
Publications
The inhibitory action of the chaperone BRICHOS against the α-Synuclein secondary nucleation pathway
– Nature communications
(2024)
15,
10038
(doi: 10.1038/s41467-024-54212-2)
On transient assemblies in amyloid formation: mechanistic insights and therapeutic strategies
(2024)
Single-molecule digital sizing of proteins in solution.
– Nat Commun
(2024)
15,
7740
(doi: 10.1038/s41467-024-50825-9)
α-Synuclein oligomers form by secondary nucleation
– Nature communications
(2024)
15,
7083
(doi: 10.1038/s41467-024-50692-4)
The role of shear forces in primary and secondary nucleation of amyloid fibrils.
– Proc Natl Acad Sci U S A
(2024)
121,
e2322572121
(doi: 10.1073/pnas.2322572121)
Aβ Oligomer Dissociation Is Catalyzed by Fibril Surfaces
– ACS Chemical Neuroscience
(2024)
15,
2296
(doi: 10.1021/acschemneuro.4c00127)
Discovery of potent inhibitors of α-synuclein aggregation using structure-based iterative learning
– Nat Chem Biol
(2024)
20,
634
(doi: 10.1038/s41589-024-01580-x)
Design of amyloidogenic peptide traps
– Nature chemical biology
(2024)
20,
981
(doi: 10.1038/s41589-024-01578-5)
Molecular chaperones and their role in amyloid formation
– Biophysical Journal
(2024)
123,
301a
(doi: 10.1016/j.bpj.2023.11.1869)
Novel methods to study amyloid oligomers
– Biophysical Journal
(2024)
123,
41a
(doi: 10.1016/j.bpj.2023.11.331)
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