SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins - Test2 - elhamkhani - TriplyDB

SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins

SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins

http://www.wikidata.org/entity/Q36858538

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A SEL1L mutation links a canine progressive early-onset cerebellar ataxia to the endoplasmic reticulum-associated protein degradation (ERAD) machinery TMTC1 and TMTC2 are novel endoplasmic reticulum tetratricopeptide repeat-containing adapter proteins involved in calcium homeostasis A high-coverage shRNA screen identifies TMEM129 as an E3 ligase involved in ER-associated protein degradation 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 MOR is not enough: identification of novel mu-opioid receptor interacting proteins using traditional and modified membrane yeast two-hybrid screens Spatial regulation of UBXD8 and p97/VCP controls ATGL-mediated lipid droplet turnover A luminal flavoprotein in endoplasmic reticulum-associated degradation The TRC8 E3 ligase ubiquitinates MHC class I molecules before dislocation from the ER Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER Ubiquilin and p97/VCP bind erasin, forming a complex involved in ERAD 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 Signal-peptide-mediated translocation is regulated by a p97-AIRAPL complex Pathogenic mutation of UBQLN2 impairs its interaction with UBXD8 and disrupts endoplasmic reticulum-associated protein degradation Unsaturated fatty acids inhibit proteasomal degradation of Insig-1 at a postubiquitination step Cancer Microenvironment and Endoplasmic Reticulum Stress Response Protein folding and quality control in the ER Recent technical developments in the study of ER-associated degradation The E2 ubiquitin-conjugating enzyme UBE2J1 is required for spermiogenesis in mice The RasGAP proteins Ira2 and neurofibromin are negatively regulated by Gpb1 in yeast and ETEA in humans.Varicella-Zoster Virus Infectious Cycle: ER Stress, Autophagic Flux, and Amphisome-Mediated Trafficking Arms Race between Enveloped Viruses and the Host ERAD Machinery Association of the SEL1L protein transmembrane domain with HRD1 ubiquitin ligase regulates ERAD-L Cleaning up in the endoplasmic reticulum: ubiquitin in charge Eeyarestatin 1 interferes with both retrograde and anterograde intracellular trafficking pathways Deficiency of suppressor enhancer Lin12 1 like (SEL1L) in mice leads to systemic endoplasmic reticulum stress and embryonic lethality Derlin-2-deficient mice reveal an essential role for protein dislocation in chondrocytes The ER-associated degradation adaptor protein Sel1L regulates LPL secretion and lipid metabolism Tay-Sachs disease mutations in HEXA target the α chain of hexosaminidase A to endoplasmic reticulum-associated degradation TMEM129 is a Derlin-1 associated ERAD E3 ligase essential for virus-induced degradation of MHC-I.Live cell imaging of protein dislocation from the endoplasmic reticulum.Monotopic topology is required for lipid droplet targeting of ancient ubiquitous protein 1 EDEM2 and OS-9 are required for ER-associated degradation of non-glycosylated sonic hedgehog.Huntingtin interacts with the cue domain of gp78 and inhibits gp78 binding to ubiquitin and p97/VCP.SEL1L deficiency impairs growth and differentiation of pancreatic epithelial cells.Ube2j2 ubiquitinates hydroxylated amino acids on ER-associated degradation substrates.Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates.A Mighty "Protein Extractor" of the Cell: Structure and Function of the p97/CDC48 ATPase.

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P2860

SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins

http://www.wikidata.org/entity/Q36858538

description

2008 nî lūn-bûn

@nan

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

2008年论文

@zh

2008年论文

@zh-cn

name

SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins

@en

type

label

SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins

@en

prefLabel

SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins

@en

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PNAS.0805371105

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins

@en

P2093

Britta Mueller

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

Elizabeth J Klemm

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

Eric Spooner

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

Hidde L Ploegh

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

Jasper H Claessen

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

P2860

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

A membrane protein required for dislocation of misfolded proteins from the ER

A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol

Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum

Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator

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

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

Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction

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

E2-25K mediates US11-triggered retro-translocation of MHC class I heavy chains in a permeabilized cell system

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12325-12330

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34

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105

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2008-08-18T00:00:00Z

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23178471

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18711132

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2527910

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