PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 28069943-8 2017 Molecular dynamics simulations have shown that the in silico acetylation of K244 induces conformational changes in TyrRS near the NLS, which may promote the nuclear translocation of acetylated TyrRS. k244 76-80 tyrosyl-tRNA synthetase 1 Homo sapiens 115-120 28069943-8 2017 Molecular dynamics simulations have shown that the in silico acetylation of K244 induces conformational changes in TyrRS near the NLS, which may promote the nuclear translocation of acetylated TyrRS. k244 76-80 tyrosyl-tRNA synthetase 1 Homo sapiens 193-198 28069943-9 2017 Herein, we show that the acetylated K244 residue of TyrRS protects against DNA damage in mammalian cells and zebrafish by activating DNA repair genes downstream of transcription factor E2F1. k244 36-40 tyrosyl-tRNA synthetase 1 Homo sapiens 52-57