메뉴 건너뛰기




Volumn 1, Issue 6, 2010, Pages 537-551

Insulin: A small protein with a long journey

Author keywords

diabetes; disulfide pairing; folding; insulin; NMR; receptor binding

Indexed keywords

ALANINE; AMYLOID; CYSTEINE; GLYCINE; GLYCOGEN; HISTIDINE; INSULIN; INSULIN ASPART; INSULIN DERIVATIVE; INSULIN LISPRO; INSULIN RECEPTOR; LYSINE; SERINE; SOMATOMEDIN C; THREONINE;

EID: 79953185744     PISSN: 1674800X     EISSN: 16748018     Source Type: Journal    
DOI: 10.1007/s13238-010-0069-z     Document Type: Review
Times cited : (58)

References (123)
  • 1
    • 0033906634 scopus 로고    scopus 로고
    • Structure and function of the type 1 insulin-like growth factor receptor
    • Adams, T. E., Epa, V. C., Garrett, T. P. J., and Ward, C. W. (2000). Structure and function of the type 1 insulin-like growth factor receptor. Cell Mol Life Sci 57, 1050-1093.
    • (2000) Cell Mol Life Sci , vol.57 , pp. 1050-1093
    • Adams, T.E.1    Epa, V.C.2    Garrett, T.P.J.3    Ward, C.W.4
  • 3
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen, C. B. (1973). Principles that govern the folding of protein chains. Science 181, 223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 6
    • 0030961788 scopus 로고    scopus 로고
    • Crystal structure of desheptapeptide(B24-B30)insulin at 1.6 A resolution: implications for receptor binding
    • Bao, S. J., Xie, D. L., Zhang, J. P., Chang, W. R., and Liang, D. C. (1997). Crystal structure of desheptapeptide(B24-B30)insulin at 1. 6 A resolution: implications for receptor binding. Proc Natl Acad Sci U S A 94, 2975-2980.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 2975-2980
    • Bao, S.J.1    Xie, D.L.2    Zhang, J.P.3    Chang, W.R.4    Liang, D.C.5
  • 11
    • 0030907673 scopus 로고    scopus 로고
    • A model of insulin fibrils derived from the x-ray crystal structure of a monomeric insulin (despentapeptide insulin)
    • Brange, J., Dodson, G. G., Edwards, D. J., Holden, P. H., and Whittingham, J. L. (1997b). A model of insulin fibrils derived from the x-ray crystal structure of a monomeric insulin (despentapeptide insulin). Proteins 27, 507-516.
    • (1997) Proteins , vol.27 , pp. 507-516
    • Brange, J.1    Dodson, G.G.2    Edwards, D.J.3    Holden, P.H.4    Whittingham, J.L.5
  • 12
    • 0030629665 scopus 로고    scopus 로고
    • Insulin formulation and delivery
    • Brange, J., and Langkjaer, L. (1997). Insulin formulation and delivery. Pharm Biotechnol 10, 343-409.
    • (1997) Pharm Biotechnol , vol.10 , pp. 343-409
    • Brange, J.1    Langkjaer, L.2
  • 14
    • 0020614069 scopus 로고
    • Transmission of conformational change in insulin
    • Chothia, C., Lesk, A. M., Dodson, G. G., and Hodgkin, D. C. (1983). Transmission of conformational change in insulin. Nature 302, 500-505.
    • (1983) Nature , vol.302 , pp. 500-505
    • Chothia, C.1    Lesk, A.M.2    Dodson, G.G.3    Hodgkin, D.C.4
  • 15
    • 0028266674 scopus 로고
    • Crystallographic evidence for dual coordination around zinc in the T3R3 human insulin hexamer
    • Ciszak, E., and Smith, G. D. (1994). Crystallographic evidence for dual coordination around zinc in the T3R3 human insulin hexamer. Biochemistry 33, 1512-1517.
    • (1994) Biochemistry , vol.33 , pp. 1512-1517
    • Ciszak, E.1    Smith, G.D.2
  • 16
    • 0032742943 scopus 로고    scopus 로고
    • Protein misfolding and prion diseases
    • Cohen, F. E. (1999). Protein misfolding and prion diseases. J Mol Biol 293, 313-320.
    • (1999) J Mol Biol , vol.293 , pp. 313-320
    • Cohen, F.E.1
  • 17
    • 45749104374 scopus 로고    scopus 로고
    • Seven mutations in the human insulin gene linked to permanent neonatal/infancy-onset diabetes mellitus
    • the Early Onset Diabetes Study Group of the Italian Society of Pediatric EndocrinologyDiabetes
    • Colombo, C., Porzio, O., Liu, M., Massa, O., Vasta, M., Salardi, S., Beccaria, L., Monciotti, C., Toni, S., Pedersen, O., et al., and the Early Onset Diabetes Study Group of the Italian Society of Pediatric Endocrinology and Diabetes (SIEDP). (2008). Seven mutations in the human insulin gene linked to permanent neonatal/infancy-onset diabetes mellitus. J Clin Invest 118, 2148-2156.
