133933-33-2Relevant academic research and scientific papers
Folate analogues. 35. synthesis and biological evaluation of 1-deaza, 3-deaza, and bridge-elongated analogues of n10-propargyl-5, 8-dideazafolic acid1
Li,Nair,Edwards,Kisliuk,Gaumont,Dev,Duch,Humphreys,Smith,Ferone
, p. 2746 - 2754 (1991)
Structural modifications at the pyrimidine ring and at the C9,N10-bridge region of the thymidylate synthase (TS) inhibitors N10-propargyl-5,8-dideazafolate (1; PDDF; CB 3717), 2-desamino-N10-propargyl-5,8-dideaz
Structurally Diverse Histone Deacetylase Photoreactive Probes: Design, Synthesis, and Photolabeling Studies in Live Cells and Tissue
Aboukhatwa, Shaimaa M.,Hanigan, Thomas W.,Taha, Taha Y.,Neerasa, Jayaprakash,Ranjan, Rajeev,El-Bastawissy, Eman E.,Elkersh, Mohamed A.,El-Moselhy, Tarek F.,Frasor, Jonna,Mahmud, Nadim,McLachlan, Alan,Petukhov, Pavel A.
supporting information, p. 1096 - 1107 (2019/04/17)
Histone deacetylase (HDAC) activity is modulated in vivo by post-translational modifications and formation of multiprotein complexes. Novel chemical tools to study how these factors affect engagement of HDAC isoforms by HDAC inhibitors (HDACi) in cells and tissues are needed. In this study, a synthetic strategy to access chemically diverse photoreactive probes (PRPs) was developed and used to prepare seven novel HDAC PRPs 9–15. The class I HDAC isoform engagement by PRPs was determined in biochemical assays and photolabeling experiments in live SET-2, HepG2, HuH7, and HEK293T cell lines and in mouse liver tissue. Unlike the HDAC protein abundance and biochemical activity against recombinant HDACs, the chemotype of the PRPs and the type of cells were key in defining the engagement of HDAC isoforms in live cells. Our findings suggest that engagement of HDAC isoforms by HDACi in vivo may be substantially modulated in a cell- and tissue-type-dependent manner.
