Two domains of Nrf2 cooperatively bind CBP, a CREB binding protein, and synergistically activate transcription

2001509 citationsJournal Article

Authors

Yasutake Katoh · Institute of Physiology and Basic Medicine

Ken Itoh · Institute of Basic Medical Sciences of the Chinese Academy of Medical Sciences

Eisaku Yoshida · Institute of Applied Biochemistry

Makoto Miyagishi · Institute of Applied Biochemistry

Akiyoshi Fukamizu · University of Tsukuba

Masayuki Yamamoto · Institute of Basic Medical Sciences of the Chinese Academy of Medical Sciences

Abstract

Our results indicate that Nrf2 exploits the cooperative binding of two independent transactivation domains to CBP in the acquisition of a potent transactivation activity.

Topics & Keywords

Genomics, phytochemicals, and oxidative stress Glutathione Transferases and Polymorphisms

Publication Details

Published in: Genes to Cells

Volume 6, Issue 10, pp. 857-868

DOI: 10.1046/j.1365-2443.2001.00469.x

Field-Weighted Citation Impact: 3.58

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Two domains of Nrf2 cooperatively bind CBP, a CREB binding protein, and synergistically activate transcription

Authors

Abstract

Topics & Keywords

Publication Details