Surprising repair activities of nonpolar analogs of 8-oxoG expose features of recognition and catalysis by base excision repair glycosylases.

@article{McKibbin2012SurprisingRA,
  title={Surprising repair activities of nonpolar analogs of 8-oxoG expose features of recognition and catalysis by base excision repair glycosylases.},
  author={Paige L. McKibbin and Akio Kobori and Yosuke Taniguchi and Eric T. Kool and Sheila S David},
  journal={Journal of the American Chemical Society},
  year={2012},
  volume={134 3},
  pages={1653-61}
}
Repair glycosylases locate and excise damaged bases from DNA, playing central roles in preservation of the genome and prevention of disease. Two key glycosylases, Fpg and hOGG1, function to remove the mutagenic oxidized base 8-oxoG (OG) from DNA. To investigate the relative contributions of conformational preferences, leaving group ability, enzyme-base hydrogen bonding, and nucleobase shape on damage recognition by these glycosylases, a series of four substituted indole nucleosides, based on… CONTINUE READING

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Molecular Cloning, A Laboratory Manual, 3rd ed.

J. A. McCann, P.J.J. Am. Berti
Cold Spring Harbor Laboratory Press: Plainview, • 2008

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