Author

M. D. Petroski

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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Approach:experimental assay· 2 Organism:human· 2 Research Focus:drug response / drug discovery· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1 Assay:structural biology· 1

Frequent Co-Authors

A. E. Stewart· 1 shared A. M. Gilbert· 1 shared A. Nagata· 1 shared A. R. Nager· 1 shared B. Bolanos· 1 shared B. Bosbach· 1 shared B. F. Cravatt· 1 shared B. Melillo· 1 shared

Activity by Year

2022-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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1 shared paperBiochemistry

A. E. Stewart

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2 papers

Recent·Most cited

Expanding the ligandable proteome by paralog hopping with covalent probes

Y. Zhang, Z. Liu, M. Hirschi, O. Brodsky, E. Johnson, S. J. Won, A. Nagata, M. D. Petroski, J. D. Majmudar, S. Niessen, T. VanArsdale, A. M. Gilbert, M. M. Hayward, A. E. Stewart, A. R. Nager, , B. F. Cravatt

The paper uses covalent probes and paralog hopping to identify ligandable pockets in proteins lacking cysteines, demonstrating a method to expand the ligandable proteome.

bioRxiv · Jan 18, 2024 · PreprintBiochemistry

Phosphorylation of SAMHD1 Thr592 increases C-terminal domain dynamics, tetramer dissociation, and ssDNA binding kinetics

B. Orris, K. W. Huynh, M. Ammirati, S. Han, B. Bolanos, J. Carmody, M. D. Petroski, B. Bosbach, D. J. Shields, J. T. Stivers

This study shows that phosphorylation of SAMHD1 at Thr592 increases tetramer dynamics and ssDNA binding, leading to rapid inactivation of dNTPase activity at stalled replication forks.

bioRxiv · Apr 5, 2022Biochemistry