Author

Anthony Asencio

University of WashingtonORCID 0000-0002-8147-0180Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Assay:ATAC-seq· 1 Assay:bulk RNA-seq· 1 Research Focus:drug response / drug discovery· 1 Organism:human· 1

Frequent Co-Authors

Michael RegnieriD· 2 shared Timothy S. McMilleniD· 2 shared Ateeqa NaimiD· 1 shared Bertrand C.W. TanneriD· 1 shared Christian MandryckyiD· 1 shared Farid Moussavi‐HaramiiD· 1 shared Galina V. FlintiD· 1 shared Jing ZhaoiD· 1 shared

Activity by Year

2025-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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2 shared papersBiochemistry

Michael RegnierORCID

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2 papers

Recent·Most cited

Revisiting the SRX paradox for myosin and myofibrils

Kerry Y. Kao, Kalen Z. Robeson, Anthony Asencio, Tristan Wasley, Timothy S. McMillen, Joseph D. Powers, Michael A. Geeves, Michael Regnier

The paper re-examines the SRX state in myosin using mant-ATP displacement assays and finds no evidence of the SRX state in isolated myosin but detects two components in myofibrils, suggesting distinct myosin populations in thick filaments.

bioRxiv · Oct 29, 2026 · PreprintBiochemistry

Myosin modulator Aficamten inhibits force in cardiac muscle by altering myosin's biochemical activity without changing thick filament structure

Saffie E. Mohran, Kristina Bezold Kooiker, Ateeqa Naim, Matvey Pilagov, Anthony Asencio, Kyrah L. Turner, Weikang Ma, Galina V. Flint, Siyao Jiang, Jing Zhao, Timothy S. McMillen, Christian Mandrycky, Max Mahoney-Schaefer, Thomas C. Irving, Bertrand C.W. Tanner, , Farid Moussavi‐Harami

This paper shows Aficamten inhibits cardiac myosin ATPase without changing thick filament structure, unlike Mavacamten, leading to similar force reduction but different kinetic effects.

bioRxiv · May 14, 2025 · PreprintBiophysics