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Glycoprotein folding and quality-control mechanisms in protein-folding diseases

Glycoprotein folding and quality-control mechanisms in protein-folding diseases

http://www.wikidata.org/entity/Q37621073

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Using pharmacological chaperones to restore proteostasis The Dependence of Carbohydrate-Aromatic Interaction Strengths on the Structure of the Carbohydrate.Interactions between N-linked glycosylation and polymerisation of neuroserpin within the endoplasmic reticulum N-linked glycosylation at Asn152 on CD147 affects protein folding and stability: promoting tumour metastasis in hepatocellular carcinoma.Arsenic Triglutathione [As(GS)3] Transport by Multidrug Resistance Protein 1 (MRP1/ABCC1) Is Selectively Modified by Phosphorylation of Tyr920/Ser921 and Glycosylation of Asn19/Asn23.N-Linked Glycosylation Is Required for Vacuolar H+ -ATPase (V-ATPase) a4 Subunit Stability, Assembly, and Cell Surface Expression.Hydrophobic Tagged Dihydrofolate Reductase for Creating Misfolded Glycoprotein Mimetics.Orphan enzyme cuts down on sugar.Neutralization function affected by single amino acid replacement in the HIV-1 antibody targets.A structure-activity relationship linking non-planar PCBs to functional deficits of neural crest cells: new roles for connexins.Degradation routes of trafficking-defective VLDLR mutants associated with Dysequilibrium syndrome.N-linked glycosylation of a subunit isoforms is critical for vertebrate vacuolar H+ -ATPase (V-ATPase) biosynthesis.Site-specific characterization of N-linked glycosylation in human urinary glycoproteins and endogenous glycopeptides.Coordinate regulation of mutant NPC1 degradation by selective ER autophagy and MARCH6-dependent ERAD

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P2860

Glycoprotein folding and quality-control mechanisms in protein-folding diseases

http://www.wikidata.org/entity/Q37621073

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on March 2014

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

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vědecký článek

@cs

name

Glycoprotein folding and quality-control mechanisms in protein-folding diseases

@en

Glycoprotein folding and quality-control mechanisms in protein-folding diseases.

@nl

type

label

Glycoprotein folding and quality-control mechanisms in protein-folding diseases

@en

Glycoprotein folding and quality-control mechanisms in protein-folding diseases.

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prefLabel

Glycoprotein folding and quality-control mechanisms in protein-folding diseases

@en

Glycoprotein folding and quality-control mechanisms in protein-folding diseases.

@nl

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Disease Models & Mechanisms

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Glycoprotein folding and quality-control mechanisms in protein-folding diseases

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Randal J Kaufman

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Sean P Ferris

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Creative Commons Attribution

P2860

Identification, expression, and characterization of a cDNA encoding human endoplasmic reticulum mannosidase I, the enzyme that catalyzes the first mannose trimming step in mammalian Asn-linked oligosaccharide biosynthesis

Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis

Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin

Malectin forms a complex with ribophorin I for enhanced association with misfolded glycoproteins

Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation

Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation steps

Calreticulin signals upstream of calcineurin and MEF2C in a critical Ca(2+)-dependent signaling cascade

Oligosaccharyltransferase-subunit mutations in nonsyndromic mental retardation

OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD

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

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331-341

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scholarly article

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10.1242/DMM.014589

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3

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7

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2014-03-01T00:00:00Z

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260645765

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24609034

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Angliavandeniai

proteostasis deficiency

quality control

protein folding

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3944493

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