Author

T. J. Purton

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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Biochemistry· 1 Biophysics· 1

Signature Assays, Organisms & Methods

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Organism:human· 2 Research Focus:cell type annotation· 1 Assay:electronic health records· 1 Approach:experimental assay· 1 Research Focus:host-pathogen & immune response· 1 Approach:microscopy & imaging analysis· 1 Assay:protein structure· 1 Organism:yeast· 1

Frequent Co-Authors

W.-F. Xue· 2 shared J. R. Hiscock· 1 shared K. Fennell· 1 shared L. C. Serpell· 1 shared L. D. Aubrey· 1 shared L. Lutter· 1 shared M. F. Tuite· 1 shared N. Koloteva-Levine· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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2 shared papersBiophysics

W.-F. Xue

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2 papers

Recent·Most cited

Structural reconstruction of individual filaments in Abeta42 fibril populations assembled in vitro reveal rare species that resemble ex vivo amyloid polymorphs from human brains

L. D. Aubrey, L. Lutter, K. Fennell, T. J. Purton, N. Ward, L. C. Serpell, W.-F. Xue

The paper uses atomic force microscopy and cryo-electron microscopy to analyze Aβ42 fibril structures in vitro, identifying rare polymorphs similar to those found in human brain amyloid.

bioRxiv · Jul 14, 2023 · PreprintBiophysics

Amyloid particles facilitate surface-catalyzed cross-seeding by acting as promiscuous nanoparticles

N. Koloteva-Levine, R. Marchante, T. J. Purton, J. R. Hiscock, M. F. Tuite, W.-F. Xue

This study shows amyloid seeds can catalyze cross-seeding without propagating their specific conformation, using Aβ42 and Sup35NM proteins.

bioRxiv · Sep 1, 2020Biochemistry