Jun Gao
This is a likely match — the affiliation was inferred from OpenAlex, ORCID, and web sources but has not been fully confirmed. Treat with appropriate caution.
Researcher
Also affiliated: University of Kansas (1996); Dalian Medical University (2018); Chinese Academy of Medical Sciences & Peking Union Medical College (2005); Liaoning Academy of Agricultural Sciences (2014); Huaiyin Institute of Technology (2021–2022); Arkansas Department of Agriculture (2014)
Faculty Researcher
Research Areas
Biomedical Subjects
Links
Biography and Research Information
OverviewAI-generated summary
Jun Gao's research focuses on the molecular mechanisms of DNA and RNA helicases, particularly their roles in unwinding G-quadruplex structures and their involvement in viral replication. His work has investigated how these helicases interact with nucleic acids, including G-rich single-stranded DNA and RNA, and how these interactions influence cellular processes. Recent publications detail the function of specific helicases, such as the eukaryotic Pif1 helicase and the Hepatitis C virus nonstructural protein NS3, in remodeling protein-nucleic acid complexes and unfolding viral RNA structures. Gao also studies the broader family of RNA helicases in the context of viral propagation in humans. His research collaborations at the University of Arkansas for Medical Sciences include extensive work with Kevin D. Raney, Alicia K. Byrd, and John C. Marecki. Gao has published 34 papers with an h-index of 15 and 695 citations.
Metrics
- h-index: 15
- Publications: 34
- Citations: 710
Selected Publications
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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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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)
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RNA helicases required for viral propagation in humans (2021)
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A structural feature of Dda helicase which enhances displacement of streptavidin and <i>trp</i> repressor from <scp>DNA</scp> (2021)
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G-quadruplex DNA inhibits unwinding activity but promotes liquid–liquid phase separation by the DEAD-box helicase Ded1p (2021)
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G-Quadruplex loops regulate PARP-1 enzymatic activation (2020)
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DEAD-box RNA helicases Dbp2, Ded1 and Mss116 bind to G-quadruplex nucleic acids and destabilize G-quadruplex RNA (2019)
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A fast approach to detect gene–gene synergy (2017)
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A biochemical and biophysical model of G-quadruplex DNA recognition by positive coactivator of transcription 4 (2017)
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Yeast Sub1 and human PC4 are G-quadruplex binding proteins that suppress genome instability at co-transcriptionally formed G4 DNA (2017)
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The Structural Recognition of G‐quadruplex DNA by PC4: How Does a ssDNA Binding Protein Decide? (2016)
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Yeast transcription co-activator Sub1 and its human homolog PC4 preferentially bind to G-quadruplex DNA (2015)
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Binding of the transcription factor Atf1 to promoters serves as a barrier to phase nucleosome arrays and avoid cryptic transcription (2014)
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
- 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
- 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>
- Two residues in the DNA binding site of Pif1 helicase are essential for nuclear functions but dispensable for mitochondrial respiratory growth
- 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>
- RNA helicases required for viral propagation in humans
- Hepatitis C virus nonstructural protein NS3 unfolds viral G-quadruplex RNA structures
- 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
- Eukaryotic Pif1 helicase unwinds G-quadruplex and dsDNA using a conserved wedge
- Two residues in the DNA binding site of Pif1 helicase are essential for nuclear functions but dispensable for mitochondrial respiratory growth
- Eukaryotic Pif1 helicase unwinds G-quadruplex and dsDNA using a conserved wedge
- Two residues in the DNA binding site of Pif1 helicase are essential for nuclear functions but dispensable for mitochondrial respiratory growth
- G-quadruplex DNA inhibits unwinding activity but promotes liquid–liquid phase separation by the DEAD-box helicase Ded1p
- G-quadruplex DNA inhibits unwinding activity but promotes liquid–liquid phase separation by the DEAD-box helicase Ded1p
- G-quadruplex DNA inhibits unwinding activity but promotes liquid–liquid phase separation by the DEAD-box helicase Ded1p
- G-quadruplex DNA inhibits unwinding activity but promotes liquid–liquid phase separation by the DEAD-box helicase Ded1p
- G-quadruplex DNA inhibits unwinding activity but promotes liquid–liquid phase separation by the DEAD-box helicase Ded1p
- G-quadruplex DNA inhibits unwinding activity but promotes liquid–liquid phase separation by the DEAD-box helicase Ded1p
- A structural feature of Dda helicase which enhances displacement of streptavidin and <i>trp</i> repressor from <scp>DNA</scp>
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