Characterization of conformational and dynamic properties of natively unfolded human and mouse alpha-synuclein ensembles by NMR: implication for aggregation.
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Exploring the accessible conformations of N-terminal acetylated α-synucleinFast hydrogen exchange affects ¹⁵N relaxation measurements in intrinsically disordered proteins.Protein (19)F NMR in Escherichia coliThe amyloidogenic SEVI precursor, PAP248-286, is highly unfolded in solution despite an underlying helical tendency.α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomerEffect of spermidine on misfolding and interactions of alpha-synucleinEffects of molecular crowding on the dynamics of intrinsically disordered proteins.The α-helical C-terminal domain of full-length recombinant PrP converts to an in-register parallel β-sheet structure in PrP fibrils: evidence from solid state nuclear magnetic resonance.Augmentation of phenotype in a transgenic Parkinson mouse heterozygous for a Gaucher mutationConformational and aggregation properties of the 1-93 fragment of apolipoprotein A-I.Temperature-dependent structural changes of Parkinson's alpha-synuclein reveal the role of pre-existing oligomers in alpha-synuclein fibrillizationPhenolic compounds prevent the oligomerization of α-synuclein and reduce synaptic toxicity.Characterization of a disordered protein during micellation: interactions of α-synuclein with sodium dodecyl sulfate.Identification of minimally interacting modules in an intrinsically disordered protein.Fibril formation from the amyloid-β peptide is governed by a dynamic equilibrium involving association and dissociation of the monomer.Biophysical characterization of intrinsically disordered proteins.Recent advances in α-synuclein functions, advanced glycation, and toxicity: implications for Parkinson's disease.α-Synuclein Misfolding Versus Aggregation Relevance to Parkinson's Disease: Critical Assessment and Modeling.Implication of Alpha-Synuclein Phosphorylation at S129 in Synucleinopathies: What Have We Learned in the Last Decade?The A53T mutation is key in defining the differences in the aggregation kinetics of human and mouse α-synuclein.Cell Biology and Pathophysiology of α-Synuclein.Coupling of the non-amyloid-component (NAC) domain and the KTK(E/Q)GV repeats stabilize the α-synuclein fibrils.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 fibrillationSaliva α-Synuclein and A High Extinction Coefficient Protein: A Novel Approach in Assessment Biomarkers of Parkinson's Disease.Mechanical resistance in unstructured proteins.Helix stabilization precedes aqueous and bilayer-catalyzed fiber formation in islet amyloid polypeptideA pH-dependent switch promotes β-synuclein fibril formation via glutamate residues.Structural reorganization of alpha-synuclein at low pH observed by NMR and REMD simulations.E46K Parkinson's-linked mutation enhances C-terminal-to-N-terminal contacts in alpha-synucleinDetection of transient interchain interactions in the intrinsically disordered protein alpha-synuclein by NMR paramagnetic relaxation enhancement.Backbone assignment and dynamics of human α-synuclein in viscous 2 M glucose solution.Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: insight into intrinsically disordered proteins.Competition between intramolecular and intermolecular interactions in an amyloid-forming protein.Distinct phases of free α-synuclein--a Monte Carlo study.Collagen mimetic peptide discs promote assembly of a broad range of natural protein fibers through hydrophobic interactions.Equilibrium properties of realistic random heteropolymers and their relevance for globular and naturally unfolded proteins.Small Molecules Attenuate the Interplay between Conformational Fluctuations, Early Oligomerization and Amyloidosis of Alpha Synuclein.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.
P2860
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P2860
Characterization of conformational and dynamic properties of natively unfolded human and mouse alpha-synuclein ensembles by NMR: implication for aggregation.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Characterization of conformati ...... : implication for aggregation.
@en
Characterization of conformati ...... : implication for aggregation.
@nl
type
label
Characterization of conformati ...... : implication for aggregation.
@en
Characterization of conformati ...... : implication for aggregation.
@nl
prefLabel
Characterization of conformati ...... : implication for aggregation.
@en
Characterization of conformati ...... : implication for aggregation.
@nl
P2093
P2860
P1476
Characterization of conformati ...... R: implication for aggregation
@en
P2093
P2860
P304
P356
10.1016/J.JMB.2008.03.017
P407
P50
P577
2008-03-18T00:00:00Z