ArticleChemical science2018
DNA-binding miniproteins based on zinc fingers. Assessment of the interaction using nanopores.
Article in Chemical science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
4 citing papers in PubMed.
- Molecular dynamics modelling of the interaction of a synthetic zinc-finger miniprotein with DNA.RSC chemical biology · 2023Article
- The convergent xenogeneic silencer MucR predisposes α-proteobacteria to integrate AT-rich symbiosis genes.Nucleic acids research · 2022Article
- Zinc at the Host-Fungus Interface: How to Uptake the Metal?Journal of fungi (Basel, Switzerland) · 2020Review
- From Interaction to Function in DNA-Templated Supramolecular Self-Assemblies.ChemistryOpen · 2020Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Obtaining artificial proteins that mimic the DNA binding properties of natural transcription factors could open new ways of manipulating gene expression at will. In this context it is particularly interesting to develop simple synthetic systems. Inspired by the modularity of natural transcription factors, we have designed synthetic miniproteins that combine the zinc finger module of the transcription factor GAGA and AT-hook peptide domains. These constructs are capable of binding to composite DNA sequences of up to 14 base pairs with high affinity and good selectivity. In particular, we have synthesized three different chimeras and characterized their DNA binding properties by electrophoresis and fluorescence anisotropy. We have also used, for the first time in the study of peptide-based DNA binders, nanopore force spectroscopy to obtain further data on the DNA interaction.
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Registered trials
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