Author

C. Spry

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 Microbiology· 2 Pharmacology & Toxicology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 7 Research Focus:drug response / drug discovery· 5 Research Focus:host-pathogen & immune response· 3 Organism:plant (other)· 3 Approach:wet-lab / biochemical assay· 2 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:development & morphogenesis· 1

Frequent Co-Authors

K. J. Saliba· 5 shared A. G. Coyne· 2 shared A. G. Maier· 2 shared C. Abell· 2 shared E. T. Tjhin· 2 shared G. G. van Dooren· 2 shared J. C. Evans· 2 shared K. Auclair· 2 shared

Activity by Year

2017-2024 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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5 shared papersMicrobiology

K. J. Saliba

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Author profile →

7 papers

Recent·Most cited

Mutation of the P. falciparum flavokinase confers resistance to roseoflavin and 8-aminoriboflavin

A. Hemasa, C. Spry, M. Mack, K. J. Saliba

This study identifies a mutation in the P. falciparum flavokinase gene that confers resistance to roseoflavin and 8-aminoriboflavin by reducing substrate binding affinity.

bioRxiv · Apr 4, 2024 · PreprintMicrobiology

A screen of drug-like molecules identifies chemically diverse electron transport chain inhibitors in apicomplexan parasites

J. A. Hayward, F. V. Makota, D. Cihalova, E. Rajendran, S. M. Zwahlen, L. Shuttleworth, U. Wiedemann, C. Spry, K. J. Saliba, A. G. Maier, G. G. van Dooren

The paper screens drug-like molecules to identify new electron transport chain inhibitors in apicomplexan parasites, finding chemically diverse compounds effective against resistant strains.

bioRxiv · Feb 13, 2022Microbiology

A novel heteromeric pantothenate kinase complex in apicomplexan parasites

E. T. Tjhin, V. M. Howieson, C. Spry, G. G. van Dooren, K. J. Saliba

The paper identifies heteromeric pantothenate kinase complexes in Plasmodium falciparum and Toxoplasma gondii, showing that PanK1 and PanK2 form functional complexes with Pf14-3-3I and are essential for parasite proliferation.

bioRxiv · Mar 16, 2021Biochemistry

Exploring heteroaromatic rings as a replacement for the labile amide of antiplasmodial pantothenamides

J. Guan, C. Spry, E. Tjhin, P. Yang, T. Kittikool, V. Howieson, H. Ling, L. Starrs, G. Burgio, K. J. Saliba, K. Auclair

This study replaces the amide group in pantothenamides with heteroaromatic rings to improve antiplasmodial activity against Plasmodium species.

bioRxiv · Oct 2, 2020Pharmacology & Toxicology

Chemical validation of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase using fragment linking and CRISPR interference

J. El Bakali, M. Blaszczyk, J. C. Evans, J. A. Boland, W. J. McCarthy, M. V. B. Dias, A. G. Coyne, V. Mizrahi, T. L. Blundell, C. Abell, C. Spry

This study identifies inhibitors of MtbPPAT, a key enzyme in CoA biosynthesis, using fragment linking and CRISPR interference to validate it as a potential anti-TB drug target.

bioRxiv · Sep 4, 2020Biochemistry

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

Mutations in the pantothenate kinase of Plasmodium falciparum confer diverse sensitivity profiles to antiplasmodial pantothenate analogues

E. T. Tjhin, C. Spry, A. L. Sewell, A. Hoegl, L. Barnard, A. E. Sexton, V. M. Howieson, A. G. Maier, D. J. Creek, E. Strauss, R. Marquez, K. Auclair, K. J. Saliba

The paper identifies mutations in Plasmodium falciparum pantothenate kinase genes that confer resistance to pantothenate analogues and reveal different mechanisms of action for these compounds.

bioRxiv · Jul 24, 2017Pharmacology & Toxicology