Reglucosylation by UDP-glucose:glycoprotein glucosyltransferase 1 delays glycoprotein secretion but not degradation.
about
Plant protein glycosylationN-linked sugar-regulated protein folding and quality control in the ERN-Glycan-based ER Molecular Chaperone and Protein Quality Control System: The Calnexin Binding CycleInterdomain conformational flexibility underpins the activity of UGGT, the eukaryotic glycoprotein secretion checkpoint.Single-particle electron microscopy structure of UDP-glucose:glycoprotein glucosyltransferase suggests a selectivity mechanism for misfolded proteins.
P2860
Reglucosylation by UDP-glucose:glycoprotein glucosyltransferase 1 delays glycoprotein secretion but not degradation.
description
2014 nî lūn-bûn
@nan
2014 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Reglucosylation by UDP-glucose ...... secretion but not degradation.
@ast
Reglucosylation by UDP-glucose ...... secretion but not degradation.
@en
type
label
Reglucosylation by UDP-glucose ...... secretion but not degradation.
@ast
Reglucosylation by UDP-glucose ...... secretion but not degradation.
@en
prefLabel
Reglucosylation by UDP-glucose ...... secretion but not degradation.
@ast
Reglucosylation by UDP-glucose ...... secretion but not degradation.
@en
P2093
P2860
P356
P1476
Reglucosylation by UDP-glucose ...... secretion but not degradation.
@en
P2093
Abla Tannous
Daniel N Hebert
Nishant Patel
P2860
P304
P356
10.1091/MBC.E14-08-1254
P50
P577
2014-11-26T00:00:00Z