PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
14675567-8	2004	Positive correlation was found between S-100B and Phe blood concentration (r = 0.46, P < 0.01).	Phenylalanine	50-53	S100 calcium binding protein B	Homo sapiens	39-45	
19469484-5	2009	The SBi279 binding site on Ca(2+)-S100B overlaps the SBi132 and SBi523 sites and contacts residues in both loop 2 (Ser-41, His-42, Phe-43, Leu-44, and Glu-45) and helix 4 (Ile-80, Ala-83, Cys-84, Phe-87, and Phe-88).	Phenylalanine	131-134	S100 calcium binding protein B	Homo sapiens	34-39	
19469484-5	2009	The SBi279 binding site on Ca(2+)-S100B overlaps the SBi132 and SBi523 sites and contacts residues in both loop 2 (Ser-41, His-42, Phe-43, Leu-44, and Glu-45) and helix 4 (Ile-80, Ala-83, Cys-84, Phe-87, and Phe-88).	Phenylalanine	196-199	S100 calcium binding protein B	Homo sapiens	34-39	
19469484-5	2009	The SBi279 binding site on Ca(2+)-S100B overlaps the SBi132 and SBi523 sites and contacts residues in both loop 2 (Ser-41, His-42, Phe-43, Leu-44, and Glu-45) and helix 4 (Ile-80, Ala-83, Cys-84, Phe-87, and Phe-88).	Phenylalanine	196-199	S100 calcium binding protein B	Homo sapiens	34-39	
14675567-10	2004	CONCLUSIONS: (a) Serum S-100B protein level, for the first time evaluated in PKU, was positively correlated with Phe blood level in PKU patients.	Phenylalanine	113-116	S100 calcium binding protein B	Homo sapiens	23-29	
10913138-3	2000	The residues in the C-terminal domain of S100B encompassing Phe(87) and Phe(88) have been implicated in interaction with target proteins.	Phenylalanine	60-63	S100 calcium binding protein B	Homo sapiens	41-46	
10913138-3	2000	The residues in the C-terminal domain of S100B encompassing Phe(87) and Phe(88) have been implicated in interaction with target proteins.	Phenylalanine	72-75	S100 calcium binding protein B	Homo sapiens	41-46	
10807905-4	2000	Interaction of Nef and hTE was abolished by point mutations in Nef at residues Asp(108), Leu(112), Phe(121), Pro(122), and Asp(123).	Phenylalanine	99-102	S100 calcium binding protein B	Homo sapiens	15-18	
10807905-4	2000	Interaction of Nef and hTE was abolished by point mutations in Nef at residues Asp(108), Leu(112), Phe(121), Pro(122), and Asp(123).	Phenylalanine	99-102	S100 calcium binding protein B	Homo sapiens	63-66	
2736040-7	1989	Proton NMR resonance broadening in the range 6.8-7.2 ppm, corresponding to phenylalanine nuclei of S100b, indicates that these residues may be involved in TFP binding.	Phenylalanine	75-88	S100 calcium binding protein B	Homo sapiens	99-104	
8688416-2	1996	Previously it has been suggested that calcium binding to S100b leads to the exposure of at least one phenylalanine residue (Mani et al., 1982, 1983).	Phenylalanine	101-114	S100 calcium binding protein B	Homo sapiens	57-62	
1931237-3	1991	Moreover, within this acidic region of transcriptional activators and the homologous sequence within the second Nef alpha-helix, is a potential transcriptional activation consensus sequence (TACS) bounded by a pair of acidic amino acids (aspartic or glutamic acids) at the N-terminus and a highly invariant phenylalanine (hydrophobic), often followed by an acidic (aspartic) residue, at the C-terminus of the sequence.	Phenylalanine	307-320	S100 calcium binding protein B	Homo sapiens	112-115	
2736040-9	1989	Thus, we suggest that Ca2+ induces the exposure of a hydrophobic domain on S100b containing one or more phenylalanine residues that will bind TFP but that this domain is different from the hydrophobic domain on calmodulin.	Phenylalanine	104-117	S100 calcium binding protein B	Homo sapiens	75-80	
26927806-7	2016	Coimmunoprecipitation and immunofluorescence analyses showed that ACOT8 Arg(45)-Phe(55) and Arg(86)-Pro(93) regions are involved in Nef association.	Phenylalanine	80-83	S100 calcium binding protein B	Homo sapiens	132-135