Author

J. M. Krahn

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· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Assay:structural biology· 3 Research Focus:protein structure prediction· 2 Organism:virus· 2 Research Focus:cell type annotation· 1 Assay:cryo-EM· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1

Frequent Co-Authors

R. E. Stanley· 4 shared J. G. Williams· 3 shared L. J. Deterding· 3 shared L. Perera· 3 shared M. J. Borgnia· 3 shared M. N. Frazier· 3 shared Z. D. Stewart· 3 shared C. K. Hayne· 2 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 43 mutual co-author links

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4 shared papersBiochemistry

R. E. Stanley

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Author profile →

4 papers

Recent·Most cited

Structural Basis for pre-tRNA Recognition and Processing by the Human tRNA Splicing Endonuclease Complex

C. K. Hayne, K. J. U. Butay, Z. D. Stewart, J. M. Krahn, L. Perera, J. G. Williams, R. M. Petrovitch, L. J. Deterding, G. Matera, M. J. Borgnia, R. E. Stanley

This study presents cryo-EM structures of the human TSEN*pre-tRNA complex, revealing its architecture and tRNA binding interfaces, and provides insights into PCH-causing mutations.

bioRxiv · Sep 2, 2022Biochemistry

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