PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 11543641-4 2001 In HL-60 cells, the general caspase inhibitor benzyloxycarbonyl-Val-Ala-Asp fluoromethyl ketone (Z-VAD.FMK) blocked activation of caspases-3/-7, cleavage of PARP, and DNA, but PS externalization and cytoplasmic changes were not significantly affected. Caspase Inhibitor VI 46-95 poly(ADP-ribose) polymerase 1 Homo sapiens 157-161 11393284-7 2001 The increased cell death, early caspase-3 activation and PARP cleavage, and flow cytometric changes seen in pro-caspase-3-expressing cells can be partially inhibited by treatment with benzyloxycarbonyl-val-ala-asp fluoromethylketone, a synthetic caspase inhibitor. Caspase Inhibitor VI 184-232 poly(ADP-ribose) polymerase 1 Homo sapiens 57-61 10075737-5 1999 Pretreatment with the pan-caspase inhibitor benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone (Z-VAD-fmk) inhibited PARP cleavage, DNA fragmentation, calpain activation, and Bax cleavage and increased cell survival by 40%. Caspase Inhibitor VI 44-92 poly(ADP-ribose) polymerase 1 Homo sapiens 115-119 10462048-4 1999 Pre-treatment with the caspase inhibitor benzyloxycarbonyl-Val-Ala-Asp fluoromethyl ketone (Z-VAD.FMK) blocked apoptosis and the resultant cleavage of these caspases and PARP. Caspase Inhibitor VI 41-90 poly(ADP-ribose) polymerase 1 Homo sapiens 170-174 10085120-4 1999 The caspase inhibitors benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone (zVAD-fmk) and benzyloxycarbonyl-Asp-Glu-Val-Asp-fluoromethylketone (zDEVD-fmk) protect cells against apoptosis and inhibit DEVD-specific caspase activity and PARP cleavage without affecting JNK1 and p38 MAPK activations. Caspase Inhibitor VI 23-71 poly(ADP-ribose) polymerase 1 Homo sapiens 231-235 10430095-7 1999 The induction of apoptosis, activation of caspase 3, and poly(ADP-ribose) polymerase cleavage in treatment regimens with paclitaxel and paclitaxel followed by flavopiridol were reversed by treatment with the caspase inhibitor benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone, which supports the notion that caspases are the executioners of apoptosis in these processes. Caspase Inhibitor VI 226-274 poly(ADP-ribose) polymerase 1 Homo sapiens 57-84 9288794-6 1997 Drug-induced apoptosis involved activation of caspases (interleukin 1beta-converting enzyme/Ced-3-like proteases) and processing of the prototype caspase substrate PARP and was completely blocked by benzyloxycarbonyl-Val-Ala-Asp-fluoromethyl ketone, a peptide inhibitor of caspases. Caspase Inhibitor VI 199-248 poly(ADP-ribose) polymerase 1 Homo sapiens 164-168