Human endoplasmic reticulum mannosidase I is subject to regulated proteolysis. - Wikidata - wikimedia - TriplyDB

Human endoplasmic reticulum mannosidase I is subject to regulated proteolysis.

Human endoplasmic reticulum mannosidase I is subject to regulated proteolysis.

http://www.wikidata.org/entity/Q37672299

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Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation Arms Race between Enveloped Viruses and the Host ERAD Machinery Senescence marker protein 30 (SMP30) expression in eukaryotic cells: existence of multiple species and membrane localization A Golgi-localized mannosidase (MAN1B1) plays a non-enzymatic gatekeeper role in protein biosynthetic quality control.ERManI is a target of miR-125b and promotes transformation phenotypes in hepatocellular carcinoma (HCC)Mammalian ER mannosidase I resides in quality control vesicles, where it encounters its glycoprotein substrates.Golgi localization of ERManI defines spatial separation of the mammalian glycoprotein quality control system.Unconventional use of LC3 by coronaviruses through the alleged subversion of the ERAD tuning pathway.Flagging and docking: dual roles for N-glycans in protein quality control and cellular proteostasis.Protein quality control in the early secretory pathway Golgi-situated endoplasmic reticulum α-1, 2-mannosidase contributes to the retrieval of ERAD substrates through a direct interaction with γ-COP.JAMP optimizes ERAD to protect cells from unfolded proteins Ubiquitin signals autophagic degradation of cytosolic proteins and peroxisomes.Single nucleotide polymorphism-mediated translational suppression of endoplasmic reticulum mannosidase I modifies the onset of end-stage liver disease in alpha1-antitrypsin deficiency.The mammalian UPR boosts glycoprotein ERAD by suppressing the proteolytic downregulation of ER mannosidase I.Protein glycosylation in Candida.Sorting things out through endoplasmic reticulum quality control.Intracellular processing of alpha1-antitrypsin.Proteostasis strategies for restoring alpha1-antitrypsin deficiency.Protein N-glycosylation, protein folding, and protein quality control.Specificity and regulation of the endoplasmic reticulum-associated degradation machinery.The Role of Lectin-Carbohydrate Interactions in the Regulation of ER-Associated Protein Degradation.Eeyarestatin I inhibits Sec61-mediated protein translocation at the endoplasmic reticulum.Two distinct pathways for cyclooxygenase-2 protein degradation.Kex2 protease converts the endoplasmic reticulum alpha1,2-mannosidase of Candida albicans into a soluble cytosolic form.Inhibition of protein translocation at the endoplasmic reticulum promotes activation of the unfolded protein response.Proteostasis: a new therapeutic paradigm for pulmonary disease.Large protein complexes retained in the ER are dislocated by non-COPII vesicles and degraded by selective autophagy.Trimming of glucosylated N-glycans by human ER α1,2-mannosidase I.

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P2860

Human endoplasmic reticulum mannosidase I is subject to regulated proteolysis.

http://www.wikidata.org/entity/Q37672299

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 13 December 2006

@en

vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Human endoplasmic reticulum mannosidase I is subject to regulated proteolysis.

@en

Human endoplasmic reticulum mannosidase I is subject to regulated proteolysis.

@nl

type

label

Human endoplasmic reticulum mannosidase I is subject to regulated proteolysis.

@en

Human endoplasmic reticulum mannosidase I is subject to regulated proteolysis.

@nl

prefLabel

Human endoplasmic reticulum mannosidase I is subject to regulated proteolysis.

@en

Human endoplasmic reticulum mannosidase I is subject to regulated proteolysis.

@nl

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Journal of Biological Chemistry

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Human endoplasmic reticulum mannosidase I is subject to regulated proteolysis.

@en

P2093

Daniel J Termine

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

Kelley W Moremen

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

Matthew T Swulius

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

Richard N Sifers

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

Ying Wu

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

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

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

Structural basis for catalysis and inhibition of N-glycan processing class I alpha 1,2-mannosidases

Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48.

Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure.

Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation

The DNA damage response: putting checkpoints in perspective

EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin

Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin

P304

4841-4849

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scholarly article

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10.1074/JBC.M607156200

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7

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282

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2006-12-13T00:00:00Z

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17166854

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endoplasmic reticulum

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3969733

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