Endoplasmic reticulum-associated degradation (ERAD) and free oligosaccharide generation in Saccharomyces cerevisiae. - Wikidata - wikimedia - TriplyDB

Endoplasmic reticulum-associated degradation (ERAD) and free oligosaccharide generation in Saccharomyces cerevisiae.

Endoplasmic reticulum-associated degradation (ERAD) and free oligosaccharide generation in Saccharomyces cerevisiae.

http://www.wikidata.org/entity/Q42122385

about

The cytoplasmic peptide:N-glycanase (Ngly1)-basic science encounters a human genetic disorder.Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: An update for 2011-2012.Structural Analysis of Free N-Glycans in α-Glucosidase Mutants of Saccharomyces cerevisiae: Lack of the Evidence for the Occurrence of Catabolic α-Glucosidase Acting on the N-Glycans.The endoplasmic reticulum-associated degradation pathways of budding yeast.Travelling-wave ion mobility and negative ion fragmentation of high-mannose N-glycans.Htm1p-Pdi1p is a folding-sensitive mannosidase that marks N-glycoproteins for ER-associated protein degradation.Generation and degradation of free asparagine-linked glycans.Brefeldin A promotes the appearance of oligosaccharyl phosphates derived from Glc3Man9GlcNAc2-PP-dolichol within the endomembrane system of HepG2 cells.Generation of free oligosaccharides from bacterial protein N-linked glycosylation systems.Lack of the evidence for the enzymatic catabolism of Man1GlcNAc2 in Saccharomyces cerevisiae.

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P2860

Endoplasmic reticulum-associated degradation (ERAD) and free oligosaccharide generation in Saccharomyces cerevisiae.

http://www.wikidata.org/entity/Q42122385

description

2011 nî lūn-bûn

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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name

Endoplasmic reticulum-associat ...... n in Saccharomyces cerevisiae.

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type

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Endoplasmic reticulum-associat ...... n in Saccharomyces cerevisiae.

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Endoplasmic reticulum-associat ...... n in Saccharomyces cerevisiae.

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JBC.M111.251371

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Journal of Biological Chemistry

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Endoplasmic reticulum-associat ...... on in Saccharomyces cerevisiae

@en

P2093

Chaïmaâ Lahmouich

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David J Harvey

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

Vidya P Kodali

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P2860

The specificity of the yeast and human class I ER alpha 1,2-mannosidases involved in ER quality control is not as strict previously reported

Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans

Cloning and analysis of the Saccharomyces cerevisiae MNN9 and MNN1 genes required for complex glycosylation of secreted proteins

PNG1, a yeast gene encoding a highly conserved peptide:N-glycanase

A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation.

Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway.

Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen.

Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins.

Free-oligosaccharide control in the yeast Saccharomyces cerevisiae: roles for peptide:N-glycanase (Png1p) and vacuolar mannosidase (Ams1p).

Structure of the N-linked oligosaccharides that show the complete loss of alpha-1,6-polymannose outer chain from och1, och1 mnn1, and och1 mnn1 alg3 mutants of Saccharomyces cerevisiae

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41786-41800

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10.1074/JBC.M111.251371

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48

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286

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Isabelle Chantret

Stuart E H Moore

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2011-10-06T00:00:00Z

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51699623

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21979948

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oligosaccharide

endoplasmic reticulum

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3308887

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