154061-64-0Relevant articles and documents
Selective Targeting of AF9 YEATS Domain by Cyclopeptide Inhibitors with Preorganized Conformation
Jiang, Yixiang,Chen, Guochao,Li, Xiao-Meng,Liu, Sha,Tian, Gaofei,Li, Yuanyuan,Li, Xin,Li, Haitao,Li, Xiang David
supporting information, p. 21450 - 21459 (2021/01/11)
YEATS domains are newly identified epigenetic "readers"of histone lysine acetylation (Kac) and crotonylation (Kcr). The malfunction of YEATS-Kac/Kcr interactions has been found to be involved in the pathogenesis of human diseases, such as cancer. These di
Synthesis of (S)-(+)-2-amino-6-(aminooxy)hexanoic acid
Adamczyk,Reddy
, p. 579 - 586 (2007/10/03)
(S)-(+)-2-Amino-6-(aminooxy)hexanoic acid (AAHA, 3), a non-proteinogenic amino acid, and its derivative, (S)-(-)-6{[(tert-butoxycarbonyl)amino]oxy}-2-{[(9H-fluoren-9-ylmethoxy) carbonyl]amino}hexanoic acid (4), were synthesized from (S)-(-)6-amino-2-{[(be
Synthesis of N(ε)-(p-bromophenyl)-L-lysine and N(τ)-(p-bromophenyl)-L-histidine as models for adducts of bromobenze 3,4-oxide to protein. Observation of an unusual Pd-catalyzed N(τ)- to N(π)-aryl substituent migration
Bambal,Hanzlik
, p. 729 - 732 (2007/10/02)
Bromobenzene 3,4-oxide (1), the putative toxic metabolite of bromobenzene, is known to alkylate protein sulfur nucleophiles in vivo and is postulated to alkylate protein nitrogen nucleophiles, the expected products of which would include, after hydrolysis