Bypass of glycan-dependent glycoprotein delivery to ERAD by up-regulated EDEM1. - Wikidata - awgldk - TriplyDB

Bypass of glycan-dependent glycoprotein delivery to ERAD by up-regulated EDEM1.

Bypass of glycan-dependent glycoprotein delivery to ERAD by up-regulated EDEM1.

http://www.wikidata.org/entity/Q38331877

about

EDEM2 initiates mammalian glycoprotein ERAD by catalyzing the first mannose trimming step The role of EDEM2 compared with EDEM1 in ricin transport from the endoplasmic reticulum to the cytosol Unfolded Protein Response and Macroautophagy in Alzheimer's, Parkinson's and Prion Diseases Modulation of the unfolded protein response by the human hepatitis B virus The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology Tyrosinase degradation is prevented when EDEM1 lacks the intrinsically disordered region A Golgi-localized mannosidase (MAN1B1) plays a non-enzymatic gatekeeper role in protein biosynthetic quality control.Elevated systemic expression of ER stress related genes is associated with stress-related mental disorders in the Detroit Neighborhood Health Study Activation of ERAD pathway by human hepatitis B virus modulates viral and subviral particle production.Glycoprotein misfolding in the endoplasmic reticulum: identification of released oligosaccharides reveals a second ER-associated degradation pathway for Golgi-retrieved proteins.Mammalian ER mannosidase I resides in quality control vesicles, where it encounters its glycoprotein substrates.ER stress-induced eIF2-alpha phosphorylation underlies sensitivity of striatal neurons to pathogenic huntingtin Hydrophobicity of protein determinants influences the recognition of substrates by EDEM1 and EDEM2 in human cells.Role of pro-oncogenic protein disulfide isomerase (PDI) family member anterior gradient 2 (AGR2) in the control of endoplasmic reticulum homeostasis.Flagging and docking: dual roles for N-glycans in protein quality control and cellular proteostasis.Cleaning up: ER-associated degradation to the rescue.Inhibition of endoplasmic reticulum associated degradation reduces endoplasmic reticulum stress and alters lysosomal morphology and distribution.Up-regulation of endoplasmic reticulum stress induced genes of the unfolded protein response in the liver of periparturient dairy cows.Specificity and regulation of the endoplasmic reticulum-associated degradation machinery.The Role of Lectin-Carbohydrate Interactions in the Regulation of ER-Associated Protein Degradation.Herp coordinates compartmentalization and recruitment of HRD1 and misfolded proteins for ERAD.Novel function of the endoplasmic reticulum degradation-enhancing α-mannosidase-like proteins in the human hepatitis B virus life cycle, mediated by the middle envelope protein.Soluble forms of polyQ-expanded huntingtin rather than large aggregates cause endoplasmic reticulum stress.A shared endoplasmic reticulum-associated degradation pathway involving the EDEM1 protein for glycosylated and nonglycosylated proteins.Inducible nitric oxide synthase is a major intermediate in signaling pathways for the survival of plasma cells.Mannosidase activity of EDEM1 and EDEM2 depends on an unfolded state of their glycoprotein substrates

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P2860

Bypass of glycan-dependent glycoprotein delivery to ERAD by up-regulated EDEM1.

http://www.wikidata.org/entity/Q38331877

description

2011 nî lūn-bûn

@nan

2011年の論文

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2011年学术文章

@wuu

2011年学术文章

@zh-cn

2011年学术文章

@zh-hans

2011年学术文章

@zh-my

2011年学术文章

@zh-sg

2011年學術文章

@yue

2011年學術文章

@zh

2011年學術文章

@zh-hant

name

Bypass of glycan-dependent glycoprotein delivery to ERAD by up-regulated EDEM1.

@en

type

label

Bypass of glycan-dependent glycoprotein delivery to ERAD by up-regulated EDEM1.

@en

prefLabel

Bypass of glycan-dependent glycoprotein delivery to ERAD by up-regulated EDEM1.

@en

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P356

MBC.E10-12-0944

P1433

Molecular Biology of the Cell

P1476

Bypass of glycan-dependent glycoprotein delivery to ERAD by up-regulated EDEM1.

@en

P2093

Bella Groisman

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

Efrat Ron

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

Gerardo Z Lederkremer

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

Julia Leitman

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

Marina Shenkman

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

Yana Izenshtein

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

P2860

The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum

Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle

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

Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for 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

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

Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP

A dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: inhibiting secretion of misfolded protein conformers and enhancing their disposal

EDEM1 recognition and delivery of misfolded proteins to the SEL1L-containing ERAD complex

A novel ER alpha-mannosidase-like protein accelerates ER-associated degradation

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3945-3954

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scholarly article

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10.1091/MBC.E10-12-0944

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21

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22

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2011-09-14T00:00:00Z

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21917589

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3204057

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