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Nature Chemistry|March 28, 2018
Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptideSamuel I A Cohen, Risto Cukalevski, Thomas C T Michaels, et al.
Biophysical Journal|March 4, 2010
The interaction of alphaB-crystallin with mature alpha-synuclein amyloid fibrils inhibits their elongationChristopher A Waudby, Tuomas P J Knowles, Glyn L Devlin, et al.
Biochemistry|February 24, 2017
Inhibition of α-Synuclein Fibril Elongation by Hsp70 Is Governed by a Kinetic Binding Competition between α-Synuclein SpeciesFrancesco A Aprile, Paolo Arosio, Giuliana Fusco, et al.
Science Advances|August 12, 2022
Uncovering the universality of self-replication in protein aggregation and its link to diseaseGeorg Meisl, Catherine K Xu, Jonathan D Taylor, et al.
Communications Chemistry|April 11, 2026
The role of N-terminal acetylation on biomolecular condensationCarolina G Oliveira, Mayra T S Silva, Emanuel Kava, et al.
ACS Nano|May 29, 2012
Selenium-enhanced electron microscopic imaging of different aggregate forms of a segment of the amyloid β peptide in cellsEva K McGuire, Michael Motskin, Benedetta Bolognesi, et al.
Scientific Reports|November 4, 2016
β-Synuclein suppresses both the initiation and amplification steps of α-synuclein aggregation via competitive binding to surfacesJames W P Brown, Alexander K Buell, Thomas C T Michaels, et al.
Molecular Pharmaceutics|November 14, 2022
Structure-Based Discovery of Small-Molecule Inhibitors of the Autocatalytic Proliferation of α-Synuclein AggregatesSean Chia, Z Faidon Brotzakis, Robert I Horne, et al.
Biophysical Journal|October 4, 2011
Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongationSarah L Shammas, Christopher A Waudby, Shuyu Wang, et al.
Nature Structural & Molecular Biology|August 12, 2020
Direct measurement of lipid membrane disruption connects kinetics and toxicity of Aβ42 aggregationPatrick Flagmeier, Suman De, Thomas C T Michaels, et al.
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