Author

T. L. Dangerfield

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· 3 Research Focus:protein folding & dynamics· 2 Approach:statistical model· 2 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:clustering· 1 Assay:cryo-EM· 1 Assay:DNA methylation· 1

Frequent Co-Authors

D. W. Taylor· 3 shared J. P. Bravo· 3 shared K. A. Johnson· 3 shared C. L. McCafferty· 1 shared E. A. Schwartz· 1 shared G. N. Hibshman· 1 shared H. Zhang· 1 shared I. J. Finkelstein· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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3 shared papersBiochemistry

D. W. Taylor

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Author profile →

4 papers

Recent·Most cited

Unraveling the mechanisms of PAMless DNA interrogation by SpRY Cas9

G. N. Hibshman, J. P. Bravo, H. Zhang, T. L. Dangerfield, I. J. Finkelstein, K. A. Johnson, D. W. Taylor

This study investigates how SpRY-Cas9 recognizes DNA targets without requiring a PAM sequence, revealing structural and kinetic mechanisms that improve genome editing versatility.

bioRxiv · Jun 22, 2023Biochemistry

Assembly of multi-subunit fusion proteins into the RNA-targeting type III-D CRISPR-Cas effector complex

E. A. Schwartz, J. P. Bravo, L. A. Macias, C. L. McCafferty, T. L. Dangerfield, J. N. Walker, J. S. Brodbelt, P. C. Fineran, R. D. Fagerlund, D. W. Taylor

The paper determines the structure of a type III-D CRISPR-Cas effector complex and characterizes its RNA cleavage mechanism, revealing how multi-subunit fusion proteins assemble into an active RNA endonuclease.

bioRxiv · Jun 13, 2022 · PreprintBiochemistry

Conformational dynamics during misincorporation and mismatch extension defined using a DNA polymerase with a fluorescent artificial amino acid

T. L. Dangerfield, S. Kirmizialtin, K. A. Johnson

This study investigates the conformational dynamics and kinetics of nucleotide misincorporation and mismatch extension in a high-fidelity DNA polymerase using fluorescent unnatural amino acids and molecular dynamics simulations.

bioRxiv · Jul 13, 2021Biochemistry

Remdesivir is a delayed translocation inhibitor of SARS CoV-2 replication in vitro

J. P. Bravo, T. L. Dangerfield, D. W. Taylor, K. A. Johnson

This study shows remdesivir inhibits SARS-CoV-2 RNA polymerase by blocking RNA translocation after three base incorporations, leading to delayed chain termination.

bioRxiv · Dec 14, 2020Biochemistry