Visualizing and trapping transient oligomers in amyloid assembly pathways
Open Access
- 1 January 2021
- journal article
- research article
- Published by Elsevier in Biophysical Chemistry
- Vol. 268, 106505
Abstract
No abstract availableKeywords
Funding Information
- European Research Council
- Engineering and Physical Sciences Research Council
- Leverhulme Trust
- Wellcome Trust
This publication has 257 references indexed in Scilit:
- Single-Molecule Measurements of Transient Biomolecular Complexes through Microfluidic DilutionAnalytical Chemistry, 2013
- Advances in ion mobility spectrometry–mass spectrometry reveal key insights into amyloid assemblyBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2013
- Direct Observation of the Interconversion of Normal and Toxic Forms of α-SynucleinCell, 2012
- Aβ(39–42) Modulates Aβ Oligomerization but Not Fibril FormationBiochemistry, 2011
- Structure and Dynamics of Oligomeric Intermediates in β2-Microglobulin Self-AssemblyBiophysical Journal, 2011
- Probing Neuroserpin Polymerization and Interaction with Amyloid-β Peptides Using Single Molecule FluorescenceBiophysical Journal, 2009
- Competition between Intramolecular and Intermolecular Interactions in an Amyloid-Forming ProteinJournal of Molecular Biology, 2009
- Structural Characteristics of α-Synuclein Oligomers Stabilized by the Flavonoid BaicaleinJournal of Molecular Biology, 2008
- Isolation of a Human Single Chain Antibody Fragment Against Oligomeric α-Synuclein that Inhibits Aggregation and Prevents α-Synuclein-induced ToxicityJournal of Molecular Biology, 2007
- Vesicle Permeabilization by Protofibrillar α-Synuclein: Implications for the Pathogenesis and Treatment of Parkinson's DiseaseBiochemistry, 2001