Futile protein folding cycles in the ER are terminated by the unfolded protein O-mannosylation pathway.
about
Plant protein glycosylationRecent technical developments in the study of ER-associated degradationForcible destruction of severely misfolded mammalian glycoproteins by the non-glycoprotein ERAD pathwayUbiquitin-dependent protein degradation at the yeast endoplasmic reticulum and nuclear envelope.PMT1 deficiency enhances basal UPR activity and extends replicative lifespan of Saccharomyces cerevisiaeN-terminal entrance loop of yeast Yps1 and O-glycosylation of substrates are determinant factors controlling the shedding activity of this GPI-anchored endopeptidase.Cellular Consequences of Diminished Protein O-Mannosyltransferase Activity in Baker's Yeast.Mining the O-mannose glycoproteome reveals cadherins as major O-mannosylated glycoproteins.Glycoprotein folding and quality-control mechanisms in protein-folding diseasesEukaryotic protein glycosylation: a primer for histochemists and cell biologistsProtein O-mannosyltransferases associate with the translocon to modify translocating polypeptide chains.Resolving the α-glycosidic linkage of arginine-rhamnosylated translation elongation factor P triggers generation of the first ArgRha specific antibody.Quality control: ER-associated degradation: protein quality control and beyondGlycobiology of α-dystroglycan and muscular dystrophy.Acetylation of N-terminus and two internal amino acids is dispensable for degradation of a protein that aberrantly engages the endoplasmic reticulum translocon.Glycosylation-directed quality control of protein folding.Cellular growth defects triggered by an overload of protein localization processes.Novel roles for O-linked glycans in protein folding.CIA2 deficiency results in impaired oxidative stress response and enhanced intracellular basal UPR activity in Saccharomyces cerevisiae.Cell biology. A sweet send-off.Conformational folding and disulfide bonding drive distinct stages of protein structure formation.Cotranslational protein assembly imposes evolutionary constraints on homomeric proteins.Using deep learning to model the hierarchical structure and function of a cell.
P2860
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P2860
Futile protein folding cycles in the ER are terminated by the unfolded protein O-mannosylation pathway.
description
2013 nî lūn-bûn
@nan
2013 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Futile protein folding cycles ...... otein O-mannosylation pathway.
@ast
Futile protein folding cycles ...... otein O-mannosylation pathway.
@en
Futile protein folding cycles ...... otein O-mannosylation pathway.
@nl
type
label
Futile protein folding cycles ...... otein O-mannosylation pathway.
@ast
Futile protein folding cycles ...... otein O-mannosylation pathway.
@en
Futile protein folding cycles ...... otein O-mannosylation pathway.
@nl
prefLabel
Futile protein folding cycles ...... otein O-mannosylation pathway.
@ast
Futile protein folding cycles ...... otein O-mannosylation pathway.
@en
Futile protein folding cycles ...... otein O-mannosylation pathway.
@nl
P2093
P2860
P3181
P356
P1433
P1476
Futile protein folding cycles ...... rotein O-mannosylation pathway
@en
P2093
Chengchao Xu
Davis T W Ng
Songyu Wang
P2860
P304
P3181
P356
10.1126/SCIENCE.1234055
P407
P577
2013-05-01T00:00:00Z