about
Conformational dynamics of the frameshift stimulatory structure in HIV-1.Partially native intermediates mediate misfolding of SOD1 in single-molecule folding trajectories.Structural characteristics and membrane interactions of tandem α-synuclein oligomers.Testing Kinetic Identities Involving Transition-Path Properties Using Single-Molecule Folding TrajectoriesEarly stages of aggregation of engineered α-synuclein monomers and oligomers in solutionCharacterizing the inhibition of α-synuclein oligomerization by a pharmacological chaperone that prevents prion formation by the protein PrP
P50
description
researcher
@en
wetenschapper
@nl
name
Michael T Woodside
@en
Michael T Woodside
@nl
type
label
Michael T Woodside
@en
Michael T Woodside
@nl
prefLabel
Michael T Woodside
@en
Michael T Woodside
@nl
P31
P496
0000-0003-4695-0397