Article
The E3 ubiquitin ligase CHIP selectively regulates mutant epidermal growth factor receptor by ubiquitination and degradation.
Biochemical and biophysical research communications - 14 Oct 2016
Chung Chaeuk, Yoo Geon, Kim Tackhoon, Lee Dahye, Lee Choong-Sik, Cha Hye Rim, Park Yeon Hee, Moon Jae Young, Jung Sung Soo, Kim Ju Ock, Lee Jae Cheol, Kim Sun Young, Park Hee Sun, Park Myoungrin, Park Dong Il, Lim Dae-Sik, Jang Kang Won, Lee Jeong Eun
Abstract excerpt
Somatic mutation in the tyrosine kinase domain of epidermal growth factor receptor (EGFR) is a decisive factor for the therapeutic response to EGFR tyrosine kinase inhibitors (EGFR-TKIs) in lung adenocarcinoma. The stability of mutant EGFR is maintained by various regulators, including heat shock protein 90 (Hsp90). The C terminus of Hsc70-interacting protein (CHIP) is a Hsp70/Hsp90 co-chaperone and exhibits E3...
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