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- 2019
- Increased Secondary Nucleation Underlies Accelerated Aggregation of the Four-Residue N-Terminally Truncated Aβ42 Species Aβ5-42
- Secondary nucleation and elongation occur at different sites on Alzheimer's amyloid-b aggregates
- Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes
- 2018
- SAR by kinetics for drug discovery in protein misfolding diseases
- Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide
- Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes
- 2017
- Modulation of electrostatic interactions to reveal a reaction network unifying the aggregation behaviour of the Aβ42 peptide and its variants
- Monomeric and fibrillar α-synuclein exert opposite effects on the catalytic cycle that promotes the proliferation of Aβ42 aggregates
- Selective targeting of primary and secondary nucleation pathways in Ab42 aggregation using a rational antibody scanning method
- Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication
- Scaling behaviour and rate-determining steps in filamentous self-assembly
- Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer's disease
- 2016
- Physical determinants of the self-replication of protein fibrils
- Molecular mechanisms of protein aggregation from global fitting of kinetic models.
- Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of α-synuclein
- Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation
- Microfluidic Diffusion Analysis of the Sizes and Interactions of Proteins under Native Solution Conditions.
- An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer's disease.
- The S/T-Rich Motif in the DNAJB6 Chaperone Delays Polyglutamine Aggregation and the Onset of Disease in a Mouse Model
- 2015
- Latent analysis of unmodified biomolecules and their complexes in solution with attomole detection sensitivity
- Protein Microgels from Amyloid Fibril Networks
- A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers.
- 2014
- Solution conditions determine the relative importance of nucleation and growth processes in alpha-synuclein aggregation
- Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides.
- Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation.
- 2013
- Proliferation of amyloid-beta 42 aggregates occurs through a secondary nucleation mechanism
- 2010
- Local Cooperativity in an Amyloidogenic State of Human Lysozyme Observed at Atomic Resolution.