PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1373816-7	1992	The other PTPase, PEP (proline-, glutamic acid-, serine-, and threonine-rich [PEST]-domain phosphatase), is distinguished by virtue of a large carboxy-terminal domain of approximately 500 amino acids that is rich in PEST residues.	Proline	23-30	prolyl endopeptidase	Mus musculus	18-21	
8068820-1	1994	Prolyl endopeptidase is a serine protease that specifically cleaves peptides on the carboxyl side of proline residues.	Proline	101-108	prolyl endopeptidase	Mus musculus	0-20	
10092092-3	1999	Among the PTP cloned by reverse transcription-PCR, mRNA expression of the proline-, glutamic acid-, serine- and threonine-rich (PEST) domain phosphatase (PEP) was selectively elevated 3.1-fold within 3 h after anti-IgM antibody stimulation.	Proline	74-81	prolyl endopeptidase	Mus musculus	154-157	
2241932-1	1990	Prolyl endopeptidase is a serine proteinase that specifically cleaves peptides on the carboxy side of proline residues.	Proline	102-109	prolyl endopeptidase	Mus musculus	0-20	
34095107-10	2021	Interestingly, PREP disruption inhibited p-ERK and p-p65 and reduced the levels of proinflammatory cytokines in response to endotoxin and proline-glycine-proline, which guided macrophage/neutrophil infiltration in mice fed a HFD for 24 weeks.	Proline	138-145	prolyl endopeptidase	Mus musculus	15-19	
34095107-10	2021	Interestingly, PREP disruption inhibited p-ERK and p-p65 and reduced the levels of proinflammatory cytokines in response to endotoxin and proline-glycine-proline, which guided macrophage/neutrophil infiltration in mice fed a HFD for 24 weeks.	Proline	154-161	prolyl endopeptidase	Mus musculus	15-19	
6358414-7	1984	Since prolyl endopeptidase readily degrades many proline-containing neuropeptides, the inhibitor should be of value in studies on the role of the enzyme in neuropeptide metabolism.	Proline	49-56	prolyl endopeptidase	Mus musculus	6-26	
33044914-1	2020	Prolyl endopeptidase (PREP), also known as prolyl oligopeptidase (POP), is an enzyme that cleaves short peptides (<30 amino acids in length) on the C-terminal side of proline.	Proline	167-174	prolyl endopeptidase	Mus musculus	0-20	
6351752-2	1983	The prolyl endopeptidase is apparently highly specific for cleaving peptides after proline residues.	Proline	83-90	prolyl endopeptidase	Mus musculus	4-24	
33044914-1	2020	Prolyl endopeptidase (PREP), also known as prolyl oligopeptidase (POP), is an enzyme that cleaves short peptides (<30 amino acids in length) on the C-terminal side of proline.	Proline	167-174	prolyl endopeptidase	Mus musculus	22-26	
33044914-1	2020	Prolyl endopeptidase (PREP), also known as prolyl oligopeptidase (POP), is an enzyme that cleaves short peptides (<30 amino acids in length) on the C-terminal side of proline.	Proline	167-174	prolyl endopeptidase	Mus musculus	43-64	
33044914-1	2020	Prolyl endopeptidase (PREP), also known as prolyl oligopeptidase (POP), is an enzyme that cleaves short peptides (<30 amino acids in length) on the C-terminal side of proline.	Proline	167-174	prolyl endopeptidase	Mus musculus	66-69	
31060637-1	2019	SummaryProlyl endopeptidase (PREP) is a post-proline cleaving enzyme.	Proline	45-52	prolyl endopeptidase	Mus musculus	29-33	
32309365-12	2020	Further mechanistic investigations indicated that the protective effect of PREP disruption on liver inflammation was associated with the suppressed production of matrix metalloproteinases (MMPs) and proline-glycine-proline (PGP) and the inhibition of neutrophil infiltration.	Proline	199-206	prolyl endopeptidase	Mus musculus	75-79	
32309365-12	2020	Further mechanistic investigations indicated that the protective effect of PREP disruption on liver inflammation was associated with the suppressed production of matrix metalloproteinases (MMPs) and proline-glycine-proline (PGP) and the inhibition of neutrophil infiltration.	Proline	215-222	prolyl endopeptidase	Mus musculus	75-79	
20600704-1	2010	Prolyl oligopeptidase (POP) is a widely distributed serine peptidase which hydrolyzes small peptides on the carboxyl side of an internal proline residue.	Proline	137-144	prolyl endopeptidase	Mus musculus	0-21	
20600704-1	2010	Prolyl oligopeptidase (POP) is a widely distributed serine peptidase which hydrolyzes small peptides on the carboxyl side of an internal proline residue.	Proline	137-144	prolyl endopeptidase	Mus musculus	23-26	
19911840-6	2009	Moreover, these experiments also supported the known preference of Prep for shorter peptides while revealing a previously unknown cleavage site specificity of Prep when processing certain multi-proline-containing peptides, including PRPs.	Proline	194-201	prolyl endopeptidase	Mus musculus	159-163	
18618130-1	2008	Prolyl oligopeptidase (POP) is a serine endopeptidase that hydrolyses proline-containing peptides shorter than 30-mer, including many bioactive peptides.	Proline	70-77	prolyl endopeptidase	Mus musculus	0-21	
18618130-1	2008	Prolyl oligopeptidase (POP) is a serine endopeptidase that hydrolyses proline-containing peptides shorter than 30-mer, including many bioactive peptides.	Proline	70-77	prolyl endopeptidase	Mus musculus	23-26