Author

T. C. Michaels

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· 7

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:drug response / drug discovery· 3 Approach:statistical model· 3 Organism:C. elegans· 2 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Assay:proteomics· 1

Frequent Co-Authors

G. Meisl· 4 shared S. LinseiD· 4 shared C. M. Dobson· 3 shared M. Vendruscolo· 3 shared T. P. Knowles· 3 shared A. Saric· 2 shared G. T. Heller· 2 shared L. Mahadevan· 2 shared

Activity by Year

2018-2023 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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4 shared papersBiophysics

G. Meisl

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Author profile →

7 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

Uncovering the universality of self-replication in protein aggregation and its link to disease.

G. Meisl, C. K. Xu, J. D. Taylor, T. C. Michaels, A. Levin, D. E. Otzen, D. Klenerman, S. Matthews, S. Linse, M. Andreasen, T. Knowles

The paper investigates self-replication in protein aggregates, finding it common in both functional and pathological contexts, with disease-related aggregates replicating faster than biological ones.

bioRxiv · Jun 8, 2022Biophysics

Liquid condensates increase potency of amyloid fibril inhibitors

T. C. Michaels, L. Mahadevan, C. Weber

The paper investigates how liquid condensates enhance the potency of amyloid fibril inhibitors by colocalizing inhibitors and aggregates within condensates.

bioRxiv · Oct 29, 2020 · PreprintBiophysics

Small molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer's disease

G. T. Heller, F. A. Aprile, T. C. Michaels, R. Limbocker, M. Perni, F. S. Ruggeri, B. Mannini, T. Lohr, M. Bonomi, C. Camilloni, A. De Simone, I. C. Felli, R. Pierattelli, T. P. Knowles, C. M. Dobson, M. Vendruscolo

This paper identifies a small molecule that binds and sequesters monomeric amyloid-β, inhibiting its aggregation and rescuing toxicity in a C. elegans model.

bioRxiv · Sep 16, 2020Biophysics

Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide

T. C. Michaels, A. Saric, S. Curk, K. Bernfur, P. Arosio, G. Meisl, A. Dear, S. Cohen, M. Vendruscolo, C. M. Dobson, S. Linse, T. P. Knowles

This study investigates the dynamics of Aβ42 oligomers during amyloid fibril formation, revealing that most oligomers dissociate into monomers rather than forming fibrils.

Nature Chemistry · Apr 13, 2020Peer-reviewedBiophysics

Thermodynamic and kinetic design principles for protein aggregation inhibitors

T. C. Michaels, A. Saric, G. Meisl, G. T. Heller, S. Curk, P. Arosio, S. Linse, C. M. Dobson, M. Vendruscolo, T. Knowles

This study develops a kinetic theory to identify thermodynamic and kinetic signatures of effective protein aggregation inhibitors.

bioRxiv · Feb 22, 2020 · PreprintBiophysics

Optimal strategies for inhibition of protein aggregation

T. C. Michaels, C. A. Weber, L. Mahadevan

The paper uses aggregation kinetics and control theory to determine optimal drug protocols for inhibiting protein aggregation, finding different strategies are needed for primary and fibril-dependent secondary nucleation.

bioRxiv · Oct 30, 2018Biophysics