ArticleChemical science2020
The noncovalent dimerization of a G-quadruplex/hemin DNAzyme improves its biocatalytic properties.
Article in Chemical science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 32 citations in OpenAlex.
- Oligonucleotide G3T19 downregulates CD44 succinylation and inhibits astrocyte-induced glioma immune escape.Cell communication and signaling : CCS · 2026Article
- Mechanozyme: An Artificial Enzyme With a Mechanophore Framework.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Rational redesign of high-activity G-quadruplex DNAzyme through flanking and looping of nucleobases.Scientific reports · 2026Article
- A thermal-activated peroxidase DNAzyme via G-quadruplex nanowires.Communications chemistry · 2025Article
- Exploring the Interactions Between RHAU Peptide and G-Quadruplex Dimers Based on Chromatographic Retention Behaviors.Molecules (Basel, Switzerland) · 2024Article
- Photodynamic Therapy Combined with Ferroptosis Is a Synergistic Antitumor Therapy Strategy.Cancers · 2023Review
- DNA-based enzymatic systems and their applications.iScience · 2022Review
- Design of a High-Sensitivity Dimeric G-Quadruplex/Hemin DNAzyme Biosensor for Norovirus Detection.Molecules (Basel, Switzerland) · 2021Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
While many protein enzymes exert their functions through multimerization, which improves both selectivity and activity, this has not yet been demonstrated for other naturally occurring catalysts. Here, we report a multimerization effect applied to catalytic DNAs (or DNAzymes) and demonstrate that the enzymatic efficiency of G-quadruplexes (GQs) in interaction with the hemin cofactor is remarkably enhanced by homodimerization. The resulting non-covalent dimeric GQ-DNAzyme system provides hemin with a structurally defined active site in which both the cofactor (hemin) and the oxidant (H
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Registered trials
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