about
Structural basis for increased toxicity of pathological aβ42:aβ40 ratios in Alzheimer disease.Heme Stabilization of α-Synuclein Oligomers during Amyloid Fibril Formation.Europium as an inhibitor of Amyloid-β(1-42) induced membrane permeationA central role for dityrosine crosslinking of Amyloid-β in Alzheimer's disease.Membrane and surface interactions of Alzheimer's Aβ peptide--insights into the mechanism of cytotoxicity.Visualization of co-localization in Aβ42-administered neuroblastoma cells reveals lysosome damage and autophagosome accumulation related to cell death.Stabilization of native amyloid β-protein oligomers by Copper and Hydrogen peroxide Induced Cross-linking of Unmodified Proteins (CHICUP).Soluble Prion Protein Binds Isolated Low Molecular Weight Amyloid-β Oligomers Causing Cytotoxicity Inhibition.Effects of Aβ exposure on long-term associative memory and its neuronal mechanisms in a defined neuronal networkCharacterizing the assembly of the Sup35 yeast prion fragment, GNNQQNY: structural changes accompany a fiber-to-crystal switch.Measurement of the binding of cholera toxin to GM1 gangliosides on solid supported lipid bilayer vesicles and inhibition by europium (III) chloride.Elucidation of insulin assembly at acidic and neutral pH: Characterization of low molecular weight oligomers.Fluorophore-encapsulated solid-supported bilayer vesicles: a method for studying membrane permeation processes.Aβ42 oligomers, but not fibrils, simultaneously bind to and cause damage to ganglioside-containing lipid membranes.The Effect of Alzheimer’s Aβ Aggregation State on the Permeation of Biomimetic Lipid VesiclesFabrication and Application of Surface-Tethered Vesicles
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description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Thomas L Williams
@ast
Thomas L Williams
@en
Thomas L Williams
@es
Thomas L Williams
@nl
type
label
Thomas L Williams
@ast
Thomas L Williams
@en
Thomas L Williams
@es
Thomas L Williams
@nl
prefLabel
Thomas L Williams
@ast
Thomas L Williams
@en
Thomas L Williams
@es
Thomas L Williams
@nl
P108
P106
P108
P1153
56391144900
P31
P496
0000-0003-1710-3914