PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8881287-4	1996	Use of deletion mutants showed that both activation functions (AF1 and AF2) of PR as well as the coiled coil and His-Cys rich domains of PML were required for transcriptional enhancement.	Histidine	113-116	PML nuclear body scaffold	Homo sapiens	137-140	
8881287-4	1996	Use of deletion mutants showed that both activation functions (AF1 and AF2) of PR as well as the coiled coil and His-Cys rich domains of PML were required for transcriptional enhancement.	Cysteine	117-120	PML nuclear body scaffold	Homo sapiens	137-140	
8881287-5	1996	The fusion protein PML-RAR, which is not localized in nuclear bodies, also enhanced the transactivating activity of PR but this effect was totally suppressed by the administration of retinoic acid.	Tretinoin	183-196	PML nuclear body scaffold	Homo sapiens	19-22	
8881287-5	1996	The fusion protein PML-RAR, which is not localized in nuclear bodies, also enhanced the transactivating activity of PR but this effect was totally suppressed by the administration of retinoic acid.	Tretinoin	183-196	retinoic acid receptor alpha	Homo sapiens	23-26	
8881287-5	1996	The fusion protein PML-RAR, which is not localized in nuclear bodies, also enhanced the transactivating activity of PR but this effect was totally suppressed by the administration of retinoic acid.	Tretinoin	183-196	progesterone receptor	Homo sapiens	116-118	
8881287-7	1996	This mechanism may also play a role in the oncogenic properties of PML-RAR and in their suppression by the retinoic acid.	Tretinoin	107-120	PML-RARA regulated adaptor molecule 1	Homo sapiens	67-74