PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22746182-1 2012 Insulin-like growth factor 1 (IGF-1) is a 70-residue hormone containing three intramolecular disulfide bridges. Disulfides 93-102 insulin like growth factor 1 Homo sapiens 0-28 29172484-3 2017 Here, we report a new method for the total chemical synthesis of IGF-1 analogs, which entails the solid-phase synthesis of two IGF-1 precursor chains that is followed by the CuI-catalyzed azide-alkyne cycloaddition ligation and by biomimetic formation of a native pattern of disulfides. Disulfides 275-285 insulin like growth factor 1 Homo sapiens 65-70 29172484-3 2017 Here, we report a new method for the total chemical synthesis of IGF-1 analogs, which entails the solid-phase synthesis of two IGF-1 precursor chains that is followed by the CuI-catalyzed azide-alkyne cycloaddition ligation and by biomimetic formation of a native pattern of disulfides. Disulfides 275-285 insulin like growth factor 1 Homo sapiens 127-132 29172484-5 2017 These new synthetic IGF-1 analogs are unique examples of disulfide bonds" rich proteins with intra main-chain triazole links. Disulfides 57-66 insulin like growth factor 1 Homo sapiens 20-25 26339260-1 2014 Human Insulin-like growth factor 1 (hIGF-1) consists of 70 amino acids in a single chain with three intermolecular disulfide bridges possessing valuable therapeutic effects. Disulfides 115-124 insulin like growth factor 1 Homo sapiens 36-42 22746182-1 2012 Insulin-like growth factor 1 (IGF-1) is a 70-residue hormone containing three intramolecular disulfide bridges. Disulfides 93-102 insulin like growth factor 1 Homo sapiens 30-35 16864583-1 2006 Oxidative folding of insulin-like growth factor I (IGF-I) and single-chain insulin analogs proceeds via one- and two-disulfide intermediates. Disulfides 117-126 insulin like growth factor 1 Homo sapiens 21-49 19959476-9 2010 Whereas wild-type IGF-I undergoes thiol-catalyzed disulfide exchange to yield IGF-swap, His(B5)-IGF-I retains canonical pairing. Disulfides 50-59 insulin like growth factor 1 Homo sapiens 18-23 17922544-0 2007 Insulin receptor substrate 1 knockdown in human MCF7 ER+ breast cancer cells by nuclease-resistant IRS1 siRNA conjugated to a disulfide-bridged D-peptide analogue of insulin-like growth factor 1. Disulfides 126-135 insulin like growth factor 1 Homo sapiens 166-194 16864583-1 2006 Oxidative folding of insulin-like growth factor I (IGF-I) and single-chain insulin analogs proceeds via one- and two-disulfide intermediates. Disulfides 117-126 insulin like growth factor 1 Homo sapiens 51-56 16864583-2 2006 A predominant one-disulfide intermediate in each case contains the canonical A20-B19 disulfide bridge (cystines 18-61 in IGF-I and 19-85 in human proinsulin). Disulfides 18-27 insulin like growth factor 1 Homo sapiens 121-126 16864583-2 2006 A predominant one-disulfide intermediate in each case contains the canonical A20-B19 disulfide bridge (cystines 18-61 in IGF-I and 19-85 in human proinsulin). Disulfides 85-94 insulin like growth factor 1 Homo sapiens 121-126 10422834-1 1999 Insulin-like growth factor (IGF-1) contains three disulfide bonds. Disulfides 50-59 insulin like growth factor 1 Homo sapiens 28-33 15567151-0 2005 1.42A crystal structure of mini-IGF-1(2): an analysis of the disulfide isomerization property and receptor binding property of IGF-1 based on the three-dimensional structure. Disulfides 61-70 insulin like growth factor 1 Homo sapiens 32-37 15567151-1 2005 Insulin and insulin-like growth factor 1 (IGF-1) share a homologous sequence, a similar three-dimensional structure and weakly overlapping biological activity, but IGF-1 folds into two thermodynamically stable disulfide isomers, while insulin folds into one unique stable tertiary structure. Disulfides 210-219 insulin like growth factor 1 Homo sapiens 12-40 15567151-1 2005 Insulin and insulin-like growth factor 1 (IGF-1) share a homologous sequence, a similar three-dimensional structure and weakly overlapping biological activity, but IGF-1 folds into two thermodynamically stable disulfide isomers, while insulin folds into one unique stable tertiary structure. Disulfides 210-219 insulin like growth factor 1 Homo sapiens 42-47 15567151-1 2005 Insulin and insulin-like growth factor 1 (IGF-1) share a homologous sequence, a similar three-dimensional structure and weakly overlapping biological activity, but IGF-1 folds into two thermodynamically stable disulfide isomers, while insulin folds into one unique stable tertiary structure. Disulfides 210-219 insulin like growth factor 1 Homo sapiens 164-169 15567151-3 2005 