Announcing a new publication for Acta Materia Medica journal. Histone lysine acylation is a major class of histone post-translational modifications involved in essential biological activities, such as transcriptional regulation, DNA-damage repair, and cell-cycle progression.
Abnormal acylation is strongly associated with various diseases, such as cancer. Thus, histone acetyltransferases (HATs), the "writers" that catalyze histone acylation, are promising targets for cancer treatment. Rapid developments in structural biology and artificial intelligence have facilitated the development of drugs targeting HATs.
To provide new ideas for exploring novel HAT modifiers with high efficiency and selectivity, this article reviews the relationships between acylation and diseases, illustrates HAT catalytic mechanisms through structural biology, and summarizes research progress in HAT modifiers.
Source:
Journal reference:
Li, N., et al. (2023) Biological functions and therapeutic potential of acylation by histone acetyltransferases. Acta Materia Medica. doi.org/10.15212/AMM-2023-0010.
Scientists map cancer mutations in EGFR gene, revealing drug resistance paths