Futile protein folding cycles in the ER are terminated by the unfolded protein O-mannosylation pathway. - Test2 - elhamkhani - TriplyDB

Futile protein folding cycles in the ER are terminated by the unfolded protein O-mannosylation pathway.

Futile protein folding cycles in the ER are terminated by the unfolded protein O-mannosylation pathway.

http://www.wikidata.org/entity/Q27932449

about

Plant protein glycosylation Recent technical developments in the study of ER-associated degradation Forcible destruction of severely misfolded mammalian glycoproteins by the non-glycoprotein ERAD pathway Ubiquitin-dependent protein degradation at the yeast endoplasmic reticulum and nuclear envelope.PMT1 deficiency enhances basal UPR activity and extends replicative lifespan of Saccharomyces cerevisiae N-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 diseases Eukaryotic protein glycosylation: a primer for histochemists and cell biologists Protein 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 beyond Glycobiology 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.

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P2860

Futile protein folding cycles in the ER are terminated by the unfolded protein O-mannosylation pathway.

http://www.wikidata.org/entity/Q27932449

description

2013 nî lūn-bûn

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2013 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2013 թվականի մայիսին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

Futile protein folding cycles ...... otein O-mannosylation pathway.

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Futile protein folding cycles ...... otein O-mannosylation pathway.

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Futile protein folding cycles ...... otein O-mannosylation pathway.

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Futile protein folding cycles ...... otein O-mannosylation pathway.

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Futile protein folding cycles ...... otein O-mannosylation pathway.

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Futile protein folding cycles ...... otein O-mannosylation pathway.

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Futile protein folding cycles ...... otein O-mannosylation pathway.

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Futile protein folding cycles ...... otein O-mannosylation pathway.

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Futile protein folding cycles ...... otein O-mannosylation pathway.

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Futile protein folding cycles ...... rotein O-mannosylation pathway

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Chengchao Xu

http://www.w3.org/2001/XMLSchema#string

Davis T W Ng

http://www.w3.org/2001/XMLSchema#string

Songyu Wang

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P2860

Characterization of an ERAD gene as VPS30/ATG6 reveals two alternative and functionally distinct protein quality control pathways: one for soluble Z variant of human alpha-1 proteinase inhibitor (A1PiZ) and another for aggregates of A1PiZ.

Protein folding and quality control in the ER

Road to ruin: targeting proteins for degradation in the endoplasmic reticulum

Global analysis of protein expression in yeast

Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation.

A complex of Pdi1p and the mannosidase Htm1p initiates clearance of unfolded glycoproteins from the endoplasmic reticulum.

Alternative modes of organellar segregation during sporulation in Saccharomyces cerevisiae

Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex.

Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum

O-mannosylation is required for degradation of the endoplasmic reticulum-associated degradation substrate Gas1*p via the ubiquitin/proteasome pathway in Saccharomyces cerevisiae.

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10.1126/SCIENCE.1234055

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340

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Guillaume Thibault

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23704572

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protein folding