In this study, the crystal structure of mini-IGF-1(2), a disulfide isomer of an artificial analog of IGF-1, was solved by the SAD/SIRAS method using our in-house X-ray source. Disulfides 57-66 insulin like growth factor 1 Homo sapiens 45-50 15567151-3 2005 In this study, the crystal structure of mini-IGF-1(2), a disulfide isomer of an artificial analog of IGF-1, was solved by the SAD/SIRAS method using our in-house X-ray source. Disulfides 57-66 insulin like growth factor 1 Homo sapiens 101-106 15567151-5 2005 Furthermore, based on the structural comparison of IGF-1 and insulin, a new assumption was made that in insulin the several hydrogen bonds formed between the N-terminal region of the B-chain and the intra-A-chain disulfide region of the A-chain are the main reason for the stability of the intra-A-chain disulfide bond and for the prevention of disulfide isomerization, while Phe B1 and His B5 are very important for the formation of these hydrogen bonds. Disulfides 213-222 insulin like growth factor 1 Homo sapiens 51-56 15567151-5 2005 Furthermore, based on the structural comparison of IGF-1 and insulin, a new assumption was made that in insulin the several hydrogen bonds formed between the N-terminal region of the B-chain and the intra-A-chain disulfide region of the A-chain are the main reason for the stability of the intra-A-chain disulfide bond and for the prevention of disulfide isomerization, while Phe B1 and His B5 are very important for the formation of these hydrogen bonds. Disulfides 304-313 insulin like growth factor 1 Homo sapiens 51-56 15567151-5 2005 Furthermore, based on the structural comparison of IGF-1 and insulin, a new assumption was made that in insulin the several hydrogen bonds formed between the N-terminal region of the B-chain and the intra-A-chain disulfide region of the A-chain are the main reason for the stability of the intra-A-chain disulfide bond and for the prevention of disulfide isomerization, while Phe B1 and His B5 are very important for the formation of these hydrogen bonds. Disulfides 304-313 insulin like growth factor 1 Homo sapiens 51-56 18759047-3 2002 However, their folding behavior is different: insulin and its recombinant precursor (PIP) fold into one unique tertiary structure, while IGF-1 folds into two disulfides isomers with similar thermodynamic stability. Disulfides 158-168 insulin like growth factor 1 Homo sapiens 137-142 11083061-0 2000 Three-dimensional solution structure of a disulfide bond isomer of the human insulin-like growth factor-I. Disulfides 42-51 insulin like growth factor 1 Homo sapiens 77-105 11083061-1 2000 The solution structure of a disulfide bond isomer of human insulin-like growth factor-I (IGF-I) was determined using homonuclear NMR methods. Disulfides 28-37 insulin like growth factor 1 Homo sapiens 59-87 11083061-1 2000 The solution structure of a disulfide bond isomer of human insulin-like growth factor-I (IGF-I) was determined using homonuclear NMR methods. Disulfides 28-37 insulin like growth factor 1 Homo sapiens 89-94 11083061-9 2000 Comparison of the biological activities of native and the disulfide bond isomer of human IGF-I highlight the importance of Tyr24, Phe25, Phe49-Cys52 and Phe16 in binding to the IGF-I receptor or specific IGFBPs. Disulfides 58-67 insulin like growth factor 1 Homo sapiens 89-94 10993229-0 2000 Direct identification of a novel disulfide bond linkage system of new isolated isomer (isomer V) in recombinantly produced h-IGF-I. Disulfides 33-42 insulin like growth factor 1 Homo sapiens 125-130 10993229-1 2000 Insulin-like growth factor I (IGF-I or somatomedin C) is a serum polypeptide with three intramolecular disulfide bonds. Disulfides 103-112 insulin like growth factor 1 Homo sapiens 0-28 10993229-1 2000 Insulin-like growth factor I (IGF-I or somatomedin C) is a serum polypeptide with three intramolecular disulfide bonds. Disulfides 103-112 insulin like growth factor 1 Homo sapiens 30-35 10993229-1 2000 Insulin-like growth factor I (IGF-I or somatomedin C) is a serum polypeptide with three intramolecular disulfide bonds. Disulfides 103-112 insulin like growth factor 1 Homo sapiens 39-52 10608814-0 1999 Probing the folding pathways of long R(3) insulin-like growth factor-I (LR(3)IGF-I) and IGF-I via capture and identification of disulfide intermediates by cyanylation methodology and mass spectrometry. Disulfides 128-137 insulin like growth factor 1 Homo sapiens 77-82 10608814-0 1999 Probing the folding pathways of long R(3) insulin-like growth factor-I (LR(3)IGF-I) and IGF-I via capture and identification of disulfide intermediates