Title : Ubiquitin-conjugating enzyme E2 B regulates the ubiquitination of O6-methylguanine-DNA methyltransferase and BCNU sensitivity in human nasopharyngeal carcinoma cells.

Pub. Date : 2018 Dec

PMID : 30449727






5 Functional Relationships(s)
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1 Previous studies indicated that 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU) facilitates the ubiquitination and degradation of MGMT in several types of cancer cells. Carmustine O-6-methylguanine-DNA methyltransferase Homo sapiens
2 Previous studies indicated that 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU) facilitates the ubiquitination and degradation of MGMT in several types of cancer cells. Carmustine O-6-methylguanine-DNA methyltransferase Homo sapiens
3 In this study, we demonstrated for the first time that ubiquitin-conjugating enzyme E2 B (UBE2B) is a novel regulator of MGMT ubiquitination mediated by BCNU in nasopharyngeal carcinoma (NPC) cells. Carmustine O-6-methylguanine-DNA methyltransferase Homo sapiens
4 The E3 ubiquitin ligase RAD18, a partner of UBE2B, is also involved in BCNU-mediated MGMT ubiquitination. Carmustine O-6-methylguanine-DNA methyltransferase Homo sapiens
5 Overexpression/knockdown of UBE2B enhanced/reduced BCNU-mediated MGMT ubiquitination. Carmustine O-6-methylguanine-DNA methyltransferase Homo sapiens