Author

C. M. Dunham

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· 6 Microbiology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 8 Assay:structural biology· 7 Organism:bacteria (other)· 4 Research Focus:protein folding & dynamics· 4 Research Focus:chromatin & epigenetic regulation· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:drug response / drug discovery· 2 Organism:E. coli· 1

Frequent Co-Authors

E. D. Hoffer· 5 shared D. Dey· 3 shared G. L. Conn· 3 shared H. A. Nguyen· 3 shared N. Zelinskaya· 3 shared P. Srinivas· 3 shared A. Mehrani· 2 shared J. N. Alumasa· 2 shared

Activity by Year

2019-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 34 mutual co-author links

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5 shared papersBiochemistry

E. D. Hoffer

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

30S subunit recognition and G1405 modification by the aminoglycoside-resistance 16S ribosomal RNA methyltransferase RmtC

P. Srinivas, M. Nosrati, N. Zelinskaya, D. Dey, L. R. Comstock, C. M. Dunham, G. L. Conn

This paper determines the structure of RmtC bound to the 30S ribosomal subunit and identifies key residues involved in G1405 modification, providing insights for inhibitor development.

Proceedings of the National Academy of Sciences · Jun 12, 2023Peer-reviewedBiochemistry

Antibiotic that inhibits trans-translation blocks binding of EF-Tu to tmRNA but not to tRNA

N. Marathe, H. A. Nguyen, J. N. Alumasa, A. B. Kuzmishin Nagy, M. Y. Vazquez, C. M. Dunham, K. C. Keiler

This paper identifies KKL-55, a tetrazole-based antibiotic that specifically inhibits EF-Tu binding to tmRNA without affecting tRNA binding, suggesting a new target for antibiotic development.

bioRxiv · Jun 9, 2023 · PreprintBiochemistry

Structural basis for reduced ribosomal A-site fidelity in response to P-site codon-anticodon mismatches

H. A. Nguyen, C. E. Fagan, E. D. Hoffer, T. Maehigashi, C. M. Dunham

The paper presents crystal structures showing how a P-site codon-anticodon mismatch reduces A-site fidelity, allowing for quality control of protein synthesis.

bioRxiv · Jan 28, 2023Biochemistry

50S subunit recognition and modification by the Mycobacterium tuberculosis ribosomal RNA methyltransferase TlyA

Z. T. Laughlin, S. Nandi, D. Dey, N. Zelinskaya, M. A. Witek, P. Srinivas, H. A. Nguyen, E. G. Kuiper, L. R. Comstock, C. M. Dunham, G. L. Conn

This paper reports the structure of the Mycobacterium tuberculosis TlyA enzyme bound to the 50S ribosomal subunit, revealing mechanisms of rRNA substrate recognition and modification that contribute to antibiotic resistance.

bioRxiv · Nov 11, 2021Biochemistry

Molecular mechanism regulating transcriptional control of the hig toxin-antitoxin locus of antibiotic-resistance plasmid Rts1 from Proteus vulgaris

I. J. Pavelich, M. A. Schureck, D. Wang, E. D. Hoffer, M. Boamah, N. Onouha, S. J. Miles, C. D. Okafor, C. M. Dunham

This paper investigates the regulation of the HigBHigA toxin-antitoxin pair from plasmid Rts1 in Proteus vulgaris, finding it functions as an on/off transcriptional switch rather than a molecular rheostat.

bioRxiv · Mar 4, 2021 · PreprintMicrobiology

Structural insights into mRNA reading frame regulation by tRNA modification and slippery codon-anticodon pairing

E. D. Hoffer, S. Hong, T. Maehigashi, R. L. Gonzalez, P. Whitford, C. M. Dunham

The paper reports ribosome structures with tRNAPro bound to codons, showing how m1G37 modification prevents frameshifting by stabilizing tRNA interactions.

bioRxiv · Sep 1, 2020Biochemistry

Ribosome rescue inhibitors clear Neisseria gonorrhoeae in vivo using a new mechanism

Z. D. Aron, A. Mehrani, E. D. Hoffer, K. L. Connolly, M. C. Torhan, J. N. Alumasa, P. Srinivas, M. Cabrera, D. Hosangadi, J. S. Barbor, S. C. Cardinale, S. M. Kwasny, L. R. Morin, M. M. Butler, T. J. Opperman, , K. C. Keiler

The paper describes the development of ribosome rescue inhibitors that clear drug-resistant Neisseria gonorrhoeae in vivo through a novel mechanism involving ribosomal conformational changes.

bioRxiv · Jun 4, 2020 · PreprintMicrobiology

Functionally critical residues in the aminoglycoside resistance-associated methyltransferase RmtC play distinct roles in 30S substrate recognition

M. Nosrati, D. Dey, A. Mehrani, S. E. Strassler, N. Zelinskaya, E. D. Hoffer, S. M. Stagg, C. M. Dunham, G. L. Conn

This study identifies functionally critical residues in RmtC that distinguish between 30S-binding affinity and 16S rRNA modification through structural and biochemical analysis.

bioRxiv · Oct 3, 2019Biochemistry