by cyanylation methodology and mass spectrometry. Disulfides 128-137 insulin like growth factor 1 Homo sapiens 88-93 10608814-5 1999 Folding pathways of IGF-I and LR(3)IGF-I are proposed based on the time-dependent distribution and disulfide structure of the corresponding trapped intermediates. Disulfides 99-108 insulin like growth factor 1 Homo sapiens 20-25 10608814-5 1999 Folding pathways of IGF-I and LR(3)IGF-I are proposed based on the time-dependent distribution and disulfide structure of the corresponding trapped intermediates. Disulfides 99-108 insulin like growth factor 1 Homo sapiens 35-40 16894147-7 2006 This module, which governs IGF1-binding specificity, shows negligible sequence identity, significantly more alpha-helix, an additional disulfide bond, and opposite electrostatic potential compared to that of the IGF1R. Disulfides 135-144 insulin like growth factor 1 Homo sapiens 27-31 12186542-0 2002 The different energetic state of the intra A-chain/domain disulfide of insulin and insulin-like growth factor 1 is mainly controlled by their B-chain/domain. Disulfides 58-67 insulin like growth factor 1 Homo sapiens 83-111 12186542-1 2002 Insulin and insulin-like growth factor 1 (IGF-1) share homologous sequence, similar three-dimensional structure, and weakly overlapping biological activity, but different folding information is stored in their homologous sequences: the sequence of insulin encodes one unique thermodynamically stable three-dimensional structure while that of IGF-1 encodes two disulfide isomers with different three-dimensional structure but similar thermodynamic stability. Disulfides 360-369 insulin like growth factor 1 Homo sapiens 12-40 12186542-1 2002 Insulin and insulin-like growth factor 1 (IGF-1) share homologous sequence, similar three-dimensional structure, and weakly overlapping biological activity, but different folding information is stored in their homologous sequences: the sequence of insulin encodes one unique thermodynamically stable three-dimensional structure while that of IGF-1 encodes two disulfide isomers with different three-dimensional structure but similar thermodynamic stability. Disulfides 360-369 insulin like growth factor 1 Homo sapiens 42-47 12186542-2 2002 Their different folding behavior probably resulted from the different energetic state of the intra A-chain/domain disulfide: the intra A-chain disulfide of insulin is a stable bond while that of IGF-1 is a strained bond with high energy. Disulfides 114-123 insulin like growth factor 1 Homo sapiens 195-200 12186542-2 2002 Their different folding behavior probably resulted from the different energetic state of the intra A-chain/domain disulfide: the intra A-chain disulfide of insulin is a stable bond while that of IGF-1 is a strained bond with high energy. Disulfides 143-152 insulin like growth factor 1 Homo sapiens 195-200 12186542-8 2002 One major equilibrium intermediate with two disulfides of Ins(A)/IGF-1(B) was purified and characterized. Disulfides 44-54 insulin like growth factor 1 Homo sapiens 65-70 12186542-10 2002 Our present results suggested that the energetic state of the intra A-chain/domain disulfide of insulin and IGF-1 was not controlled by the A-chain/domain sequence close to this disulfide but was mainly controlled by the sequence of the B-chain/domain. Disulfides 83-92 insulin like growth factor 1 Homo sapiens 108-113 12186542-10 2002 Our present results suggested that the energetic state of the intra A-chain/domain disulfide of insulin and IGF-1 was not controlled by the A-chain/domain sequence close to this disulfide but was mainly controlled by the sequence of the B-chain/domain. Disulfides 178-187 insulin like growth factor 1 Homo sapiens 108-113 11814349-1 2002 Although insulin and insulin-like growth factor 1 (IGF-1) share homologous sequence, similar tertiary structure, weakly overlapped biological activity, and a common ancestor, the two highly homologous sequences encode different folding behavior: insulin folds into one unique stable tertiary structure while IGF-1 folds into two disulfide isomers with similar thermodynamic stability. Disulfides 329-338 insulin like growth factor 1 Homo sapiens 51-56 11814349-3 2002 Both mini-IGF-1 and Ins(A)/IGF-1(B) fold into two thermodynamically stable disulfide isomers in vivo and in vitro just like that of IGF-1, while Ins(B)/IGF-1(A) folds into one unique thermodynamically stable tertiary structure in vivo and in vitro just like that of insulin. Disulfides 75-84 insulin like growth factor 1 Homo sapiens 10-15 11814349-3 2002 Both mini-IGF-1 and Ins(A)/IGF-1(B) fold