John C. Marecki Data-verified
Affiliation confirmed via AI analysis of OpenAlex, ORCID, and web sources.
Instructor
faculty
Biochemistry & Molecular Biology, College of Medicine
18 h-index
41 pubs
1,869 cited
Research Areas
Biography and Research Information
OverviewAI-generated summary
John C. Marecki's research investigates the mechanisms of viral propagation in humans and the function of RNA and DNA helicases. His work has explored how these enzymes interact with nucleic acids, including G-quadruplex DNA, and how these interactions influence their unwinding activity and phase separation properties. Marecki has also studied structural features of helicases that enhance their displacement capabilities from DNA. His recent publications also touch upon the role of biomolecular condensates in viral replication and the structural changes in viral polymerases that enable elongation. Marecki collaborates with researchers from the University of Arkansas for Medical Sciences, including Emory G. Malone, Wayne P. Wahls, and Reine U. Protacio. He has published 40 papers, with an h-index of 18 and over 1,800 citations.
Metrics
- h-index: 18
- Publications: 41
- Citations: 1,869
Selected Publications
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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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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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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)
Grants & Funding
- Functions and Mechanisms of Helicases and G-Quadruplex Nucleic Acids NIH Co-Investigator
- Mechanisms of Protection and Pathogenesis in ALS Mice NIH/Nat. Inst. of Neurological Disorders & Stroke Co-Investigator
- Coronavirus Genome Replication Subcontract UNC-CH Craig Cameron NIH/Nat. Inst. of Allergy & Infectious Diseases - Pass Through: University of North Carolina - Chapel Hill Principal Investigator
- Midwest AViDD Center NIH/Nat. Inst. of Allergy & Infectious Diseases - Pass Through: University of Minnesota Principal Investigator
- Center for Molecular Interactions in Cancer (CMIC) NIH Co-Investigator
Collaboration Network
Top Collaborators
Kevin D. Raney
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)
5 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
Alicia K. Byrd
University of Arkansas for Medical Sciences
4 shared publications
In database
- 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
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
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
Emory G. Malone
University of Arkansas for Medical Sciences
2 shared publications
In database
- 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>
Reine U. Protacio
University of Arkansas for Medical Sciences
2 shared publications
In database
- 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
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