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Structural insights into the promiscuous DNA binding and broad substrate selectivity of fowlpox virus resolvase
Fowlpox virus resolvase (Fpr) is an endonuclease that cleaves a broad range of branched DNA structures, including the Holliday junction (HJ), with little sequence-specificity. To better understand the mechanisms underlying its relaxed substrate specificity, we determined the crystal structures of Fp...
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| Gepubliceerd in: | Sci Rep |
|---|---|
| Hoofdauteurs: | , , , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
Nature Publishing Group UK
2020
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6962361/ https://ncbi.nlm.nih.gov/pubmed/31941902 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41598-019-56825-w |
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