Author

Merve Demir

Sanford Burnham Prebys Medical Discovery InstituteORCID 0000-0002-5721-8268Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biochemistry· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:human· 3 Research Focus:drug response / drug discovery· 2 Research Focus:protein folding & dynamics· 2 Approach:statistical model· 2 Assay:structural biology· 2 Research Focus:chromatin & epigenetic regulation· 1 Assay:DNA methylation· 1

Frequent Co-Authors

Andrey A. BobkoviD· 2 shared Eduard A. SergienkoiD· 2 shared Jianhua ZhaoiD· 2 shared Laura KoeppingiD· 2 shared Lynn Miya FujimotoiD· 2 shared Martin P. HorvathiD· 2 shared Sheila S. DavidiD· 2 shared Taro HitosugiiD· 2 shared

Activity by Year

2024-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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2 shared papersBiochemistry

Andrey A. BobkovORCID

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4 papers

Recent·Most cited

BiochemistryChemBioChemPeer-reviewedJun 11, 2026

Structural Basis for Nucleobase Activation by the Adenine DNA Glycosylase MutY

L. Peyton Russelburg, Merve Demir, Karina Cedeno…·Martin P. Horvath

This study investigates the role of catalytic Glu43 in MutY's mechanism by analyzing variants and showing their impact on substrate conformation and product formation.

DOI 10.1002/cbic.70414

DNA methylationexperimental assay

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BiochemistryJournal of Molecular BiologyPeer-reviewedJun 9, 2026

Uncompetitive Allosteric Inhibitor of Mitochondrial Creatine Kinase Prevents Binding and Release of Creatine by Stabilization of Loop Closure

Merve Demir, Chen-Ting Ma, Nikhil Puvvula…·Eduard A. Sergienko

The paper identifies an uncompetitive allosteric inhibitor of mitochondrial creatine kinase that stabilizes loop closure, preventing creatine binding and phosphocreatine release.

DOI 10.1016/j.jmb.2026.169896

humanexperimental 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

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BiochemistryStructurePeer-reviewedJun 18, 2024

Structural Basis for Substrate Binding, Catalysis and Inhibition of Breast Cancer Target Mitochondrial Creatine Kinase by Covalent Inhibitor via Cryo-EM

Merve Demir, Laura Koepping, Ya Li…·Eduard A. Sergienko

The paper investigates the structural and mechanistic features of mitochondrial creatine kinase (uMtCK) and evaluates the efficacy of a covalent inhibitor in breast cancer cells.

3 citations

humanstructural biology

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