PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11274478-1	2001	GTP cyclohydrolase I feedback regulatory protein (GFRP) mediates feedback inhibition of GTP cyclohydrolase I activity by 6R-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4), which is an essential cofactor for key enzymes producing catecholamines, serotonin, and nitric oxide as well as phenylalanine hydroxylase.	Catecholamines	226-240	phenylalanine hydroxylase	Homo sapiens	281-306	
12631267-8	2003	Two alternative conformations, rotated 180 degrees around an imaginary iron-catecholamine axis, were found for DA and l-DOPA in PAH and for DA in TH.	Catecholamines	76-89	phenylalanine hydroxylase	Homo sapiens	128-131	
33336311-3	2020	Hypo/hypercapnia, as well as mechanical ventilation during and after resuscitation, can affect CO2 levels and trigger a dangerous pathophysiological vicious circle related to the relationship between pH, cellular demand, and catecholamine levels.	Catecholamines	225-238	phenylalanine hydroxylase	Homo sapiens	200-202	
1959929-5	1991	The regions that have been found to be linked to TSC in different families map to the positions of three enzymes, phenylalanine hydroxylase (12q22-24), tyrosinase (11q14-22), and dopamine-beta-hydroxylase (9q34), all of which are involved in the conversion of phenylalanine to catecholamine neurotransmitters or melanin.	Catecholamines	277-290	phenylalanine hydroxylase	Homo sapiens	114-139	
34952194-1	2022	Phenylalanine hydroxylase (PAH) is involved in immune defence reactions by providing the starting material, tyrosine, to synthesise catecholamines and melanin.	Catecholamines	132-146	phenylalanine hydroxylase	Homo sapiens	0-25	
34952194-1	2022	Phenylalanine hydroxylase (PAH) is involved in immune defence reactions by providing the starting material, tyrosine, to synthesise catecholamines and melanin.	Catecholamines	132-146	phenylalanine hydroxylase	Homo sapiens	27-30	
2872999-1	1986	Phenylalanine hydroxylase (PAH) and tyrosine hydroxylase (TH) are consecutive enzymes in the metabolic pathway leading to the production of catecholamine neurotransmitters.	Catecholamines	140-153	phenylalanine hydroxylase	Homo sapiens	0-25	
2872999-1	1986	Phenylalanine hydroxylase (PAH) and tyrosine hydroxylase (TH) are consecutive enzymes in the metabolic pathway leading to the production of catecholamine neurotransmitters.	Catecholamines	140-153	phenylalanine hydroxylase	Homo sapiens	27-30	
5165490-0	1971	Two mechanisms for the inhibition in vitro of phenylalanine hydroxylase by catecholamines.	Catecholamines	75-89	phenylalanine hydroxylase	Homo sapiens	46-71	
32929770-13	2021	CONCLUSION: We introduced a method that can resolve Pi using 7 Tesla STEAM 31 P-MRS. We demonstrate the stability of Pi/PCr and myocardial pH in volunteers at rest and during catecholamine stress.	Catecholamines	175-188	phenylalanine hydroxylase	Homo sapiens	139-141	
26241318-4	2015	These solution properties are consistent with the regulatory mechanisms of the two enzymes, in that phenylalanine hydroxylase is activated by phenylalanine binding to an allosteric site, while tyrosine hydroxylase is regulated by binding of catecholamines in the active site.	Catecholamines	241-255	phenylalanine hydroxylase	Homo sapiens	100-125	
21839840-8	2011	These results indicated collectively that CfPAH, as a homologue of phenylalanine hydroxylase in scallop C. farreri, could be induced by cytokine and involved in the immunomodulation of scallops by supplying the starting material tyrosine for the synthesis of melanin and catecholamines.	Catecholamines	271-285	phenylalanine hydroxylase	Homo sapiens	67-92	
23898865-1	2013	BACKGROUND: Phenylalanine hydroxylase (PAH) is the enzyme that metabolizes phenylalanine, an essential amino acid required for catecholamine synthesis.	Catecholamines	127-140	phenylalanine hydroxylase	Homo sapiens	12-37	
23898865-1	2013	BACKGROUND: Phenylalanine hydroxylase (PAH) is the enzyme that metabolizes phenylalanine, an essential amino acid required for catecholamine synthesis.	Catecholamines	127-140	phenylalanine hydroxylase	Homo sapiens	39-42