into two thermodynamically stable disulfide isomers in vivo and in vitro just like that of IGF-1, while Ins(B)/IGF-1(A) folds into one unique thermodynamically stable tertiary structure in vivo and in vitro just like that of insulin. Disulfides 75-84 insulin like growth factor 1 Homo sapiens 27-32 11814349-3 2002 Both mini-IGF-1 and Ins(A)/IGF-1(B) fold into two thermodynamically stable disulfide isomers in vivo and in vitro just like that of IGF-1, while Ins(B)/IGF-1(A) folds into one unique thermodynamically stable tertiary structure in vivo and in vitro just like that of insulin. Disulfides 75-84 insulin like growth factor 1 Homo sapiens 27-32 11814349-3 2002 Both mini-IGF-1 and Ins(A)/IGF-1(B) fold into two thermodynamically stable disulfide isomers in vivo and in vitro just like that of IGF-1, while Ins(B)/IGF-1(A) folds into one unique thermodynamically stable tertiary structure in vivo and in vitro just like that of insulin. Disulfides 75-84 insulin like growth factor 1 Homo sapiens 27-32 10422834-2 1999 In the presence of denaturant and thiol catalyst, IGF-1 shuffles its native disulfide bonds and denatures to form a mixture of scrambled isomers. Disulfides 76-85 insulin like growth factor 1 Homo sapiens 50-55 9951525-0 1999 Probing the disulfide folding pathway of insulin-like growth factor-I. Disulfides 12-21 insulin like growth factor 1 Homo sapiens 41-69 9951525-2 1999 This problem is exemplified by insulin-like growth factor (IGF)-I which when refolded in vitro produces the native three-disulfide structure, an alternative structure with mispaired disulfide bonds and other isomeric forms. Disulfides 121-130 insulin like growth factor 1 Homo sapiens 31-65 9951525-6 1999 In addition to non-native intermediates, three native-like intermediates were identified, that appear to have a major role in the in vitro refolding pathway of Long-[Arg3]IGF-I; a single-disulfide Cys18-Cys61 intermediate, an intermediate with Cys18-Cys61 and Cys6-Cys48 disulfide bonds and another with Cys18-Cys61 and Cys47-Cys52 disulfide bonds. Disulfides 187-196 insulin like growth factor 1 Homo sapiens 171-176 9951525-6 1999 In addition to non-native intermediates, three native-like intermediates were identified, that appear to have a major role in the in vitro refolding pathway of Long-[Arg3]IGF-I; a single-disulfide Cys18-Cys61 intermediate, an intermediate with Cys18-Cys61 and Cys6-Cys48 disulfide bonds and another with Cys18-Cys61 and Cys47-Cys52 disulfide bonds. Disulfides 271-280 insulin like growth factor 1 Homo sapiens 171-176 9951525-6 1999 In addition to non-native intermediates, three native-like intermediates were identified, that appear to have a major role in the in vitro refolding pathway of Long-[Arg3]IGF-I; a single-disulfide Cys18-Cys61 intermediate, an intermediate with Cys18-Cys61 and Cys6-Cys48 disulfide bonds and another with Cys18-Cys61 and Cys47-Cys52 disulfide bonds. Disulfides 271-280 insulin like growth factor 1 Homo sapiens 171-176 8662901-8 1996 Swapping of the disulfide bridges in IGF-I and the C-region mutants decreased the affinity dramatically for IGFBP-3, primarily by decreasing the association rate. Disulfides 16-25 insulin like growth factor 1 Homo sapiens 37-42 10025946-0 1999 Insulin-like growth factors I and II are unable to form and maintain their native disulfides under in vivo redox conditions. Disulfides 82-92 insulin like growth factor 1 Homo sapiens 0-36 10025946-1 1999 Insulin-like growth factor (IGF) I does not quantitatively form its three native disulfide bonds in the presence of 10 mM reduced and 1 mM oxidized glutathione in vitro [Hober, S. et al. Disulfides 81-90 insulin like growth factor 1 Homo sapiens 0-34 10025946-4 1999 The results indicate that the previously described thermodynamic disulfide exchange folding problem of IGF-I in vitro is also present in vivo. Disulfides 65-74 insulin like growth factor 1 Homo sapiens 103-108 10025946-5 1999 Speculatively, we suggest that the thermodynamic disulfide exchange properties of IGF-I and II are biologically significant for inactivation of the unbound growth factors by disulfide exchange reactions to generate variants destined for rapid clearance. Disulfides 49-58 insulin like growth factor 1 Homo sapiens 82-87 10025946-5 1999 Speculatively, we suggest that the thermodynamic disulfide exchange properties of IGF-I and II are biologically significant for inactivation of the unbound growth factors by disulfide exchange reactions to generate variants destined for rapid clearance. Disulfides 174-183 insulin like growth factor 1 Homo sapiens 82-87 