Author

E. Cattermole

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. Burgess· 1 shared A. G. Coyne· 1 shared A. L. Kantsadi· 1 shared C. Abell· 1 shared C. Meghir· 1 shared G. A. Spyroulias· 1 shared I. Vakonakis· 1 shared J. Cory-Wright· 1 shared

Activity by Year

2020-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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1 shared paperBiochemistry

A. Burgess

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Author profile →

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

A COVID Moonshot: assessment of ligand binding to the SARS-CoV-2 main protease by saturation transfer difference NMR spectroscopy.

A. L. Kantsadi, E. Cattermole, M.-T. Matsoukas, G. A. Spyroulias, I. Vakonakis

The paper assesses ligand binding to SARS-CoV-2 main protease using STD-NMR spectroscopy and shares data to aid drug design.

bioRxiv · Jun 17, 2020Biochemistry