about
The coexistence of an equal amount of Alzheimer's amyloid-β 40 and 42 forms structurally stable and toxic oligomers through a distinct pathwayAmyloid-beta (Aβ) D7H mutation increases oligomeric Aβ42 and alters properties of Aβ-zinc/copper assembliesDiscovery of dihydrochalcone as potential lead for Alzheimer's disease: in silico and in vitro studyAmyloid oligomer conformation in a group of natively folded proteins.Temperature-dependent structural changes of Parkinson's alpha-synuclein reveal the role of pre-existing oligomers in alpha-synuclein fibrillizationDiscovery of DNA dyes Hoechst 34580 and 33342 as good candidates for inhibiting amyloid beta formation: in silico and in vitro study.Alzheimer's amyloid-β A2T variant and its N-terminal peptides inhibit amyloid-β fibrillization and rescue the induced cytotoxicity.The Glycine-Alanine Dipeptide Repeat from C9orf72 Hexanucleotide Expansions Forms Toxic Amyloids Possessing Cell-to-Cell Transmission PropertiesThe truncated C-terminal RNA recognition motif of TDP-43 protein plays a key role in forming proteinaceous aggregates.In vitro prion-like behaviour of TDP-43 in ALS.Alzheimer's Amyloid-β Sequesters Caspase-3 in Vitro via Its C-Terminal Tail.Full-length TDP-43 forms toxic amyloid oligomers that are present in frontotemporal lobar dementia-TDP patients.Using optical profilometry to characterize cell membrane roughness influenced by amyloid-beta 42 aggregates and electric fields.A novel method for expression and purification of authentic amyloid-β with and without (15)N labels.Kinetic traps in the folding/unfolding of procaspase-1 CARD domain.Molecular structure of amyloid fibrils formed by residues 127 to 147 of the human prion protein.Removal of the pro-domain does not affect the conformation of the procaspase-3 dimer.Distinct early folding and aggregation properties of Alzheimer amyloid-beta peptides Abeta40 and Abeta42: stable trimer or tetramer formation by Abeta42.Lipid-Modified Graphene-Transistor Biosensor for Monitoring Amyloid-β Aggregation.Negatively charged gold nanoparticles inhibit Alzheimer's amyloid-β fibrillization, induce fibril dissociation, and mitigate neurotoxicity.Folding stability of amyloid-beta 40 monomer is an important determinant of the nucleation kinetics in fibrillization
P50
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P50
description
researcher ORCID ID = 0000-0002-6596-6338
@en
wetenschapper
@nl
name
Yun-Ru Chen
@ast
Yun-Ru Chen
@en
Yun-Ru Chen
@es
Yun-Ru Chen
@nl
type
label
Yun-Ru Chen
@ast
Yun-Ru Chen
@en
Yun-Ru Chen
@es
Yun-Ru Chen
@nl
prefLabel
Yun-Ru Chen
@ast
Yun-Ru Chen
@en
Yun-Ru Chen
@es
Yun-Ru Chen
@nl
P106
P31
P496
0000-0002-6596-6338