Research Areas
Biomedical Subjects
Biography and Research Information
OverviewAI-generated summary
David R. Proffitt studies the Pif1 helicase, an enzyme involved in DNA repair and replication. His research investigates how this helicase functions in different cellular compartments, specifically the nucleus and mitochondria. Recent work has identified specific residues within the Pif1 helicase that are crucial for its nuclear functions, while also showing these residues are not essential for mitochondrial respiratory growth. Proffitt's publications also explore how Pif1 mediates the remodeling of protein-nucleic acid complexes, including its role in dissociating Sub1 from G-quadruplex DNA and Cdc13 from G-rich single-stranded DNA.
Proffitt collaborates with researchers at the University of Arkansas for Medical Sciences, including Kevin D. Raney, Alicia K. Byrd, Jun Gao, and John C. Marecki. His work contributes to the understanding of fundamental cellular processes, particularly those involving DNA metabolism and protein-nucleic acid interactions. His current h-index is 2, with a total of 2 publications and 10 citations.
Metrics
- h-index: 2
- Publications: 2
- Citations: 12
Selected Publications
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Two residues in the DNA binding site of Pif1 helicase are essential for nuclear functions but dispensable for mitochondrial respiratory growth (2024)
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Pif1 Helicase Mediates Remodeling of Protein-Nucleic Acid Complexes by Promoting Dissociation of Sub1 from G-Quadruplex DNA and Cdc13 from G-Rich Single-Stranded DNA (2023)
Collaboration Network
Top Collaborators
- Pif1 Helicase Mediates Remodeling of Protein-Nucleic Acid Complexes by Promoting Dissociation of Sub1 from G-Quadruplex DNA and Cdc13 from G-Rich Single-Stranded DNA
- Two residues in the DNA binding site of Pif1 helicase are essential for nuclear functions but dispensable for mitochondrial respiratory growth
- Pif1 Helicase Mediates Remodeling of Protein-Nucleic Acid Complexes by Promoting Dissociation of Sub1 from G-Quadruplex DNA and Cdc13 from G-Rich Single-Stranded DNA
- Two residues in the DNA binding site of Pif1 helicase are essential for nuclear functions but dispensable for mitochondrial respiratory growth
- Pif1 Helicase Mediates Remodeling of Protein-Nucleic Acid Complexes by Promoting Dissociation of Sub1 from G-Quadruplex DNA and Cdc13 from G-Rich Single-Stranded DNA
- Two residues in the DNA binding site of Pif1 helicase are essential for nuclear functions but dispensable for mitochondrial respiratory growth
- Pif1 Helicase Mediates Remodeling of Protein-Nucleic Acid Complexes by Promoting Dissociation of Sub1 from G-Quadruplex DNA and Cdc13 from G-Rich Single-Stranded DNA
- Pif1 Helicase Mediates Remodeling of Protein-Nucleic Acid Complexes by Promoting Dissociation of Sub1 from G-Quadruplex DNA and Cdc13 from G-Rich Single-Stranded DNA
- Two residues in the DNA binding site of Pif1 helicase are essential for nuclear functions but dispensable for mitochondrial respiratory growth
- Two residues in the DNA binding site of Pif1 helicase are essential for nuclear functions but dispensable for mitochondrial respiratory growth
- Two residues in the DNA binding site of Pif1 helicase are essential for nuclear functions but dispensable for mitochondrial respiratory growth
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