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Naringenin also attenuated hepatic apoptosis in larvae as detected by TUNEL staining, consistent with the expression of critical biomarkers of endoplasmic reticulum stress and of DNA damage genes (chop, gadd45alphaa and edem1). The present study showed that naringenin inhibited alcohol-induced liver steatosis and injury in zebrafish larvae by reducing apoptosis and DNA damage and by harmonizing alcohol and lipid metabo...
A somatic variant of EDEM1 (N198I) alters ATF6 signaling and provides a selective advantage to the transforming cells and results in hepatocellular carcinoma.
EDEM1 employs different binding modalities to interact with ERAD clients and ER quality control (ERQC) machinery partners and some of these properties are shared with its homologues EDEM2 and EDEM3.
EDEM1 colocalizes with the selective autophagy cargo receptors p62/SQSTM1, neighbor of BRCA1 gene 1 (NBR1) and autophagy-linked FYVE (Alfy) protein, and becomes engulfed by autophagic isolation membranes.
Endoplasmic reticulum degradation-enhancing alpha-mannosidase-like protein 1 targets misfolded HLA-B27 dimers for endoplasmic reticulum-associated degradation.
miR-581 promotes hepatitis B virus surface antigen expression by targeting Dicer and EDEM1 in HepG2 cells.
EDEM1 associates with lifespan in animal models, although not humans.
analysis of a shared endoplasmic reticulum-associated degradation pathway involving the EDEM1 protein for glycosylated and nonglycosylated proteins
Tyrosinase degradation is prevented when EDEM1 lacks the intrinsically disordered region
we suggest that a nascent glycoprotein can normally dissociate from EDEM1 and be rescued from endoplasmic reticulum associated degradation by reentering calnexin-refolding cycles
signal sequence cleavage functionally regulated the association of EDEM1-soluble and membrane-integrated isoforms with distinct ERAD machinery and substrates.
EDEM1 protein recognition may be determined by the structure of the endoplasmic reticulum-associated protein degradation substrate in a study of mutant ricin A-chain transport to the cytosol.
mannose trimming enables delivery of a substrate glycoprotein from EDEM1 to late endoplasmic reticulum degredation steps through association with XTP3-B
The EDEM1 activity trims mannose from the C branch of N-glycans in vivo.
EDEM1 promotes correct folding and enhanced degradation of rod opsin.
EDEM was shown to extract misfolded glycoproteins, but not glycoproteins undergoing productive folding, from the calnexin cycle [EDEM]
EDEM1 is a soluble protein of the ER lumen in HEK293 cells
These results indicate that EDEM may maintain the retrotranslocation competence of NHK by inhibiting aggregation so that unstable misfolded proteins can be accommodated by the dislocon for ERAD.
the endoplasmic reticulum quality control vesicular transport pathway using EDEM1 does not involve the COPII exit sites
Cells with defective EDEM1 turnover contain unphysiologically high levels of EDEM1, show enhanced ER associated degradation activity and are characterized by impaired capacity to efficiently complete maturation of model glycopolypeptides.
endogenous EDEM1 in cells not stressed by the expression of a transgenic misfolded protein reaches the cytosol and is degraded by basal autophagy
Japanese encephalitis virus replication is negatively regulated by autophagy and occurs on LC3-I- and EDEM1-containing membranes
Data suggest Edem1/Edem2 participate in ricin translocation; overexpression of Edem2, in contrast to Edem1, promotes ricin subunit A transport from endoplasmic reticulum (ER) to cytosol; transport of ricin P250A mutant is Edem1/Edem2-independent.
role of the lectins Htm1p/EDEM in the degradation process of CFTR
EDEM has a role in maintenance of protein folding efficiency and secretory capacity
EDEM is involved in retrotranslocation of ricin from the ER to the cytosol.
Extracts misfolded glycoproteins, but not glycoproteins undergoing productive folding, from the calnexin cycle. It is directly involved in endoplasmic reticulum-associated degradation (ERAD) and targets misfolded glycoproteins for degradation in an N-glycan-independent manner, probably by forming a complex with SEL1L. It lacks mannosidase activity.
ER degradation-enhancing alpha-mannosidase-like 1
, ER degradation enhancer, mannosidase alpha-like 1
, ER degradation-enhancing alpha-mannosidase-like 1-like
, ER degradation-enhancing alpha-mannosidase-like protein 1
, ER degradation ER degradation enhancer, mannosidase alpha-like 1