PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6321134-2	1984	To assess the relevance of the class of TSH-binding sites characterized by low affinity and high capacity to the stimulation of adenylate cyclase, we studied the interactions of desialylated hCG (as-hCG) and its beta-subunit (as-hCG beta) with human thyroid membranes.	Thyrotropin	40-43	chorionic gonadotropin subunit beta 5	Homo sapiens	191-194	
6321134-2	1984	To assess the relevance of the class of TSH-binding sites characterized by low affinity and high capacity to the stimulation of adenylate cyclase, we studied the interactions of desialylated hCG (as-hCG) and its beta-subunit (as-hCG beta) with human thyroid membranes.	Thyrotropin	40-43	chorionic gonadotropin subunit beta 5	Homo sapiens	199-202	
6321134-3	1984	In low ionic strength buffer, pH 7.8, where both classes of sites are operant, as-hCG fully inhibited and as-hCG beta partially inhibited [125I] bovine (b) TSH binding.	Thyrotropin	156-159	chorionic gonadotropin subunit beta 5	Homo sapiens	109-112	
6321134-9	1984	In contrast, the as-hCG molecule, which interacts with both classes of TSH-binding sites, fully inhibited TSH stimulation of adenylate cyclase.	Thyrotropin	71-74	chorionic gonadotropin subunit beta 5	Homo sapiens	20-23	
6321134-9	1984	In contrast, the as-hCG molecule, which interacts with both classes of TSH-binding sites, fully inhibited TSH stimulation of adenylate cyclase.	Thyrotropin	106-109	chorionic gonadotropin subunit beta 5	Homo sapiens	20-23