Author

J. Habchi

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

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:host-pathogen & immune response· 2 Approach:statistical model· 2 Organism:C. elegans· 1 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

M. Vendruscolo· 3 shared S. Chia· 3 shared R. I. Horne· 2 shared S. LinseiD· 2 shared X. Yang· 2 shared A. J. Dear· 1 shared A. Possenti· 1 shared B. Mannini· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 28 mutual co-author links

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3 shared papersBiophysics

M. Vendruscolo

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Author profile →

4 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

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

Vitamin A and vitamin E metabolites comodulate amyloid-β aggregation

P. Joshi, S. Chia, X. Yang, M. Perni, J. Habchi, M. Vendruscolo

This study identifies retinoic acid and tocopherol as vitamin metabolites that modulate amyloid-β aggregation in vitro and in a C. elegans model, with combined effects that may cancel each other.

bioRxiv · Oct 30, 2021 · PreprintBiophysics

Infrared Nanospectroscopy Reveals the Molecular Interaction Fingerprint of an Aggregation Inhibitor with Single Aβ42 Oligomers

F. S. Ruggeri, J. Habchi, S. Chia, M. Vendruscolo, T. Knowles

This study uses infrared nanospectroscopy to directly measure how bexarotene interacts with Aβ42 oligomers and fibrils, revealing a single hydrogen bond between the compound's carbonyl group and the aggregates.

bioRxiv · Jun 24, 2020Biophysics