PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7980420-10	1994	It was still a disulphide-linked dimer as judged by SDS/PAGE, indicating that there are alpha-alpha-chain disulphide bonds additional to the Cys-524 linkage in the insulin receptor dimer.	disulphide	15-25	insulin receptor	Homo sapiens	164-180	
16957736-6	2006	The structure reveals the domain arrangement in the disulphide-linked ectodomain dimer, showing that the insulin receptor adopts a folded-over conformation that places the ligand-binding regions in juxtaposition.	disulphide	52-62	insulin receptor	Homo sapiens	105-121	
3017297-1	1986	The insulin receptor is an integral membrane glycoprotein (Mr approximately 300,000) composed of two alpha-subunits (Mr approximately 130,000) and two beta-subunits (Mr approximately 95,000) linked by disulphide bonds.	disulphide	201-211	insulin receptor	Homo sapiens	4-20	
1663881-1	1991	The insulin receptor is a heterotetrameric structure consisting of two alpha-subunits of Mr 135 kilodalton on the outside of the plasma membrane connected by disulphide bonds to beta-subunits of Mr 95 kilodalton which are transmembrane proteins.	disulphide	158-168	insulin receptor	Homo sapiens	4-20	
3552593-2	1987	Two covalent receptor modifications possibly involved in producing pharmacodynamic effects as a result of insulin receptor binding are autophosphorylation and disulphide insulin binding.	disulphide	159-169	insulin receptor	Homo sapiens	106-122