLDR
It is demonstrated that neither in sporadic nor in infectiously acquired or inherited human prion diseases can the activated forms of PERK and eIF2&agr; be detected, except when concomitant neurofibrillary pathology is present; whereas the distribution of phosphorylated PERK correlates with abnormallyosphorylated tau in AD.
A Novel Stress-induced EDEM Variant Regulating Endoplasmic Reticulum-associated Glycoprotein Degradation*
TLDR
EDEM2, a novel, stress-regulated mannosidase-like protein that operates in the ER lumen is identified and characterized and it is shown that transcriptional up-regulation of EDEM2 depends on the ER stress-activated transcription factor Xbp1, that EDEM3 selectively accelerates ERAD of terminally misfolded glycoproteins by facilitating their extraction from the calnexin cycle.
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