ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway.
about
Targeting proteins to the lumen of endoplasmic reticulum using N-terminal domains of 11beta-hydroxysteroid dehydrogenase and the 50-kDa esteraseThe endoplasmic reticulum chaperone glycoprotein GRP94 with Ca(2+)-binding and antiapoptotic properties is a novel proteolytic target of calpain during etoposide-induced apoptosisA membrane protein required for dislocation of misfolded proteins from the ERMembrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI)Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradationInduction of Grp78/BiP by translational block: activation of the Grp78 promoter by ATF4 through and upstream ATF/CRE site independent of the endoplasmic reticulum stress elementsHuman factor H deficiency. Mutations in framework cysteine residues and block in H protein secretion and intracellular catabolismInvolvement of valosin-containing protein, an ATPase Co-purified with IkappaBalpha and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalphaThe tissue-specific Rep8/UBXD6 tethers p97 to the endoplasmic reticulum membrane for degradation of misfolded proteinsMultiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane.The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding siteE2-25K mediates US11-triggered retro-translocation of MHC class I heavy chains in a permeabilized cell systemA conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradationThe N-end rule: functions, mysteries, usesOne step at a time: endoplasmic reticulum-associated degradationPNG1, a yeast gene encoding a highly conserved peptide:N-glycanaseThe cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome systemMisfolded proteins are sorted by a sequential checkpoint mechanism of ER quality controlAggregation and retention of human urokinase type plasminogen activator in the yeast endoplasmic reticulum.A molecular portrait of the response to unfolded proteinsUbiquitylation of an ERAD substrate occurs on multiple types of amino acidsRecent technical developments in the study of ER-associated degradationCan too many copies spoil the broth?The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiologyBrinp1(-/-) mice exhibit autism-like behaviour, altered memory, hyperactivity and increased parvalbumin-positive cortical interneuron densityStructure characterization of the 26S proteasome.A role for the DnaJ homologue Scj1p in protein folding in the yeast endoplasmic reticulum.In 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.Saccharomyces cerevisiae Rot1 is an essential molecular chaperone in the endoplasmic reticulumPreviously unknown role for the ubiquitin ligase Ubr1 in endoplasmic reticulum-associated protein degradation.Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins.Endoplasmic Reticulum-associated Degradation of Pca1p, a Polytopic Protein, via Interaction with the Proteasome at the MembraneSec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation.Sec61p is part of the endoplasmic reticulum-associated degradation machineryProtein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48.A regulatory link between ER-associated protein degradation and the unfolded-protein response.The conserved npl4 protein complex mediates proteasome-dependent membrane-bound transcription factor activation.The protein translocation channel binds proteasomes to the endoplasmic reticulum membraneMembrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation.
P2860
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P2860
ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway.
description
1996 nî lūn-bûn
@nan
1996 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի սեպտեմբերին 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
ER degradation of a misfolded ...... ubiquitin-proteasome pathway.
@ast
ER degradation of a misfolded ...... ubiquitin-proteasome pathway.
@en
ER degradation of a misfolded ...... ubiquitin-proteasome pathway.
@nl
type
label
ER degradation of a misfolded ...... ubiquitin-proteasome pathway.
@ast
ER degradation of a misfolded ...... ubiquitin-proteasome pathway.
@en
ER degradation of a misfolded ...... ubiquitin-proteasome pathway.
@nl
prefLabel
ER degradation of a misfolded ...... ubiquitin-proteasome pathway.
@ast
ER degradation of a misfolded ...... ubiquitin-proteasome pathway.
@en
ER degradation of a misfolded ...... ubiquitin-proteasome pathway.
@nl
P2093
P3181
P1433
P1476
ER degradation of a misfolded ...... ubiquitin-proteasome pathway.
@en
P2093
P304
P3181
P356
10.1126/SCIENCE.273.5282.1725
P407
P577
1996-09-20T00:00:00Z