PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16156791-6	2005	Functional analysis showed that the deletion of OSH6 led to a significant increase in total cellular ergosterols, whereas OSH6 overexpression caused both a significant decrease in ergosterol levels and resistance to nystatin.	Ergosterol	101-112	oxysterol-binding protein OSH6	Saccharomyces cerevisiae S288C	48-52	
22622083-4	2012	This screen revealed that Osh6, a member of the oxysterol-binding protein family, can complement the vacuole fusion defect of nyv1Delta, but not erg6Delta or vac8Delta, suggesting that Osh6"s function in vacuole fusion is partly dependent on membrane ergosterol and Vac8.	Ergosterol	251-261	oxysterol-binding protein OSH6	Saccharomyces cerevisiae S288C	26-30	
22622083-4	2012	This screen revealed that Osh6, a member of the oxysterol-binding protein family, can complement the vacuole fusion defect of nyv1Delta, but not erg6Delta or vac8Delta, suggesting that Osh6"s function in vacuole fusion is partly dependent on membrane ergosterol and Vac8.	Ergosterol	251-261	oxysterol-binding protein OSH6	Saccharomyces cerevisiae S288C	185-189	
16156791-6	2005	Functional analysis showed that the deletion of OSH6 led to a significant increase in total cellular ergosterols, whereas OSH6 overexpression caused both a significant decrease in ergosterol levels and resistance to nystatin.	Ergosterol	101-111	oxysterol-binding protein OSH6	Saccharomyces cerevisiae S288C	48-52