PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2493139-1	1989	Transforming growth factor-beta (TGF-beta) (reviewed in refs 1-3) is a family of molecules that are made up as disulphide-bonded dimers of at least three different types of homologous polypeptides.	disulphide	111-121	transforming growth factor beta 1	Homo sapiens	33-41	
2493139-4	1989	The latent complex from human platelets contains one dimeric TGF-beta 1 molecules, which is noncovalently associated with a disulphide-bonded complex of one dimeric remnant of the precursor and a single molecule of the so-called TGF-beta 1 binding protein (TGF-beta 1-BP).	disulphide	124-134	transforming growth factor beta 1	Homo sapiens	61-71	
2493139-4	1989	The latent complex from human platelets contains one dimeric TGF-beta 1 molecules, which is noncovalently associated with a disulphide-bonded complex of one dimeric remnant of the precursor and a single molecule of the so-called TGF-beta 1 binding protein (TGF-beta 1-BP).	disulphide	124-134	transforming growth factor beta 1	Homo sapiens	229-239	
2493139-4	1989	The latent complex from human platelets contains one dimeric TGF-beta 1 molecules, which is noncovalently associated with a disulphide-bonded complex of one dimeric remnant of the precursor and a single molecule of the so-called TGF-beta 1 binding protein (TGF-beta 1-BP).	disulphide	124-134	transforming growth factor beta 1	Homo sapiens	229-239	
2022183-2	1991	The large latent complex of TGF-beta 1 in platelets is composed of three components, i.e. the mature TGF-beta 1, which is non-covalently associated with a disulphide-bonded complex of the N-terminal remnant of the TGF-beta 1 precursor (TGF-beta 1-latency associated peptide) and the latent TGF-beta 1 binding protein (LTBP).	disulphide	155-165	transforming growth factor beta 1	Homo sapiens	28-38	
14607119-5	2003	Previous studies have revealed that the LTBP-LAP interaction is mediated by intracellular exchange of a single disulphide bond within the third, and only the third, TB domain (TB3) with LAP.	disulphide	111-121	transforming growth factor beta 1	Homo sapiens	45-48	
18214641-2	2008	We decided to study the effect of extracellular matrix degradation and reduction of disulphide bridges reduction on the release of TGF-beta from WJ.	disulphide	84-94	transforming growth factor beta 1	Homo sapiens	131-139	
18214641-7	2008	We conclude that TGF-beta1 is bound through disulphide bonds to an extracellular matrix component of WJ.	disulphide	44-54	transforming growth factor beta 1	Homo sapiens	17-26