Biologically Active Small Molecules

Inhibits PAD4 activity (IC50 = 21.6 &muM) as well as PAD1 and PAD3 activity (IC50s = 29.5 and 350 &muM, respectively) cytotoxic to HL-60, MCF-7, and HT-29 cancer cell lines (IC50s = 0.5, 0.5 and 1 &muM, respectively).

Inhibits PAD4 activity (IC50 = 21.6 &muM) as well as PAD1 and PAD3 activity (IC50s = 29.5 and 350 &muM, respectively) cytotoxic to HL-60, MCF-7, and HT-29 cancer cell lines (IC50s = 0.5, 0.5 and 1 &muM, respectively).

Inhibits PAD4 activity (IC50 = 21.6 &muM) as well as PAD1 and PAD3 activity (IC50s = 29.5 and 350 &muM, respectively) cytotoxic to HL-60, MCF-7, and HT-29 cancer cell lines (IC50s = 0.5, 0.5 and 1 &muM, respectively).

Inhibits PAD4 activity (IC50 = 21.6 &muM) as well as PAD1 and PAD3 activity (IC50s = 29.5 and 350 &muM, respectively) cytotoxic to HL-60, MCF-7, and HT-29 cancer cell lines (IC50s = 0.5, 0.5 and 1 &muM, respectively).

F16 is a small, cationic, lipophilic molecule which binds preferentially to mitochondrial membranes and disrupts their function. F16 was discovered in high throughput screens for tumor inhibitors, where it was found to induce apoptosis in

F16 is a small, cationic, lipophilic molecule which binds preferentially to mitochondrial membranes and disrupts their function. F16 was discovered in high throughput screens for tumor inhibitors, where it was found to induce apoptosis in

F16 is a small, cationic, lipophilic molecule which binds preferentially to mitochondrial membranes and disrupts their function. F16 was discovered in high throughput screens for tumor inhibitors, where it was found to induce apoptosis in

F16 is a small, cationic, lipophilic molecule which binds preferentially to mitochondrial membranes and disrupts their function. F16 was discovered in high throughput screens for tumor inhibitors, where it was found to induce apoptosis in

Acts as a replacement for endogenously-produced farnesyl alcohol and becomes attached to proteins through normal biological processes, in cells or animals the terminal azide group can be used to readily tag farnesylated proteins via click chemistry

Acts as a replacement for endogenously-produced farnesyl alcohol and becomes attached to proteins through normal biological processes, in cells or animals the terminal azide group can be used to readily tag farnesylated proteins via click chemistry

Acts as a replacement for endogenously-produced farnesyl alcohol and becomes attached to proteins through normal biological processes, in cells or animals the terminal azide group can be used to readily tag farnesylated proteins via click chemistry

An intermediate in the HMG-CoA reductase pathway and used in the biosynthesis of terpenes, terpenoids, and sterols also serves as a donor in post-translational isoprenylation of proteins.