Author

M. Grasso

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· 3 Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Organism:human· 2 Assay:proteomics· 2 Organism:virus· 2 Research Focus:cell signaling & trafficking· 1 Assay:cryo-EM· 1 Research Focus:drug response / drug discovery· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

P. M. M. Shelton· 3 shared P. D. B. Olinares· 2 shared R. Marmorstein· 2 shared T. M. Kapoor· 2 shared A. Aher· 1 shared B. Chait· 1 shared B. Malone· 1 shared B. T. Chait· 1 shared

Activity by Year

2020-2023 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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3 shared papersBiophysics

P. M. M. Shelton

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

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, P. D. B. Olinares, L. E. Vostal, H. Soileau, M. Grasso, S. Warrington, S. Adaniya, M. Miller, S. Sun, D. J. Huggins, R. W. Myers, B. T. Chait, E. V. Vinogradova, 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.

bioRxiv · Sep 25, 2023Biochemistry

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

J. Chen, B. Malone, E. Llewellyn, M. Grasso, P. M. M. Shelton, P. D. B. Olinares, K. Maruthi, E. T. Eng, H. Vatandaslar, B. Chait, T. Kapoor, S. A. Darst, 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.

Cell · Sep 1, 2020Peer-reviewedBiophysics

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

K. J. Mickolajczyk, P. M. M. Shelton, M. Grasso, X. Cao, S. R. Warrington, A. Aher, S. Liu, 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.

bioRxiv · Jul 31, 2020Biophysics

Identification and Characterization of a B-Raf Kinase Alpha Helix Critical for the Activity of MEK Kinase in MAPK Signaling

D. Nguyen, L. Y. Lin, J. Zhou, E. Kibby, T. Sia, T. Tillis, N. Vapuryan, M.-R. Xu, R. Potluri, Y. Shin, E. Erler, N. Bronkema, D. Boehmler, C. Chung, C. Burkhard, , D. Fera

The paper identifies an alpha helix on B-Raf critical for its interaction with MEK and oncogenic activity, suggesting it as a potential drug target for melanoma treatment.

bioRxiv · Jul 19, 2020 · PreprintBiochemistry

Structural and molecular determinants of CCS-mediated copper activation of MEK1/2

M. Grasso, G. J. Bond, Y.-J. Kim, K. B. Alwan, S. Boyd, M. M. Dzebo, S. Valenzuela, T. Tsang, N. A. Schibrowsky, M. L. Matthews, G. M. Burslem, P. Wittung-Stafshede, D. D. Winkler, N. J. Blackburn, R. Marmorstein, D. C. Brady

The paper reports the X-ray structure of Cu-MEK1, revealing Cu coordination and CCS-mediated Cu transfer, and identifies molecular mechanisms for Cu-stimulated MEK1 kinase activity.

bioRxiv · May 1, 2020 · PreprintBiochemistry