Author

J. Cory-Wright

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· 2

Signature Assays, Organisms & Methods

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Research Focus:drug response / drug discovery· 2 Approach:experimental assay· 2 Approach:biophysical modeling· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1

Frequent Co-Authors

A. G. Coyne· 2 shared C. Abell· 2 shared T. L. Blundell· 2 shared V. Mendes· 2 shared A. Burgess· 1 shared C. E. Barry· 1 shared C. Meghir· 1 shared C. Spry· 1 shared

Activity by Year

2020-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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2 shared papersBiochemistry

A. G. Coyne

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2 papers

Recent·Most cited

A Fragment-based approach to assess the ligandability of ArgB, ArgC, ArgD and ArgF in the L-arginine biosynthetic pathway of Mycobacterium tuberculosis.

P. Gupta, S. E. Thomas, J. Cory-Wright, V. Sebastián-Pérez, A. Burgess, E. Cattermole, C. Meghir, C. Abell, A. G. Coyne, W. R. Jacobs, T. L. Blundell, S. Tiwari, V. Mendes

This study uses a fragment-based approach to assess the ligandability of four enzymes in the L-arginine biosynthesis pathway of M. tuberculosis, identifying potential drug targets.

bioRxiv · Mar 12, 2021Biochemistry

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