PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7896089-3	1994	The phenylalanine residues of calmodulin were implicated in function both by structural studies of calmodulin bound to target peptides and by their extraordinary conservation in evolution.	Phenylalanine	4-17	calmodulin	Saccharomyces cerevisiae S288C	30-40	
7896089-3	1994	The phenylalanine residues of calmodulin were implicated in function both by structural studies of calmodulin bound to target peptides and by their extraordinary conservation in evolution.	Phenylalanine	4-17	calmodulin	Saccharomyces cerevisiae S288C	99-109	
7896089-12	1994	The contributions of individual phe-->ala changes to mutant phenotypes support the idea of internal functional redundancy in the symmetrical calmodulin protein molecule.	Phenylalanine	32-35	calmodulin	Saccharomyces cerevisiae S288C	144-154	
7896089-13	1994	These results suggest that the several phenylalanine residues in calmodulin are required to different extents in different combinations in order to carry out each of the several essential tasks.	Phenylalanine	39-52	calmodulin	Saccharomyces cerevisiae S288C	65-75	
8310294-2	1994	Examination of 14 temperature-sensitive yeast mutants bearing one or more phenylalanine to alanine substitutions in the single essential calmodulin gene of yeast (CMD1) revealed diverse essential functions.	Phenylalanine	74-87	calmodulin	Saccharomyces cerevisiae S288C	137-147	
8310294-2	1994	Examination of 14 temperature-sensitive yeast mutants bearing one or more phenylalanine to alanine substitutions in the single essential calmodulin gene of yeast (CMD1) revealed diverse essential functions.	Phenylalanine	74-87	calmodulin	Saccharomyces cerevisiae S288C	163-167	
8310294-5	1994	Phenylalanine residues implicated in calmodulin localization and nuclear division are located in the amino-terminal half of the protein, whereas those implicated in actin organization and bud emergence are located in the carboxyl-terminal half.	Phenylalanine	0-13	calmodulin	Saccharomyces cerevisiae S288C	37-47	
15113827-0	2004	A novel mechanism of intragenic complementation between Phe to Ala calmodulin mutations.	Phenylalanine	56-59	calmodulin	Saccharomyces cerevisiae S288C	67-77	
15113827-2	2004	Previously, we isolated fourteen temperature-sensitive Phe-to-Ala mutations of the CaM-encoding gene CMD1.	Phenylalanine	55-58	calmodulin	Saccharomyces cerevisiae S288C	83-86	
15113827-2	2004	Previously, we isolated fourteen temperature-sensitive Phe-to-Ala mutations of the CaM-encoding gene CMD1.	Phenylalanine	55-58	calmodulin	Saccharomyces cerevisiae S288C	101-105	
12836012-1	2003	The role of calmodulin (CaM) during mating in Saccharomyces cerevisiae was examined by using a set of Phe-to-Ala substitutions.	Phenylalanine	102-105	calmodulin	Saccharomyces cerevisiae S288C	24-27	
8626680-1	1996	Recent studies have shown that substitution of Ala for one or more Phe residues in calmodulin (CaM) imparts a temperature-sensitive phenotype to yeast (Ohya, Y., and Botstein, D. (1994) Science 263, 963-966).	Phenylalanine	67-70	calmodulin	Saccharomyces cerevisiae S288C	83-93	
9756868-0	1998	Importance of phenylalanine residues of yeast calmodulin for target binding and activation.	Phenylalanine	14-27	calmodulin	Saccharomyces cerevisiae S288C	46-56	
9756868-1	1998	Recent genetic studies of yeast calmodulin (yCaM) have shown that alterations of different sets of Phe residues result in distinct functional defects (Ohya, Y., and Botstein, D. (1994) Science 263, 963-966).	Phenylalanine	99-102	calmodulin	Saccharomyces cerevisiae S288C	32-42	
8626680-1	1996	Recent studies have shown that substitution of Ala for one or more Phe residues in calmodulin (CaM) imparts a temperature-sensitive phenotype to yeast (Ohya, Y., and Botstein, D. (1994) Science 263, 963-966).	Phenylalanine	67-70	calmodulin	Saccharomyces cerevisiae S288C	95-98