John C. Marecki
Affiliation confirmed via AI analysis of OpenAlex, ORCID, and web sources.
Instructor
Also affiliated: Johns Hopkins University (2006–2007); Johns Hopkins Medicine (2007); Allegheny General Hospital (2006); University of Colorado Health (1993–2006); Pulmonary Associates (2005); Arkansas Children's Nutrition Center (2007–2013); Webb Institute (1993); University of California, Davis (2005); University of Colorado Denver (2006)
Faculty Researcher
Biochemistry & Molecular Biology, College of Medicine
Research Areas
Biomedical Subjects
Biography and Research Information
OverviewAI-generated summary
John C. Marecki's research investigates the function of RNA helicases, enzymes crucial for viral propagation in humans. His work explores how these helicases interact with nucleic acids, specifically focusing on G-quadruplex DNA, which can inhibit their unwinding activity while promoting liquid-liquid phase separation. Marecki has also studied the structural features of helicases that influence their DNA-binding and displacement capabilities.
His recent publications examine the coupling of RNA polymerase and helicase in viral replication, enabling rapid elongation through duplex RNA. He has also investigated the role of biomolecular condensates in controlling and defining RNA-RNA interactions during viral replication. Marecki's scholarship is supported by a publication record contributing to an h-index of 18 and over 1,800 citations, with key collaborations at the University of Arkansas for Medical Sciences.
Metrics
- h-index: 18
- Publications: 44
- Citations: 1,888
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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Abstract 5612 The UAMS Center for Molecular Interactions in Cancer (CMIC) Biomolecular Interactions Core (BIC) (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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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
As listed on this researcher's institutional profile.
- 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 via University of North Carolina - Chapel Hill Principal Investigator
- Midwest AViDD Center NIH/Nat. Inst. of Allergy & Infectious Diseases via University of Minnesota Principal Investigator
- Center for Molecular Interactions in Cancer (CMIC) NIH Co-Investigator
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
- 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
- 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
- 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
- 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>
- 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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