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Mary H. O'Dea

Researcher at Laboratory of Molecular Biology

Publications -  18
Citations -  4069

Mary H. O'Dea is an academic researcher from Laboratory of Molecular Biology. The author has contributed to research in topics: DNA supercoil & DNA gyrase. The author has an hindex of 18, co-authored 18 publications receiving 3960 citations. Previous affiliations of Mary H. O'Dea include National Institutes of Health.

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The interaction of the F plasmid killer protein, CcdB, with DNA gyrase: induction of DNA cleavage and blocking of transcription.

TL;DR: It is confirmed that CcdB can induce DNA cleavage by gyrase and show that this cleavage reaction requires ATP hydrolysis when the substrate is linear DNA, but is independent of hydroleysis when negatively supercoiled DNA is used.
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DNA supercoiling by DNA gyrase. A static head analysis.

TL;DR: Using purified DNA gyrase to supercoil circular plasmid pBR322 DNA, the linking number attained at the steady state (‘static head’) varies with the concentrations of ATP and ADP, both in the absence and presence of spermidine.
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Energy Coupling in Escherichia coli DNA Gyrase: the Relationship between Nucleotide Binding, Strand Passage, and DNA Supercoiling†

TL;DR: The previously observed slow binding of ADPNP to the complex of gyrase with linear DNA is accelerated 16-fold when the substrate DNA is negatively supercoiled, suggesting a functional interaction between the nucleotide-binding and DNA-binding domains which is independent of the strand-passage process.
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Neutron and light-scattering studies of DNA gyrase and its complex with DNA☆

TL;DR: Both Rg and Rh values change very little upon addition of DNA, suggesting that DNA binds in a manner that does not significantly change the shape of the protein, and several classes of models were rejected based on SANS data obtained in 2H2O at larger scattering angles.
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Effect of HIV integrase inhibitors on the RAG1/2 recombinase

TL;DR: The results further underscore the similarities between RAG1/2 and integrase and suggest that certain integrase inhibitors may have the potential to interfere with aspects of B and T cell development.