Conformational changes and cleavage by the homing endonuclease I-PpoI: a critical role for a leucine residue in the active site.

By Eric A. Galburt, Meggen S. Chadsey, M. Jurica, B. Chevalier, D. Erho, Weiliang Tang, R. Monnat, Barry L. Stoddard. 2000

38 citations recorded by the source corpus.

Subfields: Molecular Biology

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1. J. Eklund
2. Umut Y. Ulge
3. J. Eastberg
4. Kimberly A. Aeling
5. Nicholas R. Steffen
6. R. Lathrop
7. D. F. Senear
8. G. W. Hatfield

Citations in the corpus

• DNA Deformation Energy as an Indirect Recognition Mechanism in Protein-DNA Interactions (2007, background): “Considered in this light, these differences may reflect the different catalytic mechanisms that are employed by these two endonucleases [24], [25], [26].”
• Altered target site specificity variants of the I-PpoI His-Cys box homing endonuclease (2007, methodology): “The H98A substitution was incorporated to abolish the catalytic activity of I-PpoI without disrupting high affinity site binding [Figure 2A; (22,23,26)].”