PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9056263-4	1997	The purified AhR retained in vitro DRE binding activity in the presence of carrier protein and dithiothreitol, and its affinity for the DRE oligonucleotide was equivalent to that of the other receptor preparations (crude and partially purified cytosolic and crude nuclear).	Oligonucleotides	140-155	aryl hydrocarbon receptor	Homo sapiens	13-16	
9056263-5	1997	When the ligand.receptor complex was bound to a DRE oligonucleotide containing BrdU and then UV-irradiated, two proteins in each of the receptor preparations were found to crosslink to BrdU-DRE, and we concluded that they are the AhR monomer and ARNT protein.	Oligonucleotides	52-67	aryl hydrocarbon receptor	Homo sapiens	230-233