PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9066677-0	1997	N-ethylmaleimide increases P-glycoprotein photoaffinity labeling with iodoaryl-azidoprazosin in multidrug resistant cells.	Ethylmaleimide	0-16	ATP binding cassette subfamily B member 1	Homo sapiens	27-41	
9066677-3	1997	In this report, we have examined the effects of N-ethylmaleimide, a potent inhibitor of the P-gp ATPase, on P-gp drug binding in intact MDR cells and in plasma membranes.	Ethylmaleimide	48-64	ATP binding cassette subfamily B member 1	Homo sapiens	92-96	
9066677-3	1997	In this report, we have examined the effects of N-ethylmaleimide, a potent inhibitor of the P-gp ATPase, on P-gp drug binding in intact MDR cells and in plasma membranes.	Ethylmaleimide	48-64	ATP binding cassette subfamily B member 1	Homo sapiens	108-112	
9066677-4	1997	Our results show that short term treatment of MDR cells with 1-50 microM N-ethylmaleimide led to a concentration dependent increase in P-gp photoaffinity labeling with iodoaryl-azidoparazosin (IAAP).	Ethylmaleimide	73-89	ATP binding cassette subfamily B member 1	Homo sapiens	135-139	
9066677-7	1997	Thus, the observed increase in P-gp photolabeling with IAAP in N-ethylmaleimide treated cells is not due to photolabeling at different sites.	Ethylmaleimide	63-79	ATP binding cassette subfamily B member 1	Homo sapiens	31-35	
9066677-8	1997	Incubation of MDR cells with [14C] N-ethylmaleimide showed that P-gp is directly modified at several Cysteine residues, as found from a complete proteolytic digestion of [14C] Nethylmaleimide labeled P-gp.	Ethylmaleimide	36-51	ATP binding cassette subfamily B member 1	Homo sapiens	64-68	
9066677-8	1997	Incubation of MDR cells with [14C] N-ethylmaleimide showed that P-gp is directly modified at several Cysteine residues, as found from a complete proteolytic digestion of [14C] Nethylmaleimide labeled P-gp.	Ethylmaleimide	36-51	ATP binding cassette subfamily B member 1	Homo sapiens	200-204	
9066677-8	1997	Incubation of MDR cells with [14C] N-ethylmaleimide showed that P-gp is directly modified at several Cysteine residues, as found from a complete proteolytic digestion of [14C] Nethylmaleimide labeled P-gp.	Ethylmaleimide	176-191	ATP binding cassette subfamily B member 1	Homo sapiens	64-68	
9066677-8	1997	Incubation of MDR cells with [14C] N-ethylmaleimide showed that P-gp is directly modified at several Cysteine residues, as found from a complete proteolytic digestion of [14C] Nethylmaleimide labeled P-gp.	Ethylmaleimide	176-191	ATP binding cassette subfamily B member 1	Homo sapiens	200-204	
9066677-11	1997	Interestingly, N-ethylmaleimide increases P-gp phosphorylation by inhibiting the turnover of Pgp phosphates.	Ethylmaleimide	15-31	ATP binding cassette subfamily B member 1	Homo sapiens	42-46	
9066677-13	1997	Taken together, the results of this study suggest that N-ethylmaleimide potentiates P-gp photolabeling with IAAP by inhibiting P-gp ATPase thereby increasing the local concentration of IAAP in intact MDR cells.	Ethylmaleimide	55-71	ATP binding cassette subfamily B member 1	Homo sapiens	84-88	
9066677-13	1997	Taken together, the results of this study suggest that N-ethylmaleimide potentiates P-gp photolabeling with IAAP by inhibiting P-gp ATPase thereby increasing the local concentration of IAAP in intact MDR cells.	Ethylmaleimide	55-71	ATP binding cassette subfamily B member 1	Homo sapiens	127-131	
9066677-14	1997	Furthermore, inhibition of P-gp ATPase by N-ethylmaleimide does not lead to conformational changes that affects P-gp drug binding.	Ethylmaleimide	42-58	ATP binding cassette subfamily B member 1	Homo sapiens	27-31	
7608182-6	1995	Transport was prevented by omission of Mg2+, by substitution of nonhydrolyzable adenylyl-beta,gamma-imidodiphosphate for ATP, by inhibition of the ATPase activity of P-glycoprotein with vanadate and N-ethylmaleimide, and by the chemosensitizers verapamil and amiodarone.	Ethylmaleimide	199-215	ATP binding cassette subfamily B member 1	Homo sapiens	166-180	
7559432-1	1995	The ATPase activity of P-glycoprotein is inactivated by N-ethylmaleimide (NEM), which is postulated to modify cysteine residues within either of the homology A consensus sequences for nucleotide binding (GNSGCGKS and GSSGCGKS, respectively) (Al-Shawi, M. K., Urbatsch, I. L., and Senior, A. E. (1994) J. Biol.	Ethylmaleimide	56-72	ATP binding cassette subfamily B member 1	Homo sapiens	23-37	
7559432-1	1995	The ATPase activity of P-glycoprotein is inactivated by N-ethylmaleimide (NEM), which is postulated to modify cysteine residues within either of the homology A consensus sequences for nucleotide binding (GNSGCGKS and GSSGCGKS, respectively) (Al-Shawi, M. K., Urbatsch, I. L., and Senior, A. E. (1994) J. Biol.	Ethylmaleimide	74-77	ATP binding cassette subfamily B member 1	Homo sapiens	23-37	
12820887-6	2003	The role of residues at each of the introduced sites in the catalytic cycle of Pgp was investigated by the effect of covalent conjugation with N-ethyl-maleimide (NEM).	Ethylmaleimide	143-160	ATP binding cassette subfamily B member 1	Homo sapiens	79-82	
12820887-6	2003	The role of residues at each of the introduced sites in the catalytic cycle of Pgp was investigated by the effect of covalent conjugation with N-ethyl-maleimide (NEM).	Ethylmaleimide	162-165	ATP binding cassette subfamily B member 1	Homo sapiens	79-82