Eric John Enemark, PhD
Full Member
Research Program:
Cancer Biology
Faculty Rank:
Associate Professor
Campus:
University of Arkansas for Medical Sciences
College:
College of Medicine
Department:
Biochemistry & Molecular Biology
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Cancer Research Interest
- Disease Site Focus: No Specific Disease Site
- Research Focus Area: Diagnosis/ Prognosis, Carcinogenesis
- Type of Research: Basic
- Research Interest Statement: The following is the Relevance Statement from my R35 grant: A major focus of the project is DNA replication, a fundamental event that is required in all life forms, and its disruption can lead to several forms of disease, including cancer. The central engine of the replication machinery is the hexameric MCM complex that unwinds DNA at the replication fork once the tightly regulated replication process begins. MCMs and the kinases that activate them are logical, promising targets for anti-cancer therapies. A second focus of the project is the human RNA helicase DDX3X, which is associated with several human diseases, including HIV, HCV, and the brain cancer medulloblastoma. Mutation of this gene has been linked to medulloblastoma by genetic sequencing studies.
Contact Information
- Email Address: EJENEMARK@UAMS.EDU
- Profiles Research Networking Software: View Profile
Active Grants
- NIGMS – 1P20GM152281“Structural Biology Core”Principal Investigator3/5/2024 – 12/31/2028
- NIH/Nat. Inst. of General Medical Sciences – 7R35GM136313“Molecular mechanisms of nucleic acid machines”Principal Investigator11/24/2020 – 5/31/2025
Recent Publications
- Meagher M, Myasnikov A, Enemark EJ. Two Distinct Modes of DNA Binding by an MCM Helicase Enable DNA Translocation. International journal of molecular sciences. 2022 23(23). PMID: 36499022. PMCID: PMC9735655.
- Yeager C, Carter G, Gohara DW, [et al., including Enemark EJ]. Enteroviral 2C protein is an RNA-stimulated ATPase and uses a two-step mechanism for binding to RNA and ATP. Nucleic acids research. 2022 50(20):11775-11798. PMID: 36399514. PMCID: PMC9723501.
- Meagher M, Spence MN, Enemark EJ. Structure of a dimer of the Sulfolobus solfataricus MCM N-terminal domain reveals a potential role in MCM ring opening. Acta crystallographica. Section F, Structural biology communications. 2021 77(Pt 6):177-186. PMID: 34100776. PMCID: PMC8186412.