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Loss of UGT1 expression is associated with neonatal hyperbilirubinemia.
Increased UGGT1 levels elevated viral growth rates, while viral pathogenicity was observed to be lower in heterozygous knockout mice (Uggt1 +/- mice). These findings provide important insight on the role of UPR and host UGGT1 in regulating RNA virus replication and pathogenicity.
study demonstrates that UGGT1 enzymatic activity, in conjunction with lectin-like chaperones, helps to limit aggregation and polymer formation of misfolded glycoprotein substrates, decreasing their BiP (show HSPA5 ELISA Kits) association and ER stress
the expression of two UGGT isoforms, UGGT1 and UGGT2 (show UGT2 ELISA Kits) was demonstrated and both isoforms are active mouse hybridoma cells.
UGT1 aids in the folding of sequential domain-containing proteins such as prosaposin (show PSAP ELISA Kits).
The cysteine-rich domain of Sep15 (show SEP15 ELISA Kits) exclusively mediates protein-protein interactions with UDP-glucose:glycoprotein glucosyltransferase.
both vIL (show VIL1 ELISA Kits)-6 and VKORC1v2 interact with calnexin (show CANX ELISA Kits) cycle proteins UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1), which catalyzes monoglucosylation of N-glycans, and oppositely acting glucosidase II (GlucII), and that vIL (show VIL1 ELISA Kits)-6 can promote protein folding.
These findings provide important insight on the role of unfolded protein response (UPR) and host UGGT1 in regulating RNA virus replication and pathogenicity.
The results demonstrated that FAM5C is an N-glycosylated protein, and N-glycosylation by UGGT1 is necessary for the secretion of FAM5C.
A novel UGGT1- and p97 (show EIF4G2 ELISA Kits)-dependent protein quality checkpoint is shown. This checkpoint is alerted to prevent secretion of a polypeptide that passes the luminal quality control scrutiny by BiP (show GDF10 ELISA Kits) and CNX (show CANX ELISA Kits) but contains an intramembrane ionizable residue.
Kyte-Doolittle analysis as well as homology modeling revealed a cluster of hydrophobic amino acids that may be functional in the folding sensing mechanism of HUGT1
Results indicate that glycan structures are similar to endogenous glycans at low expression levels of uridine 5'-diphosphate-glucose: glycoprotein glucosyltransferase (UGGT1).
The UGGT1 is a well-documented enzyme which functions as a folding sensor in the endoplasmic reticulum, by the virtue of its ability to transfer a glucose residue to non-glucosylated high-mannose-type glycans of immature glycoproteins.
UGT1 (show SLC35A2 ELISA Kits) aids in the folding of sequential domain-containing proteins such as prosaposin (show PSAP ELISA Kits).
the amino-terminal 80% of HUGT1 is required for activation of the catalytic domain
a lack of UGGT activity alters plant vegetative development and impairs the response to several abiotic and biotic stresses.
a missense mutation in the Arabidopsis EMS-mutagenized bri1 suppressor 3 (EBS3) gene suppresses a dwarf mutant, bri1-9, the phenotypes of which are caused by ER retention and ERAD of a brassinosteroid receptor, BRASSINOSTEROID-INSENSITIVE 1 (BR1)
UDP-glucose soluble protein of the endoplasmic reticulum (ER) that selectively reglucosylates unfolded glycoproteins, thus providing quality control for protein transport out of the ER.
UDP-glucose ceramide glucosyltransferase-like 1
, UDP-glucose glycoprotein glucosyltransferase 2
, UDP-glucose glycoprotein glucosyltransferase 1
, UDP-glucose:glycoprotein glucosyltransferase 1-like
, UDP--Glc:glycoprotein glucosyltransferase
, UDP-glucose:glycoprotein glucosyltransferase
, UDP-glucose:glycoprotein glucosyltransferase 1
, UDP-glucose glycoprotein: glucosyltransferase UGGT