9294820-15 1997 Human IGF-I appears to dimerize covalently by both disulfide scrambling and by a radical-promoted nondisulfide pathway. Disulfides 51-60 insulin like growth factor 1 Homo sapiens 6-11 9186491-1 1997 Insulin-like growth factor-I (IGF-I) has three disulfide bonds and refolding of the fully reduced molecule generates varying ratios of correctly (PII) and incorrectly (PI) folded forms via several intermediates. Disulfides 47-56 insulin like growth factor 1 Homo sapiens 0-28 9186491-1 1997 Insulin-like growth factor-I (IGF-I) has three disulfide bonds and refolding of the fully reduced molecule generates varying ratios of correctly (PII) and incorrectly (PI) folded forms via several intermediates. Disulfides 47-56 insulin like growth factor 1 Homo sapiens 30-35 9186491-7 1997 It was concluded from these results that the intermediate forms of IGF-1 can rapidly reshuffle between different disulfide structures, and that formation of the last disulfide bond is not as favorable a process as the conversion to other intermediates. Disulfides 113-122 insulin like growth factor 1 Homo sapiens 67-72 9109671-0 1997 Disulfide exchange folding of disulfide mutants of insulin-like growth factor I in vitro. Disulfides 0-9 insulin like growth factor 1 Homo sapiens 51-79 9109671-0 1997 Disulfide exchange folding of disulfide mutants of insulin-like growth factor I in vitro. Disulfides 30-39 insulin like growth factor 1 Homo sapiens 51-79 9109671-1 1997 We have previously concluded that insulin-like growth factor-I (IGF-I) is thermodynamically unable to quantitatively form its disulfide bonds under reversible redox conditions in vitro. Disulfides 126-135 insulin like growth factor 1 Homo sapiens 64-69 9109671-2 1997 From detailed analyses it was hypothesized that the 47-52 disulfide is energetically unfavorable in the native IGF-I structure [Hober et al. Disulfides 58-67 insulin like growth factor 1 Homo sapiens 111-116 9109671-4 1997 In this paper, this hypothesis has been tested by refolding of IGF-I mutant proteins lacking either the 47-52 or 6-48 disulfide bond. Disulfides 118-127 insulin like growth factor 1 Homo sapiens 63-68 9109671-5 1997 The disulfide exchange folding equilibrium behavior of these mutated IGF-I variants were examined in a glutathione redox buffer. Disulfides 4-13 insulin like growth factor 1 Homo sapiens 69-74 9109671-6 1997 The mutant protein IGF-I(C47A,C52A) was demonstrated to form both remaining native disulfide bonds. Disulfides 83-92 insulin like growth factor 1 Homo sapiens 19-24 9109671-7 1997 In contrast, IGF-I(C6A,C48A) was unable to quantitatively form both of its disulfides and was shown to accumulate a one disulfide variant lacking the 47-52 disulfide bond. Disulfides 75-85 insulin like growth factor 1 Homo sapiens 13-18 9109671-7 1997 In contrast, IGF-I(C6A,C48A) was unable to quantitatively form both of its disulfides and was shown to accumulate a one disulfide variant lacking the 47-52 disulfide bond. Disulfides 75-84 insulin like growth factor 1 Homo sapiens 13-18 9109671-7 1997 In contrast, IGF-I(C6A,C48A) was unable to quantitatively form both of its disulfides and was shown to accumulate a one disulfide variant lacking the 47-52 disulfide bond. Disulfides 120-129 insulin like growth factor 1 Homo sapiens 13-18 9109671-8 1997 These folding data corroborate the hypothesis that the 47-52 disulfide bond of IGF-I is energetically unfavorable also in the absence of the 6-48 disulfide bond. Disulfides 61-70 insulin like growth factor 1 Homo sapiens 79-84 9109671-9 1997 The two IGF-I variants were purified in oxidized forms where both native disulfides are formed. Disulfides 73-83 insulin like growth factor 1 Homo sapiens 8-13 9109671-11 1997 Further, binding affinities to the IGF binding protein 1 and a soluble IGF type I receptor, respectively, were severely lowered in both disulfide mutant proteins compared to the native IGF-I molecule. Disulfides 136-145 insulin like growth factor 1 Homo sapiens 185-190 9109671-13 1997 Thus, the structural changes due to removal of the 6-48 or 47-52 disulfide bonds, respectively, yield structural changes in different regions of the IGF-I molecule reflected in the different binding activities. Disulfides 65-74 insulin like growth factor 1 Homo sapiens 149-154 7794252-4 1995 Most of the recombinant IGF1 molecules, secreted from yeast, are a conglomeration of inactive multimers which are either disulfide-linked or mere physical aggregates. Disulfides 121-130 insulin like growth factor 1 Homo sapiens 24-28 1483466-7 1992 The mature IGF-1, which is secreted from the