PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19435523-0	2009	Chibby forms a homodimer through a heptad repeat of leucine residues in its C-terminal coiled-coil motif.	Leucine	52-59	chibby family member 1, beta catenin antagonist	Homo sapiens	0-6	
19435523-5	2009	Alanine substitutions of two or more of four critical leucine residues within the C-terminal heptad repeats completely eliminate the Cby-Cby interaction.	Alanine	0-7	chibby family member 1, beta catenin antagonist	Homo sapiens	133-136	
19435523-5	2009	Alanine substitutions of two or more of four critical leucine residues within the C-terminal heptad repeats completely eliminate the Cby-Cby interaction.	Alanine	0-7	chibby family member 1, beta catenin antagonist	Homo sapiens	137-140	
19435523-5	2009	Alanine substitutions of two or more of four critical leucine residues within the C-terminal heptad repeats completely eliminate the Cby-Cby interaction.	Leucine	54-61	chibby family member 1, beta catenin antagonist	Homo sapiens	133-136	
19435523-5	2009	Alanine substitutions of two or more of four critical leucine residues within the C-terminal heptad repeats completely eliminate the Cby-Cby interaction.	Leucine	54-61	chibby family member 1, beta catenin antagonist	Homo sapiens	137-140	
19435523-9	2009	CONCLUSION: Our comprehensive mutational analysis of the Cby coiled-coil domain reveals that the four heptad leucine residues play an essential role in mediating Cby homodimerization.	Leucine	109-116	chibby family member 1, beta catenin antagonist	Homo sapiens	57-60	
19435523-9	2009	CONCLUSION: Our comprehensive mutational analysis of the Cby coiled-coil domain reveals that the four heptad leucine residues play an essential role in mediating Cby homodimerization.	Leucine	109-116	chibby family member 1, beta catenin antagonist	Homo sapiens	162-165