PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1666284-6	1991	The removal of a portion of propeptides results in conformational changes around the Gln80-Phe81 and His82-Phe83 bonds in respective intermediates of MMP-1 and MMP-3 and render them to rapid specific cleavage by MMP-3 to generate stable, fully active enzymes.	propeptides	28-39	matrix metallopeptidase 3	Homo sapiens	160-165	
9642125-8	1998	Dibasic sites also exist in the propeptides of several MMPs including proMMP-3.	propeptides	32-43	matrix metallopeptidase 3	Homo sapiens	55-59	
30422384-0	2019	Propeptide glycosylation and galectin-3 binding decrease proteolytic activation of human proMMP-9/progelatinase B. Matrix metalloproteinases (MMPs) are secreted as proenzymes, containing propeptides that interact with the catalytic zinc, thereby controlling MMP activation.	propeptides	187-198	matrix metallopeptidase 3	Homo sapiens	142-146	
1666284-6	1991	The removal of a portion of propeptides results in conformational changes around the Gln80-Phe81 and His82-Phe83 bonds in respective intermediates of MMP-1 and MMP-3 and render them to rapid specific cleavage by MMP-3 to generate stable, fully active enzymes.	propeptides	28-39	matrix metallopeptidase 3	Homo sapiens	212-217