PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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 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 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 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 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 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 0-20 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 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 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 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