Author

M. C. Pillon

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· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Assay:cryo-EM· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1 Assay:structural biology· 1 Organism:virus· 1

Frequent Co-Authors

J. G. Williams· 2 shared J. M. Krahn· 2 shared L. J. Deterding· 2 shared L. Perera· 2 shared M. J. Borgnia· 2 shared M. N. Frazier· 2 shared R. E. Stanley· 2 shared Z. D. Stewart· 2 shared

Activity by Year

2020-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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2 shared papersBiochemistry

J. G. Williams

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Author profile →

2 papers

Recent·Most cited

Characterization of SARS2 Nsp15 Nuclease Activity Reveals it's Mad About U

M. N. Frazier, L. B. Dillard, J. M. Krahn, L. Perera, J. G. Williams, I. M. Wilson, Z. D. Stewart, M. C. Pillon, L. J. Deterding, M. J. Borgnia, R. E. Stanley

This study characterizes SARS2 Nsp15 nuclease activity, revealing its preference for purines 3 of cleaved uridines and its role in viral RNA processing.

bioRxiv · Jun 1, 2021Biochemistry

Cryo-EM Structures of the SARS-CoV-2 Endoribonuclease Nsp15

M. C. Pillon, M. N. Frazier, L. Dillard, J. G. Williams, S. Kocaman, J. M. Krahn, L. Perera, C. K. Hayne, J. Gordon, Z. D. Stewart, M. Sobhany, L. J. Deterding, A. L. Hsu, V. P. Dandey, M. J. Borgnia, R. E. Stanley

This study determines the cryo-EM structures of SARS-CoV-2 Nsp15, revealing its active site interactions with uridine and conformational changes, which inform potential therapeutic targets.

bioRxiv · Aug 11, 2020 · PreprintBiochemistry