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Published in 2018 at "Current opinion in cell biology"
DOI: 10.1016/j.ceb.2018.04.004
Abstract: Misfolded proteins of the endoplasmic reticulum (ER) are discarded by a conserved process, called ER-associated protein degradation (ERAD). ERAD substrates are retro-translocated into the cytosol, polyubiquitinated, extracted from the ER membrane, and ultimately degraded by…
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Keywords:
associated protein;
insights associated;
erad;
protein degradation ... See more keywords
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Published in 2020 at "Fungal biology"
DOI: 10.1016/j.funbio.2020.06.004
Abstract: Aspergillus oryzae can secrete large amounts of enzymes. However, the production of abundant secretory proteins triggers the unfolded protein response (UPR) in the endoplasmic reticulum (ER), and it is not clear how ER-associated protein degradation…
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Keywords:
atpase cdc48;
aaa atpase;
aspergillus oryzae;
erad ... See more keywords
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Published in 2018 at "Trends in biochemical sciences"
DOI: 10.1016/j.tibs.2018.06.005
Abstract: Endoplasmic reticulum (ER)-associated degradation (ERAD) and the unfolded protein response (UPR) are two key quality-control machineries in the cell. ERAD is responsible for the clearance of misfolded proteins in the ER for cytosolic proteasomal degradation,…
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Keywords:
quality control;
crosstalk;
endoplasmic reticulum;
erad ... See more keywords
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Published in 2020 at "Environmental microbiology"
DOI: 10.1111/1462-2920.15069
Abstract: Most secretory proteins are folded and modified in the endoplasmic reticulum (ER), but protein folding is error-prone, resulting in toxic protein aggregation and cause ER stress. Irreversibly misfolded proteins are subjected to ER-associated degradation (ERAD),…
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Keywords:
protein;
mohrd1 moder1;
degradation;
erad ... See more keywords
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Published in 2022 at "Science Advances"
DOI: 10.1126/sciadv.abl4222
Abstract: Chondrocytes secrete massive extracellular matrix (ECM) molecules that are produced, folded, and modified in the endoplasmic reticulum (ER). Thus, the ER-associated degradation (ERAD) complex—which removes misfolded and unfolded proteins to maintain proteostasis in the ER—…
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Keywords:
associated degradation;
maintenance;
cartilage;
erad ... See more keywords
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Published in 2020 at "Science"
DOI: 10.1126/science.aay2494
Abstract: 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…
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Keywords:
degradation;
endoplasmic reticulum;
erad;
brown adipocytes ... See more keywords
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Published in 2022 at "Circulation"
DOI: 10.1161/circulationaha.122.061557
Abstract: Background: Cardiac hypertrophy increases demands on protein folding, which causes an accumulation of misfolded proteins in the endoplasmic reticulum (ER). These misfolded proteins can be removed by the adaptive retrotranslocation, polyubiquitylation, and a proteasome-mediated degradation…
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Keywords:
transverse aortic;
cardiac hypertrophy;
erad;
heart ... See more keywords
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Published in 2022 at "International Journal of Molecular Sciences"
DOI: 10.3390/ijms23105811
Abstract: Redundancy and lethality is a long-standing problem in genetics but generating minimal and lethal phenotypes in the knockouts of the same gene by different approaches drives this problem to a new high. In Asn (N)-linked…
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Keywords:
endoplasmic reticulum;
reticulum associated;
erad;
alg12 ebs4 ... See more keywords