PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11707449-3	2002	We found that this defect can be overcome by the appearance of a second mutation substituting the leucine at position 286 in the ef loop of cytochrome b with a phenylalanine.	Phenylalanine	160-173	mitochondrially encoded cytochrome b	Homo sapiens	140-152	
10663786-6	2000	A nucleotide exchange was detected at np14894 replacing an evolutionarily conserved phenylalanine by a leucine in the cytochrome b gene.	Phenylalanine	84-97	mitochondrially encoded cytochrome b	Homo sapiens	118-130	
8866430-8	1996	The second mutation of interest at 14798 is a T to C transition changing a phenylalanine to leucine in a relatively conserved domain of the cytochrome b.	Phenylalanine	75-88	mitochondrially encoded cytochrome b	Homo sapiens	140-152	
1312344-9	1992	We conclude that properties of arginine valine, isoleucine, and phenylalanine side chains within an RGVHFIF-containing domain of gp91-phox contribute significantly to cytochrome b558-mediated activation of the oxidase.	Phenylalanine	64-77	mitochondrially encoded cytochrome b	Homo sapiens	167-179	
2982817-10	1985	Ten minutes after stimulation, PMA, fMet-Leu-Phe, and A23187 induced translocation of 27, 8, and 49%, respectively, of the cytochrome b from the specific granule-rich fraction to the plasma membrane.	Phenylalanine	45-48	mitochondrially encoded cytochrome b	Homo sapiens	123-135