PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28867741-3	2017	These findings suggest that the inhibition of PEPT1, which were up-regulated in inflamed or non-inflamed site on UC and CD patients, contribute to the clinical effect of commercially available drugs for IBD patients through the inhibition of uptake of antigenic proinflammatory oligopeptides such as formyl-methionine (Met)-leucine (Leu)-phenylalanine (Phe) via PEPT1.	Phenylalanine	353-356	solute carrier family 15 member 1	Homo sapiens	46-51	
28867741-3	2017	These findings suggest that the inhibition of PEPT1, which were up-regulated in inflamed or non-inflamed site on UC and CD patients, contribute to the clinical effect of commercially available drugs for IBD patients through the inhibition of uptake of antigenic proinflammatory oligopeptides such as formyl-methionine (Met)-leucine (Leu)-phenylalanine (Phe) via PEPT1.	Phenylalanine	353-356	solute carrier family 15 member 1	Homo sapiens	362-367	
26590007-2	2016	Among the quinolones examined, lomefloxacin, moxifloxacin (MFLX) and purlifloxacin significantly inhibited the uptake of PEPT1 substrate phenylalanine-Psi(CN-S)-alanine (Phe-Psi-Ala) in HeLa/PEPT1 cells to 31.6 +- 1.3%, 27.6 +- 2.9%, 36.8 +- 2.2% and 32.6 +- 1.4%, respectively.	Phenylalanine	137-150	solute carrier family 15 member 1	Homo sapiens	121-126	
26590007-2	2016	Among the quinolones examined, lomefloxacin, moxifloxacin (MFLX) and purlifloxacin significantly inhibited the uptake of PEPT1 substrate phenylalanine-Psi(CN-S)-alanine (Phe-Psi-Ala) in HeLa/PEPT1 cells to 31.6 +- 1.3%, 27.6 +- 2.9%, 36.8 +- 2.2% and 32.6 +- 1.4%, respectively.	Phenylalanine	137-150	solute carrier family 15 member 1	Homo sapiens	191-196	
26590007-2	2016	Among the quinolones examined, lomefloxacin, moxifloxacin (MFLX) and purlifloxacin significantly inhibited the uptake of PEPT1 substrate phenylalanine-Psi(CN-S)-alanine (Phe-Psi-Ala) in HeLa/PEPT1 cells to 31.6 +- 1.3%, 27.6 +- 2.9%, 36.8 +- 2.2% and 32.6 +- 1.4%, respectively.	Phenylalanine	170-173	solute carrier family 15 member 1	Homo sapiens	121-126	
10848990-5	2000	Ac-Phe-NH2 had a very weak interaction with PepT1 (Ki = 16.8+/-5.64 mM); neither Phe nor Phe-NH2 interacted with PepT1 with measurable affinity.	Phenylalanine	3-6	solute carrier family 15 member 1	Homo sapiens	44-49	
23735006-3	2013	Herein the structure-activity relationship (SAR) of a set of modified H-Phe-Phe-NH2 analogues is presented together with their potential active uptake by PEPT1 transporter, intestinal permeability, and metabolic stability.	Phenylalanine	72-75	solute carrier family 15 member 1	Homo sapiens	154-159	
23735006-3	2013	Herein the structure-activity relationship (SAR) of a set of modified H-Phe-Phe-NH2 analogues is presented together with their potential active uptake by PEPT1 transporter, intestinal permeability, and metabolic stability.	Phenylalanine	76-79	solute carrier family 15 member 1	Homo sapiens	154-159	
17932227-8	2007	Mutational analysis showed that phenylalanine 293, phenylalanine 297, and threonine 281 in transmembrane segment 7 of the human di/tripeptide transporter, hPepT1, are important for the targeting to lipid rafts and transport activity of hPepT1.	Phenylalanine	32-45	solute carrier family 15 member 1	Homo sapiens	155-161	
17932227-8	2007	Mutational analysis showed that phenylalanine 293, phenylalanine 297, and threonine 281 in transmembrane segment 7 of the human di/tripeptide transporter, hPepT1, are important for the targeting to lipid rafts and transport activity of hPepT1.	Phenylalanine	32-45	solute carrier family 15 member 1	Homo sapiens	236-242	
17932227-8	2007	Mutational analysis showed that phenylalanine 293, phenylalanine 297, and threonine 281 in transmembrane segment 7 of the human di/tripeptide transporter, hPepT1, are important for the targeting to lipid rafts and transport activity of hPepT1.	Phenylalanine	51-64	solute carrier family 15 member 1	Homo sapiens	155-161	
17932227-8	2007	Mutational analysis showed that phenylalanine 293, phenylalanine 297, and threonine 281 in transmembrane segment 7 of the human di/tripeptide transporter, hPepT1, are important for the targeting to lipid rafts and transport activity of hPepT1.	Phenylalanine	51-64	solute carrier family 15 member 1	Homo sapiens	236-242	
9126331-3	1997	Functional expression of PepT1 was determined in different recombinant clones by flux studies employing the radiolabeled dipeptide 3H-(D)-Phe-(L)-Ala. One clone (GS-PepT1) displayed high level functional expression that was pH dependent and saturable with an app.	Phenylalanine	138-141	solute carrier family 15 member 1	Homo sapiens	25-30