The ubiquitin proteasome system in Huntington's disease and the spinocerebellar ataxias
about
The importance of integrating basic and clinical research toward the development of new therapies for Huntington diseasePhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Formation and toxicity of soluble polyglutamine oligomers in living cells.The ubiquitin system, disease, and drug discovery.Activation of proteasome by insulin-like growth factor-I may enhance clearance of oxidized proteins in the brain.Early autophagic response in a novel knock-in model of Huntington diseaseHuntington's disease (HD): degeneration of select nuclei, widespread occurrence of neuronal nuclear and axonal inclusions in the brainstem.Profiling ubiquitin linkage specificities of deubiquitinating enzymes with branched ubiquitin isopeptide probes.Curcumin prevents formation of polyglutamine aggregates by inhibiting Vps36, a component of the ESCRT-II complex.Human Umbilical Tissue-Derived Cells Promote Synapse Formation and Neurite Outgrowth via Thrombospondin Family ProteinsEmerging evidence of coding mutations in the ubiquitin-proteasome system associated with cerebellar ataxiasNetwork analysis of human post-mortem microarrays reveals novel genes, microRNAs, and mechanistic scenarios of potential importance in fighting huntington's disease.Basic mechanisms of neurodegeneration: a critical update.Bringing natural products into the fold - exploring the therapeutic lead potential of secondary metabolites for the treatment of protein-misfolding-related neurodegenerative diseases.Convergent pathogenic pathways in Alzheimer's and Huntington's diseases: shared targets for drug development.Studying polyglutamine diseases in Drosophila.Ubiquitin C-terminal electrophiles are activity-based probes for identification and mechanistic study of ubiquitin conjugating machinery.Inhibition of Rho kinases enhances the degradation of mutant huntingtin.Hsp104 is essential for the selective degradation in yeast of polyglutamine expanded ataxin-1 but not most misfolded proteins generally.Cellular protein quality control and the evolution of aggregates in spinocerebellar ataxia type 3 (SCA3).
P2860
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P2860
The ubiquitin proteasome system in Huntington's disease and the spinocerebellar ataxias
description
2007 nî lūn-bûn
@nan
2007 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
The ubiquitin proteasome system in Huntington's disease and the spinocerebellar ataxias
@ast
The ubiquitin proteasome system in Huntington's disease and the spinocerebellar ataxias
@en
The ubiquitin proteasome system in Huntington's disease and the spinocerebellar ataxias.
@nl
type
label
The ubiquitin proteasome system in Huntington's disease and the spinocerebellar ataxias
@ast
The ubiquitin proteasome system in Huntington's disease and the spinocerebellar ataxias
@en
The ubiquitin proteasome system in Huntington's disease and the spinocerebellar ataxias.
@nl
prefLabel
The ubiquitin proteasome system in Huntington's disease and the spinocerebellar ataxias
@ast
The ubiquitin proteasome system in Huntington's disease and the spinocerebellar ataxias
@en
The ubiquitin proteasome system in Huntington's disease and the spinocerebellar ataxias.
@nl
P2093
P2860
P921
P1433
P1476
The ubiquitin proteasome system in Huntington's disease and the spinocerebellar ataxias
@en
P2093
David C Rubinsztein
Janet E Davies
Sovan Sarkar
P2860
P2888
P356
10.1186/1471-2091-8-S1-S2
P478
P5008
P577
2007-11-22T00:00:00Z
P6179
1040446072