Author

M. N. Frazier

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· 3 Cell Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:virus· 3 Assay:cryo-EM· 2 Research Focus:host-pathogen & immune response· 2 Assay:structural biology· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Organism:human· 1

Frequent Co-Authors

R. E. Stanley· 4 shared I. M. Wilson· 3 shared J. M. Krahn· 3 shared J. G. Williams· 2 shared L. B. Dillard· 2 shared L. J. Deterding· 2 shared L. Perera· 2 shared M. C. Pillon· 2 shared

Activity by Year

2019-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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4 shared papersBiochemistry

R. E. Stanley

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Biochemical Characterization of Emerging SARS-CoV-2 Nsp15 Endoribonuclease Variants

I. M. Wilson, M. N. Frazier, J.-L. N. Li, T. A. Randall, R. E. Stanley

This study characterizes SARS-CoV-2 Nsp15 variants' nuclease activity and oligomerization, finding mutations reduce activity and increase monomeric form.

bioRxiv · May 10, 2022Microbiology

Flipped Over U: Structural Basis for dsRNA Cleavage by the SARS-CoV-2 Endoribonuclease

M. N. Frazier, I. M. Wilson, J. M. Krahn, K. J. Butay, L. B. Dillard, M. J. N. Borgnia, R. E. Stanley

This study determines the structure of SARS-CoV-2 Nsp15 bound to dsRNA, revealing a base-flipping mechanism for dsRNA cleavage and its ability to process both ss- and dsRNA.

bioRxiv · Mar 2, 2022Biochemistry

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

Mammalian retromer is an adaptable scaffold for cargo sorting from endosomes

A. K. Kendall, B. Xie, P. Xu, J. Wang, R. Burcham, M. N. Frazier, E. Binshtein, H. Wei, T. R. Graham, T. Nakagawa, L. P. Jackson

This study identifies adaptable retromer structures and their role in cargo sorting from endosomes to the TGN or plasma membrane in mammals.

bioRxiv · May 15, 2019Cell Biology