Results 11 to 20 of about 232,488 (209)

Cyclosporine A-sensitive, cyclophilin B-dependent endoplasmic reticulum-associated degradation. [PDF]

open access: yesPLoS ONE, 2010
Peptidyl-prolyl cis/trans isomerases (PPIs) catalyze cis/trans isomerization of peptide bonds preceding proline residues. The involvement of PPI family members in protein refolding has been established in test tube experiments.
Riccardo Bernasconi   +5 more
doaj   +6 more sources

Ubiquitin-specific protease 25 functions in Endoplasmic Reticulum-associated degradation. [PDF]

open access: yesPLoS ONE, 2012
Endoplasmic Reticulum (ER)-associated degradation (ERAD) discards abnormal proteins synthesized in the ER. Through coordinated actions of ERAD components, misfolded/anomalous proteins are recognized, ubiquitinated, extracted from the ER and ultimately ...
Jessica R Blount   +4 more
doaj   +5 more sources

AUP1 Regulates the Endoplasmic Reticulum-Associated Degradation and Polyubiquitination of NKCC2 [PDF]

open access: yesCells
Inactivating mutations of kidney Na-K-2Cl cotransporter NKCC2 lead to antenatal Bartter syndrome (BS) type 1, a life-threatening salt-losing tubulopathy.
Nadia Frachon   +5 more
doaj   +2 more sources

Endoplasmic reticulum-associated degradation regulates mitochondrial dynamics in brown adipocytes. [PDF]

open access: yesScience, 2020
Organelle cross-talk Endoplasmic reticulum (ER)–associated degradation (ERAD) is a quality control mechanism that allows for targeted degradation of proteins in the ER. Zhou et al. found that a particular protein complex in ERAD, Sel1L-Hrd1, regulates the dynamics of another organelle, the mitochondrion ...
Zhou Z   +19 more
europepmc   +7 more sources

Chaperoning Endoplasmic Reticulum-Associated Degradation (ERAD) and Protein Conformational Diseases. [PDF]

open access: yesCold Spring Harb Perspect Biol, 2019
Misfolded proteins compromise cellular homeostasis. This is especially problematic in the endoplasmic reticulum (ER), which is a high-capacity protein-folding compartment and whose function requires stringent protein quality-control systems. Multiprotein complexes in the ER are able to identify, remove, ubiquitinate, and deliver misfolded proteins to ...
Needham PG, Guerriero CJ, Brodsky JL.
europepmc   +4 more sources

Gallic Acid Prevents the Oxidative and Endoplasmic Reticulum Stresses in the Hippocampus of Adult-Onset Hypothyroid Rats

open access: yesFrontiers in Pharmacology, 2021
Thyroid hormone is essential for hippocampal redox environment and neuronal viability in adulthood, where its deficiency causes hypothyroidism related to oxidative and endoplasmic reticulum stresses in the hippocampus, resulting in neuronal death.
Vanessa Blas-Valdivia   +5 more
doaj   +1 more source

Insights into endoplasmic reticulum‐associated degradation in plants [PDF]

open access: yesNew Phytologist, 2020
SummarySecretory and transmembrane protein synthesis and initial modification are essential processes in protein maturation, and these processes are important for maintaining protein homeostasis in the endoplasmic reticulum (ER). ER homeostasis can be disrupted by the accumulation of misfolded proteins, resulting in ER stress, due to specific intra‐ or
Qian Chen, Feifei Yu, Qi Xie
openaire   +2 more sources

Cytosolic chaperones influence the fate of a toxin dislocated from the endoplasmic reticulum [PDF]

open access: yes, 2008
The plant cytotoxin ricin enters target mammalian cells by receptor-mediated endocytosis and undergoes retrograde transport to the endoplasmic reticulum (ER).
R. A. Spooner   +32 more
core   +4 more sources

EFFECT OF EDEM1 OVEREXPRESSION ON THE GENERATION AND ASSEMBLY OF MAJOR HISTOCOMPATIBILITY COMPLEXES [PDF]

open access: yesRomanian Journal of Rheumatology, 2016
Background. A better understanding of the role of endoplasmic reticulum degradation-enhancing alpha-mannosidase – like protein 1 (EDEM1) in endoplasmic reticulum associated degradation (ERAD) may open new therapeutic approaches in autoimmune diseases ...
Alexandra Circiumaru   +4 more
doaj   +1 more source

The Crucial Role of Demannosylating Asparagine-Linked Glycans in ERADicating Misfolded Glycoproteins in the Endoplasmic Reticulum

open access: yesFrontiers in Plant Science, 2021
Most membrane and secreted proteins are glycosylated on certain asparagine (N) residues in the endoplasmic reticulum (ER), which is crucial for their correct folding and function.
Jianjun Zhang   +8 more
doaj   +1 more source

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