Kevin D. Raney Institution-verified
Sourced from institutional research profiles (UAMS TRI or ARA).
Federal Grant PI
High Impact
Department Chairperson
faculty
Department Chairs, College of Medicine
43 h-index
127 pubs
4,666 cited
Research Areas
Biography and Research Information
OverviewAI-generated summary
Kevin D. Raney's research focuses on the molecular mechanisms of helicases and their roles in nucleic acid metabolism and processing. His work investigates how these enzymes function, particularly in relation to G-quadruplex structures, which are non-canonical DNA and RNA secondary structures implicated in various biological processes. Raney has received federal funding from the NIH/National Institute of General Medical Sciences for two grants totaling over $1.1 million, supporting his investigations into the functions, mechanisms, and signaling pathways involving helicases and G-quadruplex nucleic acids.
His publications detail the unwinding activities of various helicases, including eukaryotic Pif1 helicase and viral helicases such as the Hepatitis C virus nonstructural protein NS3. Raney's group has explored how these helicases interact with and remodel protein-nucleic acid complexes, and how specific structural features can enhance their activity or influence their interactions with DNA. His research also touches upon the role of helicases in viral replication and the formation of biomolecular condensates, which are crucial for cellular processes and can arise during viral replication.
Raney leads a research group and collaborates with researchers at the University of Arkansas for Medical Sciences and the University of Arkansas at Fayetteville. His scholarship metrics include an h-index of 43, with over 128 publications and 4,632 citations, reflecting a significant contribution to his field. He holds the designation of a high-impact researcher.
Metrics
- h-index: 43
- Publications: 127
- Citations: 4,666
Selected Publications
-
Template switching by coronavirus polymerase requires helicase activity and is stimulated by remdesivir and molnupiravir (2025)
-
A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent (2025)
-
Biomolecular condensates control and are defined by RNA-RNA interactions that arise in viral replication (2025)
-
RNA virus polymerase-helicase coupling enables rapid elongation through duplex RNA (2025)
-
A post-assembly conformational change makes the SARS-CoV-2 polymerase elongation-competent (2025)
-
Autophosphorylation of the Tousled-like kinases TLK1 and TLK2 regulates recruitment to damaged chromatin via PCNA interaction (2024)
-
Biomolecular condensates control and are defined by RNA-RNA interactions that arise in viral replication (2024)
-
Eukaryotic Pif1 helicase unwinds G-quadruplex and dsDNA using a conserved wedge (2024)
-
Two residues in the DNA binding site of Pif1 helicase are essential for nuclear functions but dispensable for mitochondrial respiratory growth (2024)
-
Autophosphorylation of the Tousled-like kinases TLK1 and TLK2 regulates recruitment to damaged chromatin via PCNA interaction (2024)
-
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)
-
Hepatitis C virus nonstructural protein NS3 unfolds viral G-quadruplex RNA structures (2022)
-
Primary acute lymphoblastic leukemia cells are susceptible to microtubule depolymerization in G1 and M phases through distinct cell death pathways (2022)
-
RNA helicases required for viral propagation in humans (2021)
-
A structural feature of Dda helicase which enhances displacement of streptavidin and <i>trp</i> repressor from <scp>DNA</scp> (2021)
Federal Grants 2 $1,128,259 total
NIH/National Institute of General Medical Sciences
Contact PI
Jan 2025 - Dec 2029
NIH/National Institute of General Medical Sciences
Contact PI
May 2017 - Apr 2023
Functions and Mechanisms of Helicases and G-Quadruplex Nucleic Acids
Collaboration Network
Top Collaborators
John C. Marecki
University of Arkansas for Medical Sciences
11 shared publications
In database
- 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
Jun Gao
University of Arkansas for Medical Sciences (US)
7 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
Alicia K. Byrd
University of Arkansas for Medical Sciences
7 shared publications
In database
- 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 7 shared publications
Arnab Das
Vrije Universiteit Amsterdam (NL)
4 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
Subhas Chandra Bera
Friedrich-Alexander-Universität Erlangen-Nürnberg (DE)
4 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
Flávia S. Papini
Friedrich-Alexander-Universität Erlangen-Nürnberg (DE)
4 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
Jamie J. Arnold
University of North Carolina at Chapel Hill (US)
4 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
David Dulin
Friedrich-Alexander-Universität Erlangen-Nürnberg (DE)
4 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
Binyam Belachew
University of Arkansas for Medical Sciences
3 shared publications
In database
- RNA helicases required for viral propagation in humans
- Hepatitis C virus nonstructural protein NS3 unfolds viral G-quadruplex RNA structures
- Alignment of helicases on single-stranded DNA increases activity
Reine U. Protacio
University of Arkansas for Medical Sciences
3 shared publications
In database
- 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
Misha Klein
Vrije Universiteit Amsterdam (NL)
3 shared publications
- 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
Thomas K. Anderson
University of Wisconsin–Madison (US)
3 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
Craig Cameron
University of North Carolina at Chapel Hill (US)
3 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
Robert N. Kirchdoerfer
University of Wisconsin–Madison (US)
3 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
Martin Depken
Delft University of Technology (NL)
3 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
Similar Researchers
Based on overlapping research topics
Jennifer Hall
University of Arkansas for Medical Sciences
DNA Repair Mechanisms
Protein Structure and Dynamics
Disease Mechanisms Research
Emily Bosche
Hendrix College
DNA Repair Mechanisms
Protein Structure and Dynamics
Molecular Biology Techniques and Applications
J.A. Jamsen
University of Arkansas for Medical Sciences
DNA Repair Mechanisms
Protein Structure and Dynamics
Disease Mechanisms Research
David R. Proffitt
University of Arkansas for Medical Sciences
DNA Repair Mechanisms
Protein Structure and Dynamics
Molecular Biology Techniques and Applications
Shula R. Raney
University of Arkansas for Medical Sciences
DNA Repair Mechanisms
Protein Structure and Dynamics
Disease Mechanisms Research
Lane Smith
University of Arkansas for Medical Sciences
DNA Repair Mechanisms
Protein Structure and Dynamics
Molecular Biology Techniques and Applications