PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
16309216-0	2005	Caspase-3 activation and induction of PARP cleavage by cyclic dipeptide cyclo(Phe-Pro) in HT-29 cells.	Phe-Pro	78-85	poly(ADP-ribose) polymerase 1	Homo sapiens	38-42
16309216-6	2005	RESULTS: Cyclo(Phe-Pro) (10 mM) induced time-dependent cleavage of PARP, detected as early as 8 hours post treatment.	Phe-Pro	15-22	poly(ADP-ribose) polymerase 1	Homo sapiens	67-71
16309216-7	2005	PARP cleavage was blocked by co-administration with the broad-range caspase inhibitor Z-VAD-FMK Cyclo(Phe-Pro) also induced a time-dependent increase (p < 0.01) in caspase-3 activity.	Phe-Pro	102-109	poly(ADP-ribose) polymerase 1	Homo sapiens	0-4
16309216-7	2005	PARP cleavage was blocked by co-administration with the broad-range caspase inhibitor Z-VAD-FMK Cyclo(Phe-Pro) also induced a time-dependent increase (p < 0.01) in caspase-3 activity.	Phe-Pro	102-109	caspase 3	Homo sapiens	167-176
35625882-5	2022	We discovered that the incorporation of two amino acids (Phe-Pro, Phe-Trp or Phe-Arg) within the bicyclic peptide framework maintains an enhanced binding affinity for the Grb7-SH2 domain compared to that of the first-generation monocyclic peptide G7-18NATE.	Phe-Pro	57-64	growth factor receptor bound protein 7	Homo sapiens	171-175
8515421-0	1993	The solution conformation of (D)Phe-Pro-containing peptides: implications on the activity of Ac-(D)Phe-Pro-boroArg-OH, a potent thrombin inhibitor.	Phe-Pro	32-39	coagulation factor II, thrombin	Homo sapiens	128-136
8821003-5	1995	In addition, both the transporter and the prolidase activities affected the overall transport of Phe when given as the dipeptide Phe-Pro, supporting the notion that intestinal absorption of peptides is an essential component of amino acid absorption.	Phe-Pro	129-136	peptidase D	Homo sapiens	42-51
8069586-10	1994	In conclusion, the transmembrane uptake of Phe-Pro is dependent on a proton gradient, and the intracellular metabolism of Phe-Pro is complete via hydrolysis by prolidase.	Phe-Pro	43-50	peptidase D	Homo sapiens	160-169
8069586-10	1994	In conclusion, the transmembrane uptake of Phe-Pro is dependent on a proton gradient, and the intracellular metabolism of Phe-Pro is complete via hydrolysis by prolidase.	Phe-Pro	122-129	peptidase D	Homo sapiens	160-169
4084535-6	1985	There was also no indication that prolidase could cleave the dipeptide Phe-Pro when the active bond itself is in the cis form.	Phe-Pro	71-78	peptidase D	Homo sapiens	34-43
570405-1	1979	The rates of hydrolysis of glycy-L-proline and L-phenylalanyl-L-proline, catalyzed by prolidase, have been measured at several temperatures under conditions where a high ratio of prolidase activity to substrate concentration existed.	Phe-Pro	47-71	peptidase D	Homo sapiens	86-95
570405-1	1979	The rates of hydrolysis of glycy-L-proline and L-phenylalanyl-L-proline, catalyzed by prolidase, have been measured at several temperatures under conditions where a high ratio of prolidase activity to substrate concentration existed.	Phe-Pro	47-71	peptidase D	Homo sapiens	179-188