    • (2008) J Clin Invest , vol.118 , pp. 2148-2156
    • Colombo, C.1    Porzio, O.2    Liu, M.3    Massa, O.4    Vasta, M.5    Salardi, S.6    Beccaria, L.7    Monciotti, C.8    Toni, S.9    Pedersen, O.10
  • 18
    • 0025822851 scopus 로고
    • Solution structure of human insulin-like growth factor 1: a nuclear magnetic resonance and restrained molecular dynamics study
    • Cooke, R. M., Harvey, T. S., and Campbell, I. D. (1991). Solution structure of human insulin-like growth factor 1: a nuclear magnetic resonance and restrained molecular dynamics study. Biochemistry 30, 5484-5491.
    • (1991) Biochemistry , vol.30 , pp. 5484-5491
    • Cooke, R.M.1    Harvey, T.S.2    Campbell, I.D.3
  • 19
    • 0030586703 scopus 로고    scopus 로고
    • Characteristic, activity and conformational studies of [A6-Ser, A11-Ser]-insulin
    • Dai, Y., and Tang, J. G. (1996). Characteristic, activity and conformational studies of [A6-Ser, A11-Ser]-insulin. Biochim Biophys Acta 1296, 63-68.
    • (1996) Biochim Biophys Acta , vol.1296 , pp. 63-68
    • Dai, Y.1    Tang, J.G.2
  • 20
    • 0028146822 scopus 로고
    • The structural basis of insulin and insulin-like growth factor-I receptor binding and negative co-operativity, and its relevance to mitogenic versus metabolic signalling
    • De Meyts, P. (1994). The structural basis of insulin and insulin-like growth factor-I receptor binding and negative co-operativity, and its relevance to mitogenic versus metabolic signalling. Diabetologia 37, S135-S148.
    • (1994) Diabetologia , vol.37
    • de Meyts, P.1
  • 21
    • 0036782071 scopus 로고    scopus 로고
    • Structural biology of insulin and IGF1 receptors: implications for drug design
    • De Meyts, P., and Whittaker, J. (2002). Structural biology of insulin and IGF1 receptors: implications for drug design. Nat Rev Drug Discov 1, 769-783.
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 769-783
    • de Meyts, P.1    Whittaker, J.2
  • 23
    • 0025880180 scopus 로고
    • X-ray analysis of the single chain B29-A1 peptide-linked insulin molecule. A completely inactive analogue
    • Derewenda, U., Derewenda, Z., Dodson, E. J., Dodson, G. G., Bing, X., and Markussen, J. (1991). X-ray analysis of the single chain B29-A1 peptide-linked insulin molecule. A completely inactive analogue. J Mol Biol 220, 425-433.
    • (1991) J Mol Biol , vol.220 , pp. 425-433
    • Derewenda, U.1    Derewenda, Z.2    Dodson, E.J.3    Dodson, G.G.4    Bing, X.5    Markussen, J.6
  • 25
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson, C. M. (1999). Protein misfolding, evolution and disease. Trends Biochem Sci 24, 329-332.
    • (1999) Trends Biochem Sci , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 26
    • 0032054714 scopus 로고    scopus 로고
    • The role of assembly in insulin's biosynthesis
    • Dodson, G., and Steiner, D. (1998). The role of assembly in insulin's biosynthesis. Curr Opin Struct Biol 8, 189-194.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 189-194
    • Dodson, G.1    Steiner, D.2
  • 27
    • 0043179085 scopus 로고
    • Conditions for successful resynthesis of insulin from its glycyl and phenylalanyl chains
    • Du, Y. C., Jiang, R. Q., and Tsou, C. L. (1965). Conditions for successful resynthesis of insulin from its glycyl and phenylalanyl chains. Sci Sin 14, 229-236.
    • (1965) Sci Sin , vol.14 , pp. 229-236
    • Du, Y.C.1    Jiang, R.Q.2    Tsou, C.L.3
  • 28
    • 0031895566 scopus 로고    scopus 로고
    • New insulin-like proteins with atypical disulfide bond pattern characterized in Caenorhabditis elegans by comparative sequence analysis and homology modeling
    • Duret, L., Guex, N., Peitsch, M. C., and Bairoch, A. (1998). New insulin-like proteins with atypical disulfide bond pattern characterized in Caenorhabditis elegans by comparative sequence analysis and homology modeling. Genome Res 8, 348-353.
    • (1998) Genome Res , vol.8 , pp. 348-353
    • Duret, L.1    Guex, N.2    Peitsch, M.C.3    Bairoch, A.4
  • 29
    • 42449134450 scopus 로고    scopus 로고
    • Insulin mutation screening in 1,044 patients with diabetes: mutations in the INS gene are a common cause of neonatal diabetes but a rare cause of diabetes diagnosed in childhood or adulthood
    • the Neonatal Diabetes International Collaborative Group
    • Edghill, E. L., Flanagan, S. E., Patch, A. M., Boustred, C., Parrish, A., Shields, B., Shepherd, M. H., Hussain, K., Kapoor, R. R., Malecki, M., et al., and the Neonatal Diabetes International Collaborative Group. (2008). Insulin mutation screening in 1, 044 patients with diabetes: mutations in the INS gene are a common cause of neonatal diabetes but a rare cause of diabetes diagnosed in childhood or adulthood. Diabetes 57, 1034-1042.
