Author

J. M. Hogle

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· 1 Immunology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Assay:cryo-EM· 1 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

D. J. Filman· 2 shared D. Rowlands· 2 shared J. S. Snowden· 2 shared K. Grehan· 2 shared N. J. Kingston· 2 shared N. J. Stonehouse· 2 shared A. J. Macadam· 1 shared A. Martyna· 1 shared

Activity by Year

2020-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 34 mutual co-author links

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2 shared papersMicrobiology

D. J. Filman

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Mechanism of enterovirus VP0 maturation cleavage based on the structure of a stabilised assembly intermediate.

N. J. Kingston, J. S. Snowden, K. Grehan, P. K. Hall, E. V. Hietanen, T. C. Passchier, S. J. Polyak, D. J. Filman, J. M. Hogle, D. Rowlands, N. J. Stonehouse

The paper determines the molecular mechanism of VP0 cleavage in enteroviruses using structural and bioinformatic analysis of a provirion intermediate.

bioRxiv · Apr 6, 2024Microbiology

Production of antigenically stable enterovirus A71 virus-like particles in Pichia pastoris as a vaccine candidate.

N. J. Kingston, J. S. Snowden, A. Martyna, M. Shegdar, K. Grehan, A. Tedcastle, E. Pegg, H. Fox, A. J. Macadam, J. Martin, J. M. Hogle, D. Rowlands, N. J. Stonehouse

This study produces antigenically stable EVA71 virus-like particles in Pichia pastoris, showing they retain native antigenic conformation and elicit neutralising antibodies comparable to inactivated virus vaccines.

bioRxiv · Jan 30, 2023 · PreprintImmunology

Cryo-EM structures reveal two distinct conformational states in a picornavirus cell entry intermediate.

P. N. M. Shah, D. J. Filman, K. S. Karunatilaka, E. L. Hesketh, E. Groppelli, M. Strauss, J. M. Hogle

The paper identifies two distinct conformational states of the 135S poliovirus particle using cryo-EM, showing that VP1 N-terminus externalization and VP4 retention vary between states.

PLOS Pathogens · Sep 30, 2020Peer-reviewedBiophysics