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