PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8494497-6	1993	The ATMP pigment markedly inhibited the enzyme ferrochelatase in vitro, thus supporting its identification as N-methyl protoporphyrin.	N-methylprotoporphyrin IX	110-133	ferrochelatase	Mus musculus	47-61	
2012610-2	1991	A hepatic green pigment with inhibitory properties towards the enzyme ferrochelatase has been isolated from the liver of mice treated with griseofulvin and identified as N-methylprotoporphyrin.	N-methylprotoporphyrin IX	170-192	ferrochelatase	Mus musculus	70-84	
2283668-1	1990	A hepatic green pigment, inhibitory toward ferrochelatase, has been isolated from the liver of mice treated with griseofulvin, isogriseofulvin, or 3,5-diethoxycarbonyl-1,4-dihydrocollidine and has been shown to exhibit identical chromatographic characteristics to authentic N-methyl protoporphyrin.	N-methylprotoporphyrin IX	274-297	ferrochelatase	Mus musculus	43-57	
32716567-7	2020	An intravitreal injection of the FECH inhibitor N-methyl protoporphyrin had similar effects.	N-methylprotoporphyrin IX	48-71	ferrochelatase	Mus musculus	33-37	
2804139-4	1989	The data obtained demonstrate that mouse ferrochelatase binds a wide variety of porphyrins and metalloporphyrins with kd values ranging from 6 nM for N-methylprotoporphyrin to 1.08 microM for coproporphyrin III.	N-methylprotoporphyrin IX	150-172	ferrochelatase	Mus musculus	41-55	
3477226-4	1987	N-Methylprotoporphyrin at nanomolar concentrations also strongly inhibited ferrochelatase activity, but had no inhibitory effect on cellular haem production.	N-methylprotoporphyrin IX	0-22	ferrochelatase	Mus musculus	75-89	
26343413-7	2015	N-methyl PPIX strongly inhibits ferrochelatase, the enzyme that converts PPIX to heme, and leads to PPIX accumulation.	N-methylprotoporphyrin IX	0-13	ferrochelatase	Mus musculus	32-46	
16792525-3	2006	To create ferrochelatase variants with different extents of tolerance towards NMPP and to understand further the mechanism of ferrochelatase inhibition by NMPP, we isolated variants with increased NMPP resistance, bearing mutations in an active-site loop (murine ferrochelatase residues 248-257), which was previously shown to mediate a protein conformational change triggered by porphyrin binding.	N-methylprotoporphyrin IX	155-159	ferrochelatase	Mus musculus	126-140	
16792525-3	2006	To create ferrochelatase variants with different extents of tolerance towards NMPP and to understand further the mechanism of ferrochelatase inhibition by NMPP, we isolated variants with increased NMPP resistance, bearing mutations in an active-site loop (murine ferrochelatase residues 248-257), which was previously shown to mediate a protein conformational change triggered by porphyrin binding.	N-methylprotoporphyrin IX	155-159	ferrochelatase	Mus musculus	126-140	
16792525-3	2006	To create ferrochelatase variants with different extents of tolerance towards NMPP and to understand further the mechanism of ferrochelatase inhibition by NMPP, we isolated variants with increased NMPP resistance, bearing mutations in an active-site loop (murine ferrochelatase residues 248-257), which was previously shown to mediate a protein conformational change triggered by porphyrin binding.	N-methylprotoporphyrin IX	155-159	ferrochelatase	Mus musculus	126-140	
16792525-3	2006	To create ferrochelatase variants with different extents of tolerance towards NMPP and to understand further the mechanism of ferrochelatase inhibition by NMPP, we isolated variants with increased NMPP resistance, bearing mutations in an active-site loop (murine ferrochelatase residues 248-257), which was previously shown to mediate a protein conformational change triggered by porphyrin binding.	N-methylprotoporphyrin IX	155-159	ferrochelatase	Mus musculus	126-140	
16792525-5	2006	While the binding affinity of the P255X variants for NMPP decreased by one order of magnitude in relation to that of wild-type enzyme, the inhibition constant increased by approximately two orders of magnitude (K(i)(app) values of 1 microM and 2.3 microM for P255R and P255G respectively, as against 3 nM for wild-type ferrochelatase).	N-methylprotoporphyrin IX	53-57	ferrochelatase	Mus musculus	319-333