ArticleNucleic acids research2004
Interaction of the Zalpha domain of human ADAR1 with a negatively supercoiled plasmid visualized by atomic force microscopy.
Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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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.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Cryo-EM structures of anti Z-DNA antibodies in complex with antigen reveal distinct recognition modes of a left-handed geometry.Nucleic acids research · 2026Article
- Adoption of A-Z Junctions in RNAs by Binding of Zα Domains.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Visualization of DNA and protein-DNA complexes with atomic force microscopy.Methods in molecular biology (Clifton, N.J.) · 2014Article
- Structural basis for Z-DNA binding and stabilization by the zebrafish Z-DNA dependent protein kinase PKZ.Nucleic acids research · 2013Article
- Article
- Mica functionalization for imaging of DNA and protein-DNA complexes with atomic force microscopy.Methods in molecular biology (Clifton, N.J.) · 2013Article
- Atomic force microscopy studies provide direct evidence for dimerization of the HIV restriction factor APOBEC3G.The Journal of biological chemistry · 2011Article
- AFM for analysis of structure and dynamics of DNA and protein-DNA complexes.Methods (San Diego, Calif.) · 2009Article
- Detecting ultraviolet damage in single DNA molecules by atomic force microscopy.Biophysical journal · 2007Article
- Effect of DNA supercoiling on the geometry of holliday junctions.Biochemistry · 2006Article
- DNA strand arrangement within the SfiI-DNA complex: atomic force microscopy analysis.Biochemistry · 2006Article
- Site-specific labeling of supercoiled DNA.Nucleic acids research · 2006Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Interest to the left-handed DNA conformation has been recently boosted by the findings that a number of proteins contain the Zalpha domain, which has been shown to specifically recognize Z-DNA. The biological function of Zalpha is presently unknown, but it has been suggested that it may specifically direct protein regions of Z-DNA induced by negative supercoiling in actively transcribing genes. Many studies, including a crystal structure in complex with Z-DNA, have focused on the human ADAR1 Zalpha domain in isolation. We have hypothesized that the recognition of a Z-DNA sequence by the Zalpha(ADAR1) domain is context specific, occurring under energetic conditions, which favor Z-DNA formation. To test this hypothesis, we have applied atomic force microscopy to image Zalpha(ADAR1) complexed with supercoiled plasmid DNAs. We have demonstrated that the Zalpha(ADAR1) binds specifically to Z-DNA and preferentially to d(CG)(n) inserts, which require less energy for Z-DNA induction compared to other sequences. A notable finding is that site-specific Zalpha binding to d(GC)(13) or d(GC)(2)C(GC)(10) inserts is observed when DNA supercoiling is insufficient to induce Z-DNA formation. These results indicate that Zalpha(ADAR1) binding facilities the B-to-Z transition and provides additional support to the model that Z-DNA binding proteins may regulate biological processes through structure-specific recognition.
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