Author

M. M. Kashipathy

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· 1 Biophysics· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 2 Assay:structural biology· 2 Approach:biophysical modeling· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Approach:statistical model· 1

Frequent Co-Authors

D. K. Johnson· 2 shared K. P. Battaile· 2 shared A. R. Fehr· 1 shared A. Roy· 1 shared B. D. Freudenthal· 1 shared B. J. Ryan· 1 shared C. B. Schaffer· 1 shared C. J. Kupitz· 1 shared

Activity by Year

2020-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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2 shared papersMicrobiology

D. K. Johnson

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Molecular basis for the activation of the Fatty Acid Kinase complex of Staphylococcus aureus

M. J. Myers, Z. Xu, B. J. Ryan, Z. R. DeMars, M. J. Ridder, D. K. Johnson, C. N. Krute, T. S. Flynn, M. M. Kashipathy, K. P. Battaile, N. J. Schnicker, S. Lovell, B. D. Freudenthal, J. L. Bose

This study investigates the structure and function of the Fatty Acid Kinase complex in Staphylococcus aureus using modeling, biochemical, and cell-based approaches, revealing key residues and interactions essential for its activity.

bioRxiv · Mar 19, 2024 · PreprintMicrobiology

RNA structures and dynamics with A resolution revealed by x-ray free electron lasers

K. A. Zielinski, S. Sui, S. A. Pabit, D. A. Rivera, T. Wang, Q. Hu, M. M. Kashipathy, S. Lisova, C. B. Schaffer, V. Mariani, M. S. Hunter, C. J. Kupitz, F. R. Moss, F. P. Poitevin, T. D. Grant, L. Pollack

This paper reveals RNA structures and dynamics at near-atomic resolution using x-ray free electron lasers, showing how RNA folds through intermediate states and forms triplexes.

bioRxiv · May 24, 2023Biophysics

The SARS-CoV-2 conserved macrodomain is a mono-ADP-ribosylhydrolase

Y. M. O. Alhammad, M. M. Kashipathy, A. Roy, J.-P. Gagne, P. McDonald, P. Gao, L. Nonfoux, K. P. Battaile, D. K. Johnson, E. D. Holmstrom, G. G. Poirier, S. W. Lovell, A. R. Fehr

This paper identifies SARS-CoV-2's Mac1 as a mono-ADP-ribosylhydrolase, showing it binds and hydrolyzes mono-ADP-ribose, with implications for antiviral therapy.

bioRxiv · May 11, 2020Biochemistry