Eric J. Enemark
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); W. M. Keck Foundation (2014); Winthrop Rockefeller Foundation (2024–2026); University of Tennessee at Knoxville (2013); Stanford University (1995–1998)
Faculty Researcher
Biochemistry & Molecular Biology, College of Medicine
Research Areas
Biomedical Subjects
Biography and Research Information
OverviewAI-generated summary
Eric J. Enemark investigates the molecular mechanisms underlying nucleic acid machines, focusing on the structure and function of viral and cellular proteins involved in DNA replication and RNA binding. His research group utilizes structural biology techniques, including X-ray crystallography, to elucidate the atomic details of these protein complexes. Recent work has characterized the RNA-stimulated ATPase activity of the enteroviral 2C protein and described the distinct DNA binding modes of the MCM helicase, which are critical for DNA translocation. Enemark's laboratory also studies the structural basis of protein-nucleic acid interactions, as evidenced by their work on the GINS tetramer and the functional characterization of SNPs affecting protein interactions, such as those in the HELB gene.
His work has been supported by federal funding, including a grant from the National Institute of General Medical Sciences (NIGMS) for the "Molecular mechanisms of nucleic acid machines." Enemark is a highly cited researcher with a significant publication record and has established collaborations with researchers at the University of Arkansas for Medical Sciences. His research contributes to understanding fundamental biological processes in DNA replication, viral pathogenesis, and protein function at a molecular level.
Metrics
- h-index: 21
- Publications: 76
- Citations: 2,672
Selected Publications
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Archaeal and eukaryotic MCM rings sequentially melt DNA for replication initiation (2026)
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MCM Setting RMSD Calculations (2026)
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MCM Inter-Tier Dihedral Calculations (2026)
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MCM Inter-Tier Dihedral Calculations (2026)
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MCM Setting RMSD Calculations (2026)
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Rare SNP in the <i>HELB</i> gene interferes with RPA interaction and cellular function of HELB (2025)
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Structure of the <i>Saccharolobus solfataricus</i> GINS tetramer (2025)
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Rare SNP in the <i>HELB</i> gene interferes with RPA interaction and cellular function of HELB (2024)
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Structural and functional characterization of Enteroviral 2C protein, an RNA-stimulated ATPase (2023)
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Two Distinct Modes of DNA Binding by an MCM Helicase Enable DNA Translocation (2022)
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Enteroviral 2C protein is an RNA-stimulated ATPase and uses a two-step mechanism for binding to RNA and ATP (2022)
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Enteroviral 2C protein is an RNA-stimulated ATPase and uses a two-step mechanism for binding to RNA and ATP (2022)
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Structure of a dimer of the <i>Sulfolobus solfataricus</i> MCM N-terminal domain reveals a potential role in MCM ring opening (2021)
Federal Grants 1 $380,002 total
Collaboration Network
Top Collaborators
- 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
- 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
- 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
- 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
- Two Distinct Modes of DNA Binding by an MCM Helicase Enable DNA Translocation
- Structure of a dimer of the <i>Sulfolobus solfataricus</i> MCM N-terminal domain reveals a potential role in MCM ring opening
- 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
- 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
- Rare SNP in the <i>HELB</i> gene interferes with RPA interaction and cellular function of HELB
- Rare SNP in the <i>HELB</i> gene interferes with RPA interaction and cellular function of HELB
- Rare SNP in the <i>HELB</i> gene interferes with RPA interaction and cellular function of HELB
- Rare SNP in the <i>HELB</i> gene interferes with RPA interaction and cellular function of HELB
- Rare SNP in the <i>HELB</i> gene interferes with RPA interaction and cellular function of HELB
- Rare SNP in the <i>HELB</i> gene interferes with RPA interaction and cellular function of HELB
- Rare SNP in the <i>HELB</i> gene interferes with RPA interaction and cellular function of HELB
- Rare SNP in the <i>HELB</i> gene interferes with RPA interaction and cellular function of HELB
- Rare SNP in the <i>HELB</i> gene interferes with RPA interaction and cellular function of HELB
- Rare SNP in the <i>HELB</i> gene interferes with RPA interaction and cellular function of HELB
- Rare SNP in the <i>HELB</i> gene interferes with RPA interaction and cellular function of HELB
- Rare SNP in the <i>HELB</i> gene interferes with RPA interaction and cellular function of HELB
- Rare SNP in the <i>HELB</i> gene interferes with RPA interaction and cellular function of HELB
- Rare SNP in the <i>HELB</i> gene interferes with RPA interaction and cellular function of HELB
- Structure of a dimer of the <i>Sulfolobus solfataricus</i> MCM N-terminal domain reveals a potential role in MCM ring opening
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