Eric J. Enemark

Federal Grant PI High Impact

Associate Professor

Last publication 2026 Last refreshed 2026-05-22

faculty

Biochemistry & Molecular Biology, College of Medicine

ejenemark@uams.edu

21 h-index 76 pubs 2,650 cited

Biography and Research Information

OverviewAI-generated summary

Eric J. Enemark, an Associate Professor in Biochemistry & Molecular Biology at the University of Arkansas for Medical Sciences, investigates the molecular mechanisms underlying nucleic acid machines. His research group focuses on the structural and functional characterization of proteins involved in DNA replication and viral RNA/ATP interactions. He is a Principal Investigator on a $380,002 NIH/National Institute of General Medical Sciences grant aimed at elucidating these molecular mechanisms.

Dr. Enemark's recent publications include studies on the ATP-binding and RNA-binding mechanisms of enteroviral 2C protein, the structural basis for DNA translocation by MCM helicases, and the functional impact of genetic variations in the HELB gene. He has also published work on the structure of the GINS tetramer from *Saccharolobus solfataricus*. His scholarly contributions are recognized by an h-index of 21, with over 75 publications and 2,630 citations. He collaborates with several researchers at the University of Arkansas for Medical Sciences, including Maroof K. Zafar, Alicia K. Byrd, Matthew D. Thompson, and Kirk L. West.

Metrics

  • h-index: 21
  • Publications: 76
  • Citations: 2,650

Selected Publications

  • Rare SNP in the <i>HELB</i> gene interferes with RPA interaction and cellular function of HELB (2025)
  • Structure of the <i>Saccharolobus solfataricus</i> GINS tetramer (2025)
  • Rare SNP in the <i>HELB</i> gene interferes with RPA interaction and cellular function of HELB (2024)
  • Structural and functional characterization of Enteroviral 2C protein, an RNA-stimulated ATPase (2023)
  • Two Distinct Modes of DNA Binding by an MCM Helicase Enable DNA Translocation (2022)
    4 citations DOI OpenAlex
  • Enteroviral 2C protein is an RNA-stimulated ATPase and uses a two-step mechanism for binding to RNA and ATP (2022)
    18 citations DOI OpenAlex
  • Enteroviral 2C protein is an RNA-stimulated ATPase and uses a two-step mechanism for binding to RNA and ATP (2022)
    1 citation DOI OpenAlex
  • Structure of a dimer of the <i>Sulfolobus solfataricus</i> MCM N-terminal domain reveals a potential role in MCM ring opening (2021)

View all publications on OpenAlex →

Federal Grants 1 $380,002 total

NIH/National Institute of General Medical Sciences Contact PI Jun 2020 - May 2026

Molecular mechanisms of nucleic acid machines

National Institute of General Medical Sciences $380,002 R35

Collaboration Network

36 Collaborators 8 Institutions 1 Country

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