Expression of mutant or cytosolic PrP in transgenic mice and cells is not associated with endoplasmic reticulum stress or proteasome dysfunction

Expression of mutant or cytosolic PrP in transgenic mice and cells is not associated with endoplasmic reticulum stress or proteasome dysfunction

Item
http://www.wikidata.org/entity/Q28477995
Oral treatment targeting the unfolded protein response prevents neurodegeneration and clinical disease in prion-infected miceMutant PrP suppresses glutamatergic neurotransmission in cerebellar granule neurons by impairing membrane delivery of VGCC α(2)δ-1 SubunitRepurposed drugs targeting eIF2α-P-mediated translational repression prevent neurodegeneration in mice.Protein disulfide isomerase regulates endoplasmic reticulum stress and the apoptotic process during prion infection and PrP mutant-induced cytotoxicity.Snord 3A: a molecular marker and modulator of prion disease progressionMisfolded PrP impairs the UPS by interaction with the 20S proteasome and inhibition of substrate entryTransgenic fatal familial insomnia mice indicate prion infectivity-independent mechanisms of pathogenesis and phenotypic expression of disease.The elusive role of the prion protein and the mechanism of toxicity in prion disease.Familial prion protein mutants inhibit Hrd1-mediated retrotranslocation of misfolded proteins by depleting misfolded protein sensor BiP.Activation of the unfolded protein response and granulovacuolar degeneration are not common features of human prion pathology.Synaptic dysfunction in prion diseases: a trafficking problem?Misfolded PrP and a novel mechanism of proteasome inhibitionThe Protein-disulfide Isomerase ERp57 Regulates the Steady-state Levels of the Prion Protein.Misfolding leads the way to unraveling signaling pathways in the pathophysiology of prion diseases.Transgenic mice recapitulate the phenotypic heterogeneity of genetic prion diseases without developing prion infectivity: Role of intracellular PrP retention in neurotoxicityPrion-induced and spontaneous formation of transmissible toxicity in PrP transgenic Drosophila.Crosstalk between Endoplasmic Reticulum Stress and Protein Misfolding in Neurodegenerative Diseases
P2860

Expression of mutant or cytosolic PrP in transgenic mice and cells is not associated with endoplasmic reticulum stress or proteasome dysfunction

Item
http://www.wikidata.org/entity/Q28477995
description
2011 nî lūn-bûn
@nan
2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Expression of mutant or cytoso ...... ress or proteasome dysfunction
@ast
Expression of mutant or cytoso ...... ress or proteasome dysfunction
@en
Expression of mutant or cytoso ...... ress or proteasome dysfunction
@nl
type
label
Expression of mutant or cytoso ...... ress or proteasome dysfunction
@ast
Expression of mutant or cytoso ...... ress or proteasome dysfunction
@en
Expression of mutant or cytoso ...... ress or proteasome dysfunction
@nl
prefLabel
Expression of mutant or cytoso ...... ress or proteasome dysfunction
@ast
Expression of mutant or cytoso ...... ress or proteasome dysfunction
@en
Expression of mutant or cytoso ...... ress or proteasome dysfunction
@nl
P1433
P1476
P2093
P2860
P304
P31
P3181
P356
P407
P433
P478
P50
P577
P5875
P698
P921
P932
P3181
P356
P1433
P1476
Expression of mutant or cytoso ...... ress or proteasome dysfunction
@en
P2093
P2860
P304
P31
P3181
P356
10.1371/JOURNAL.PONE.0019339
P407
P433
P478
P50
P577
P5875
P698
P921
P932