Author

Andrew J. Fisher

University of California, DavisORCID 0000-0003-3488-6594Unclaimed ORCID profile · follow to get notified of new preprints

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· 3 Organism:human· 2 Assay:structural biology· 2 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:protein structure· 1 Approach:statistical model· 1

Frequent Co-Authors

Carlos H. Trasviña‐ArenasiD· 3 shared Sheila S. DavidiD· 3 shared Melody MalekiD· 2 shared Mohammad Hashemian· 2 shared Alam X León Cardona· 1 shared April Lu· 1 shared Gerardo Andrés CisnerosiD· 1 shared Martin P. HorvathiD· 1 shared

Activity by Year

2025-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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3 shared papersBiochemistry

Carlos H. Trasviña‐ArenasORCID

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3 papers

Recent·Most cited

BiochemistrybioRxivPreprintMay 30, 2026

Structural Connectivity Between the Zinc Linchpin Motif, the cluster, and the active site orchestrates DNA repair in MUTYH

Mohammad H. Hashemian, Melody Malek, Tian Xia…·Sheila S. David

This study presents MUTYH crystal structures showing how the Zn linchpin and Fe-S cluster interact to facilitate DNA repair, revealing how mutations disrupt this process.

DOI 10.64898/2026.05.27.728240

humanstructural biology

𝕏 PostBluesky

BiochemistryNucleic Acids ResearchPeer-reviewedNov 13, 2025

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…·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.

1 citation

protein structureexperimental assay

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BiochemistryNature CommunicationsPeer-reviewedApr 15, 2025

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…·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.

21 citationstop 2%

humanstructural biology

𝕏 PostBluesky