PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1761059-0	1991	Disulfide-bonded dimerization of fibronectin in vitro.	Disulfides	0-9	fibronectin 1	Homo sapiens	33-44	
1761059-4	1991	Low concentrations (less than 1 mM) of Fe3+ enhanced the redimerization of fibronectin, suggesting that metal ions may mediate oxidative reactions in the formation of the disulfides.	Disulfides	171-181	fibronectin 1	Homo sapiens	75-86	
1761059-6	1991	Dimerization of fibronectin took place most effectively at pH greater than or equal to 8.8 but decreased strongly at lower pH, representing more unfavourable conditions for the action of the thiolate anion in the thiol/disulfide exchange reaction.	Disulfides	219-228	fibronectin 1	Homo sapiens	16-27	
1761059-7	1991	Redimerized fibronectin, however, lost many of its binding properties to macromolecular ligands, suggesting that the disulfide bonding did not entirely regenerate the proper conformation of the protein.	Disulfides	117-126	fibronectin 1	Homo sapiens	12-23	
1761059-9	1991	SDS/PAGE analysis of the dialyzed urea-denatured/reduced thrombin and plasmin digests of fibronectin revealed that the NH2-terminal 30-kDa fragment and other fragments that contained intrachain disulfides quantitatively regained their non-reduced electrophoretic mobility.	Disulfides	194-204	fibronectin 1	Homo sapiens	89-100	
1761059-10	1991	The results show that the dimerization and formation of intrachain disulfides of fibronectin may occur, in part, spontaneously, based on the amino acid sequence information of the protein.	Disulfides	67-77	fibronectin 1	Homo sapiens	81-92