    • (2008) Diabetes , vol.57 , pp. 1034-1042
    • Edghill, E.L.1    Flanagan, S.E.2    Patch, A.M.3    Boustred, C.4    Parrish, A.5    Shields, B.6    Shepherd, M.H.7    Hussain, K.8    Kapoor, R.R.9    Malecki, M.10
  • 30
    • 0025812626 scopus 로고
    • X-ray structure of human relaxin at 1.5 A. Comparison to insulin and implications for receptor binding determinants
    • Eigenbrot, C., Randal, M., Quan, C., Burnier, J., O"Connell, L., Rinderknecht, E., and Kossiakoff, A. A. (1991). X-ray structure of human relaxin at 1. 5 A. Comparison to insulin and implications for receptor binding determinants. J Mol Biol 221, 15-21.
    • (1991) J Mol Biol , vol.221 , pp. 15-21
    • Eigenbrot, C.1    Randal, M.2    Quan, C.3    Burnier, J.4    O"Connell, L.5    Rinderknecht, E.6    Kossiakoff, A.A.7
  • 31
    • 0041743075 scopus 로고    scopus 로고
    • Native-like partially folded conformations and folding process revealed in the N-terminal large fragments of staphylococcal nuclease: a study by NMR spectroscopy
    • Feng, Y., Liu, D., and Wang, J. (2003). Native-like partially folded conformations and folding process revealed in the N-terminal large fragments of staphylococcal nuclease: a study by NMR spectroscopy. J Mol Biol 330, 821-837.
    • (2003) J Mol Biol , vol.330 , pp. 821-837
    • Feng, Y.1    Liu, D.2    Wang, J.3
  • 32
    • 79953182489 scopus 로고    scopus 로고
    • Kerala, India: Transworld Research Network
    • Feng, Y. M. (2010). Chinese work on insulin (Kerala, India: Transworld Research Network).
    • (2010) Chinese Work on Insulin
    • Feng, Y.M.1
  • 33
    • 0032930155 scopus 로고    scopus 로고
    • Modelling of the disulphide-swapped isomer of human insulin-like growth factor-1: implications for receptor binding
    • Gill, R., Verma, C., Wallach, B., Ursø, B., Pitts, J., Wollmer, A., De Meyts, P., and Wood, S. (1999). Modelling of the disulphide-swapped isomer of human insulin-like growth factor-1: implications for receptor binding. Protein Eng 12, 297-303.
    • (1999) Protein Eng , vol.12 , pp. 297-303
    • Gill, R.1    Verma, C.2    Wallach, B.3    Ursø, B.4    Pitts, J.5    Wollmer, A.6    de Meyts, P.7    Wood, S.8
  • 34
    • 0035037739 scopus 로고    scopus 로고
    • Effects of cysteine to serine substitutions in the two inter-chain disulfide bonds of insulin
    • Guo, Z. Y., and Feng, Y. M. (2001). Effects of cysteine to serine substitutions in the two inter-chain disulfide bonds of insulin. Biol Chem 382, 443-448.
    • (2001) Biol Chem , vol.382 , pp. 443-448
    • Guo, Z.Y.1    Feng, Y.M.2
  • 35
    • 36148978188 scopus 로고    scopus 로고
    • The in vitro oxidative folding of the insulin superfamily
    • Guo, Z. Y., Qiao, Z. S., and Feng, Y. M. (2008). The in vitro oxidative folding of the insulin superfamily. Antioxid Redox Signal 10, 127-139.
    • (2008) Antioxid Redox Signal , vol.10 , pp. 127-139
    • Guo, Z.Y.1    Qiao, Z.S.2    Feng, Y.M.3
  • 36
    • 0030932132 scopus 로고    scopus 로고
    • Disulfide exchange folding of disulfide mutants of insulin-like growth factor I in vitro
    • Hober, S., Uhlén, M., and Nilsson, B. (1997). Disulfide exchange folding of disulfide mutants of insulin-like growth factor I in vitro. Biochemistry 36, 4616-4622.
    • (1997) Biochemistry , vol.36 , pp. 4616-4622
    • Hober, S.1    Uhlén, M.2    Nilsson, B.3
  • 37
    • 1642501551 scopus 로고    scopus 로고
    • Insight into folding, binding and stability of insulin by NMR
    • Hua, Q. X. (2004). Insight into folding, binding and stability of insulin by NMR. Prog Biochem Biophys 31, 1-26.
    • (2004) Prog Biochem Biophys , vol.31 , pp. 1-26
    • Hua, Q.X.1
  • 38
    • 0037044828 scopus 로고    scopus 로고
    • Mechanism of insulin chain combination. Asymmetric roles of A-chain alpha-helices in disulfide pairing
    • Hua, Q. X., Chu, Y. C., Jia, W., Phillips, N. F., Wang, R. Y., Katsoyannis, P. G., and Weiss, M. A. (2002a). Mechanism of insulin chain combination. Asymmetric roles of A-chain alpha-helices in disulfide pairing. J Biol Chem 277, 43443-43453.
    • (2002) J Biol Chem , vol.277 , pp. 43443-43453
    • Hua, Q.X.1    Chu, Y.C.2    Jia, W.3    Phillips, N.F.4    Wang, R.Y.5    Katsoyannis, P.G.6    Weiss, M.A.7
  • 40
    • 0030606309 scopus 로고    scopus 로고
    • Mapping the functional surface of insulin by design: structure and function of a novel A-chain analogue
    • Hua, Q. X., Hu, S. Q., Frank, B. H., Jia, W., Chu, Y. C., Wang, S. H., Burke, G. T., Katsoyannis, P. G., and Weiss, M. A. (1996a). Mapping the functional surface of insulin by design: structure and function of a novel A-chain analogue. J Mol Biol 264, 390-403.
