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Ratan Rai

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Articles

Chemically induced partial unfolding of the multifunctional apurinic/apyrimidinic endonuclease 1

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By Ratan Rai, Olabode Dawodu, Jingwei Meng, Steven Johnson
| Wiley Online Library Verified
1 INTRODUCTION The reliance of cancer cells on robust DNA repair has spurred the development of small molecule inhibitors targeting DNA repair proteins including the multifunctional apurinic/apyrimidinic endonuclease 1/redox effector factor 1 (referred to here as APE1) (Kaur et al., 2014; Laev et al., 2017). APE1 is critical for the repair of damaged bases in the base excision repair pathway.
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Chemically induced partial unfolding of the multifunctional Apurinic/apyrimidinic endonuclease 1

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By Ratan Rai, Olabode Dawodu, Jingwei Meng, Steven Johnson
| biorxiv.org
Abstract Apurinic/apyrimidinic endonuclease I (APE1) acts as both an endonuclease and a redox factor to ensure cell survival. The two activities require different conformations of APE1. As an endonuclease, APE1 is fully folded. As a redox factor, APE1 must be partially unfolded to expose the buried residue Cys65, which reduces transcription factors including AP-1, NF-κB, and HIF-1α and thereby enables them to bind DNA.
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Chemically induced partial unfolding of the multifunctional Apurinic/apyrimidinic endonuclease 1

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By Steven Johnson, Jonah Z. Vilseck, Ratan Rai, Olabode Dawodu
| biorxiv.org
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