1 – 36 of 36
- show: 250
- |
- sort: year (new to old)
Close
Embed this list
<iframe src=" "
width=" "
height=" "
allowtransparency="true"
frameborder="0">
</iframe>
- 2021
- A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers (
- 2020
- Structural characterization of covalently stabilized human cystatin c oligomers (
- Kinetic diversity of amyloid oligomers (
- Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors (
- Screening of small molecules using the inhibition of oligomer formation in α-synuclein aggregation as a selection parameter (
- Direct measurement of lipid membrane disruption connects kinetics and toxicity of Aβ42 aggregation (
- Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide (
- Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies (
- 2019
- Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils (
- 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 (
- Selective targeting of primary and secondary nucleation pathways in Ab42 aggregation using a rational antibody scanning method (
- Monomeric and fibrillar α-synuclein exert opposite effects on the catalytic cycle that promotes the proliferation of Aβ42 aggregates (
- 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
- Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of α-synuclein (
- Molecular mechanisms of protein aggregation from global fitting of kinetic models. (
- Physical determinants of the self-replication of protein fibrils (
- 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. (