PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23934150-2	2013	The crystal structure of the N-terminally acetylated BAH domain of Saccharomyces cerevisiae Sir3 bound to the nucleosome core particle reveals that the N-terminal acetylation stabilizes the interaction of Sir3 with the nucleosome.	bis(5-amidino-2-benzimidazolyl)methane ketone hydrate	53-56	chromatin-silencing protein SIR3	Saccharomyces cerevisiae S288C	92-96	
23934152-0	2013	Nalpha-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain.	bis(5-amidino-2-benzimidazolyl)methane ketone hydrate	87-90	chromatin-silencing protein SIR3	Saccharomyces cerevisiae S288C	18-22	
23934150-2	2013	The crystal structure of the N-terminally acetylated BAH domain of Saccharomyces cerevisiae Sir3 bound to the nucleosome core particle reveals that the N-terminal acetylation stabilizes the interaction of Sir3 with the nucleosome.	bis(5-amidino-2-benzimidazolyl)methane ketone hydrate	53-56	chromatin-silencing protein SIR3	Saccharomyces cerevisiae S288C	205-209	
18391024-9	2008	Our results suggest that the BAH domain of Sir3 binds to histone H3K79 and that acetylation of the BAH domain is required for the binding specificity of Sir3 for nucleosomes unmethylated at H3K79.	bis(5-amidino-2-benzimidazolyl)methane ketone hydrate	29-32	chromatin-silencing protein SIR3	Saccharomyces cerevisiae S288C	43-47	
19171939-10	2009	We propose that the functional specialization of Sir3, itself a paralog of Orc1, as a silencing protein was facilitated by the tandem duplication of the OIR domain in the Sir1 family, allowing distinct Sir1-Sir3 and Sir1-Orc1 interactions through OIR-BAH domain interactions.	bis(5-amidino-2-benzimidazolyl)methane ketone hydrate	251-254	chromatin-silencing protein SIR3	Saccharomyces cerevisiae S288C	49-53	
18794362-5	2008	The BAH point mutants, but not the L738P mutant, disrupted the interaction between Sir3 and nucleosomes.	bis(5-amidino-2-benzimidazolyl)methane ketone hydrate	4-7	chromatin-silencing protein SIR3	Saccharomyces cerevisiae S288C	83-87	
18391024-9	2008	Our results suggest that the BAH domain of Sir3 binds to histone H3K79 and that acetylation of the BAH domain is required for the binding specificity of Sir3 for nucleosomes unmethylated at H3K79.	bis(5-amidino-2-benzimidazolyl)methane ketone hydrate	99-102	chromatin-silencing protein SIR3	Saccharomyces cerevisiae S288C	153-157	
16581798-10	2006	This superhelix may be relevant to the function of the BAH domain of Sir3 in silencing.	bis(5-amidino-2-benzimidazolyl)methane ketone hydrate	55-58	chromatin-silencing protein SIR3	Saccharomyces cerevisiae S288C	69-73