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 (1994–2009); University of Arizona (2003); Vanderbilt University (1989–2002); University of Arkansas Medical Center (2004–2020); University of Arkansas System (2018); Winthrop Rockefeller Foundation (2019); University of Chinese Academy of Sciences (2009); Case Western Reserve University (2008)
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 and functions of helicases and G-quadruplex nucleic acids. He has received significant federal funding from the National Institutes of Health (NIH)/National Institute of General Medical Sciences for two grants totaling over $1.1 million, investigating helicase mechanisms and G-quadruplex signaling. His work has led to a publication record of 131 papers, with approximately 4,896 citations, and an h-index of 45, designating him as a high-impact researcher.
Raney's research group has explored various aspects of helicase activity, including protein displacement by helicase assemblies on single-stranded DNA and the development of fluorescence-based assays for monitoring helicase activity. His publications also include work on Hepatitis C Virus (HCV) nonstructural proteins, specifically NS5A as an RNA-binding protein and NS3 as a multifunctional antiviral target. Additionally, his earlier work investigated the metabolism and toxicity of mycotoxins like aflatoxin B1, including its epoxidation and conjugation with glutathione by human enzymes.
He collaborates with several researchers at the University of Arkansas for Medical Sciences, including John C. Marecki (11 shared publications), Alicia K. Byrd (7 shared publications), and Jun Gao (7 shared publications). Raney also serves as the Department Chairperson for the Department Chairs in the College of Medicine at the University of Arkansas for Medical Sciences.
Metrics
- h-index: 45
- Publications: 131
- Citations: 5,031
Positions
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University of Arkansas for Medical Science 1995–presentBiochemistry and Molecular Biology ORCID
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Department Chairperson publications 1998–2026University of Arkansas for Medical Sciences Department Chairs, College of Medicine Institutional directory
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
- Protein displacement by an assembly of helicase molecules aligned along single-stranded DNA
- Evidence That G-quadruplex DNA Accumulates in the Cytoplasm and Participates in Stress Granule Assembly in Response to Oxidative Stress
- Structure and Mechanisms of SF1 DNA Helicases
- Pre-steady-state DNA unwinding by bacteriophage T4 Dda helicase reveals a monomeric molecular motor
- A CRISPR-based approach for proteomic analysis of a single genomic locus
Showing 5 of 41 shared publications
- Evidence That G-quadruplex DNA Accumulates in the Cytoplasm and Participates in Stress Granule Assembly in Response to Oxidative Stress
- G-Quadruplex loops regulate PARP-1 enzymatic activation
- DEAD-box RNA helicases Dbp2, Ded1 and Mss116 bind to G-quadruplex nucleic acids and destabilize G-quadruplex RNA
- RNA helicases required for viral propagation in humans
- N-Naphthoyl-substituted indole thio-barbituric acid analogs inhibit the helicase activity of the hepatitis C virus NS3
Showing 5 of 20 shared publications
- Hepatitis C Virus Nonstructural Protein 5A (NS5A) Is an RNA-binding Protein
- Hepatitis C Virus Non-structural Protein 3 (HCV NS3): A Multifunctional Antiviral Target
- Hepatitis C Virus Nonstructural Protein 5A: Biochemical Characterization of a Novel Structural Class of RNA-Binding Proteins
- Structural and Biological Identification of Residues on the Surface of NS3 Helicase Required for Optimal Replication of the Hepatitis C Virus
- Purification and characterization of hepatitis C virus non-structural protein 5A expressed in Escherichia coli
Showing 5 of 18 shared publications
- Evidence That G-quadruplex DNA Accumulates in the Cytoplasm and Participates in Stress Granule Assembly in Response to Oxidative Stress
- A CRISPR-based approach for proteomic analysis of a single genomic locus
- G-Quadruplex loops regulate PARP-1 enzymatic activation
- Yeast Sub1 and human PC4 are G-quadruplex binding proteins that suppress genome instability at co-transcriptionally formed G4 DNA
- Yeast transcription co-activator Sub1 and its human homolog PC4 preferentially bind to G-quadruplex DNA
Showing 5 of 15 shared publications
- Pre-steady-state DNA unwinding by bacteriophage T4 Dda helicase reveals a monomeric molecular motor
- A CRISPR-based approach for proteomic analysis of a single genomic locus
- Multiple Full-length NS3 Molecules Are Required for Optimal Unwinding of Oligonucleotide DNA in Vitro
- Hepatitis C Virus NS3 and Simian Virus 40 T Antigen Helicases Displace Streptavidin from 5‘-Biotinylated Oligonucleotides but Not from 3‘-Biotinylated Oligonucleotides: Evidence for Directional Bias in Translocation on Single-Stranded DNA
