An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel beta -fibrils.
about
Identification of human proteins that modify misfolding and proteotoxicity of pathogenic ataxin-1Valosin-containing protein (VCP/p97) is an activator of wild-type ataxin-3The role of the central flexible region on the aggregation and conformational properties of human ataxin-3An arginine/lysine-rich motif is crucial for VCP/p97-mediated modulation of ataxin-3 fibrillogenesis.Secondary Structure of Huntingtin Amino-Terminal RegionBeta conformation of polyglutamine track revealed by a crystal structure of Huntingtin N-terminal region with insertion of three histidine residuesExtended polyglutamine tracts cause aggregation and structural perturbation of an adjacent beta barrel protein.Trinucleotide repeats: a structural perspectiveParallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p.PolyQ-expanded ataxin-3 interacts with full-length ataxin-3 in a polyQ length-dependent manner.Stable polyglutamine dimers can contain β-hairpins with interdigitated side chains-but not α-helices, β-nanotubes, β-pseudohelices, or steric zippers.Monomeric, oligomeric and polymeric proteins in huntington disease and other diseases of polyglutamine expansionEnergy landscape of amyloidogenic peptide oligomerization by parallel-tempering molecular dynamics simulation: significant role of Asn ladder.Deubiquitinating function of ataxin-3: insights from the solution structure of the Josephin domain.The polyglutamine neurodegenerative protein ataxin 3 regulates aggresome formation.Genomic structure, promoter activity, and developmental expression of the mouse homologue of the Machado-Joseph disease (MJD) genePolyglutamine shows a urea-like affinity for unfolded cytosolic protein.The stability and dynamics of the human calcitonin amyloid peptide DFNKFA structural model of polyglutamine determined from a host-guest method combining experiments and landscape theory.p62/sequestosome 1 regulates aggresome formation of pathogenic ataxin-3 with expanded polyglutamineFunctional interactions as a survival strategy against abnormal aggregationSide-chain interactions determine amyloid formation by model polyglutamine peptides in molecular dynamics simulations.The Josephin domain determines the morphological and mechanical properties of ataxin-3 fibrils.Location trumps length: polyglutamine-mediated changes in folding and aggregation of a host proteinThe Toxic Effects of Pathogenic Ataxin-3 Variants in a Yeast Cellular ModelThe de novo synthesis of ubiquitin: identification of deubiquitinases acting on ubiquitin precursors.The Machado-Joseph Disease Deubiquitinase Ataxin-3 Regulates the Stability and Apoptotic Function of p53Machado-Joseph disease/spinocerebellar ataxia type 3.Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitroAggregation of polyglutamine-expanded ataxin-3 sequesters its specific interacting partners into inclusions: implication in a loss-of-function pathology.Polyglutamine diseases: where does toxicity come from? what is toxicity? where are we going?Current understanding on the pathogenesis of polyglutamine diseases.Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence.Polyglutamine Aggregation in Huntington Disease: Does Structure Determine Toxicity?Flanking domain stability modulates the aggregation kinetics of a polyglutamine disease proteinCompromised mitochondrial complex II in models of Machado-Joseph disease.The deubiquitinating enzyme ataxin-3, a polyglutamine disease protein, edits Lys63 linkages in mixed linkage ubiquitin chains.Striatal and nigral pathology in a lentiviral rat model of Machado-Joseph disease.Kaposi's sarcoma-associated herpesvirus latency-associated nuclear antigen 1 mimics Epstein-Barr virus EBNA1 immune evasion through central repeat domain effects on protein processing.Defining the role of ubiquitin-interacting motifs in the polyglutamine disease protein, ataxin-3.
P2860
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P2860
An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel beta -fibrils.
description
2001 nî lūn-bûn
@nan
2001 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի սեպտեմբերին 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
An expanded glutamine repeat d ...... ion of parallel beta -fibrils.
@ast
An expanded glutamine repeat d ...... ion of parallel beta -fibrils.
@en
type
label
An expanded glutamine repeat d ...... ion of parallel beta -fibrils.
@ast
An expanded glutamine repeat d ...... ion of parallel beta -fibrils.
@en
prefLabel
An expanded glutamine repeat d ...... ion of parallel beta -fibrils.
@ast
An expanded glutamine repeat d ...... ion of parallel beta -fibrils.
@en
P2860
P356
P1476
An expanded glutamine repeat d ...... ion of parallel beta -fibrils.
@en
P2093
A E Bevivino
P2860
P304
11955-11960
P356
10.1073/PNAS.211305198
P407
P577
2001-09-25T00:00:00Z