In this issue of Cell Chemical Biology, Harvey et al. (2020) identify 4E14, a sulfhydryl-containing N-acetyltryptophan analog that selectively disrupts binding to the previously undruggable anti-apoptotic BCL2 paralog BFL1, and elucidate a BFL1 conformational change that facilitates 4E14 interaction. These results provide insight that will accelerate development of BFL1 inhibitors.

中文翻译：

---

BFL1的选择性抑制：全部与寻找合适的合作伙伴有关。

在本期细胞化学生物学中，Harvey等。（2020）确定4E14，一种含巯基的N-乙酰基色氨酸类似物，它选择性地破坏与先前不可吸收的抗凋亡BCL2旁系同源物BFL1的结合，并阐明促进4E14相互作用的BFL1构象变化。这些结果提供了将加速BFL1抑制剂开发的见解。