Author

P. M. M. Shelton

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 Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:human· 2 Organism:virus· 2 Approach:biophysical modeling· 1 Assay:ChIP-seq· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:cryo-EM· 1 Research Focus:drug response / drug discovery· 1

Frequent Co-Authors

M. Grasso· 3 shared P. D. B. Olinares· 2 shared T. M. Kapoor· 2 shared A. Aher· 1 shared B. Chait· 1 shared B. Malone· 1 shared B. Roeder· 1 shared B. T. Chait· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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3 shared papersBiophysics

M. Grasso

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Author profile →

4 papers

Recent·Most cited

BiochemistrybioRxivSep 25, 2023

Using a function-first "scout fragment"-based approach to develop allosteric covalent inhibitors of conformationally dynamic helicase mechanoenzymes

J. R. Ramsey, P. M. M. Shelton, T. K. Heiss…·T. M. Kapoor

The paper develops covalent inhibitors for conformationally dynamic helicases using electrophilic scout fragments and a function-first approach, targeting SARS-CoV-2 nsp13 and human helicases BLM and WRN.

DOI 10.1021/jacs.3c10581

humanvirus

𝕏 PostBluesky

BiochemistrybioRxivApr 8, 2021

Sumoylation of the human histone H4 tail inhibits p300-mediated transcription by RNA polymerase II in cellular extracts

C. J. A. Leonen, M. Shimada, C. E. Weller…·C. Chatterjee

This study shows that sumoylation of H4K12 inhibits p300-mediated transcription and H3K4 methylation in vitro.

DOI 10.7554/elife.67952

humanChIP-seq

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BiophysicsCellPeer-reviewedSep 1, 2020

Structural basis for helicase-polymerase coupling in the SARS-CoV-2 replication-transcription complex

J. Chen, B. Malone, E. Llewellyn…·E. A. Campbell

The paper presents cryo-EM structures of the SARS-CoV-2 holo-RdRp complex with nsp13 helicase, revealing interactions and a new therapeutic target.

DOI 10.1016/j.cell.2020.07.033

viruscryo-EM

𝕏 PostBluesky

BiophysicsbioRxivJul 31, 2020

Force-dependent stimulation of RNA unwinding by SARS-CoV-2 nsp13 helicase

K. J. Mickolajczyk, P. M. M. Shelton, M. Grasso…·T. M. Kapoor

This study investigates the force-dependent unwinding activity of SARS-CoV-2 nsp13 helicase using optical tweezers, revealing increased unwinding frequency, processivity, and velocity under destabilizing force.

DOI 10.1016/j.bpj.2020.11.2276

experimental assay

𝕏 PostBluesky