PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 30230185-5 2018 Proinsulin foldability is manifest in the ER, in which the local environment is designed to assist in the overall load of proinsulin folding and to favour its disulphide bond formation (while limiting misfolding), all of which is closely tuned to ER stress response pathways that have complex (beneficial, as well as potentially damaging) effects on pancreatic beta-cells. disulphide 159-169 insulin Homo sapiens 0-10 7735138-4 1995 The double-C-peptide human proinsulin shows a 1.86-fold human C-peptide immune activity as compared with that of human proinsulin and gives a good yield of the molecule with correct disulphide bonds in reconstitution studies strongly suggesting the existence of very flexible conformation of the C-peptide. disulphide 182-192 insulin Homo sapiens 11-20 23227203-0 2012 UV-light exposure of insulin: pharmaceutical implications upon covalent insulin dityrosine dimerization and disulphide bond photolysis. disulphide 108-118 insulin Homo sapiens 21-28 23227203-4 2012 Furthermore, UV-excitation of insulin induces disulphide bridge breakage. disulphide 46-56 insulin Homo sapiens 30-37 23227203-6 2012 In native insulin, the A and B chains are held together by two disulphide bridges. disulphide 63-73 insulin Homo sapiens 10-17 19292763-5 2009 We identified a human leucocyte antigen-DR4-restricted epitope comprising the first 13 amino acids of the insulin A-chain (A1-13), dependent upon generation of a vicinal disulphide bond between adjacent cysteines (A6-A7). disulphide 170-180 insulin Homo sapiens 106-113 12686455-7 2003 A similar treatment of small amounts of purified diglycated proinsulin revealed a fragment with Phe(1)-Glu(13) linked by a disulphide bridge to Gln(70)-Glu(82) containing two glucitol adducts (M(r) 3292.7 Da). disulphide 123-133 insulin Homo sapiens 60-70 11705463-3 2001 It is possible that CPZ causes insulin aggregation by the reduction of disulphide bonds, thereby inactivating insulin and hence causing hyperglycaemia. disulphide 71-81 insulin Homo sapiens 31-38 10493922-0 1999 Intra-A chain disulphide bond forms first during insulin precursor folding. disulphide 14-24 insulin Homo sapiens 49-56 10493922-2 1999 The intra-A chain disulphide bond was found to form early in insulin precursor folding, whereas the corresponding disulphide bond in IGF-I formed late. disulphide 18-28 insulin Homo sapiens 61-68 10493922-7 1999 Time courses of oxidation of reduced insulin A chains, reduced A and B chains, and reduced proinsulins showed that the intra-A chain disulphide bond formed first during insulin precursor folding. disulphide 133-143 insulin Homo sapiens 37-44 10493922-7 1999 Time courses of oxidation of reduced insulin A chains, reduced A and B chains, and reduced proinsulins showed that the intra-A chain disulphide bond formed first during insulin precursor folding. disulphide 133-143 insulin Homo sapiens 94-101 10493922-9 1999 The time course of helix structure formation of insulin A chains also indicated that the intra-A chain disulphide bond formed first, and could stabilize partially folded A chain helix structure. disulphide 103-113 insulin Homo sapiens 48-55 10493922-10 1999 The rate of intra-A chain disulphide bond formation was almost the same as that for both helix structure formation and insulin molecule formation, indicating that the formation of the intra-A chain disulphide bond was the rate limiting step for the folding of insulin precursor. disulphide 26-36 insulin Homo sapiens 260-267 10493922-10 1999 The rate of intra-A chain disulphide bond formation was almost the same as that for both helix structure formation and insulin molecule formation, indicating that the formation of the intra-A chain disulphide bond was the rate limiting step for the folding of insulin precursor. disulphide 198-208 insulin Homo sapiens 119-126 10493922-10 1999 The rate of intra-A chain disulphide bond formation was almost the same as that for both helix