Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
about
The yeast split-ubiquitin membrane protein two-hybrid screen identifies BAP31 as a regulator of the turnover of endoplasmic reticulum-associated protein tyrosine phosphatase-like BStress-inducible protein 1 is a cell surface ligand for cellular prion that triggers neuroprotection.The concept of translocational regulationMinimotif miner 2nd release: a database and web system for motif searchUnfolded Protein Response and Macroautophagy in Alzheimer's, Parkinson's and Prion DiseasesLimited ER quality control for GPI-anchored proteins.The ubiquitin-proteasome system in spongiform degenerative disordersExpression of mutant or cytosolic PrP in transgenic mice and cells is not associated with endoplasmic reticulum stress or proteasome dysfunctionPronounced cytosolic aggregation of cellular prion protein in pancreatic beta-cells in response to hyperglycemiaThe Role of Unfolded Protein Response and Mitogen-Activated Protein Kinase Signaling in Neurodegenerative Diseases with Special Focus on Prion DiseasesFrom structure to redox: The diverse functional roles of disulfides and implications in disease.Cytoplasmic prion protein induces forebrain neurotoxicityFunctional depletion of mahogunin by cytosolically exposed prion protein contributes to neurodegenerationAlternative translation initiation generates cytoplasmic sheep prion protein.Selective processing and metabolism of disease-causing mutant prion proteins.The efficiency of protein compartmentalization into the secretory pathway.Perturbation of endoplasmic reticulum homeostasis facilitates prion replication.Signal sequence insufficiency contributes to neurodegeneration caused by transmembrane prion protein.Cell type-specific neuroprotective activity of untranslocated prion protein.Evasion of endoplasmic reticulum surveillance makes Wsc1p an obligate substrate of Golgi quality controlPrion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress.Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation.The ubiquitin-proteasome system in neurodegenerative diseases: precipitating factor, yet part of the solutionMetabolism of minor isoforms of prion proteins: Cytosolic prion protein and transmembrane prion proteinScrapie-like prion protein accumulates in aggresomes of cyclosporin A-treated cells.Detection of new quantitative trait Loci for susceptibility to transmissible spongiform encephalopathies in mice.Selective re-routing of prion protein to proteasomes and alteration of its vesicular secretion prevent PrP(Sc) formation.Development of kinomic analyses to identify dysregulated signaling pathways in cells expressing cytoplasmic PrP.The endoplasmic reticulum (ER)-associated degradation system regulates aggregation and degradation of mutant neuroserpin.Prion protein biosynthesis and its emerging role in neurodegeneration.Ubiquitin ligase gp78 targets unglycosylated prion protein PrP for ubiquitylation and degradation.The interplay of glycosylation and disulfide formation influences fibrillization in a prion protein fragment.Proteasomal dysfunction and endoplasmic reticulum stress enhance trafficking of prion protein aggregates through the secretory pathway and increase accumulation of pathologic prion proteinProtein folding as a driving force for dual protein targeting in eukaryotesPrion diseases: from molecular biology to intervention strategies.Ubiquitin-specific protease 14 modulates degradation of cellular prion proteinPhosphorothioate oligonucleotides reduce PrP levels and prion infectivity in cultured cells.Rational targeting for prion therapeutics.Mechanistic insights into the cure of prion disease by novel antiprion compoundsCytosol-endoplasmic reticulum interplay by Sec61alpha translocon in polyglutamine-mediated neurotoxicity in Drosophila.
P2860
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P2860
Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
description
2001 nî lūn-bûn
@nan
2001 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
@ast
Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
@en
Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
@nl
type
label
Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
@ast
Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
@en
Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
@nl
prefLabel
Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
@ast
Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
@en
Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
@nl
P2093
P2860
P3181
P356
P1433
P1476
Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
@en
P2093
P2860
P304
P3181
P356
10.1093/EMBOJ/20.19.5383
P407
P577
2001-10-01T00:00:00Z