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Endoplasmic Reticulum-Associated Degradation

Known as: Pathway, ERAD, Reticulum-Associated Degradation, Endoplasmic, Degradation, Endoplasmic Reticulum-Associated 
The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with… 
National Institutes of Health

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Endoplasmic Reticulum StressProteolysisUbiquitinationaspects of radiation effects

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Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2018
2018
HRD1-mediated PTEN degradation promotes cell proliferation and hepatocellular carcinoma progression.
Review
2017
Review
2017
The evolving role of ubiquitin modification in endoplasmic reticulum-associated degradation.
The endoplasmic reticulum (ER) serves as a warehouse for factors that augment and control the biogenesis of nascent proteins… 
Review
2015
Review
2015
Endoplasmic reticulum quality control in cancer: Friend or foe.
2015
2015
UBXN2A regulates nicotinic receptor degradation by modulating the E3 ligase activity of CHIP.
Review
2014
Review
2014
Apolipoprotein B100 quality control and the regulation of hepatic very low density lipoprotein secretion
Abstract Apolipoprotein B (apoB) is the main protein component of very low density lipoprotein (VLDL) and is necessary for the… 
2013
2013
A unique IBMPFD-related P97/VCP mutation with differential binding pattern and subcellular localization.
Review
2011
Review
2011
The complexities of p97 function in health and disease.
p97 is a homohexameric, toroidal machine that harnesses the energy of ATP binding and hydrolysis to effect structural… 
2009
2009
Endoplasmic reticulum-associated degradation of a degron-containing polytopic membrane protein
Abstract The presence of two basic amino acids strategically located within a single spanning transmembrane region has previously… 
2008
2008
Ro52 functionally interacts with IgG1 and regulates its quality control via the ERAD system.
2008
2008
SEL1L and HRD1 are involved in the degradation of unassembled secretory Ig‐µ chains
When expressed in the absence of light chains, secretory Ig‐µ chains (µs) undergo endoplasmic reticulum associated degradation… 
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