Author

Mohammad Hashemian

University of California, Davis

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

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 2 Assay:structural biology· 2 Research Focus:chromatin & epigenetic regulation· 1 Organism:human· 1 Approach:mechanistic / dynamical model· 1 Assay:protein structure· 1 Approach:statistical model· 1

Frequent Co-Authors

Carlos H. Trasviña‐ArenasiD· 3 shared Sheila S. DavidiD· 3 shared Andrew J. FisheriD· 2 shared Abigayle F. VitoiD· 1 shared Bret FreudenthaliD· 1 shared Caleb S JacquesiD· 1 shared Emmanuelle BignoniD· 1 shared Gerardo Andrés CisnerosiD· 1 shared

Activity by Year

2025-2025 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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3 shared papersBiochemistry

Carlos H. Trasviña‐ArenasORCID

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3 papers

Recent·Most cited

Crystal structure of MutYX: A novel clusterless adenine DNA glycosylase with a distinct C-terminal domain and 8-Oxoguanine recognition sphere

Carlos H. Trasviña‐Arenas, Mohammad Hashemian, Melody Malek, Steven Merrill, Andrew J. Fisher, Sheila S. David

The paper determines the crystal structure of MutYX, a clusterless adenine DNA glycosylase, revealing structural adaptations that enable OG recognition without a [4Fe-4S] cofactor.

Nucleic Acids Research · Nov 13, 2025Peer-reviewedBiochemistry

Structure, dynamics, and processing of 8oxoG:A in the nucleosome

Abigayle F. Vito, Justin A. Ling, Julia C. Ferrara, Caleb S Jacques, Natacha Gillet, Roy González‐Alemán, Yuya Qiu, Mohammad Hashemian, Carlos H. Trasviña‐Arenas, Sheila S. David, Sarah Delaney, Emmanuelle Bignon, Bret Freudenthal

This study determines the structure and dynamics of 8oxoG:C and 8oxoG:A base pairs in the nucleosome and characterizes MUTYH activity, revealing that 8oxoG:A is less processable by MUTYH.

bioRxiv · Sep 2, 2025 · PreprintBiochemistry

Structure of human MUTYH and functional profiling of cancer-associated variants reveal an allosteric network between its cluster cofactor and active site required for DNA repair

Carlos H. Trasviña‐Arenas, Upeksha C. Dissanayake, Nikole Tamayo, Mohammad Hashemian, Wen-Jen Lin, Merve Demir, Nallely Hoyos-Gonzalez, Andrew J. Fisher, Gerardo Andrés Cisneros, Martin P. Horvath, Sheila S. David

The paper investigates the role of the [4Fe-4S] cofactor in MUTYH DNA repair by analyzing cancer variants and solving the enzyme's crystal structure.

Nature Communications · Apr 15, 2025Peer-reviewedBiochemistry