Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway.
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The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding siteAlpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's modelsIn vivo action of the HRD ubiquitin ligase complex: mechanisms of endoplasmic reticulum quality control and sterol regulation.Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation.The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitmentThe yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degronAn HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transportUbc8p functions in catabolite degradation of fructose-1, 6-bisphosphatase in yeastDer3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins.A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradationA Complex of Htm1 and the Oxidoreductase Pdi1 Accelerates Degradation of Misfolded Glycoproteins.The deubiquitinating enzyme Ubp1 affects sorting of the ATP-binding cassette-transporter Ste6 in the endocytic pathway.INSIG: a broadly conserved transmembrane chaperone for sterol-sensing domain proteinsYos9p assists in the degradation of certain nonglycosylated proteins from the endoplasmic reticulumCatabolite inactivation of the galactose transporter in the yeast Saccharomyces cerevisiae: ubiquitination, endocytosis, and degradation in the vacuoleDegradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure.Sec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane.Ubx4 modulates cdc48 activity and influences degradation of misfolded proteins of the endoplasmic reticulumHtm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding.Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6pAnalysis of ER resident proteins in Saccharomyces cerevisiae: implementation of H/KDEL retrieval sequences.BiP clustering facilitates protein folding in the endoplasmic reticulumDegradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiaeUsa1 protein facilitates substrate ubiquitylation through two separate domainsUsa1p is required for optimal function and regulation of the Hrd1p endoplasmic reticulum-associated degradation ubiquitin ligase.Role for the ubiquitin-proteasome system in the vacuolar degradation of Ste6p, the a-factor transporter in Saccharomyces cerevisiaePolyubiquitination is required for US11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosolThe yeast C-type cyclin Ctk2p is phosphorylated and rapidly degraded by the ubiquitin-proteasome pathway.TRAM1 is involved in disposal of ER membrane degradation substrates.Analysis of the key elements of FFAT-like motifs identifies new proteins that potentially bind VAP on the ER, including two AKAPs and FAPP2.Mutant membrane protein of the budding yeast spindle pole body is targeted to the endoplasmic reticulum degradation pathway.Degradation of unassembled Vph1p reveals novel aspects of the yeast ER quality control system.Exposed hydrophobicity is a key determinant of nuclear quality control degradation.For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection.Ubiquitin-dependent protein degradation at the yeast endoplasmic reticulum and nuclear envelope.Translocation channel gating kinetics balances protein translocation efficiency with signal sequence recognition fidelityParathyroid hormone leads to the lysosomal degradation of the renal type II Na/Pi cotransporterFlip-flop of fluorescently labeled phospholipids in proteoliposomes reconstituted with Saccharomyces cerevisiae microsomal proteins.Dislocation of type I membrane proteins from the ER to the cytosol is sensitive to changes in redox potential.
P2860
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P248
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P2860
Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway.
description
1996 nî lūn-bûn
@nan
1996 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Degradation of subunits of the ...... ubiquitin-proteasome pathway.
@ast
Degradation of subunits of the ...... ubiquitin-proteasome pathway.
@en
Degradation of subunits of the ...... ubiquitin-proteasome pathway.
@nl
type
label
Degradation of subunits of the ...... ubiquitin-proteasome pathway.
@ast
Degradation of subunits of the ...... ubiquitin-proteasome pathway.
@en
Degradation of subunits of the ...... ubiquitin-proteasome pathway.
@nl
prefLabel
Degradation of subunits of the ...... ubiquitin-proteasome pathway.
@ast
Degradation of subunits of the ...... ubiquitin-proteasome pathway.
@en
Degradation of subunits of the ...... ubiquitin-proteasome pathway.
@nl
P2093
P2860
P1433
P1476
Degradation of subunits of the ...... e ubiquitin-proteasome pathway
@en
P2093
P2860
P304
P356
10.1002/J.1460-2075.1996.TB00560.X
P407
P577
1996-05-01T00:00:00Z