Author

R. I. Horne

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 4 Pharmacology & Toxicology· 1

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Research Focus:drug response / drug discovery· 3 Approach:deep learning· 2 Approach:experimental assay· 2 Assay:proteomics· 2 Approach:statistical model· 2 Organism:C. elegans· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

M. Vendruscolo· 4 shared S. Chia· 3 shared Z. F. Brotzakis· 3 shared A. Possenti· 2 shared J. Habchi· 2 shared M. Nowinska· 2 shared R. C. Gregory· 2 shared R. Staats· 2 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 43 mutual co-author links

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4 shared papersBiophysics

M. Vendruscolo

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Author profile →

5 papers

Recent·Most cited

Molecular mechanism of α-synuclein aggregation on lipid membranes revealed.

A. J. Dear, X. Teng, S. R. Ball, J. Lewin, R. I. Horne, D. Clow, N. Harper, K. Yahya, T. C. Michaels, S. Linse, T. P. Knowles, X. Yang, S. C. Brewerton, J. Thomson, J. Habchi, G. Meisl

This study reveals that lipids promote α-synuclein aggregation by enabling elongation, using a kinetic model to describe the co-aggregation process in vitro.

bioRxiv · Oct 20, 2023Biophysics

Multiplexed Digital Characterisation of Misfolded Protein Oligomers via Solid-State Nanopores

S. E. Sandler, R. I. Horne, S. Rocchetti, R. Novak, N.-S. Hsu, M. C. Cruz, Z. F. Brotzakis, R. C. Gregory, S. Chia, G. J. L. Bernardes, U. F. Keyser, M. Vendruscolo

This paper introduces a single-molecule method using solid-state nanopores and DNA barcoding to detect and characterize misfolded protein oligomers, demonstrating its application to α-synuclein in Parkinson's disease.

bioRxiv · Aug 9, 2023 · PreprintBiophysics

Structure-based discovery of small molecule inhibitors of the autocatalytic proliferation of alpha-synuclein aggregates

S. Chia, Z. F. Brotzakis, R. I. Horne, A. Possenti, B. Mannini, R. Cataldi, M. Nowinska, R. Staats, S. Linse, T. P. J. Knowles, J. Habchi, M. Vendruscolo

This study identifies small molecules that inhibit alpha-synuclein aggregate proliferation using structure-based and kinetic assays.

Molecular Pharmaceutics · Nov 14, 2022Peer-reviewedBiophysics

A Rapid in vivo Pipeline to Identify Small Molecule Inhibitors of Amyloid Aggregation

M. Kamal, J. Knox, R. I. Horne, O. S. Tiwari, A. Burns, D. Han, D. L. Bar-Yosef, E. Gazit, K. C. Nguyen, D. H. Hall, M. Vendruscolo, P. J. Roy

This paper presents an in vivo pipeline to identify small molecule inhibitors of amyloid aggregation by screening compounds that suppress crystal formation in C. elegans.

bioRxiv · Apr 11, 2022 · PreprintPharmacology & Toxicology

Discovery of Potent Inhibitors of α-Synuclein Aggregation Using Structure-Based Iterative Learning

R. I. Horne, E. Andrzejewska, P. Alam, Z. F. Brotzakis, A. Srivastava, A. Aubert, M. Nowinska, R. C. Gregory, R. Staats, A. Possenti, S. Chia, P. Sormanni, B. Ghetti, B. Caughey, T. P. J. Knowles, M. Vendruscolo

This paper uses structure-based machine learning to identify potent small molecule inhibitors of α-synuclein aggregation, achieving compounds two orders of magnitude more potent than previous reports.

bioRxiv · Nov 10, 2021Biophysics