Eric J. Enemark

Federal Grant PI High Impact

Associate Professor

University of Arkansas for Medical Sciences

faculty

Biochemistry & Molecular Biology, College of Medicine

ejenemark@uams.edu

21 h-index 71 pubs 2,622 cited

Research Areas

Molecular Biology Techniques and Applications RNA and protein synthesis mechanisms DNA Repair Mechanisms Protein Structure and Dynamics Microbial infections and disease research Genomics and Phylogenetic Studies

Links

ORCID Lab Website Research Group UAMS TRI Profile

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OverviewAI-generated summary

Eric J. Enemark's research focuses on the molecular mechanisms of nucleic acid machines, particularly investigating the functions of viral proteins and cellular helicases. He is a recipient of a National Institute of General Medical Sciences (NIH/NIGMS) grant totaling $380,002, which supports his work on these molecular machines. His laboratory group has published research on the enteroviral 2C protein, characterizing it as an RNA-stimulated ATPase with a two-step mechanism for binding RNA and ATP. Additional studies have explored the DNA binding modes of MCM helicase and the functional impact of specific genetic variations, such as a rare SNP in the HELB gene affecting its interaction with RPA. Enemark's scholarly contributions include 71 publications, with an h-index of 21 and over 2,600 citations. He also collaborates with researchers at the University of Arkansas for Medical Sciences and other institutions, including Maroof Zafar, Kirk L. West, and Benjamin May.

Metrics

  • h-index: 21
  • Publications: 71
  • Citations: 2,622

Selected Publications

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

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

Collaborators

Researchers in the database who share publications

Maroof Zafar University of Arkansas for Medical Sciences 2 shared publications Matthew D. Thompson Lyon College 2 shared publications Kirk L. West University of Arkansas for Medical Sciences 2 shared publications Benjamin May University of Arkansas for Medical Sciences 2 shared publications Bertha Osei University of Arkansas for Medical Sciences 2 shared publications Duah Alkam University of Arkansas for Medical Sciences 1 shared publication J. L. Beard University of Arkansas for Medical Sciences 1 shared publication Srihari Shankar University of Arkansas for Medical Sciences 1 shared publication

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