Correlation of amyloid fibril beta-structure with the unfolded state of alpha-synuclein.
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Conformational equilibria in monomeric alpha-synuclein at the single-molecule levelSequestration of a β-hairpin for control of α-synuclein aggregationCold-induced changes in the protein ubiquitinImplications of protein structure instability: from physiological to pathological secondary structure.Sleep disorders in neurodegenerative diseases.The amyloidogenic SEVI precursor, PAP248-286, is highly unfolded in solution despite an underlying helical tendency.Cross dimerization of amyloid-β and αsynuclein proteins in aqueous environment: a molecular dynamics simulations study.Conformational and aggregation properties of the 1-93 fragment of apolipoprotein A-I.Proteasome inhibition induces α-synuclein SUMOylation and aggregate formation.A Monte Carlo Study of the Early Steps of Functional Amyloid FormationIdentification of minimally interacting modules in an intrinsically disordered protein.Transient β-hairpin formation in α-synuclein monomer revealed by coarse-grained molecular dynamics simulation.Short protein segments can drive a non-fibrillizing protein into the amyloid state.Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket.Treadmill exercise alleviates nigrostriatal dopaminergic loss of neurons and fibers in rotenone-induced Parkinson rats.Role of metal ions in aggregation of intrinsically disordered proteins in neurodegenerative diseases.Intrinsically disordered proteins: from sequence and conformational properties toward drug discovery.Electrochemical analysis of the fibrillation of Parkinson's disease α-synuclein.Investigation of the Polymeric Properties of α-Synuclein and Comparison with NMR Experiments: A Replica Exchange Molecular Dynamics Study.19F NMR studies of alpha-synuclein conformation and fibrillationCharacterization of conformational and dynamic properties of natively unfolded human and mouse alpha-synuclein ensembles by NMR: implication for aggregation.Mechanical resistance in unstructured proteins.Identification of fibril-like tertiary contacts in soluble monomeric α-synucleinStructural characterization of alpha-synuclein in an aggregation prone state.Distinct phases of free α-synuclein--a Monte Carlo study.Creation of aggregation-defective α-synuclein variants by engineering the sequence connecting β-strand-forming domains.DNP-Enhanced MAS NMR: A Tool to Snapshot Conformational Ensembles of α-Synuclein in Different States.Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH.Remaining structures at the N- and C-terminal regions of alpha-synuclein accurately elucidated by amide-proton exchange NMR with fitting.Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations
P2860
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P2860
Correlation of amyloid fibril beta-structure with the unfolded state of alpha-synuclein.
description
2007 nî lūn-bûn
@nan
2007 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի սեպտեմբերին 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
Correlation of amyloid fibril beta-structure with the unfolded state of alpha-synuclein.
@ast
Correlation of amyloid fibril beta-structure with the unfolded state of alpha-synuclein.
@en
Correlation of amyloid fibril beta-structure with the unfolded state of alpha-synuclein.
@nl
type
label
Correlation of amyloid fibril beta-structure with the unfolded state of alpha-synuclein.
@ast
Correlation of amyloid fibril beta-structure with the unfolded state of alpha-synuclein.
@en
Correlation of amyloid fibril beta-structure with the unfolded state of alpha-synuclein.
@nl
prefLabel
Correlation of amyloid fibril beta-structure with the unfolded state of alpha-synuclein.
@ast
Correlation of amyloid fibril beta-structure with the unfolded state of alpha-synuclein.
@en
Correlation of amyloid fibril beta-structure with the unfolded state of alpha-synuclein.
@nl
P50
P356
P1433
P1476
Correlation of amyloid fibril beta-structure with the unfolded state of alpha-synuclein.
@en
P2093
Hai-Young Kim
P304
P356
10.1002/CBIC.200700366
P577
2007-09-01T00:00:00Z