Author

C. E. Barry

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 Immunology· 2 Microbiology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 7 Research Focus:drug response / drug discovery· 3 Organism:human· 3 Research Focus:host-pathogen & immune response· 2 Organism:non-human primate· 2 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1

Frequent Co-Authors

H. I. M. Boshoff· 3 shared L. E. Via· 3 shared B. G. Davis· 2 shared D. L. Barber· 2 shared F. Gomez· 2 shared K. D. Kauffman· 2 shared P. C. Ray· 2 shared P. G. Wyatt· 2 shared

Activity by Year

2018-2026 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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3 shared papersMicrobiology

H. I. M. Boshoff

Mutual co-authors in cluster

Author profile →

7 papers

Recent·Most cited

Thienothiazolocarboxamides: rapidly cidal agents causing catastrophic thiol collapse in Mycobacterium tuberculosis.

S. Oh, G. Prosser, H. I. M. Boshoff, S. R. Green, N. Quadir, J. S. O. Roma, A. Kumar, N. Mukundan, S. Hanson, J. P. Sarathy, K. I. Buchanan, P. C. Ray, P. G. Wyatt, T. R. Ioerger, A. L. Schwan, , C. E. Barry

This paper identifies thienothiazolocarboxamides as rapidly cidal antituberculosis agents that cause thiol collapse in Mycobacterium tuberculosis through EthA-mediated activation.

bioRxiv · Nov 9, 2026 · PreprintMicrobiology

Distributable, Metabolic PET Reporting of Tuberculosis

R. M. N. Khan, Y.-M. Ahn, G. A. Marriner, L. E. Via, F. D'Hooge, S. S. Lee, N. Yang, F. Basuli, A. G. White, J. A. Tomko, L. J. Frye, C. A. Scanga, D. M. Weiner, M. L. Sutphen, D. M. Schimel, , B. G. Davis

This paper introduces [18F]FDT, a PET tracer that specifically images Mycobacterium tuberculosis lesions and monitors treatment, enabling global access through a simple synthesis method from [18F]FDG.

Nature Communications · Jun 27, 2024Peer-reviewedBiochemistry

DNA-dependent binding of nargenicin to DnaE1 inhibits replication in Mycobacterium tuberculosis

M. D. Chengalroyen, M. K. Mason, A. Borsellini, R. Tassoni, G. L. Abrahams, S. Lynch, Y.-M. Ahn, J. Ambler, K. Young, B. M. Crowley, D. B. Olsen, D. F. Warner, C. E. Barry, H. I. M. Boshoff, M. Lamers, V. Mizrahi

This study shows nargenicin binds to Mtb DnaE1 DNA-dependent polymerase, inhibiting replication and inducing DNA damage response in tuberculosis bacteria.

bioRxiv · Oct 27, 2021Microbiology

Eosinophils are an integral component of the pulmonary granulocyte response in Tuberculosis and promote host resistance in mice

A. C. Bohrer, E. Castro, Z. Hu, A. T. L. Queiroz, C. E. Tocheny, M. Assmann, S. Sakai, C. Nelson, P. J. Baker, H. Ma, L. Wang, W. Zilu, E. du Bruyn, C. Riou, K. D. Kauffman, , K. D. Mayer-Barber

This study shows eosinophils are recruited to tuberculosis-infected lung tissue in mice and contribute to host resistance against Mtb infection.

bioRxiv · May 29, 2021Immunology

Functional inactivation of pulmonary MAIT cells following 5-OP-RU treatment of non-human primates

S. Sakai, N. E. Lora, K. D. Kauffman, D. E. Dorosky, S. Oh, S. Namasivayam, F. Gomez, J. D. Fleegle, C. S. Lindestam Arlehamn, A. Sher, G. J. Freeman, L. E. Via, C. E. Barry, D. L. Barber

This study shows that 5-OP-RU treatment of M. tuberculosis-infected rhesus macaques leads to MAIT cell dysfunction rather than expansion, with upregulated PD-1 and loss of cytokine production.

bioRxiv · Jan 29, 2021Immunology

Inhibiting Mycobacterium tuberculosis CoaBC by targeting a new allosteric site.

V. Mendes, S. R. Green, J. C. Evans, J. Hess, M. Blaszczyk, C. Spry, O. Bryant, J. Cory-Wright, D. S.-H. Chan, P. H. M. Torres, Z. Wang, S. O'Neill, S. Damerow, J. Post, T. Bayliss, , T. L. Blundell

The paper identifies potent inhibitors of Mycobacterium tuberculosis CoaB by targeting a novel allosteric site, based on structural and biochemical analyses of CoaBC.

bioRxiv · Jan 15, 2020 · PreprintBiochemistry

Structures of DPAGT1 explain glycosylation disease mechanisms and advance TB antibiotic design

Y. Y. Dong, H. Wang, A. C. Pike, S. J. Cochrane, S. Hamedzade, F. J. Wyszynsk, S. R. Bushell, S. F. Royer, D. A. Widdick, A. Sajid, H. I. Boshoff, R. Lucas, W.-M. Liu, S. S. Lee, T. Machida, , E. P. Carpenter

This paper determines the structures of DPAGT1 with substrates and inhibitors, revealing catalytic mechanisms and disease-causing mutations, and designs non-toxic antibiotics for tuberculosis.

bioRxiv · Apr 2, 2018Biochemistry