PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8681377-3	1996	FLICE binds to the death effector domain of FADD and upon overexpression induces apoptosis that is blocked by the ICE family inhibitors, CrmA and z-VAD-fmk.	benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone	146-155	Fas associated via death domain	Homo sapiens	44-48	
10200559-2	1999	Death signaling as well as JNK/SAPK activation by TRAIL in these cells is FADD- and caspase-dependent since dominant-negative FADD or the caspase inhibitor zVAD prevented both, apoptosis and JNK/SAPK activity.	benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone	156-160	Fas associated via death domain	Homo sapiens	74-78	
9935184-2	1999	Apoptosis induced by gamma-irradiation or doxorubicin engages a FADD- and caspase-dependent apoptosis pathway which is inhibited by dominant negative FADD or the caspase inhibitor zVAD.	benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone	180-184	Fas associated via death domain	Homo sapiens	64-81	
9935184-2	1999	Apoptosis induced by gamma-irradiation or doxorubicin engages a FADD- and caspase-dependent apoptosis pathway which is inhibited by dominant negative FADD or the caspase inhibitor zVAD.	benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone	180-184	Fas associated via death domain	Homo sapiens	64-68	
17575108-4	2007	The cells expressing the modified FADD underwent apoptosis through the typical apoptosis cascade via activation of caspase-3, and apoptosis was inhibited by a caspase inhibitor (i.e., z-VAD-fmk).	benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone	184-193	Fas associated via death domain	Homo sapiens	34-38