Conformational ensemble of native α-synuclein in solution as determined by short-distance crosslinking constraint-guided discrete molecular dynamics simulations.
Brodie, Nicholas I; Popov, Konstantin I; Petrotchenko, Evgeniy V; Dokholyan, Nikolay V; Borchers, Christoph H.
PLoS Comput Biol
; 15(3): e1006859, 2019 03.
Artigo em Inglês | MEDLINE | ID: mdl-30917118
Conformational dynamics of α-synuclein: insights from mass spectrometry.
Structural characterization of the interaction of α-synuclein nascent chains with the ribosomal surface and trigger factor.
Dynamical properties of α-synuclein in soluble and fibrillar forms by Quasi Elastic Neutron Scattering.
Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation.
Interplay between desolvation and secondary structure in mediating cosolvent and temperature induced alpha-synuclein aggregation.
Membrane remodeling and mechanics: Experiments and simulations of α-Synuclein.
Morphological Evaluation of Meta-stable Oligomers of α-Synuclein with Small-Angle Neutron Scattering.
A relationship between the transient structure in the monomeric state and the aggregation propensities of α-synuclein and ß-synuclein.
Structural features of α-synuclein amyloid fibrils revealed by Raman spectroscopy.
Amyloid fibril structure of α-synuclein determined by cryo-electron microscopy.