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Centre for Misfolding Diseases,
Department of Chemistry,
Centre for Misfolding Diseases, Department of Chemistry
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A Fragment-Based Method of Creating Small-Molecule Libraries to Target the Aggregation of Intrinsically Disordered Proteins.
ACS combinatorial science Mar, 2016 | Pubmed ID: 26923286
An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer's disease.
Science advances Feb, 2016 | Pubmed ID: 26933687
Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer's disease.
Proceedings of the National Academy of Sciences of the United States of America 01, 2017 | Pubmed ID: 28011763
Monomeric and fibrillar α-synuclein exert opposite effects on the catalytic cycle that promotes the proliferation of Aβ42 aggregates.
Proceedings of the National Academy of Sciences of the United States of America 07, 2017 | Pubmed ID: 28698377
Chemical Kinetics for Bridging Molecular Mechanisms and Macroscopic Measurements of Amyloid Fibril Formation.
Annual review of physical chemistry 04, 2018 | Pubmed ID: 29490200
Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes.
Nature chemistry Jun, 2018 | Pubmed ID: 29736006
Stabilization and Characterization of Cytotoxic Aβ Oligomers Isolated from an Aggregation Reaction in the Presence of Zinc Ions.
ACS chemical neuroscience Aug, 2018 | Pubmed ID: 29986583
Microfluidic deposition for resolving single-molecule protein architecture and heterogeneity.
Nature communications Sep, 2018 | Pubmed ID: 30250131
SAR by kinetics for drug discovery in protein misfolding diseases.
Proceedings of the National Academy of Sciences of the United States of America 10, 2018 | Pubmed ID: 30257937
Chemical and mechanistic analysis of photodynamic inhibition of Alzheimer's β-amyloid aggregation.
Chemical communications (Cambridge, England) Jan, 2019 | Pubmed ID: 30632567
Trodusquemine enhances Aβ aggregation but suppresses its toxicity by displacing oligomers from cell membranes.
Nature communications 01, 2019 | Pubmed ID: 30644384
University of Cambridge
Francesco Simone Ruggeri1,
Tomas Šneideris1,2,
Sean Chia1,
Michele Vendruscolo1,
Tuomas P. J. Knowles1,3
1Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge,
2Institute of Biotechnology, Life Sciences Center, Vilnius University,
3Cavendish Laboratory, Department of Physics, University of Cambridge
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