PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
33855492-0	2019	Feedback Regulation of Cathepsin C by the Propeptide Dipeptides of Granzymes A and B.	Dipeptides	53-63	cathepsin C	Homo sapiens	23-34	
33855492-1	2019	Granzymes A and B are activated by proteolytic removal of their N-terminal dipeptides by cathepsin C (dipeptidyl-peptidase I).	Dipeptides	75-85	cathepsin C	Homo sapiens	89-100	
33855492-1	2019	Granzymes A and B are activated by proteolytic removal of their N-terminal dipeptides by cathepsin C (dipeptidyl-peptidase I).	Dipeptides	75-85	cathepsin C	Homo sapiens	102-124	
33855492-4	2019	Cathepsin C is known to generate cytotoxic polymers from various dipeptides, however, in the case of the dipeptides Glu-Lys and Gly-Glu, cathepsin C was unable to polymerize them.	Dipeptides	65-75	cathepsin C	Homo sapiens	0-11	
33855492-4	2019	Cathepsin C is known to generate cytotoxic polymers from various dipeptides, however, in the case of the dipeptides Glu-Lys and Gly-Glu, cathepsin C was unable to polymerize them.	Dipeptides	105-115	cathepsin C	Homo sapiens	0-11	
33855492-4	2019	Cathepsin C is known to generate cytotoxic polymers from various dipeptides, however, in the case of the dipeptides Glu-Lys and Gly-Glu, cathepsin C was unable to polymerize them.	Dipeptides	105-115	cathepsin C	Homo sapiens	137-148	
33855492-5	2019	Unexpectedly the dipeptides were found to be inhibitors of the transferase activity of cathepsin C (IC50 < 20 mM), and weak competitive inhibitors of the peptidase activity with Ki values in the millimolar range.	Dipeptides	17-27	cathepsin C	Homo sapiens	87-98	
33855492-6	2019	This suggests that the dipeptides can play role in a feedback loop that controls transferase and proteolytic activities of cathepsin C in various biological processes.	Dipeptides	23-33	cathepsin C	Homo sapiens	123-134