PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1944771-5	1991	Although essentially no hydrogen peroxide is formed during the fully coupled oxidation of tetrahydrobiopterin or 6-methyltetrahydropterin by phenylalanine hydroxylase when phenylalanine is the amino acid substrate, significant amounts of hydrogen peroxide are formed during the partially uncoupled oxidation of 6-methyltetrahydropterin when para-fluorophenylalanine or para-chlorophenylalanine are used in place of phenylalanine.	Fenclonine	369-393	phenylalanine hydroxylase	Homo sapiens	141-166	
136660-0	1976	What is the mechanism of the irreversible inhibition of phenylalanine hydroxylase by p-chlorophenylalanine?	Fenclonine	85-106	phenylalanine hydroxylase	Homo sapiens	56-81	
2949745-2	1987	We investigated the effect of p-chlorophenylalanine on production of human phenylalanine hydroxylase in human hepatoma cells and cells transformed with the recombinant human phenylalanine hydroxylase gene.	Fenclonine	30-51	phenylalanine hydroxylase	Homo sapiens	75-100	
234440-0	1975	p-Chlorphenylalanine effect on phenylalanine hydroxylase in hepatoma cells in culture.	Fenclonine	0-20	phenylalanine hydroxylase	Homo sapiens	31-56	
234440-2	1975	The similarity of the effect of p-chlorophenylalanine on phenylalanine hydroxylase in the hepatoma cells and that reported from studies in vivo indicates that the loss of phenylalanine hydroxylase activity is due to a direct interaction of the amino acid analogue with the liver.	Fenclonine	32-53	phenylalanine hydroxylase	Homo sapiens	57-82	
234440-2	1975	The similarity of the effect of p-chlorophenylalanine on phenylalanine hydroxylase in the hepatoma cells and that reported from studies in vivo indicates that the loss of phenylalanine hydroxylase activity is due to a direct interaction of the amino acid analogue with the liver.	Fenclonine	32-53	phenylalanine hydroxylase	Homo sapiens	171-196	
4280309-0	1974	Inhibition of phenylalanine hydroxylase by p-chlorophenylalanine; dependence on cofactor structure.	Fenclonine	43-64	phenylalanine hydroxylase	Homo sapiens	14-39