MD
Merve Demir
Sanford Burnham Prebys Medical Discovery Institute, University of California, Davis, Boğaziçi University
Research areas: Biochemistry, Genetics and Molecular Biology · Molecular Biology · Enzyme Structure and Function · DNA Repair Mechanisms · DNA and Nucleic Acid Chemistry
0000-0002-5721-8268
Employment
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Sanford Burnham Prebys Medical Discovery Institute Postdoctoral Associate2022 - Present
Education
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UC Davis PhD2016 - 2022
- 2011 - 2016
- 2011 - 2016
Projects & Funding
Projects & funding information is unavailable.
Publications (13)
- Uncompetitive Allosteric Inhibitor of Mitochondrial Creatine Kinase Prevents Binding and Release of Creatine by Stabilization of Loop Closure Save
- Structural Basis for Nucleobase Activation by the Adenine DNA Glycosylase MutY Save
- Structural Basis for Nucleobase Activation by the Adenine DNA Glycosylase MutY Save
- Uncompetitive Allosteric Inhibitor of Mitochondrial Creatine Kinase Prevents Binding and Release of Creatine by Stabilization of Loop Closure Save
- Uncompetitive Allosteric Inhibitor of Mitochondrial Creatine Kinase Prevents Binding and Release of Creatine by Stabilization of Loop Closure Save
- Structural basis for substrate binding, catalysis, and inhibition of cancer target mitochondrial creatine kinase by a covalent inhibitor Save
- Structure of human MUTYH and functional profiling of cancer-associated variants reveal an allosteric network between its [4Fe-4S] cluster cofactor and active site required for DNA repair Save
- FSHing for DNA Damage: Key Features of MutY Detection of 8-Oxoguanine:Adenine Mismatches Save
- Structural Basis for Substrate Binding, Catalysis and Inhibition of Breast Cancer Target Mitochondrial Creatine Kinase by Covalent Inhibitor via Cryo-EM Save
- Structure of human MUTYH and functional profiling of cancer-associated variants reveal an allosteric network between its [4Fe-4S] cluster cofactor and active site required for DNA repair Save
- Structural snapshots of base excision by the cancer-associated variant MutY N146S reveal a retaining mechanism Save
- Structure, function and evolution of the Helix-hairpin-Helix DNA glycosylase superfamily: Piecing together the evolutionary puzzle of DNA base damage repair mechanisms Save
- Structural Basis for Finding OG Lesions and Avoiding Undamaged G by the DNA Glycosylase MutY Save