PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31363986-0	2019	Acylpeptide hydrolase (APEH) sequence variants with potential impact on the metabolism of the antiepileptic drug valproic acid.	Valproic Acid	113-126	acylaminoacyl-peptide hydrolase	Homo sapiens	0-21	
31363986-0	2019	Acylpeptide hydrolase (APEH) sequence variants with potential impact on the metabolism of the antiepileptic drug valproic acid.	Valproic Acid	113-126	acylaminoacyl-peptide hydrolase	Homo sapiens	23-27	
31363986-2	2019	Beyond that, APEH participates in the metabolism of the antiepileptic drug valproic acid (2-propylpentanoic acid; VPA) by catalyzing the hydrolysis of the VPA metabolite valproylglucuronide (VPA-G) to its aglycon.	Valproic Acid	75-88	acylaminoacyl-peptide hydrolase	Homo sapiens	13-17	
31363986-2	2019	Beyond that, APEH participates in the metabolism of the antiepileptic drug valproic acid (2-propylpentanoic acid; VPA) by catalyzing the hydrolysis of the VPA metabolite valproylglucuronide (VPA-G) to its aglycon.	Valproic Acid	90-112	acylaminoacyl-peptide hydrolase	Homo sapiens	13-17	
31363986-2	2019	Beyond that, APEH participates in the metabolism of the antiepileptic drug valproic acid (2-propylpentanoic acid; VPA) by catalyzing the hydrolysis of the VPA metabolite valproylglucuronide (VPA-G) to its aglycon.	Valproic Acid	114-117	acylaminoacyl-peptide hydrolase	Homo sapiens	13-17	
21770850-0	2011	Inhibition mechanism of carbapenem antibiotics on acylpeptide hydrolase, a key enzyme in the interaction with valproic acid.	Valproic Acid	110-123	acylaminoacyl-peptide hydrolase	Homo sapiens	50-71	
27406852-0	2016	Influence of acylpeptide hydrolase polymorphisms on valproic acid level in Chinese epilepsy patients.	Valproic Acid	52-65	acylaminoacyl-peptide hydrolase	Homo sapiens	13-34	
26075835-2	2016	Our previous in vitro studies suggest that inhibition of the acylpeptide hydrolase (APEH) activity as valproic acid glucuronide (VPA-G) hydrolase by carbapenems in human liver cytosol is a key process for clinical drug-drug interaction (DDI) of valproic acid (VPA) with carbapenems.	Valproic Acid	102-115	acylaminoacyl-peptide hydrolase	Homo sapiens	61-82	
26075835-2	2016	Our previous in vitro studies suggest that inhibition of the acylpeptide hydrolase (APEH) activity as valproic acid glucuronide (VPA-G) hydrolase by carbapenems in human liver cytosol is a key process for clinical drug-drug interaction (DDI) of valproic acid (VPA) with carbapenems.	Valproic Acid	102-115	acylaminoacyl-peptide hydrolase	Homo sapiens	84-88	
26075835-2	2016	Our previous in vitro studies suggest that inhibition of the acylpeptide hydrolase (APEH) activity as valproic acid glucuronide (VPA-G) hydrolase by carbapenems in human liver cytosol is a key process for clinical drug-drug interaction (DDI) of valproic acid (VPA) with carbapenems.	Valproic Acid	129-132	acylaminoacyl-peptide hydrolase	Homo sapiens	61-82	
26075835-2	2016	Our previous in vitro studies suggest that inhibition of the acylpeptide hydrolase (APEH) activity as valproic acid glucuronide (VPA-G) hydrolase by carbapenems in human liver cytosol is a key process for clinical drug-drug interaction (DDI) of valproic acid (VPA) with carbapenems.	Valproic Acid	129-132	acylaminoacyl-peptide hydrolase	Homo sapiens	84-88	
21770850-1	2011	We have reported that inhibition of acylpeptide hydrolase (APEH), identified as valproic acid glucuronide hydrolase in human liver cytosol, by carbapenem antibiotics could lead to a decrease of plasma levels of valproic acid.	Valproic Acid	80-93	acylaminoacyl-peptide hydrolase	Homo sapiens	36-57	
21770850-1	2011	We have reported that inhibition of acylpeptide hydrolase (APEH), identified as valproic acid glucuronide hydrolase in human liver cytosol, by carbapenem antibiotics could lead to a decrease of plasma levels of valproic acid.	Valproic Acid	80-93	acylaminoacyl-peptide hydrolase	Homo sapiens	59-63