structure formation and insulin molecule formation, indicating that the formation of the intra-A chain disulphide bond was the rate limiting step for the folding of insulin precursor. disulphide 198-208 insulin Homo sapiens 260-267 7749917-1 1995 We have determined the structure of a metastable disulphide isomer of human insulin. disulphide 49-59 insulin Homo sapiens 76-83 7735138-4 1995 The double-C-peptide human proinsulin shows a 1.86-fold human C-peptide immune activity as compared with that of human proinsulin and gives a good yield of the molecule with correct disulphide bonds in reconstitution studies strongly suggesting the existence of very flexible conformation of the C-peptide. disulphide 182-192 insulin Homo sapiens 27-37 2676073-1 1989 The insulin molecule contains 51 amino acids; it is made up of two peptide chains linked by disulphide bonds. disulphide 92-102 insulin Homo sapiens 4-11 3242681-3 1988 C6----C48, C47----C52 and C18----C61 assignments have been previously proposed for the three disulphide bonds linking six cysteine residues (C6, C18, C47, C48, C52 and C61), on the basis of analogy (and homology) with proinsulin. disulphide 93-103 insulin Homo sapiens 218-228 3520336-3 1986 Insulin consists of two polypeptide chains (A and B, linked by disulphide bonds) that are derived from the proteolytic cleavage of proinsulin, generating equimolar amounts of the mature insulin and a connecting peptide (C-peptide). disulphide 63-73 insulin Homo sapiens 0-7 2843552-2 1988 As previously reported, these cells synthesize a disulphide-bonded alpha 2 beta 2 tetrameric insulin receptor. disulphide 49-59 insulin Homo sapiens 93-100 3545904-4 1987 Thus, correct disulphide bridges can be established in proinsulin-like molecules devoid of a normal C-peptide region. disulphide 14-24 insulin Homo sapiens 55-65 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 Homo sapiens 106-113 6181016-5 1982 The rationale of the Orcein reaction in B cells seems to depend on the oxidation of disulphide bonds present in insulin and its precursors rich in cystine. disulphide 84-94 insulin Homo sapiens 112-119 4038277-1 1985 The structure of naturally-formed covalent disulphide-linked complexes between insulin and its receptor was examined by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. disulphide 43-53 insulin Homo sapiens 79-86 4038277-7 1985 These findings indicate that disulphide exchange of insulin occurs with the Mr 130000 (alpha) binding subunit within partially reduced species of the native, oligomeric receptor. disulphide 29-39 insulin Homo sapiens 52-59 4038277-8 1985 The degree of disulphide binding of insulin could therefore depend on the relative abundance of partially reduced receptor species and on the redox state of the cell membrane. disulphide 14-24 insulin Homo sapiens 36-43 6347188-3 1983 measurements enable direct observation of the rate of formation of dehydroalanine residues resulting from lysis of the disulphide bonds of insulin and oxidized glutathione in base at pD13. disulphide 119-129 insulin Homo sapiens 139-146 511097-1 1979 We synthesized seventeen analogues of human insulin, applying the principle of stepwise, selective formation of the disulphide bonds. disulphide 116-126 insulin Homo sapiens 44-51 7052070-5 1982 Sephadex G-75 chromatography of the acid-soluble products of insulin digestion by cathepsin D or L suggested that thiols can reduce disulphide bonds in proteins after limited proteolysis. disulphide 132-142 insulin Homo sapiens 61-68 6756616-12 1982 We conclude that the receptors for basic SM and insulin are highly homologous structures, particularly with respect to their glycoprotein nature, their hydrodynamic properties, their disulphide cross-linked composition, and with respect to the size of the major constituent detected by selective affinity labeling. disulphide 183-193 insulin Homo sapiens 48-55 857407-4 1977 The effect of insulin on the hexokinase activity was postulated to occur due to reaction of