    • (1996) J Mol Biol , vol.264 , pp. 390-403
    • Hua, Q.X.1    Hu, S.Q.2    Frank, B.H.3    Jia, W.4    Chu, Y.C.5    Wang, S.H.6    Burke, G.T.7    Katsoyannis, P.G.8    Weiss, M.A.9
  • 41
    • 0037126725 scopus 로고    scopus 로고
    • A protein caught in a kinetic trap: structures and stabilities of insulin disulfide isomers
    • Hua, Q. X., Jia, W., Frank, B. H., Phillips, N. F., and Weiss, M. A. (2002b). A protein caught in a kinetic trap: structures and stabilities of insulin disulfide isomers. Biochemistry 41, 14700-14715.
    • (2002) Biochemistry , vol.41 , pp. 14700-14715
    • Hua, Q.X.1    Jia, W.2    Frank, B.H.3    Phillips, N.F.4    Weiss, M.A.5
  • 42
    • 0026549524 scopus 로고
    • Structure and dynamics of des-pentapeptide-insulin in solution: the moltenglobule hypothesis
    • Hua, Q. X., Kochoyan, M., and Weiss, M. A. (1992a). Structure and dynamics of des-pentapeptide-insulin in solution: the moltenglobule hypothesis. Proc Natl Acad Sci U S A 89, 2379-2383.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 2379-2383
    • Hua, Q.X.1    Kochoyan, M.2    Weiss, M.A.3
  • 44
    • 33748785712 scopus 로고    scopus 로고
    • The folding nucleus of the insulin superfamily: a flexible peptide model foreshadows the native state
    • Hua, Q. X., Mayer, J. P., Jia, W., Zhang, J., and Weiss, M. A. (2006b). The folding nucleus of the insulin superfamily: a flexible peptide model foreshadows the native state. J Biol Chem 281, 28131-28142.
    • (2006) J Biol Chem , vol.281 , pp. 28131-28142
    • Hua, Q.X.1    Mayer, J.P.2    Jia, W.3    Zhang, J.4    Weiss, M.A.5
  • 45
    • 33747670241 scopus 로고    scopus 로고
    • Toward the active conformation of insulin: stereospecific modulation of a structural switch in the B-chain
    • Hua, Q. X., Nakagawa, S. H., Hu, S. Q., Jia, W., Wang, S., and Weiss, M. A. (2006c). Toward the active conformation of insulin: stereospecific modulation of a structural switch in the B-chain. J Biol Chem 281, 24900-24909.
    • (2006) J Biol Chem , vol.281 , pp. 24900-24909
    • Hua, Q.X.1    Nakagawa, S.H.2    Hu, S.Q.3    Jia, W.4    Wang, S.5    Weiss, M.A.6
  • 46
    • 0035899983 scopus 로고    scopus 로고
    • Hierarchical protein folding: asymmetric unfolding of an insulin analogue lacking the A7-B7 interchain disulfide bridge
    • Hua, Q. X., Nakagawa, S. H., Jia, W., Hu, S. Q., Chu, Y. C., Katsoyannis, P. G., and Weiss, M. A. (2001). Hierarchical protein folding: asymmetric unfolding of an insulin analogue lacking the A7-B7 interchain disulfide bridge. Biochemistry 40, 12299-12311.
    • (2001) Biochemistry , vol.40 , pp. 12299-12311
    • Hua, Q.X.1    Nakagawa, S.H.2    Jia, W.3    Hu, S.Q.4    Chu, Y.C.5    Katsoyannis, P.G.6    Weiss, M.A.7
  • 47
    • 47249140371 scopus 로고    scopus 로고
    • Design of an active ultrastable single-chain insulin analog: synthesis, structure, and therapeutic implications
    • Hua, Q. X., Nakagawa, S. H., Jia, W., Huang, K., Phillips, N. B., Hu, S. Q., and Weiss, M. A. (2008). Design of an active ultrastable single-chain insulin analog: synthesis, structure, and therapeutic implications. J Biol Chem 283, 14703-14716.
    • (2008) J Biol Chem , vol.283 , pp. 14703-14716
    • Hua, Q.X.1    Nakagawa, S.H.2    Jia, W.3    Huang, K.4    Phillips, N.B.5    Hu, S.Q.6    Weiss, M.A.7
  • 48
    • 0345073631 scopus 로고    scopus 로고
    • A divergent INS protein in Caenorhabditis elegans structurally resembles human insulin and activates the human insulin receptor
    • Hua, Q. X., Nakagawa, S. H., Wilken, J., Ramos, R. R., Jia, W., Bass, J., and Weiss, M. A. (2003). A divergent INS protein in Caenorhabditis elegans structurally resembles human insulin and activates the human insulin receptor. Genes Dev 17, 826-831.
    • (2003) Genes Dev , vol.17 , pp. 826-831
    • Hua, Q.X.1    Nakagawa, S.H.2    Wilken, J.3    Ramos, R.R.4    Jia, W.5    Bass, J.6    Weiss, M.A.7
  • 49
    • 0029991679 scopus 로고    scopus 로고
    • Native and non-native structure in a protein-folding intermediate: spectroscopic studies of partially reduced IGF-I and an engineered alanine model
    • Hua, Q. X., Narhi, L., Jia, W., Arakawa, T., Rosenfeld, R., Hawkins, N., Miller, J. A., and Weiss, M. A. (1996b). Native and non-native structure in a protein-folding intermediate: spectroscopic studies of partially reduced IGF-I and an engineered alanine model. J Mol Biol 259, 297-313.
