PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
20009557-3	2009	Recombinant ACBP4 and ACBP5 proteins were observed to bind oleoyl-CoA ester comparably better than recombinant ACBP6, suggesting that ACBP4 and ACBP5 are promising candidates in the trafficking of oleoyl-CoA from the plastids to the endoplasmic reticulum (ER) for the biosynthesis of non-plastidial membrane lipids.	oleoyl-coenzyme A	59-69	acyl-CoA binding protein 4	Arabidopsis thaliana	12-17	
19121948-9	2009	The transcriptionally light-induced ACBP4 and ACBP5, which encode the two largest forms of Arabidopsis ACBPs, bind oleoyl-CoA esters and likely transfer oleoyl-CoAs from the plastids (the site of de novo fatty acid biosynthesis) to the endoplasmic reticulum for the biosynthesis of non-plastidial membrane lipids in Arabidopsis.	oleoyl-coenzyme A	153-164	acyl-CoA binding protein 4	Arabidopsis thaliana	36-41	
15604682-0	2004	ACBP4 and ACBP5, novel Arabidopsis acyl-CoA-binding proteins with kelch motifs that bind oleoyl-CoA.	oleoyl-coenzyme A	89-99	acyl-CoA binding protein 4	Arabidopsis thaliana	0-5	
15604682-9	2004	Both (His)6-ACBP4 and (His)6-ACBP5 bind [14C]oleoyl-CoA with high affinity, [14C]palmitoyl-CoA with lower affinity and did not bind [14C]arachidonyl-CoA.	oleoyl-coenzyme A	45-55	acyl-CoA binding protein 4	Arabidopsis thaliana	12-17