about
Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer's diseaseChaperones as Suppressors of Protein Misfolded Oligomer ToxicityBis(indolyl)phenylmethane derivatives are effective small molecules for inhibition of amyloid fibril formation by hen lysozyme.Toxicity of protein oligomers is rationalized by a function combining size and surface hydrophobicity.Transthyretin suppresses the toxicity of oligomers formed by misfolded proteins in vitro.Toxic HypF-N Oligomers Selectively Bind the Plasma Membrane to Impair Cell Adhesion Capability.Stabilization and Characterization of Cytotoxic Aβ40 Oligomers Isolated from an Aggregation Reaction in the Presence of Zinc IonsMultistep Inhibition of α-Synuclein Aggregation and Toxicity in Vitro and in Vivo by TrodusquemineTrodusquemine enhances Aβ aggregation but suppresses its toxicity by displacing oligomers from cell membranesDifferential Interactome and Innate Immune Response Activation of Two Structurally Distinct Misfolded Protein OligomersProteome-wide observation of the phenomenon of life on the edge of solubilityRational design of a conformation-specific antibody for the quantification of Aβ oligomersSingle molecule secondary structure determination of proteins through infrared absorption nanospectroscopy
P50
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P50
description
onderzoeker
@nl
researcher ORCID ID = 0000-0001-6812-7348
@en
name
Benedetta Mannini
@ast
Benedetta Mannini
@en
Benedetta Mannini
@es
Benedetta Mannini
@nl
type
label
Benedetta Mannini
@ast
Benedetta Mannini
@en
Benedetta Mannini
@es
Benedetta Mannini
@nl
prefLabel
Benedetta Mannini
@ast
Benedetta Mannini
@en
Benedetta Mannini
@es
Benedetta Mannini
@nl
P106
P31
P496
0000-0001-6812-7348