Serine residues in the cytosolic tail of the T-cell antigen receptor alpha-chain mediate ubiquitination and endoplasmic reticulum-associated degradation of the unassembled protein.
about
Deubiquitinases sharpen substrate discrimination during membrane protein degradation from the ERHECT and RING finger families of E3 ubiquitin ligases at a glanceUbiquitylation of an ERAD substrate occurs on multiple types of amino acidsProtein folding and quality control in the ERThe delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiologyThe predator becomes the prey: regulating the ubiquitin system by ubiquitylation and degradationDegradation-mediated protein quality control at the inner nuclear membraneEndoplasmic reticulum-associated ubiquitin-conjugating enzyme Ube2j1 is a novel substrate of MK2 (MAPKAP kinase-2) involved in MK2-mediated TNFα productionCleaning up in the endoplasmic reticulum: ubiquitin in chargeUbiquitin-dependent proteasomal degradation of human liver cytochrome P450 2E1: identification of sites targeted for phosphorylation and ubiquitinationKLHL12 Promotes Non-Lysine Ubiquitination of the Dopamine Receptors D4.2 and D4.4, but Not of the ADHD-Associated D4.7 VariantDefective transport of the obesity mutant PC1/3 N222D contributes to loss of function.Ubiquitylation in ERAD: reversing to go forward?Lys11- and Lys48-linked ubiquitin chains interact with p97 during endoplasmic-reticulum-associated degradation.The Unfolded Protein Response, Degradation from Endoplasmic Reticulum and CancerPiecing together the family portrait of TCR-CD3 complexes.Protein folding and quality control in the endoplasmic reticulum: Recent lessons from yeast and mammalian cell systems.What has the study of the K3 and K5 viral ubiquitin E3 ligases taught us about ubiquitin-mediated receptor regulation?gp78 functions downstream of Hrd1 to promote degradation of misfolded proteins of the endoplasmic reticulumHrd1 and ER-Associated Protein Degradation, ERAD, are Critical Elements of the Adaptive ER Stress Response in Cardiac MyocytesMeans of self-preservation: how an intrinsically disordered ubiquitin-protein ligase averts self-destruction.Decoupling the role of ubiquitination for the dislocation versus degradation of major histocompatibility complex (MHC) class I proteins during endoplasmic reticulum-associated degradation (ERAD)MHC class I molecules are preferentially ubiquitinated on endoplasmic reticulum luminal residues during HRD1 ubiquitin E3 ligase-mediated dislocation.TEC and MAPK Kinase Signalling Pathways in T helper (TH) cell Development, TH2 Differentiation and Allergic Asthma.Ubiquitination of substrates by esterification.Protein quality control in the ER: balancing the ubiquitin checkbook.Chemistry and biology of the ubiquitin signal.The exportomer: the peroxisomal receptor export machinery.Specificity and regulation of the endoplasmic reticulum-associated degradation machinery.Regulation of Endoplasmic Reticulum-Associated Protein Degradation (ERAD) by Ubiquitin.The evolving role of ubiquitin modification in endoplasmic reticulum-associated degradation.Membrane Protein Quantity Control at the Endoplasmic Reticulum.E3 ubiquitin ligases: ubiquitous actors in plant development and abiotic stress responses.ERAD of proteins containing aberrant transmembrane domains requires ubiquitylation of cytoplasmic lysine residues.Lysine Residues Are Not Required for Proteasome-Mediated Proteolysis of the Auxin/Indole Acidic Acid Protein IAA1.Hepatic cytochromes P450: structural degrons and barcodes, posttranslational modifications and cellular adapters in the ERAD-endgame.Atypical ubiquitylation in yeast targets lysine-less Asi2 for proteasomal degradation.Just a trim, please: refining ER degradation through deubiquitination.Quality control of integral membrane proteins by assembly-dependent membrane integration.A Novel Peptide-Based SILAC Method to Identify the Posttranslational Modifications Provides Evidence for Unconventional Ubiquitination in the ER-Associated Degradation Pathway.
P2860
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P2860
Serine residues in the cytosolic tail of the T-cell antigen receptor alpha-chain mediate ubiquitination and endoplasmic reticulum-associated degradation of the unassembled protein.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Serine residues in the cytosol ...... on of the unassembled protein.
@ast
Serine residues in the cytosol ...... on of the unassembled protein.
@en
Serine residues in the cytosol ...... on of the unassembled protein.
@nl
type
label
Serine residues in the cytosol ...... on of the unassembled protein.
@ast
Serine residues in the cytosol ...... on of the unassembled protein.
@en
Serine residues in the cytosol ...... on of the unassembled protein.
@nl
prefLabel
Serine residues in the cytosol ...... on of the unassembled protein.
@ast
Serine residues in the cytosol ...... on of the unassembled protein.
@en
Serine residues in the cytosol ...... on of the unassembled protein.
@nl
P2093
P2860
P356
P1476
Serine residues in the cytosol ...... on of the unassembled protein.
@en
P2093
Allan M Weissman
Juan S Bonifacino
Shuhei Ishikura
P2860
P304
23916-23924
P356
10.1074/JBC.M110.127936
P407
P577
2010-06-02T00:00:00Z