thiol-disulphide exchange between disulphide group of insulin and free sulfhydryl group of hexokinase. disulphide 98-108 insulin Homo sapiens 14-21 920500-0 1977 Thiolation and disulphide cross-linking of insulin to form macromolecules of potential therapeutic value. disulphide 15-25 insulin Homo sapiens 43-50 920500-1 1977 Macromolecules have been prepared containing native insulin carried by a modified insulin skeleton made by partially thiolating the insulin hexamer and forming intermolecular cross-links through disulphide bridges. disulphide 195-205 insulin Homo sapiens 82-89 920500-1 1977 Macromolecules have been prepared containing native insulin carried by a modified insulin skeleton made by partially thiolating the insulin hexamer and forming intermolecular cross-links through disulphide bridges. disulphide 195-205 insulin Homo sapiens 82-89 34704-0 1979 Disulphide cross-linked macromolecules formed by thiolated insulin and globin. disulphide 0-10 insulin Homo sapiens 59-66 627397-0 1978 Synthesis and biological activity of two disulphide bond isomers of human insulin: [A7-A11,A6-B7-cystine]- and [A6-A7,A11-B7-cystine]insulin (human). disulphide 41-51 insulin Homo sapiens 74-81 627397-0 1978 Synthesis and biological activity of two disulphide bond isomers of human insulin: [A7-A11,A6-B7-cystine]- and [A6-A7,A11-B7-cystine]insulin (human). disulphide 41-51 insulin Homo sapiens 133-140 857407-4 1977 The effect of insulin on the hexokinase activity was postulated to occur due to reaction of thiol-disulphide exchange between disulphide group of insulin and free sulfhydryl group of hexokinase. disulphide 98-108 insulin Homo sapiens 146-153 857407-4 1977 The effect of insulin on the hexokinase activity was postulated to occur due to reaction of thiol-disulphide exchange between disulphide group of insulin and free sulfhydryl group of hexokinase. disulphide 126-136 insulin Homo sapiens 14-21 857407-4 1977 The effect of insulin on the hexokinase activity was postulated to occur due to reaction of thiol-disulphide exchange between disulphide group of insulin and free sulfhydryl group of hexokinase. disulphide 126-136 insulin Homo sapiens 146-153 13808707-0 1960 The reaction of the disulphide groups of insulin with sodium sulphite. disulphide 20-30 insulin Homo sapiens 41-48 14342222-5 1965 Derivatives of the polypeptide B chain of insulin obtained by chemical scission of the interchain disulphide bonds have been separated by conventional techniques. disulphide 98-108 insulin Homo sapiens 42-49 5346365-7 1969 It is suggested that each of the four tyrosyl groups in insulin has a different environment: Tyr-A-14 is fully exposed to the solvent; Tyr-A-19 is sterically influenced by the environmental structure, possibly by the vicinity of a disulphide interchain bond; Tyr-B-16 is embedded into a non-polar area whose stability is virtually independent of the molecular conformation; Tyr-B-26 is probably in a situation similar to Tyr-B-16 with the difference that its non-polar environment depends on the preservation of the native structure. disulphide 231-241 insulin Homo sapiens 56-63 5665887-0 1968 The effect of chemical modifications induced in insulin on the reactivity of the interchain disulphide bonds towards sodium sulphite. disulphide 92-102 insulin Homo sapiens 48-55 5665887-1 1968 The reactivity of the three disulphide bridges of insulin towards sodium sulphite was studied by amperometric titration of the liberated thiol groups. disulphide 28-38 insulin Homo sapiens 50-57 6067894-0 1967 Effect of the insulin iodination on the reactivity of the inter-chain disulphide bonds towards sodium sulphite. disulphide 70-80 insulin Homo sapiens 14-21 5838098-0 1964 The electroreduction of the disulphide bonds of insulin and other proteins. disulphide 28-38 insulin Homo sapiens 48-55 13249947-0 1955 The disulphide bonds of insulin. disulphide 4-14 insulin Homo sapiens 24-31 13198880-0 1954 The disulphide bridges of insulin. disulphide 4-14 insulin Homo sapiens 26-33