PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9119038-1	1997	P-glycoprotein, a plasma membrane protein overexpressed in multidrug-resistant (MDR) cells, exhibits in vitro an ATPase activity and is responsible for the energy-dependent efflux of structurally unrelated cytotoxic drugs (like vinblastine) and various MDR-reversing agents (like verapamil and progesterone) from these MDR cells.	Progesterone	294-306	ATP binding cassette subfamily B member 1	Homo sapiens	0-14	
9119038-3	1997	The basal P-glycoprotein ATPase activity is increased by verapamil and progesterone, with respective half-maximal activating concentrations of approximately 1.5 microM and approximately 25 microM, and activation factors of approximately 1.7 and approximately 2.2.	Progesterone	71-83	ATP binding cassette subfamily B member 1	Homo sapiens	10-24	
9119038-4	1997	Vinblastine inhibits the activation of P-glycoprotein ATPase induced by verapamil or progesterone with an inhibition constant approximately 0.5 microM in both cases.	Progesterone	85-97	ATP binding cassette subfamily B member 1	Homo sapiens	39-53	
9119038-8	1997	In contrast, the combined modulation of P-glycoprotein ATPase by vinblastine and progesterone reveals a non-competitive relationship between these two drugs, and hence shows that they can independently and simultaneously bind P-glycoprotein on distinct sites.	Progesterone	81-93	ATP binding cassette subfamily B member 1	Homo sapiens	40-54	
9119038-8	1997	In contrast, the combined modulation of P-glycoprotein ATPase by vinblastine and progesterone reveals a non-competitive relationship between these two drugs, and hence shows that they can independently and simultaneously bind P-glycoprotein on distinct sites.	Progesterone	81-93	ATP binding cassette subfamily B member 1	Homo sapiens	226-240	
9119038-9	1997	Since verapamil and progesterone are mutual inhibitors of P-glycoprotein ATPase stimulation in a non-competitive manner, these two molecules can also bind independently P-glycoprotein on separated sites.	Progesterone	20-32	ATP binding cassette subfamily B member 1	Homo sapiens	58-72	
9119038-9	1997	Since verapamil and progesterone are mutual inhibitors of P-glycoprotein ATPase stimulation in a non-competitive manner, these two molecules can also bind independently P-glycoprotein on separated sites.	Progesterone	20-32	ATP binding cassette subfamily B member 1	Homo sapiens	169-183	
9119038-10	1997	This is confirmed here by the observation of a synergistic effect when mixtures of verapamil and progesterone are tested for the modulation of P-glycoprotein ATPase.	Progesterone	97-109	ATP binding cassette subfamily B member 1	Homo sapiens	143-157