Unassembled CD147 is an endogenous endoplasmic reticulum-associated degradation substrate - Wikidata - awgldk - TriplyDB

Unassembled CD147 is an endogenous endoplasmic reticulum-associated degradation substrate

Unassembled CD147 is an endogenous endoplasmic reticulum-associated degradation substrate

http://www.wikidata.org/entity/Q36465057

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How, with whom and when: an overview of CD147-mediated regulatory networks influencing matrix metalloproteinase activity Recent technical developments in the study of ER-associated degradation Five Questions (with their Answers) on ER-Associated Degradation Importance of N-glycosylation on CD147 for its biological functions Cleavage by signal peptide peptidase is required for the degradation of selected tail-anchored proteins.The biological function and clinical utilization of CD147 in human diseases: a review of the current scientific literature SEL1L regulates adhesion, proliferation and secretion of insulin by affecting integrin signaling.A novel UGGT1 and p97-dependent checkpoint for native ectodomains with ionizable intramembrane residue MHC class I molecules are preferentially ubiquitinated on endoplasmic reticulum luminal residues during HRD1 ubiquitin E3 ligase-mediated dislocation.Partial IFN-γR2 deficiency is due to protein misfolding and can be rescued by inhibitors of glycosylation.The unfolded protein response transducer ATF6 represents a novel transmembrane-type endoplasmic reticulum-associated degradation substrate requiring both mannose trimming and SEL1L protein N-linked glycosylation at Asn152 on CD147 affects protein folding and stability: promoting tumour metastasis in hepatocellular carcinoma.Inhibition of endoplasmic reticulum associated degradation reduces endoplasmic reticulum stress and alters lysosomal morphology and distribution.Sel1L is indispensable for mammalian endoplasmic reticulum-associated degradation, endoplasmic reticulum homeostasis, and survival.Lipid disequilibrium disrupts ER proteostasis by impairing ERAD substrate glycan trimming and dislocation.Specificity and regulation of the endoplasmic reticulum-associated degradation machinery.Glycosylation-directed quality control of protein folding.The evolving role of ubiquitin modification in endoplasmic reticulum-associated degradation.Membrane Protein Quantity Control at the Endoplasmic Reticulum.New Insights into the Physiological Role of Endoplasmic Reticulum-Associated Degradation.Establishing the lipid droplet proteome: Mechanisms of lipid droplet protein targeting and degradation.The Sel1L-Hrd1 Endoplasmic Reticulum-Associated Degradation Complex Manages a Key Checkpoint in B Cell Development.Loss of CD147 results in impaired epithelial cell differentiation and malformation of the meibomian gland.Enterovirus 71 protease 2Apro and 3Cpro differentially inhibit the cellular endoplasmic reticulum-associated degradation (ERAD) pathway via distinct mechanisms, and enterovirus 71 hijacks ERAD component p97 to promote its replication.Characterization of the Grp94/OS-9 chaperone-lectin complex.Characterization of protein complexes of the endoplasmic reticulum-associated degradation E3 ubiquitin ligase Hrd1.A Proximity Labeling Strategy Provides Insights into the Composition and Dynamics of Lipid Droplet Proteomes.Conserved cytoplasmic domains promote Hrd1 ubiquitin ligase complex formation for ER-associated degradation (ERAD).The endoplasmic reticulum-associated protein, OS-9, behaves as a lectin in targeting the immature calcium-sensing receptor.A VCP inhibitor substrate trapping approach (VISTA) enables proteomic profiling of endogenous ERAD substrates.Redundant and Antagonistic Roles of XTP3B and OS9 in Decoding Glycan and Non-glycan Degrons in ER-Associated Degradation.MARCH6 and TRC8 facilitate the quality control of cytosolic and tail-anchored proteins.Proteomic characterization of endogenous substrates of mammalian ubiquitin ligase Hrd1

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Unassembled CD147 is an endogenous endoplasmic reticulum-associated degradation substrate

http://www.wikidata.org/entity/Q36465057

description

2012 nî lūn-bûn

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2012年の論文

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

@zh-my

2012年学术文章

@zh-sg

2012年學術文章

@yue

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2012年學術文章

@zh-hant

name

Unassembled CD147 is an endogenous endoplasmic reticulum-associated degradation substrate

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Unassembled CD147 is an endogenous endoplasmic reticulum-associated degradation substrate

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type

label

Unassembled CD147 is an endogenous endoplasmic reticulum-associated degradation substrate

@ast

Unassembled CD147 is an endogenous endoplasmic reticulum-associated degradation substrate

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prefLabel

Unassembled CD147 is an endogenous endoplasmic reticulum-associated degradation substrate

@ast

Unassembled CD147 is an endogenous endoplasmic reticulum-associated degradation substrate

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MBC.E12-06-0428

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Molecular Biology of the Cell

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Unassembled CD147 is an endogenous endoplasmic reticulum-associated degradation substrate

@en

P2093

Margaret M P Pearce

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

Ron R Kopito

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

Ryan E Tyler

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

Thomas A Shaler

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P2860

Ubiquitin-dependent intramembrane rhomboid protease promotes ERAD of membrane proteins

Defining human ERAD networks through an integrative mapping strategy

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

The role of charged residues in the transmembrane helices of monocarboxylate transporter 1 and its ancillary protein basigin in determining plasma membrane expression and catalytic activity

Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane

HRD1 and UBE2J1 target misfolded MHC class I heavy chains for endoplasmic reticulum-associated degradation

The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site

A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.

CD147 is tightly associated with lactate transporters MCT1 and MCT4 and facilitates their cell surface expression

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

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4668-4678

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scholarly article

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10.1091/MBC.E12-06-0428

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24

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23

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Ethan J. Greenblatt

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2012-10-24T00:00:00Z

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23097496

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endoplasmic reticulum

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3521676

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