Biography and Research Information
OverviewAI-generated summary
David R. Proffitt's research investigates the function of the Pif1 helicase, a protein involved in DNA repair and replication. His work has identified specific residues within the Pif1 helicase's DNA binding site that are crucial for its nuclear functions, while being dispensable for mitochondrial respiratory growth. Proffitt's publications also explore how Pif1 helicase remodels protein-nucleic acid complexes, specifically its role in the dissociation of Sub1 from G-quadruplex DNA and Cdc13 from G-rich single-stranded DNA. His research is conducted in collaboration with scientists at the University of Arkansas for Medical Sciences, including Kevin D. Raney, Alicia K. Byrd, and Wayne P. Wahls, as well as John C. Marecki at the University of Arkansas at Fayetteville. Proffitt has authored two publications, has a total of 8 citations, and an h-index of 1.
Metrics
- h-index: 2
- Publications: 2
- Citations: 9
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
Jun Gao
University of Arkansas for Medical Sciences (US)
2 shared publications
- 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
Alicia K. Byrd
University of Arkansas for Medical Sciences
2 shared publications
In database
- 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
Kevin D. Raney
University of Arkansas for Medical Sciences
2 shared publications
In database
- 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
Shubeena Chib
University of Arkansas for Medical Sciences (US)
1 shared publication
- 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
Wezley C. Griffin
University of Arkansas for Medical Sciences (US)
1 shared publication
- 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
John C. Marecki
University of Arkansas for Medical Sciences
1 shared publication
In database
- Two residues in the DNA binding site of Pif1 helicase are essential for nuclear functions but dispensable for mitochondrial respiratory growth
Reine U. Protacio
University of Arkansas for Medical Sciences
1 shared publication
In database
- Two residues in the DNA binding site of Pif1 helicase are essential for nuclear functions but dispensable for mitochondrial respiratory growth
Wayne P. Wahls
University of Arkansas for Medical Sciences
1 shared publication
In database
- 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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Based on overlapping research topics
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