    • (1996) J Mol Biol , vol.259 , pp. 297-313
    • Hua, Q.X.1    Narhi, L.2    Jia, W.3    Arakawa, T.4    Rosenfeld, R.5    Hawkins, N.6    Miller, J.A.7    Weiss, M.A.8
  • 50
    • 0025996911 scopus 로고
    • Receptor binding redefined by a structural switch in a mutant human insulin
    • Hua, Q. X., Shoelson, S. E., Kochoyan, M., and Weiss, M. A. (1991). Receptor binding redefined by a structural switch in a mutant human insulin. Nature 354, 238-241.
    • (1991) Nature , vol.354 , pp. 238-241
    • Hua, Q.X.1    Shoelson, S.E.2    Kochoyan, M.3    Weiss, M.A.4
  • 51
    • 0026482979 scopus 로고
    • Nonlocal structural perturbations in a mutant human insulin: sequential resonance assignment and 13C-isotope-aided 2D-NMR studies of [PheB24→Gly]insulin with implications for receptor recognition
    • Hua, Q. X., Shoelson, S. E., and Weiss, M. A. (1992b). Nonlocal structural perturbations in a mutant human insulin: sequential resonance assignment and 13C-isotope-aided 2D-NMR studies of [PheB24→Gly]insulin with implications for receptor recognition. Biochemistry 31, 11940-11951.
    • (1992) Biochemistry , vol.31 , pp. 11940-11951
    • Hua, Q.X.1    Shoelson, S.E.2    Weiss, M.A.3
  • 52
    • 0025778802 scopus 로고
    • Comparative 2D NMR studies of human insulin and des-pentapeptide insulin: sequential resonance assignment and implications for protein dynamics and receptor recognition
    • Hua, Q. X., and Weiss, M. A. (1991). Comparative 2D NMR studies of human insulin and des-pentapeptide insulin: sequential resonance assignment and implications for protein dynamics and receptor recognition. Biochemistry 30, 5505-5515.
    • (1991) Biochemistry , vol.30 , pp. 5505-5515
    • Hua, Q.X.1    Weiss, M.A.2
  • 53
    • 2442715309 scopus 로고    scopus 로고
    • Mechanism of insulin fibrillation: the structure of insulin under amyloidogenic conditions resembles a protein-folding intermediate
    • Hua, Q. X., and Weiss, M. A. (2004). Mechanism of insulin fibrillation: the structure of insulin under amyloidogenic conditions resembles a protein-folding intermediate. J Biol Chem 279, 21449-21460.
    • (2004) J Biol Chem , vol.279 , pp. 21449-21460
    • Hua, Q.X.1    Weiss, M.A.2
  • 54
    • 67649811215 scopus 로고    scopus 로고
    • Enhancing the activity of a protein by stereospecific unfolding: conformational life cycle of insulin and its evolutionary origins
    • Hua, Q. X., Xu, B., Huang, K., Hu, S. Q., Nakagawa, S., Jia, W., Wang, S., Whittaker, J., Katsoyannis, P. G., and Weiss, M. A. (2009). Enhancing the activity of a protein by stereospecific unfolding: conformational life cycle of insulin and its evolutionary origins. J Biol Chem 284, 14586-14596.
    • (2009) J Biol Chem , vol.284 , pp. 14586-14596
    • Hua, Q.X.1    Xu, B.2    Huang, K.3    Hu, S.Q.4    Nakagawa, S.5    Jia, W.6    Wang, S.7    Whittaker, J.8    Katsoyannis, P.G.9    Weiss, M.A.10
  • 55
    • 36849051281 scopus 로고    scopus 로고
    • The A-chain of insulin contacts the insert domain of the receptor. Photo-cross-linking and nonstandard mutagenesis of the diabetes-related A3 crevice
    • Huang, K., Chan, S. J., Hua, Q. X., Chu, Y. C., Wang, R., Klaproth, B., Jia, W., Whittaker, J., De Meyts, P., Nakagawa, S. H., et al. (2007). The A-chain of insulin contacts the insert domain of the receptor. Photo-cross-linking and nonstandard mutagenesis of the diabetes-related A3 crevice. J Biol Chem 282, 35337-35349.
    • (2007) J Biol Chem , vol.282 , pp. 35337-35349
    • Huang, K.1    Chan, S.J.2    Hua, Q.X.3    Chu, Y.C.4    Wang, R.5    Klaproth, B.6    Jia, W.7    Whittaker, J.8    de Meyts, P.9    Nakagawa, S.H.10
  • 56
    • 29644434204 scopus 로고    scopus 로고
    • Proinsulin is refractory to protein fibrillation: topological protection of a precursor protein from cross-beta assembly
    • Huang, K., Dong, J., Phillips, N. B., Carey, P. R., and Weiss, M. A. (2005). Proinsulin is refractory to protein fibrillation: topological protection of a precursor protein from cross-beta assembly. J Biol Chem 280, 42345-42355.
    • (2005) J Biol Chem , vol.280 , pp. 42345-42355
    • Huang, K.1    Dong, J.2    Phillips, N.B.3    Carey, P.R.4    Weiss, M.A.5
  • 57
    • 33748660053 scopus 로고    scopus 로고
    • Structure-specific effects of protein topology on cross-beta assembly: studies of insulin fibrillation
    • Huang, K., Maiti, N. C., Phillips, N. B., Carey, P. R., and Weiss, M. A. (2006). Structure-specific effects of protein topology on cross-beta assembly: studies of insulin fibrillation. Biochemistry 45, 10278-10293.
