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

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

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

http://www.wikidata.org/entity/Q24312778

about

A SEL1L mutation links a canine progressive early-onset cerebellar ataxia to the endoplasmic reticulum-associated protein degradation (ERAD) machinery Endoplasmic reticulum stress and Parkinson's disease: the role of HRD1 in averting apoptosis in neurodegenerative disease Identification of the PDI-family member ERp90 as an interaction partner of ERFAD TMTC1 and TMTC2 are novel endoplasmic reticulum tetratricopeptide repeat-containing adapter proteins involved in calcium homeostasis Defining human ERAD networks through an integrative mapping strategy SEL1L protein critically determines the stability of the HRD1-SEL1L endoplasmic reticulum-associated degradation (ERAD) complex to optimize the degradation kinetics of ERAD substrates SGTA recognizes a noncanonical ubiquitin-like domain in the Bag6-Ubl4A-Trc35 complex to promote endoplasmic reticulum-associated degradation Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation steps A luminal flavoprotein in endoplasmic reticulum-associated degradation Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans The UBX protein SAKS1 negatively regulates endoplasmic reticulum-associated degradation and p97-dependent degradation An endoplasmic reticulum (ER) membrane complex composed of SPFH1 and SPFH2 mediates the ER-associated degradation of inositol 1,4,5-trisphosphate receptors Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP ERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein degradation of misfolded surfactant protein C Protein disulphide isomerase is required for signal peptide peptidase-mediated protein degradation 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 A deubiquitinase negatively regulates retro-translocation of nonubiquitinated substrates HRD1 and UBE2J1 target misfolded MHC class I heavy chains for endoplasmic reticulum-associated degradation EDEM1 recognition and delivery of misfolded proteins to the SEL1L-containing ERAD complex Folding-competent and folding-defective forms of ricin A chain have different fates after retrotranslocation from the endoplasmic reticulum Histone deacetylase inhibitor (HDACi) suberoylanilide hydroxamic acid (SAHA)-mediated correction of α1-antitrypsin deficiency Cytosolic chaperones influence the fate of a toxin dislocated from the endoplasmic reticulum Combinatorial drug design targeting multiple cancer signaling networks controlled by mitochondrial Hsp90 One step at a time: endoplasmic reticulum-associated degradation Glycoprotein Quality Control and Endoplasmic Reticulum Stress Protein folding and quality control in the ER Recent technical developments in the study of ER-associated degradation Selective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradation Molecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradation GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum Road to ruin: targeting proteins for degradation in the endoplasmic reticulum The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology The E2 ubiquitin-conjugating enzyme UBE2J1 is required for spermiogenesis in mice Tyrosinase degradation is prevented when EDEM1 lacks the intrinsically disordered region How Polyomaviruses Exploit the ERAD Machinery to Cause Infection Structural and Biochemical Basis of Yos9 Protein Dimerization and Possible Contribution to Self-association of 3-Hydroxy-3-methylglutaryl-Coenzyme A Reductase Degradation Ubiquitin-Ligase Complex A novel role for Gtb1p in glucose trimming of N-linked glycans.Five Questions (with their Answers) on ER-Associated Degradation Arms Race between Enveloped Viruses and the Host ERAD Machinery Myelin-associated glycoprotein gene mutation causes Pelizaeus-Merzbacher disease-like disorder

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P2860

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

http://www.wikidata.org/entity/Q24312778

description

2008 nî lūn-bûn

@nan

2008 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի մարտին հրատարակված գիտական հոդված

@hy

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

OS-9 and GRP94 deliver mutant ...... quitin ligase complex for ERAD

@ast

OS-9 and GRP94 deliver mutant ...... quitin ligase complex for ERAD

@en

OS-9 and GRP94 deliver mutant ...... quitin ligase complex for ERAD

@en-gb

OS-9 and GRP94 deliver mutant ...... quitin ligase complex for ERAD

@nl

type

label

OS-9 and GRP94 deliver mutant ...... quitin ligase complex for ERAD

@ast

OS-9 and GRP94 deliver mutant ...... quitin ligase complex for ERAD

@en

OS-9 and GRP94 deliver mutant ...... quitin ligase complex for ERAD

@en-gb

OS-9 and GRP94 deliver mutant ...... quitin ligase complex for ERAD

@nl

prefLabel

OS-9 and GRP94 deliver mutant ...... quitin ligase complex for ERAD

@ast

OS-9 and GRP94 deliver mutant ...... quitin ligase complex for ERAD

@en

OS-9 and GRP94 deliver mutant ...... quitin ligase complex for ERAD

@en-gb

OS-9 and GRP94 deliver mutant ...... quitin ligase complex for ERAD

@nl

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P356

P1433

Nature Cell Biology

P1476

OS-9 and GRP94 deliver mutant ...... quitin ligase complex for ERAD

@en

P2093

John C Christianson

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

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

P2860

Hsp90: a specialized but essential protein-folding tool

OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha

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

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

The MRH protein Erlectin is a member of the endoplasmic reticulum synexpression group and functions in N-glycan recognition

Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane.

Heat shock protein gp96 is a master chaperone for toll-like receptors and is important in the innate function of macrophages

Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells

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

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

P2888

P304

272-82

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

P31

scholarly article

P3181

881482

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

P356

10.1038/NCB1689

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

P407

P433

3

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

P478

10

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

P577

2008-03-01T00:00:00Z

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

P5875

5588213

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

P6179

1009760622

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

P698

18264092

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

P921

OS9 endoplasmic reticulum lectin

Heat shock protein 90 beta family member 1

Endoplasmic reticulum lectin 1

P932

2757077

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