intracellular pool of precursor proteins, is predominantly an active, monomeric molecule, corroborating observations that early removal of the pro region before folding in the ER helps to prevent aberrant intermolecular disulfide-bond formation in IGF-1. Disulfides 265-274 insulin like growth factor 1 Homo sapiens 11-16 8257688-3 1993 The molecular size of the nonreduced hybrid receptor was approximately 350K, indicating that the IGF-I and insulin receptor alpha beta halves were disulfide-linked. Disulfides 147-156 insulin like growth factor 1 Homo sapiens 97-102 8397784-0 1993 Mutation of Arg55/56 to Leu55/Ala56 in insulin-like growth factor-I results in two forms different in disulfide structure and native conformation but similar under reverse-phase conditions. Disulfides 102-111 insulin like growth factor 1 Homo sapiens 39-67 7515683-1 1994 Insulin-like growth factor I (IGF-I) is thermodynamically unable to quantitatively form its native disulfides under reversible redox conditions in vitro [Hober et al. Disulfides 99-109 insulin like growth factor 1 Homo sapiens 0-28 7515683-1 1994 Insulin-like growth factor I (IGF-I) is thermodynamically unable to quantitatively form its native disulfides under reversible redox conditions in vitro [Hober et al. Disulfides 99-109 insulin like growth factor 1 Homo sapiens 30-35 7515683-5 1994 However, correct disulfide bonds are formed very efficiently when insulin-like growth factor binding protein 1 is added in equimolar amounts to IGF-I to the refolding mixture. Disulfides 17-26 insulin like growth factor 1 Homo sapiens 144-149 7515683-6 1994 On the basis of these results, we propose that one important function of at least one of the six homologous insulin-like growth factor binding proteins is to assist in the formation and maintenance of the native disulfides of IGF-I. Disulfides 212-222 insulin like growth factor 1 Homo sapiens 226-231 8494897-3 1993 This observation is of particular interest in light of the recent demonstration that two of the three disulfide bonds in native IGF-1 rearrange in the presence of dithiothreitol [Hober, S., et al. Disulfides 102-111 insulin like growth factor 1 Homo sapiens 128-133 8494898-0 1993 Role of native disulfide bonds in the structure and activity of insulin-like growth factor 1: genetic models of protein-folding intermediates. Disulfides 15-24 insulin like growth factor 1 Homo sapiens 64-92 8494898-2 1993 Here we examine the role of these disulfide bonds in the folding and function of one family member, human insulin-like growth factor 1 (IGF-1). Disulfides 34-43 insulin like growth factor 1 Homo sapiens 106-134 8494898-2 1993 Here we examine the role of these disulfide bonds in the folding and function of one family member, human insulin-like growth factor 1 (IGF-1). Disulfides 34-43 insulin like growth factor 1 Homo sapiens 136-141 8494898-4 1993 An analogue lacking all three disulfide bonds (designated des-Cys-IGF-1) is inactive and unfolded. Disulfides 30-39 insulin like growth factor 1 Homo sapiens 66-71 1618297-0 1992 A modified Kex2 enzyme retained in the endoplasmic reticulum prevents disulfide-linked dimerisation of recombinant human insulin-like growth factor-1 secreted from yeast. Disulfides 70-79 insulin like growth factor 1 Homo sapiens 121-149 1606975-0 1992 Disulfide arrangement of human insulin-like growth factor I derived from yeast and plasma. Disulfides 0-9 insulin like growth factor 1 Homo sapiens 31-59 1606975-1 1992 The disulfide arrangement of yeast derived human insulin-like growth factor I (yIGF-I) was determined using a combination of Staphylococcus aureus V8 protease mapping, fast-atom-bombardment mass spectrometry as well as amino acid sequence and composition analysis. Disulfides 4-13 insulin like growth factor 1 Homo sapiens 49-77 1606975-3 1992 IGF-I isolated from human plasma (pIGF-I) was found to have an identical disulfide configuration. Disulfides 73-82 insulin like growth factor 1 Homo sapiens 0-5 1606975-4 1992 A yeast-derived isomeric form of IGF-I (yisoIGF-I) exhibited an altered disulfide arrangement: Cys6-Cys47, Cys48-Cys52 and Cys18-Cys61. Disulfides 72-81 insulin like growth factor 1 Homo sapiens 33-38 1606975-7 1992 The data demonstrate the importance of correct disulfide arrangement in IGF-I for full biological activity. Disulfides 47-56 insulin like growth factor 1 Homo sapiens 72-77 1618297-1 1992 The majority of the recombinant human insulin-like growth factor-1 (IGF1) molecules, secreted from yeast using the prepro sequence of the prepro-alpha-factor, are not active monomers but inactive, disulfide-linked