Match tier
Listed
Presence
Current · Arkansas
Last published
2026
Sources
OpenAlex · ORCID
Refreshed
2026-10-09
E
Eric J. Enemark
Federal Grant PI
High Impact
Associate Professor
Also affiliated: St. Jude Children's Research Hospital (2013–2026); University of Tennessee Health Science Center (2013–2015); Cold Spring Harbor Laboratory (2000–2014); Stanford University (1995–1998)
Biochemistry & Molecular Biology, College of Medicine
21 h-index
823 pubs
2,703 cited
Research Areas
Biomedical Subjects
Biography and Research Information
OverviewAI-generated summary
Eric J. Enemark studies the molecular mechanisms underlying nucleic acid machines, focusing on the structure and function of helicases. His research group investigates these essential proteins, which play critical roles in DNA replication and repair. Enemark's work utilizes structural biology techniques, including X-ray crystallography, to elucidate the atomic-level details of how these molecular motors operate.
His publications include studies on the DNA translocation mechanisms of replicative hexameric helicases and the fundamental characteristics of the AAA+ protein family. Enemark has received federal funding from the NIH/National Institute of General Medical Sciences for his research on molecular mechanisms of nucleic acid machines. He has a significant publication record, with over 700 publications and an h-index of 21, indicating a substantial impact in his field. Enemark 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: 823
- Citations: 2,703
Positions
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Associate Professor 2021–presentUniversity of Arkansas for Medical Sciences Biochemistry & Molecular Biology, College of Medicine Institutional directory
Selected Publications
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Data for EMSL Project 50414 from February 2025 (2026)
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Data for EMSL Project 50414 from January 2025 (2026)
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Data for EMSL Project 50414 from October 2024 (2026)
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Data for EMSL Project 50414 from June 2024 (2026)
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Data for EMSL Project 50414 from March 2025 (2026)
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Data for EMSL Project 50414 from January 2025 (2026)
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Data for EMSL Project 50414 from December 2024 (2026)
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Data for EMSL Project 50414 from October 2024 (2026)
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Data for EMSL Project 50414 from March 2025 (2026)
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Data for EMSL Project 50414 from September 2024 (2026)
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Data for EMSL Project 50414 from September 2024 (2026)
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Data for EMSL Project 50414 from September 2024 (2026)
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Data for EMSL Project 50414 from October 2024 (2026)
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Data for EMSL Project 50414 from February 2025 (2026)
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Data for EMSL Project 50414 from August 2024 (2026)
Federal Grants 1 $380,002 total
NIH
Contact PI
Jun 2020 - May 2026
Collaboration Network
Top Collaborators
Calvin Yeager
University of North Carolina at Chapel Hill (US)
3 shared publications
- Enteroviral 2C protein is an RNA-stimulated ATPase and uses a two-step mechanism for binding to RNA and ATP
- Enteroviral 2C protein is an RNA-stimulated ATPase and uses a two-step mechanism for binding to RNA and ATP
- Structural and functional characterization of Enteroviral 2C protein, an RNA-stimulated ATPase
David W. Gohara
Washington University in St. Louis (US)
3 shared publications
- Enteroviral 2C protein is an RNA-stimulated ATPase and uses a two-step mechanism for binding to RNA and ATP
- Enteroviral 2C protein is an RNA-stimulated ATPase and uses a two-step mechanism for binding to RNA and ATP
- Structural and functional characterization of Enteroviral 2C protein, an RNA-stimulated ATPase
Neela H. Yennawar
Pennsylvania State University (US)
3 shared publications
- Enteroviral 2C protein is an RNA-stimulated ATPase and uses a two-step mechanism for binding to RNA and ATP
- Enteroviral 2C protein is an RNA-stimulated ATPase and uses a two-step mechanism for binding to RNA and ATP
- Structural and functional characterization of Enteroviral 2C protein, an RNA-stimulated ATPase
Craig E. Cameron
University of North Carolina at Chapel Hill (US)
3 shared publications
- Enteroviral 2C protein is an RNA-stimulated ATPase and uses a two-step mechanism for binding to RNA and ATP
- Enteroviral 2C protein is an RNA-stimulated ATPase and uses a two-step mechanism for binding to RNA and ATP
- Structural and functional characterization of Enteroviral 2C protein, an RNA-stimulated ATPase
Martin Meagher
St. Jude Children's Research Hospital (US)
2 shared publications
- Two Distinct Modes of DNA Binding by an MCM Helicase Enable DNA Translocation
- Structure of a dimer of the Sulfolobus solfataricus MCM N-terminal domain reveals a potential role in MCM ring opening
Griffin Carter
University of North Carolina at Chapel Hill (US)
2 shared publications
- Enteroviral 2C protein is an RNA-stimulated ATPase and uses a two-step mechanism for binding to RNA and ATP
- Enteroviral 2C protein is an RNA-stimulated ATPase and uses a two-step mechanism for binding to RNA and ATP
Jamie J. Arnold
University of North Carolina at Chapel Hill (US)
2 shared publications
- Enteroviral 2C protein is an RNA-stimulated ATPase and uses a two-step mechanism for binding to RNA and ATP
- Enteroviral 2C protein is an RNA-stimulated ATPase and uses a two-step mechanism for binding to RNA and ATP
Bertha Osei
University of Arkansas for Medical Sciences
2 shared publications
In database
- Rare SNP in the HELB gene interferes with RPA interaction and cellular function of HELB
- Rare SNP in the HELB gene interferes with RPA interaction and cellular function of HELB
Benjamin May
University of Arkansas for Medical Sciences
2 shared publications
In database
- Rare SNP in the HELB gene interferes with RPA interaction and cellular function of HELB
- Rare SNP in the HELB gene interferes with RPA interaction and cellular function of HELB
Kirk L. West
Winthrop Rockefeller Foundation
2 shared publications
In database
- Rare SNP in the HELB gene interferes with RPA interaction and cellular function of HELB
- Rare SNP in the HELB gene interferes with RPA interaction and cellular function of HELB
Maroof K. Zafar
University of Arkansas for Medical Sciences
2 shared publications
In database
- Rare SNP in the HELB gene interferes with RPA interaction and cellular function of HELB
- Rare SNP in the HELB gene interferes with RPA interaction and cellular function of HELB
Matthew D. Thompson
University of Arkansas for Medical Sciences
2 shared publications
In database
- Rare SNP in the HELB gene interferes with RPA interaction and cellular function of HELB
- Rare SNP in the HELB gene interferes with RPA interaction and cellular function of HELB
Erik N. Bergstrom
Missouri University of Science and Technology (US)
2 shared publications
- Rare SNP in the HELB gene interferes with RPA interaction and cellular function of HELB
- Rare SNP in the HELB gene interferes with RPA interaction and cellular function of HELB
Alicia K. Byrd
Winthrop Rockefeller Foundation
2 shared publications
In database
- Rare SNP in the HELB gene interferes with RPA interaction and cellular function of HELB
- Rare SNP in the HELB gene interferes with RPA interaction and cellular function of HELB
Madison N. Spence
St. Jude Children's Research Hospital (US)
1 shared publication
- Structure of a dimer of the Sulfolobus solfataricus MCM N-terminal domain reveals a potential role in MCM ring opening
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