PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16675661-6	2006	Analysis of mutations of amino acid residues adjacent to the selectivity filter led to identification of Phe-1013 and Tyr-1021, whose mutation causes substantial changes in DHP binding.	Phenylalanine	105-108	dihydropyrimidinase	Homo sapiens	173-176	
16675661-8	2006	We propose that DHP binding stabilizes a nonconducting state containing a single Ca(2+) ion in the pore through which Phe-1013 and Tyr-1021 are energetically coupled.	Phenylalanine	118-121	dihydropyrimidinase	Homo sapiens	16-19	
14660664-8	2004	First, unlike villin headpiece that contains a single buried salt bridge, DHP contains a buried charged cluster comprising residues Glu(39), Arg(66), Lys(70), and the C-terminal carboxylate of Phe(76).	Phenylalanine	193-196	dihydropyrimidinase	Homo sapiens	74-77	
14993732-5	2004	We identified Phe(1112) and Ser(1115) in the pore-forming IIIS5-S6 linker region of the alpha(1C) subunit as critical determinants of the binding of dihydropyridines (DHP).	Phenylalanine	14-17	dihydropyrimidinase	Homo sapiens	167-170	
14993732-7	2004	We proposed that Phe(1112) and Ser(1115) in the pore-forming IIIS5-S6 linker region is required for the stabilization of the Ca(2+) channel in the open state by Ca(2+) channel agonists and further proposed a novel model for the DHP-binding pocket of the alpha(1C) subunit.	Phenylalanine	17-20	dihydropyrimidinase	Homo sapiens	228-231	
7601731-8	1995	Infusion of 2,3-DHP resulted in a plasma 2,3-DHP content of 9.4 mumol/L and increased plasma THR, ARG, VAL, PHE, ILE, LEU, and LYS concentrations (P < .10).	Phenylalanine	108-111	dihydropyrimidinase	Homo sapiens	16-19