dimers. Disulfides 197-206 insulin like growth factor 1 Homo sapiens 38-66 1618297-1 1992 The majority of the recombinant human insulin-like growth factor-1 (IGF1) molecules, secreted from yeast using the prepro sequence of the prepro-alpha-factor, are not active monomers but inactive, disulfide-linked dimers. Disulfides 197-206 insulin like growth factor 1 Homo sapiens 68-72 1618297-5 1992 We find that co-expression of a novel ER-retained Kex2p variant, soluble Kex2pHDEL, can prevent intermolecular disulfide bond formation between two IGF1 molecules, implying that the presence of the proregion during the folding of IGF1 in the ER could be a reason for disulfide-linked dimerisation. Disulfides 111-120 insulin like growth factor 1 Homo sapiens 148-152 1756863-0 1991 A Lys27-to-Glu27 mutation in the human insulin-like growth factor-1 prevents disulfide linked dimerization and allows secretion of BiP when expressed in yeast. Disulfides 77-86 insulin like growth factor 1 Homo sapiens 39-67 1737028-0 1992 Disulfide exchange folding of insulin-like growth factor I. Disulfides 0-9 insulin like growth factor 1 Homo sapiens 30-58 1737028-1 1992 The disulfide exchange folding properties of insulin-like growth factor I (IGF-I) have been analyzed in a redox buffer containing reduced (10 mM) and oxidized (1 mM) glutathione. Disulfides 4-13 insulin like growth factor 1 Homo sapiens 45-73 1737028-1 1992 The disulfide exchange folding properties of insulin-like growth factor I (IGF-I) have been analyzed in a redox buffer containing reduced (10 mM) and oxidized (1 mM) glutathione. Disulfides 4-13 insulin like growth factor 1 Homo sapiens 75-80 1737028-3 1992 Instead, five major forms of IGF-I were detected, and these components were concluded to be in equilibrium as their relative amounts were similar starting from either reduced, native, or a mismatched variant of IGF-I containing two non-native disulfides. Disulfides 243-253 insulin like growth factor 1 Homo sapiens 29-34 1737028-10 1992 On the basis of the disulfide bond patterns of the different components in the equilibrium mixtures, we conclude that the disulfide between cysteines-47 and -52 in IGF-I is an unfavorable high-energy bond that may exist in the native molecule in a strained configuration. Disulfides 20-29 insulin like growth factor 1 Homo sapiens 164-169 1737028-10 1992 On the basis of the disulfide bond patterns of the different components in the equilibrium mixtures, we conclude that the disulfide between cysteines-47 and -52 in IGF-I is an unfavorable high-energy bond that may exist in the native molecule in a strained configuration. Disulfides 122-131 insulin like growth factor 1 Homo sapiens 164-169 1320041-1 1992 Insulin and IGF-I receptors are homologous disulfide linked alpha 2 beta 2 tetramers. Disulfides 43-52 insulin like growth factor 1 Homo sapiens 12-17 1756863-2 1991 A majority of the IGF1-like molecules are disulfide bonded dimers. Disulfides 42-51 insulin like growth factor 1 Homo sapiens 18-22 1756863-5 1991 These results imply that by preventing ionic interactions between two IGF1 molecules, intermolecular disulfide bonds do not form in yeast, and that in the mutant there is a structural change which induces BiP, allowing its secretion. Disulfides 101-110 insulin like growth factor 1 Homo sapiens 70-74 1888034-6 1991 It was also observed that the digestion of insulin-like growth factor I with V8 protease normally yields two peptides V4(13-20) and V9(59-70) linked by a disulfide bridge. Disulfides 154-163 insulin like growth factor 1 Homo sapiens 43-71 2050146-5 1991 HPLC analysis of secreted IGFI revealed the presence of the correctly folded, genuine molecule as well as an isomeric byproduct of equal molecular mass but with two of the three disulfide bonds interchanged. Disulfides 178-187 insulin like growth factor 1 Homo sapiens 26-30 2201313-1 1990 We report the synthesis and biological evaluation of a two-chain, disulfide-linked, insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to the A- and D- domains of human insulin-like growth factor-I (IGF-I) in which the A-domain amino-acid residues -Phe49-Arg50-Ser51-found in IGF-I have been replaced by -Ala-Gly-Val-, the homologous region of sheep insulin. Disulfides 66-75 insulin like growth factor 1 Homo sapiens 213-241 2201313-1 1990 We report the synthesis and biological evaluation of a two-chain, disulfide-linked, insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to the A- and D- domains of human insulin-like growth factor-I (IGF-I) in which the A-domain amino-acid residues -Phe49-Arg50-Ser51-found in