    • (2006) Biochemistry , vol.45 , pp. 10278-10293
    • Huang, K.1    Maiti, N.C.2    Phillips, N.B.3    Carey, P.R.4    Weiss, M.A.5
  • 58
    • 3342960841 scopus 로고    scopus 로고
    • How insulin binds: the B-chain alpha-helix contacts the L1 beta-helix of the insulin receptor
    • Huang, K., Xu, B., Hu, S. Q., Chu, Y. C., Hua, Q. X., Qu, Y., Li, B., Wang, S., Wang, R. Y., Nakagawa, S. H., et al. (2004). How insulin binds: the B-chain alpha-helix contacts the L1 beta-helix of the insulin receptor. J Mol Biol 341, 529-550.
    • (2004) J Mol Biol , vol.341 , pp. 529-550
    • Huang, K.1    Xu, B.2    Hu, S.Q.3    Chu, Y.C.4    Hua, Q.X.5    Qu, Y.6    Li, B.7    Wang, S.8    Wang, R.Y.9    Nakagawa, S.H.10
  • 59
    • 84894405346 scopus 로고
    • Insulin-like growth factors I and II
    • Humbel, R. E. (1990). Insulin-like growth factors I and II. Eur J Biol 277, 103-118.
    • (1990) Eur J Biol , vol.277 , pp. 103-118
    • Humbel, R.E.1
  • 60
    • 0037312881 scopus 로고    scopus 로고
    • Dominant negative pathogenesis by mutant proinsulin in the Akita diabetic mouse
    • Izumi, T., Yokota-Hashimoto, H., Zhao, S., Wang, J., Halban, P. A., and Takeuchi, T. (2003). Dominant negative pathogenesis by mutant proinsulin in the Akita diabetic mouse. Diabetes 52, 409-416.
    • (2003) Diabetes , vol.52 , pp. 409-416
    • Izumi, T.1    Yokota-Hashimoto, H.2    Zhao, S.3    Wang, J.4    Halban, P.A.5    Takeuchi, T.6
  • 61
    • 0142241183 scopus 로고    scopus 로고
    • Peptide models of four possible insulin folding intermediates with two disulfides
    • Jia, X. Y., Guo, Z. Y., Wang, Y., Xu, Y., Duan, S. S., and Feng, Y. M. (2003). Peptide models of four possible insulin folding intermediates with two disulfides. Protein Sci 12, 2412-2419.
    • (2003) Protein Sci , vol.12 , pp. 2412-2419
    • Jia, X.Y.1    Guo, Z.Y.2    Wang, Y.3    Xu, Y.4    Duan, S.S.5    Feng, Y.M.6
  • 62
    • 0013914317 scopus 로고
    • Insulin synthesis by recombination of A and B-chains: a highly efficient method
    • Katsoyannis, P. G., and Tometsko, A. (1966). Insulin synthesis by recombination of A and B-chains: a highly efficient method. Proc Natl Acad Sci U S A 55, 1554-1561.
    • (1966) Proc Natl Acad Sci U S A , vol.55 , pp. 1554-1561
    • Katsoyannis, P.G.1    Tometsko, A.2
  • 65
    • 0030941110 scopus 로고    scopus 로고
    • Inactive conformation of an insulin despite its wild-type sequence
    • Kurapkat, G., De Wolf, E., Grötzinger, J., and Wollmer, A. (1997). Inactive conformation of an insulin despite its wild-type sequence. Protein Sci 6, 580-587.
    • (1997) Protein Sci , vol.6 , pp. 580-587
    • Kurapkat, G.1    de Wolf, E.2    Grötzinger, J.3    Wollmer, A.4
  • 66
    • 0027960567 scopus 로고
    • Cross-linking of a B25 azidophenylalanine insulin derivative to the carboxyl-terminal region of the alpha-subunit of the insulin receptor. Identification of a new insulin-binding domain in the insulin receptor
    • Kurose, T., Pashmforoush, M., Yoshimasa, Y., Carroll, R., Schwartz, G. P., Burke, G. T., Katsoyannis, P. G., and Steiner, D. F. (1994). Cross-linking of a B25 azidophenylalanine insulin derivative to the carboxyl-terminal region of the alpha-subunit of the insulin receptor. Identification of a new insulin-binding domain in the insulin receptor. J Biol Chem 269, 29190-29197.
    • (1994) J Biol Chem , vol.269 , pp. 29190-29197
    • Kurose, T.1    Pashmforoush, M.2    Yoshimasa, Y.3    Carroll, R.4    Schwartz, G.P.5    Burke, G.T.6    Katsoyannis, P.G.7    Steiner, D.F.8
  • 67
    • 36549015742 scopus 로고    scopus 로고
    • Insulin receptor structure and its implications for the IGF-1 receptor
    • Lawrence, M. C., McKern, N. M., and Ward, C. W. (2007). Insulin receptor structure and its implications for the IGF-1 receptor. Curr Opin Struct Biol 17, 699-705.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 699-705
    • Lawrence, M.C.1    McKern, N.M.2    Ward, C.W.3
  • 69
    • 0346565748 scopus 로고
    • The possible mechanism of binding interaction of insulin molecule with its receptor
    • Liang, D. C., Chang, W. R., Zhang, J. P., and Wan, Z. L. (1992). The possible mechanism of binding interaction of insulin molecule with its receptor. Sci China B 35, 547-557.
