Author

R. M. Kohli

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 Organism:bacteria (other)· 2 Research Focus:host-pathogen & immune response· 2 Assay:proteomics· 2 Research Focus:chromatin & epigenetic regulation· 1 Assay:CRISPR screen· 1 Approach:deep learning· 1 Assay:DNA methylation· 1

Frequent Co-Authors

A. Barka· 2 shared A. Li· 2 shared C. M. Hurley· 2 shared E. J. Petersson· 2 shared K. N. Berrios· 2 shared M. B. Cory· 2 shared Y. Venkatesh· 2 shared Z. M. Hostetler· 2 shared

Activity by Year

2021-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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2 shared papersBiochemistry

A. Barka

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Cooperativity between Cas9 and hyperactive AID establishes broad and diversifying mutational footprints in base editors

K. N. Berrios, A. Barka, J. Gill, J. C. Serrano, P. F. Bailer, J. B. Parker, N. H. Evitt, K. S. Gajula, J. Shi, R. M. Kohli

This study develops hyperactive base editors by exploring Cas9 and AID cooperation, revealing mechanisms that expand mutational diversity and efficiency in base editing.

Nucleic Acids Research · Jan 23, 2024Peer-reviewedBiochemistry

The LexA-RecA* structure reveals a lock-and-key mechanism for SOS activation

M. B. Cory, A. Li, C. M. Hurley, P. J. Carman, R. A. Pumroy, Z. M. Hostetler, Y. Venkatesh, K. B. Gupta, E. J. Petersson, R. M. Kohli

The paper determines the structure of the LexA-RecA* complex, revealing a lock-and-key mechanism that triggers SOS response gene induction by enabling LexA cleavage.

bioRxiv · Oct 30, 2023 · PreprintBiochemistry

Engineered RecA constructs reveal the minimal SOS activation complex

M. B. Cory, A. Li, C. M. Hurley, Z. M. Hostetler, Y. Venkatesh, C. M. Jones, E. J. Petersson, R. M. Kohli

This study identifies the minimal RecA* filament required for LexA cleavage by showing that three linked RecA units can bind ssDNA and trigger LexA degradation.

bioRxiv · Sep 30, 2022Biochemistry

The base-editing enzyme APOBEC3A catalyzes cytosine deamination in RNA with low proficiency and high selectivity

A. Barka, K. N. Berrios, P. Bailer, E. K. Schutsky, T. Wang, R. M. Kohli

This study investigates how APOBEC3A preferentially targets DNA over RNA by analyzing substrate selectivity and deamination efficiency.

bioRxiv · Nov 26, 2021Biochemistry