Ontology highlight
ABSTRACT:
SUBMITTER: Wang X
PROVIDER: S-EPMC3378808 | biostudies-literature | 2012 Sep
REPOSITORIES: biostudies-literature
Wang Xiaohui X Saludes Jonel P JP Zhao Tina X TX Csakai Adam A Fiorini Zeno Z Chavez Sherry A SA Li Jing J Lee Gui-in GI Varga Krisztina K Yin Hang H
Biochimica et biophysica acta 20120517 9
The lateral transmembrane protein-protein interaction has been regarded as "undruggable" despite its importance in many biological processes. The homo-trimerization of transmembrane domain 5 (TMD-5) of latent membrane protein 1 (LMP-1) is critical for the constitutive oncogenic activation of the Epstein-Barr virus (EBV). Herein, we report a small molecule agent, NSC 259242 (compound 1), to be a TMD-5 self-association disruptor. Both the positively charged acetimidamide functional groups and the ...[more]