PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7915013-1	1994	Tetrahydrobiopterin (BH4), the obligatory cofactor of the aromatic amino acid hydroxylases, decreased the in situ 32P-phosphorylation of tyrosine hydroxylase (TH) in rat striatal synaptosomes.	Phosphorus-32	114-117	tyrosine hydroxylase	Rattus norvegicus	137-157	
7915013-1	1994	Tetrahydrobiopterin (BH4), the obligatory cofactor of the aromatic amino acid hydroxylases, decreased the in situ 32P-phosphorylation of tyrosine hydroxylase (TH) in rat striatal synaptosomes.	Phosphorus-32	114-117	tyrosine hydroxylase	Rattus norvegicus	159-161	
7915013-2	1994	Incubation of pre-32P-labeled synaptosomes with BH4 in the presence of a permeant analogue of cAMP decreased the cAMP-stimulated level of 32P label incorporation into TH by about 50%, as determined by immunoprecipitation and autoradiography of SDS-polyacrylamide gels.	Phosphorus-32	18-21	tyrosine hydroxylase	Rattus norvegicus	167-169	
7915013-2	1994	Incubation of pre-32P-labeled synaptosomes with BH4 in the presence of a permeant analogue of cAMP decreased the cAMP-stimulated level of 32P label incorporation into TH by about 50%, as determined by immunoprecipitation and autoradiography of SDS-polyacrylamide gels.	Phosphorus-32	138-141	tyrosine hydroxylase	Rattus norvegicus	167-169	
7915013-4	1994	A similar decrease in the amount of TH 32P-labeling was observed with the precursor of BH4, sepiapterin.	Phosphorus-32	39-42	tyrosine hydroxylase	Rattus norvegicus	36-38