IGF-I have been replaced by -Ala-Gly-Val-, the homologous region of sheep insulin. Disulfides 66-75 insulin like growth factor 1 Homo sapiens 243-248 2201313-1 1990 We report the synthesis and biological evaluation of a two-chain, disulfide-linked, insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to the A- and D- domains of human insulin-like growth factor-I (IGF-I) in which the A-domain amino-acid residues -Phe49-Arg50-Ser51-found in IGF-I have been replaced by -Ala-Gly-Val-, the homologous region of sheep insulin. Disulfides 66-75 insulin like growth factor 1 Homo sapiens 320-325 2611257-9 1989 However, IAN treatment of the alpha beta heterodimeric IGF-1 receptors inhibited the IGF-1-dependent covalent formation of the disulfide-linked alpha 2 beta 2 heterotetrameric complex. Disulfides 127-136 insulin like growth factor 1 Homo sapiens 55-60 2611257-9 1989 However, IAN treatment of the alpha beta heterodimeric IGF-1 receptors inhibited the IGF-1-dependent covalent formation of the disulfide-linked alpha 2 beta 2 heterotetrameric complex. Disulfides 127-136 insulin like growth factor 1 Homo sapiens 85-90 2611257-10 1989 These data indicate that IGF-1 induces the covalent association of isolated alpha beta heterodimeric IGF-1 receptor complexes into a disulfide-linked alpha 2 beta 2 heterotetrameric state whereas Mn/MgATP induces a noncovalent association. Disulfides 133-142 insulin like growth factor 1 Homo sapiens 25-30 2611257-10 1989 These data indicate that IGF-1 induces the covalent association of isolated alpha beta heterodimeric IGF-1 receptor complexes into a disulfide-linked alpha 2 beta 2 heterotetrameric state whereas Mn/MgATP induces a noncovalent association. Disulfides 133-142 insulin like growth factor 1 Homo sapiens 101-106 3056519-1 1988 A two-chain, disulfide linked, insulin-like compound embodying the A-domain of insulin-like growth factor I (IGF-I) and the B-chain of insulin has been synthesized and characterized with respect to insulin-like biological activity and growth-promoting potency. Disulfides 13-22 insulin like growth factor 1 Homo sapiens 79-107 3056519-1 1988 A two-chain, disulfide linked, insulin-like compound embodying the A-domain of insulin-like growth factor I (IGF-I) and the B-chain of insulin has been synthesized and characterized with respect to insulin-like biological activity and growth-promoting potency. Disulfides 13-22 insulin like growth factor 1 Homo sapiens 109-114 6572973-1 1983 Human insulin-like growth factor I (somatomedin C) with 70 amino acid residues and three disulfide bridges has been synthesized by the solid-phase method. Disulfides 89-98 insulin like growth factor 1 Homo sapiens 6-34 6572973-1 1983 Human insulin-like growth factor I (somatomedin C) with 70 amino acid residues and three disulfide bridges has been synthesized by the solid-phase method. Disulfides 89-98 insulin like growth factor 1 Homo sapiens 36-49 632300-2 1978 IGF-I is a single chain polypeptide of 70 amino acid residues cross-linked by three disulfide bridges. Disulfides 84-93 insulin like growth factor 1 Homo sapiens 0-5 2628430-0 1989 Direct identification of disulfide bond linkages in human insulin-like growth factor I (IGF-I) by chemical synthesis. Disulfides 25-34 insulin like growth factor 1 Homo sapiens 58-86 2628430-0 1989 Direct identification of disulfide bond linkages in human insulin-like growth factor I (IGF-I) by chemical synthesis. Disulfides 25-34 insulin like growth factor 1 Homo sapiens 88-93 2628430-1 1989 The primary structure of human IGF-I, except for the disulfide bond system, has been reported by Rinderknecht and Humbel. Disulfides 53-62 insulin like growth factor 1 Homo sapiens 31-36 2628430-4 1989 The disulfide bond system of IGF-I was unequivocally determined to be the Type II form along with Cys18-Cys61. Disulfides 4-13 insulin like growth factor 1 Homo sapiens 29-34 2628430-5 1989 Interestingly, the Type I system was included in the disulfide bond isomer produced as the main by-product in the refolding step on IGF-I synthesis by the recombinant DNA method. Disulfides 53-62 insulin like growth factor 1 Homo sapiens 132-137 3884381-1 1985 The insulin disulfide reducing thioredoxin system from E. coli was used to investigate a possible mechanism of degradation for the two somatomedins, insulin-like growth factor I and II (IGF-I and -II). Disulfides 12-21 insulin like growth factor 1 Homo sapiens 186-199 3884381-3 1985 The results show that both IGF-I and -II were as sensitive to disulfide reduction as insulin. Disulfides 62-71 insulin like growth factor 1 Homo sapiens 27-40