Temperature-induced reversible conformational change in the first 100 residues of alpha-synuclein.
about
Sequestration of a β-hairpin for control of α-synuclein aggregationSensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: implications for fibrillationFast hydrogen exchange affects ¹⁵N relaxation measurements in intrinsically disordered proteins.Early aggregation steps in alpha-synuclein as measured by FCS and FRET: evidence for a contagious conformational change.A bioreactor for in-cell protein NMR.α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomerA relationship between the transient structure in the monomeric state and the aggregation propensities of α-synuclein and β-synucleinDisordered Protein Diffusion under Crowded Conditions.Influence of crowded cellular environments on protein folding, binding, and oligomerization: biological consequences and potentials of atomistic modeling.Protein nuclear magnetic resonance under physiological conditionsEffects of Macromolecular Crowding on the Conformational Ensembles of Disordered Proteins.Mimicking the plant cell interior under water stress by macromolecular crowding: disordered dehydrin proteins are highly resistant to structural collapse.Differential dynamical effects of macromolecular crowding on an intrinsically disordered protein and a globular protein: implications for in-cell NMR spectroscopy.Hydrogen exchange of monomeric alpha-synuclein shows unfolded structure persists at physiological temperature and is independent of molecular crowding in Escherichia coli.In-cell protein NMR and protein leakageAlpha-, Beta-, and Gamma-synuclein Quantification in Cerebrospinal Fluid by Multiple Reaction Monitoring Reveals Increased Concentrations in Alzheimer's and Creutzfeldt-Jakob Disease but No Alteration in SynucleinopathiesAlpha-Synuclein conformation affects its tyrosine-dependent oxidative aggregation.NMR determination of pKa values in α-synuclein.Fluorescence spectroscopy reveals N-terminal order in fibrillar forms of α-synuclein.Using a FRET Library with Multiple Probe Pairs To Drive Monte Carlo Simulations of α-Synuclein.An NMR study of the N-terminal domain of wild-type hERG and a T65P trafficking deficient hERG mutant.
P2860
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P2860
Temperature-induced reversible conformational change in the first 100 residues of alpha-synuclein.
description
2006 nî lūn-bûn
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2006年の論文
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2006年学术文章
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2006年学术文章
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@zh-hans
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name
Temperature-induced reversible ...... 0 residues of alpha-synuclein.
@en
Temperature-induced reversible ...... 0 residues of alpha-synuclein.
@nl
type
label
Temperature-induced reversible ...... 0 residues of alpha-synuclein.
@en
Temperature-induced reversible ...... 0 residues of alpha-synuclein.
@nl
prefLabel
Temperature-induced reversible ...... 0 residues of alpha-synuclein.
@en
Temperature-induced reversible ...... 0 residues of alpha-synuclein.
@nl
P2093
P2860
P356
P1433
P1476
Temperature-induced reversible ...... 0 residues of alpha-synuclein.
@en
P2093
Ashutosh Tripathy
Brian C McNulty
Gary J Pielak
Gregory B Young
Jillian Orans
Lisa M Charlton
P2860
P304
P356
10.1110/PS.051867106
P577
2006-02-01T00:00:00Z