PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
14559231-5	2003	These interactions were confirmed by glutathione S-transferase (GST) pull-down assays in which the MH2 domain of Smad 3 fused to GST interacted strongly with in vitro translated, 35S-labeled collagen types I, III, and V. Each collagen also bound to the MH2 domains of Smads 4 and 7 and, to a lesser extent, full-length Smads 1, 2, 3, and 4.	Sulfur-35	179-182	SMAD family member 3	Homo sapiens	113-119