| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5508011 | Biochimica et Biophysica Acta (BBA) - General Subjects | 2017 | 30 Pages |
Abstract
The crystallographic models provide structural insights into the substrate binding of the SIAH family E3 ubiquitin ligases that are critically involved in regulating cancer-related pathways. Our results suggest caution should be taken when using menadione as a specific SIAH2 inhibitor.
Keywords
seven in absentia homologZNFDUBDeubiquitinaseUSPESISIAHSBDITCERADHEPES4-(2-hydroxyethyl)-1-piperazineethanesulfonic acidE3 ubiquitin ligasetris(2-carboxyethyl)phosphineZinc fingercrystallographyTevProtein-protein interactionMaximum-likelihoodRingsubstrate binding domainTCEPmenadioneSmall molecule inhibitorsTobacco etch virusubiquitin-specific proteaseIsothermal titration calorimetryelectrospray ionization
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Authors
Qi Zhang, Zhongduo Wang, Feng Hou, Rachel Harding, Xinyi Huang, Aiping Dong, John R. Walker, Yufeng Tong,