Covalent Modification at Cys151 Dissociates the Electrophile Sensor Keap1 from the Ubiquitin Ligase CUL3-Reference-Cited by-同舟云学术

Covalent Modification at Cys151 Dissociates the Electrophile Sensor Keap1 from the Ubiquitin Ligase CUL3

Published:2008-02-06 Issue:3 Volume:21 Page:705-710
ISSN:0893-228X
Container-title:Chemical Research in Toxicology
language:en
Short-container-title:Chem. Res. Toxicol.

Author:

Rachakonda Girish¹,Xiong Ying¹,Sekhar Konjeti R.¹,Stamer Sheryl L.¹,Liebler Daniel C.¹,Freeman Michael L.¹

Affiliation:

1. Department of Radiation Oncology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, Department of Biochemistry and Vanderbilt-Ingram Cancer Center, Vanderbilt University School of Medicine, Nashville, Tennessee 37232

Publisher

American Chemical Society (ACS)

Subject

Toxicology,General Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/tx700302s

Reference33 articles.

1. Molecular Mechanisms Activating the Nrf2-Keap1 Pathway of Antioxidant Gene Regulation

2. Mechanistic Studies of the Nrf2-Keap1 Signaling Pathway

3. Nrf2–Keap1 defines a physiologically important stress response mechanism

4. Nrf2 and Nrf1 in association with Jun proteins regulate antioxidant response element-mediated expression and coordinated induction of genes encoding detoxifying enzymes

5. Identification of Activating Transcription Factor 4 (ATF4) as an Nrf2-interacting Protein

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