Kevin D. Raney
Sourced from institutional research profiles (UAMS TRI or ARA).
Department Chairperson
Also affiliated: University of North Carolina at Chapel Hill (2021); Pennsylvania State University (1994–2008); University of Arizona (2003); Vanderbilt University (1989–2002); University of Arkansas Medical Center (2010–2024); Princess Anne Hospital (2024); University Hospital Southampton NHS Foundation Trust (2024); Winthrop Rockefeller Foundation (2016–2021); Epoch Biosciences (United States) (2003); Conway School of Landscape Design (2000); Arkansas Department of Agriculture (2014); University of Chinese Academy of Sciences (2009)
Faculty Researcher
Department Chairs, College of Medicine
Research Areas
Biomedical Subjects
Biography and Research Information
OverviewAI-generated summary
Kevin D. Raney's research focuses on the mechanisms of helicases and their interactions with nucleic acids, particularly G-quadruplexes. He has received significant federal funding from the NIH/National Institute of General Medical Sciences for projects investigating the functions and mechanisms of these enzymes and their roles in G-quadruplex nucleic acid signaling. His work has led to publications detailing how viral proteins, such as the Hepatitis C virus nonstructural protein NS3, interact with and unfold viral G-quadruplex RNA structures. Further investigations explore how G-quadruplex DNA can influence helicase activity and promote phase separation, as observed with the DEAD-box helicase Ded1p. Raney's group also studies the unwinding mechanisms of eukaryotic Pif1 helicases on G-quadruplex and double-stranded DNA, and how these enzymes remodel protein-nucleic acid complexes. His research group includes collaborators such as John C. Marecki, Alicia K. Byrd, and Jun Gao from the University of Arkansas for Medical Sciences, with whom he has co-authored multiple publications. Raney is recognized as a high-impact researcher with an h-index of 43 and over 4,700 citations.
Metrics
- h-index: 43
- Publications: 130
- Citations: 4,724
Selected Publications
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The nucleoside analog CMX521 inhibits coronavirus RNA-dependent RNA polymerase via a two-pronged mechanism (2026)
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Copy-back RNA synthesis by coronavirus polymerase requires helicase activity and is stimulated by remdesivir and molnupiravir (2026)
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RNA virus polymerase-helicase coupling enables rapid elongation through duplex RNA (2026)
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Template switching by coronavirus polymerase requires helicase activity and is stimulated by remdesivir and molnupiravir (2025)
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A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent (2025)
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Biomolecular condensates control and are defined by RNA-RNA interactions that arise in viral replication (2025)
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RNA virus polymerase-helicase coupling enables rapid elongation through duplex RNA (2025)
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A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent (2025)
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Autophosphorylation of the Tousled-like kinases TLK1 and TLK2 regulates recruitment to damaged chromatin via PCNA interaction (2024)
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Biomolecular condensates control and are defined by RNA-RNA interactions that arise in viral replication (2024)
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Eukaryotic Pif1 helicase unwinds G-quadruplex and dsDNA using a conserved wedge (2024)
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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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Autophosphorylation of the Tousled-like kinases TLK1 and TLK2 regulates recruitment to damaged chromatin via PCNA interaction (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)
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Hepatitis C virus nonstructural protein NS3 unfolds viral G-quadruplex RNA structures (2022)
Federal Grants 2 $1,128,259 total
Functions and Mechanisms of Helicases and G-Quadruplex Nucleic Acids
Collaboration Network
Top Collaborators
- RNA helicases required for viral propagation in humans
- G-quadruplex DNA inhibits unwinding activity but promotes liquid–liquid phase separation by the DEAD-box helicase Ded1p
- Eukaryotic Pif1 helicase unwinds G-quadruplex and dsDNA using a conserved wedge
- A structural feature of Dda helicase which enhances displacement of streptavidin and <i>trp</i> repressor from <scp>DNA</scp>
- Biomolecular condensates control and are defined by RNA-RNA interactions that arise in viral replication
Showing 5 of 11 shared publications
- RNA helicases required for viral propagation in humans
- G-quadruplex DNA inhibits unwinding activity but promotes liquid–liquid phase separation by the DEAD-box helicase Ded1p
- Hepatitis C virus nonstructural protein NS3 unfolds viral G-quadruplex RNA structures
- Eukaryotic Pif1 helicase unwinds G-quadruplex and dsDNA using a conserved wedge
- A structural feature of Dda helicase which enhances displacement of streptavidin and <i>trp</i> repressor from <scp>DNA</scp>
Showing 5 of 7 shared publications
- G-quadruplex DNA inhibits unwinding activity but promotes liquid–liquid phase separation by the DEAD-box helicase Ded1p
- Hepatitis C virus nonstructural protein NS3 unfolds viral G-quadruplex RNA structures
- Eukaryotic Pif1 helicase unwinds G-quadruplex and dsDNA using a conserved wedge
- A structural feature of Dda helicase which enhances displacement of streptavidin and <i>trp</i> repressor from <scp>DNA</scp>
- 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
Showing 5 of 6 shared publications
- A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent
- RNA virus polymerase-helicase coupling enables rapid elongation through duplex RNA
- A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent
- Template switching by coronavirus polymerase requires helicase activity and is stimulated by remdesivir and molnupiravir
- A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent
- RNA virus polymerase-helicase coupling enables rapid elongation through duplex RNA
- A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent
- Template switching by coronavirus polymerase requires helicase activity and is stimulated by remdesivir and molnupiravir
- A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent
- RNA virus polymerase-helicase coupling enables rapid elongation through duplex RNA
- A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent
- Template switching by coronavirus polymerase requires helicase activity and is stimulated by remdesivir and molnupiravir
- A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent
- RNA virus polymerase-helicase coupling enables rapid elongation through duplex RNA
- A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent
- Template switching by coronavirus polymerase requires helicase activity and is stimulated by remdesivir and molnupiravir
- A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent
- RNA virus polymerase-helicase coupling enables rapid elongation through duplex RNA
- A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent
- Template switching by coronavirus polymerase requires helicase activity and is stimulated by remdesivir and molnupiravir
- Eukaryotic Pif1 helicase unwinds G-quadruplex and dsDNA using a conserved wedge
- Primary acute lymphoblastic leukemia cells are susceptible to microtubule depolymerization in G1 and M phases through distinct cell death pathways
- Two residues in the DNA binding site of Pif1 helicase are essential for nuclear functions but dispensable for mitochondrial respiratory growth
- A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent
- A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent
- Template switching by coronavirus polymerase requires helicase activity and is stimulated by remdesivir and molnupiravir
- A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent
- RNA virus polymerase-helicase coupling enables rapid elongation through duplex RNA
- A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent
- A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent
- RNA virus polymerase-helicase coupling enables rapid elongation through duplex RNA
- A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent
- A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent
- RNA virus polymerase-helicase coupling enables rapid elongation through duplex RNA
- A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent
- A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent
- RNA virus polymerase-helicase coupling enables rapid elongation through duplex RNA
- A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent
- Eukaryotic Pif1 helicase unwinds G-quadruplex and dsDNA using a conserved wedge
- A structural feature of Dda helicase which enhances displacement of streptavidin and <i>trp</i> repressor from <scp>DNA</scp>
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