Rapid degradation of a large fraction of newly synthesized proteins by proteasomes.
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Folding efficiency is rate-limiting in dopamine D4 receptor biogenesismTORC2 can associate with ribosomes to promote cotranslational phosphorylation and stability of nascent Akt polypeptideDiversity in tissue expression, substrate binding, and SCF complex formation for a lectin family of ubiquitin ligasesUbiquitin receptor proteins hHR23a and hPLIC2 interactERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein degradation of misfolded surfactant protein CGlucocerebrosidase is shaking up the synucleinopathiesTranslational control in the stress adaptive response of cancer cells: a novel role for the heat shock protein TRAP126S proteasomes and immunoproteasomes produce mainly N-extended versions of an antigenic peptide.Subcellular recruitment of fibrillarin to nucleoplasmic proteasomes: implications for processing of a nucleolar autoantigen.Retroviruses have differing requirements for proteasome function in the budding processSystematic and quantitative assessment of the ubiquitin-modified proteomeProteasome inhibition interferes with gag polyprotein processing, release, and maturation of HIV-1 and HIV-2Autophagy and the ubiquitin-proteasome system: collaborators in neuroprotectionA novel mechanism for the regulation of amyloid precursor protein metabolismDEC-205 receptor on dendritic cells mediates presentation of HIV gag protein to CD8+ T cells in a spectrum of human MHC I haplotypesUnscrambling an egg: protein disaggregation by AAA+ proteinsRegulated interaction between polypeptide chain elongation factor-1 complex with the 26S proteasome during Xenopus oocyte maturationThe stress response against denatured proteins in the deletion of cytosolic chaperones SSA1/2 is different from heat-shock response in Saccharomyces cerevisiaeRibosome-based quality control of mRNA and nascent peptidesCHIP: A new modulator of human malignant disordersMitochondrial and Ubiquitin Proteasome System Dysfunction in Ageing and Disease: Two Sides of the Same Coin?DangER: protein ovERload. Targeting protein degradation to treat myelomaVirus budding and the ESCRT pathwayThe unfolded protein response in retinal vascular diseases: implications and therapeutic potential beyond protein foldingRegulation of cardiac proteasomes by ubiquitination, SUMOylation, and beyondMHC class I antigen processing and presenting machinery: organization, function, and defects in tumor cellsPharmacoperones: a new therapeutic approach for diseases caused by misfolded G protein-coupled receptorsDRiPs solidify: progress in understanding endogenous MHC class I antigen processingRoles for the ubiquitin-proteasome pathway in protein quality control and signaling in the retina: implications in the pathogenesis of age-related macular degenerationThe delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiologyThe Not4 RING E3 Ligase: A Relevant Player in Cotranslational Quality ControlNiclosamide prevents the formation of large ubiquitin-containing aggregates caused by proteasome inhibitionSpecific SKN-1/Nrf stress responses to perturbations in translation elongation and proteasome activityUbr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins.Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomesYeast Pth2 is a UBL domain-binding protein that participates in the ubiquitin-proteasome pathway.Analysis of polyubiquitin conjugates reveals that the Rpn10 substrate receptor contributes to the turnover of multiple proteasome targets.The promoter of filamentation (POF1) protein from Saccharomyces cerevisiae is an ATPase involved in the protein quality control process.A proteasomal ATPase contributes to dislocation of endoplasmic reticulum-associated degradation (ERAD) substrates.Yeast Uri1p promotes translation initiation and may provide a link to cotranslational quality control.
P2860
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P2860
Rapid degradation of a large fraction of newly synthesized proteins by proteasomes.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年学术文章
@wuu
2000年学术文章
@zh-cn
2000年学术文章
@zh-hans
2000年学术文章
@zh-my
2000年学术文章
@zh-sg
2000年學術文章
@yue
2000年學術文章
@zh
2000年學術文章
@zh-hant
name
Rapid degradation of a large fraction of newly synthesized proteins by proteasomes.
@en
type
label
Rapid degradation of a large fraction of newly synthesized proteins by proteasomes.
@en
prefLabel
Rapid degradation of a large fraction of newly synthesized proteins by proteasomes.
@en
P2093
P356
P1433
P1476
Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
@en
P2093
C C Norbury
J R Bennink
J W Yewdell
U Schubert
P2888
P304
P356
10.1038/35008096
P407
P577
2000-04-01T00:00:00Z
P5875
P6179
1045409760