    • (1992) Sci China B , vol.35 , pp. 547-557
    • Liang, D.C.1    Chang, W.R.2    Zhang, J.P.3    Wan, Z.L.4
  • 70
    • 33747584896 scopus 로고    scopus 로고
    • The first three domains of the insulin receptor differ structurally from the insulin-like growth factor 1 receptor in the regions governing ligand specificity
    • Lou, M., Garrett, T. P., McKern, N. M., Hoyne, P. A., Epa, V. C., Bentley, J. D., Lovrecz, G. O., Cosgrove, L. J., Frenkel, M. J., and Ward, C. W. (2006). The first three domains of the insulin receptor differ structurally from the insulin-like growth factor 1 receptor in the regions governing ligand specificity. Proc Natl Acad Sci U S A 103, 12429-12434.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 12429-12434
    • Lou, M.1    Garrett, T.P.2    McKern, N.M.3    Hoyne, P.A.4    Epa, V.C.5    Bentley, J.D.6    Lovrecz, G.O.7    Cosgrove, L.J.8    Frenkel, M.J.9    Ward, C.W.10
  • 72
    • 0027177107 scopus 로고
    • Oxidative refolding of insulin-like growth factor 1 yields two products of similar thermodynamic stability: a bifurcating protein-folding pathway
    • Miller, J. A., Narhi, L. O., Hua, Q. X., Rosenfeld, R., Arakawa, T., Rohde, M., Prestrelski, S., Lauren, S., Stoney, K. S., Tsai, L., et al. (1993). Oxidative refolding of insulin-like growth factor 1 yields two products of similar thermodynamic stability: a bifurcating protein-folding pathway. Biochemistry 32, 5203-5213.
    • (1993) Biochemistry , vol.32 , pp. 5203-5213
    • Miller, J.A.1    Narhi, L.O.2    Hua, Q.X.3    Rosenfeld, R.4    Arakawa, T.5    Rohde, M.6    Prestrelski, S.7    Lauren, S.8    Stoney, K.S.9    Tsai, L.10
  • 73
    • 0033586410 scopus 로고    scopus 로고
    • Probing the disulfide folding pathway of insulin-like growth factor-I
    • Milner, S. J., Carver, J. A., Ballard, F. J., and Francis, G. L. (1999). Probing the disulfide folding pathway of insulin-like growth factor-I. Biotechnol Bioeng 62, 693-703.
    • (1999) Biotechnol Bioeng , vol.62 , pp. 693-703
    • Milner, S.J.1    Carver, J.A.2    Ballard, F.J.3    Francis, G.L.4
  • 74
    • 42449127920 scopus 로고    scopus 로고
    • Mutations in the insulin gene can cause MODY and autoantibodynegative type 1 diabetes
    • the Norwegian Childhood Diabetes Study Group
    • Molven, A., Ringdal, M., Nordbø, A. M., Raeder, H., Støy, J., Lipkind, G. M., Steiner, D. F., Philipson, L. H., Bergmann, I., Aarskog, D., et al., and the Norwegian Childhood Diabetes Study Group. (2008). Mutations in the insulin gene can cause MODY and autoantibodynegative type 1 diabetes. Diabetes 57, 1131-1135.
    • (2008) Diabetes , vol.57 , pp. 1131-1135
    • Molven, A.1    Ringdal, M.2    Nordbø, A.M.3    Raeder, H.4    Støy, J.5    Lipkind, G.M.6    Steiner, D.F.7    Philipson, L.H.8    Bergmann, I.9    Aarskog, D.10
  • 75
    • 0026859563 scopus 로고
    • Structure and evolution of insulins: implications for receptor binding
    • Murray-Rust, J., McLeod, A. N., Blundell, T. L., and Wood, S. P. (1992). Structure and evolution of insulins: implications for receptor binding. Bioessays 14, 325-331.
    • (1992) Bioessays , vol.14 , pp. 325-331
    • Murray-Rust, J.1    McLeod, A.N.2    Blundell, T.L.3    Wood, S.P.4
  • 76
    • 0028868961 scopus 로고
    • Identification of the receptor-recognition surface of bombyxin-II, an insulin-like peptide of the silkmoth Bombyx mori: critical importance of the B-chain central part
    • Nagata, K., Hatanaka, H., Kohda, D., Kataoka, H., Nagasawa, H., Isogai, A., Ishizaki, H., Suzuki, A., and Inagaki, F. (1995a). Identification of the receptor-recognition surface of bombyxin-II, an insulin-like peptide of the silkmoth Bombyx mori: critical importance of the B-chain central part. J Mol Biol 253, 759-770.
    • (1995) J Mol Biol , vol.253 , pp. 759-770
    • Nagata, K.1    Hatanaka, H.2    Kohda, D.3    Kataoka, H.4    Nagasawa, H.5    Isogai, A.6    Ishizaki, H.7    Suzuki, A.8    Inagaki, F.9
  • 77
    • 0028868960 scopus 로고
    • Three-dimensional solution structure of bombyxin-II an insulin-like peptide of the silkmoth Bombyx mori: structural comparison with insulin and relaxin
    • Nagata, K., Hatanaka, H., Kohda, D., Kataoka, H., Nagasawa, H., Isogai, A., Ishizaki, H., Suzuki, A., and Inagaki, F. (1995b). Three-dimensional solution structure of bombyxin-II an insulin-like peptide of the silkmoth Bombyx mori: structural comparison with insulin and relaxin. J Mol Biol 253, 749-758.
