Role of E3 Ubiquitin Ligases in Oligodendrocyte Health and Disease. [PDF]
Mabb AM, Pyaram DN, Samanta J.
europepmc +1 more source
SEL1L regulates ER homeostasis in Sertoli cells but is dispensable for their function. [PDF]
Tushi NJ, Lu Y, Zhang Z, Sun S.
europepmc +1 more source
Protein sorting and proteostasis mechanisms in CFTR-related exocrine pancreas dysfunction: A systematic narrative review. [PDF]
Niyomugabo AP +2 more
europepmc +1 more source
Endoplasmic reticulum stress in Hashimoto's thyroiditis: a candidate amplification node linking thyroid-specific vulnerability and immune dysregulation. [PDF]
Si X +10 more
europepmc +1 more source
Characterization of protein complexes of the endoplasmic reticulum-associated degradation E3 ubiquitin ligase Hrd1 [PDF]
Hrd1 is the core structural component of a large endoplasmic reticulum membrane-embedded protein complex that coordinates the destruction of folding-defective proteins in the early secretory pathway.
Ron Kopito +2 more
exaly +2 more sources
[[abstract]]Endoplasmic reticulum-associated degradation (ERAD) is an important system that eliminates misfolded proteins from the ER. Three derlins have been implicated in this process, but their precise function remains unknown.
Yihong Ye
exaly +2 more sources
Herp Regulates Hrd1-mediated Ubiquitylation in a Ubiquitin-like Domain-dependent Manner*
Accumulation of aberrant proteins in the endoplasmic reticulum (ER) triggers the unfolded protein response pathway that helps the cell to survive under these stress conditions.
Melanie Kny, Rasmus Hartmann-Petersen
exaly +2 more sources
A ubiquitin ligase HRD1 promotes the degradation of Pael receptor, a substrate of Parkin. [PDF]
It has been proposed that in autosomal recessive juvenile parkinsonism (AR-JP), a ubiquitin ligase (E3) Parkin, which is involved in endoplasmic reticulum-associated degradation (ERAD), lacks E3 activity.
Tomohiro Omura, Masayuki Kaneko
exaly +2 more sources
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