Author

M. T. Kemp

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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Microbiology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1 Assay:protein structure· 1 Organism:virus· 1

Frequent Co-Authors

M. D. Sacco· 2 shared Y. Chen· 2 shared A. C. Jaskolka-Brown· 1 shared D. Bhattacharya· 1 shared F. Meilleur· 1 shared I. Gelis· 1 shared J. J. Madsen· 1 shared J. Wang· 1 shared

Activity by Year

2022-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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2 shared papersMicrobiology

M. D. Sacco

Mutual co-authors in cluster

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2 papers

Recent·Most cited

Staphylococcus aureus FtsZ and PBP4 bind to the conformationally dynamic N-terminal domain of GpsB

M. D. Sacco, L. R. Hammond, R. E. Noor, D. Bhattacharya, J. J. Madsen, X. Zhang, S. G. Butler, M. T. Kemp, A. C. Jaskolka-Brown, S. J. Khan, I. Gelis, P. J. Eswara, Y. Chen

This study determines the structure of S. aureus GpsB's N-terminal domain, revealing its interaction with FtsZ and PBP4, and shows its essential role in cell division.

bioRxiv · Oct 25, 2022Microbiology

The P132H mutation in the main protease of Omicron SARS-CoV-2 decreases thermal stability without compromising catalysis or small-molecule drug inhibition

M. D. Sacco, Y. Hu, M. V. Gongora, F. Meilleur, M. T. Kemp, X. Zhang, J. Wang, Y. Chen

This study examines the P132H mutation in Omicron SARS-CoV-2 Mpro, finding it reduces thermal stability without affecting catalytic activity or drug inhibition.

bioRxiv · Jan 26, 2022Microbiology