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TranscriptomicsThe ER-Associated Degradation Adapter Protein Sel1L Regulates Triglyceride Metabolism via Lipoprotein Lipase
Sel1L is an adaptor protein for the E3 ligase Hrd1 in the endoplasmic reticulum-associated degradation (ERAD), but its physiological role in a cell-type-specific manner remains unclear. Here we show that mice with adipocyte-specific Sel1L deficiency are resistant to diet-induced obesity and exhibit ...
ORGANISM(S): Mus musculus 
2015-05-18 | E-GEOD-56918 | biostudies-arrayexpress
ProteomicsER-associated degradation ligase HRD1 links ER stress to DNA damage repair by modulating the activity of DNA-PKcs
ER-associated degradation ligase HRD1 links ER stress to DNA damage repair by modulating the activity of DNA-PKcs
ORGANISM(S): Homo Sapiens 
PXD055020 |
ProteomicsOligosaccharyltransferase is involved in targeting to ER-associated degradation
The majority of secretory proteins undergo N-glycosylation, a process catalyzed by oligosaccharyltransferase (OST), a membrane-bound protein complex that associates with the translocation channels within the endoplasmic reticulum (ER). Proteins failing quality control undergo ER-associated degradati...
ORGANISM(S): Homo sapiens (Human) 
2025-10-14 | PXD067654 | Pride
Oligosaccharyltransferase Er-associated degradation Protein quality control Protein--folding 
ProteomicsAn ERAD independent role for rhomboid pseudoprotease Dfm1 in mediating sphingolipid homeostasis
Nearly one-third of nascent proteins are initially targeted to the endoplasmic reticulum (ER) where they are correctly folded and assembled before being delivered to their final cellular destinations. To prevent the accumulation of misfolded membrane proteins, ER-associated-degradation (ERAD) remove...
ORGANISM(S): Saccharomyces Cerevisiae (ncbitaxon:4932) 
MSV000090333 | MassIVE
ProteomicsCharacterization of Endoplasmic Reticulum-Associated Degradation in the human fungal pathogen C. albicans
C. albicans is the most prevalent human fungal pathogen. In immunocompromised individuals, C. albicans can cause serious systemic disease and patients infected with drug-resistant isolates have few treatment options. The Ubiquitin-Proteasome System has not been thoroughly characterized in C. albica...
ORGANISM(S): Candida Albicans (ncbitaxon:5476) 
2023-05-03 | MSV000091843 | MassIVE
GenomicsER-associated degradation maintains postnatal muscle hypertophy and systemic energy metabolism
ER-associated degradation maintains postnatal muscle hypertophy and systemic energy metabolism
PRJNA994154 | ENA
TranscriptomicsTranscription profiling of human cell cancer line treated with bortezomib or Eeyarestatin I (EerI) reveals ERAD inhibitors integrate ER stress with an epigenetic mechanism to activate BH3 only protein NOXA in cancer cells
The ubiquitin-proteasome system (UPS) has recently emerged as a major target for drug development in cancer therapy. The proteasome inhibitor bortezomib has clinical activity in multiple myeloma and mantle cell lymphoma. Here we report that Eeyarestatin I (EerI), a chemical inhibitor that blocks ER-...
ORGANISM(S): Homo sapiens 
2009-02-28 | E-GEOD-14003 | biostudies-arrayexpress
TranscriptomicsIRE1alpha is an endogenous substrate of endoplasmic reticulum-associated degradation
Endoplasmic reticulum-associated degradation (ERAD) represents a principle quality control (QC) mechanism to clear misfolded proteins in the ER; however, its physiological significance and the nature of endogenous ERAD substrates remain largely unknown. Here we discover that IRE1alpha, the sensor of...
ORGANISM(S): Mus musculus 
2015-11-04 | E-GEOD-70563 | biostudies-arrayexpress
GenomicsHepatic Sel1L-Hrd1 ER-Associated Degradation (ERAD) manages FGF21 levels and systemic metabolism via CREBH
Hepatic Sel1L-Hrd1 ER-Associated Degradation (ERAD) manages FGF21 levels and systemic metabolism via CREBH
PRJNA486359 | ENA
GenomicsER-associated degradation is required for the maintenance of β cell identity via TGFβ signaling
ER-associated degradation is required for the maintenance of β cell identity via TGFβ signaling
PRJNA601502 | ENA
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