Oligomeric and polymeric aggregates formed by proteins containing expanded polyglutamine
about
Physio-pathological roles of transglutaminase-catalyzed reactionsPossible involvement of transglutaminase-catalyzed reactions in the physiopathology of neurodegenerative diseasesProteomic screening for amyloid proteinsPolyQ-expanded ataxin-3 interacts with full-length ataxin-3 in a polyQ length-dependent manner.Monomeric, oligomeric and polymeric proteins in huntington disease and other diseases of polyglutamine expansionPharmacological induction of heat-shock proteins alleviates polyglutamine-mediated motor neuron disease.Secondary structure and dynamics of an intrinsically unstructured linker domain.Integration-independent Transgenic Huntington Disease Fragment Mouse Models Reveal Distinct Phenotypes and Life Span in Vivo.Role of tissue transglutaminase type 2 in calbindin-D28k interaction with ataxin-1Xyloketal-derived small molecules show protective effect by decreasing mutant Huntingtin protein aggregates in Caenorhabditis elegans model of Huntington's disease.Tissue transglutaminase crosslinks ataxin-1: possible role in SCA1 pathogenesis.Aggregation of expanded huntingtin in the brains of patients with Huntington disease.Loss of Hsp70 exacerbates pathogenesis but not levels of fibrillar aggregates in a mouse model of Huntington's disease.Mechanism of cis-inhibition of polyQ fibrillation by polyP: PPII oligomers and the hydrophobic effect.From pathways to targets: understanding the mechanisms behind polyglutamine disease.Polyglutamine Aggregation in Huntington Disease: Does Structure Determine Toxicity?Role of tissue transglutaminase-2 (TG2)-mediated aminylation in biological processes.Detection of ubiquitinated huntingtin species in intracellular aggregates.Possible role of the transglutaminases in the pathogenesis of Alzheimer's disease and other neurodegenerative diseases.Protein aggregation and polyasparagine-mediated cellular toxicity in Saccharomyces cerevisiae.Prefibrillar huntingtin oligomers isolated from HD brain potently seed amyloid formation.
P2860
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P2860
Oligomeric and polymeric aggregates formed by proteins containing expanded polyglutamine
description
2003 nî lūn-bûn
@nan
2003 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Oligomeric and polymeric aggregates formed by proteins containing expanded polyglutamine
@ast
Oligomeric and polymeric aggregates formed by proteins containing expanded polyglutamine
@en
Oligomeric and polymeric aggregates formed by proteins containing expanded polyglutamine
@nl
type
label
Oligomeric and polymeric aggregates formed by proteins containing expanded polyglutamine
@ast
Oligomeric and polymeric aggregates formed by proteins containing expanded polyglutamine
@en
Oligomeric and polymeric aggregates formed by proteins containing expanded polyglutamine
@nl
prefLabel
Oligomeric and polymeric aggregates formed by proteins containing expanded polyglutamine
@ast
Oligomeric and polymeric aggregates formed by proteins containing expanded polyglutamine
@en
Oligomeric and polymeric aggregates formed by proteins containing expanded polyglutamine
@nl
P2093
P2860
P356
P1476
Oligomeric and polymeric aggregates formed by proteins containing expanded polyglutamine
@en
P2093
P2860
P304
P356
10.1073/PNAS.0437660100
P407
P577
2003-02-18T00:00:00Z