- Yeast transcription co-activator Sub1 and its human homolog PC4 preferentially bind to G-quadruplex DNA
Showing 5 of 13 shared publications
- Evidence That G-quadruplex DNA Accumulates in the Cytoplasm and Participates in Stress Granule Assembly in Response to Oxidative Stress
- Pre-steady-state DNA unwinding by bacteriophage T4 Dda helicase reveals a monomeric molecular motor
- DNA Unwinding by Escherichia coli DNA Helicase I (TraI) Provides Evidence for a Processive Monomeric Molecular Motor
- Intermediates revealed in the kinetic mechanism for DNA unwinding by a monomeric helicase
- Chemically Modified DNA Substrates Implicate the Importance of Electrostatic Interactions for DNA Unwinding by Dda Helicase
Showing 5 of 10 shared publications
- Evidence That G-quadruplex DNA Accumulates in the Cytoplasm and Participates in Stress Granule Assembly in Response to Oxidative Stress
- Yeast Sub1 and human PC4 are G-quadruplex binding proteins that suppress genome instability at co-transcriptionally formed G4 DNA
- Yeast Pif1 Helicase Exhibits a One-base-pair Stepping Mechanism for Unwinding Duplex DNA
- Yeast transcription co-activator Sub1 and its human homolog PC4 preferentially bind to G-quadruplex DNA
- Yeast Helicase Pif1 Unwinds RNA:DNA Hybrids with Higher Processivity than DNA:DNA Duplexes
Showing 5 of 10 shared publications
- Evidence That G-quadruplex DNA Accumulates in the Cytoplasm and Participates in Stress Granule Assembly in Response to Oxidative Stress
- A CRISPR-based approach for proteomic analysis of a single genomic locus
- Structural and Biological Identification of Residues on the Surface of NS3 Helicase Required for Optimal Replication of the Hepatitis C Virus
- DNA unwinding and protein displacement by superfamily 1 and superfamily 2 helicases
- Yeast transcription co-activator Sub1 and its human homolog PC4 preferentially bind to G-quadruplex DNA
Showing 5 of 8 shared publications
- Hepatitis C Virus Nonstructural Protein 5A (NS5A) Is an RNA-binding Protein
- Phosphate release contributes to the rate-limiting step for unwinding by an RNA helicase
- 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
Showing 5 of 8 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
- RNA virus polymerase-helicase coupling enables rapid elongation through duplex RNA
- Template switching by coronavirus polymerase requires helicase activity and is stimulated by remdesivir and molnupiravir
Showing 5 of 7 shared publications
- Structure and Mechanisms of SF1 DNA Helicases
- Erratum to: Structure and Mechanisms of SF1 DNA Helicases
- Yeast Pif1 Helicase Exhibits a One-base-pair Stepping Mechanism for Unwinding Duplex DNA
- Dda Helicase Tightly Couples Translocation on Single-Stranded DNA to Unwinding of Duplex DNA: Dda Is an Optimally Active Helicase
- N-Naphthoyl-substituted indole thio-barbituric acid analogs inhibit the helicase activity of the hepatitis C virus NS3
Showing 5 of 6 shared publications
- Structural and Biological Identification of Residues on the Surface of NS3 Helicase Required for Optimal Replication of the Hepatitis C Virus
- NS3 Helicase from the Hepatitis C Virus Can Function as a Monomer or Oligomer Depending on Enzyme and Substrate Concentrations
- Hepatitis C Virus NS3 Helicase Forms Oligomeric Structures That Exhibit Optimal DNA Unwinding Activity in Vitro
- RNA Unwinding Activity of the Hepatitis C Virus NS3 Helicase Is Modulated by the NS5B Polymerase
- Binding by the Hepatitis C Virus NS3 Helicase Partially Melts Duplex DNA
Showing 5 of 6 shared publications
- Evidence That G-quadruplex DNA Accumulates in the Cytoplasm and Participates in Stress Granule Assembly in Response to Oxidative Stress
- Yeast transcription co-activator Sub1 and its human homolog PC4 preferentially bind to G-quadruplex DNA
- DEAD-box RNA helicases Dbp2, Ded1 and Mss116 bind to G-quadruplex nucleic acids and destabilize G-quadruplex RNA
- G4-quadruplexes and genome instability
- XLPM: efficient algorithm for the analysis of protein-protein contacts using chemical cross-linking mass spectrometry
Showing 5 of 6 shared publications
- Evidence That G-quadruplex DNA Accumulates in the Cytoplasm and Participates in Stress Granule Assembly in Response to Oxidative Stress
- Yeast Sub1 and human PC4 are G-quadruplex binding proteins that suppress genome instability at co-transcriptionally formed G4 DNA
- Yeast transcription co-activator Sub1 and its human homolog PC4 preferentially bind to G-quadruplex DNA
- A biochemical and biophysical model of G-quadruplex DNA recognition by positive coactivator of transcription 4
- 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
- RNA virus polymerase-helicase coupling enables rapid elongation through duplex RNA
- Copy-back RNA synthesis by coronavirus polymerase requires helicase activity and is stimulated by remdesivir and molnupiravir
Showing 5 of 6 shared publications