    • (1995) J Mol Biol , vol.253 , pp. 749-758
    • Nagata, K.1    Hatanaka, H.2    Kohda, D.3    Kataoka, H.4    Nagasawa, H.5    Isogai, A.6    Ishizaki, H.7    Suzuki, A.8    Inagaki, F.9
  • 78
    • 0025992754 scopus 로고
    • Implications of invariant residue LeuB6 in insulin-receptor interactions
    • Nakagawa, S. H., and Tager, H. S. (1991). Implications of invariant residue LeuB6 in insulin-receptor interactions. J Biol Chem 266, 11502-11509.
    • (1991) J Biol Chem , vol.266 , pp. 11502-11509
    • Nakagawa, S.H.1    Tager, H.S.2
  • 79
    • 0026634650 scopus 로고
    • Importance of aliphatic sidechain structure at positions 2 and 3 of the insulin A chain in insulinreceptor interactions
    • Nakagawa, S. H., and Tager, H. S. (1992). Importance of aliphatic sidechain structure at positions 2 and 3 of the insulin A chain in insulinreceptor interactions. Biochemistry 31, 3204-3214.
    • (1992) Biochemistry , vol.31 , pp. 3204-3214
    • Nakagawa, S.H.1    Tager, H.S.2
  • 80
    • 16344376210 scopus 로고    scopus 로고
    • Chiral mutagenesis of insulin. Foldability and function are inversely regulated by a stereospecific switch in the B-chain
    • Nakagawa, S. H., Zhao, M., Hua, Q. X., Hu, S. Q., Wan, Z. L., Jia, W., and Weiss, M. A. (2005). Chiral mutagenesis of insulin. Foldability and function are inversely regulated by a stereospecific switch in the B-chain. Biochemistry 44, 4984-4999.
    • (2005) Biochemistry , vol.44 , pp. 4984-4999
    • Nakagawa, S.H.1    Zhao, M.2    Hua, Q.X.3    Hu, S.Q.4    Wan, Z.L.5    Jia, W.6    Weiss, M.A.7
  • 81
    • 0022549577 scopus 로고
    • Diabetes due to secretion of a structurally abnormal insulin (insulin Wakayama). Clinical and functional characteristics of [LeuA3] insulin
    • Nanjo, K., Sanke, T., Miyano, M., Okai, K., Sowa, R., Kondo, M., Nishimura, S., Iwo, K., Miyamura, K., Given, B. D., et al. (1986). Diabetes due to secretion of a structurally abnormal insulin (insulin Wakayama). Clinical and functional characteristics of [LeuA3] insulin. J Clin Invest 77, 514-519.
    • (1986) J Clin Invest , vol.77 , pp. 514-519
    • Nanjo, K.1    Sanke, T.2    Miyano, M.3    Okai, K.4    Sowa, R.5    Kondo, M.6    Nishimura, S.7    Iwo, K.8    Miyamura, K.9    Given, B.D.10
  • 82
    • 0027311222 scopus 로고
    • Role of native disulfide bonds in the structure and activity of insulin-like growth factor 1: genetic models of protein-folding intermediates
    • Narhi, L. O., Hua, Q. X., Arakawa, T., Fox, G. M., Tsai, L., Rosenfeld, R., Holst, P., Miller, J. A., and Weiss, M. A. (1993). Role of native disulfide bonds in the structure and activity of insulin-like growth factor 1: genetic models of protein-folding intermediates. Biochemistry 32, 5214-5221.
    • (1993) Biochemistry , vol.32 , pp. 5214-5221
    • Narhi, L.O.1    Hua, Q.X.2    Arakawa, T.3    Fox, G.M.4    Tsai, L.5    Rosenfeld, R.6    Holst, P.7    Miller, J.A.8    Weiss, M.A.9
  • 83
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism
    • Nielsen, L., Khurana, R., Coats, A., Frokjaer, S., Brange, J., Vyas, S., Uversky, V. N., and Fink, A. L. (2001). Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry 40, 6036-6046.
    • (2001) Biochemistry , vol.40 , pp. 6036-6046
    • Nielsen, L.1    Khurana, R.2    Coats, A.3    Frokjaer, S.4    Brange, J.5    Vyas, S.6    Uversky, V.N.7    Fink, A.L.8
  • 84
    • 0036175128 scopus 로고    scopus 로고
    • Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes
    • Oyadomari, S., Koizumi, A., Takeda, K., Gotoh, T., Akira, S., Araki, E., and Mori, M. (2002). Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes. J Clin Invest 109, 525-532.
    • (2002) J Clin Invest , vol.109 , pp. 525-532
    • Oyadomari, S.1    Koizumi, A.2    Takeda, K.3    Gotoh, T.4    Akira, S.5    Araki, E.6    Mori, M.7
  • 85
    • 0009718890 scopus 로고
    • Insulin's crystal structure at 2.5A resolution
    • Peking, I. R. G. (1971). Insulin's crystal structure at 2. 5A resolution. Peking Rev 40, 11-16.
    • (1971) Peking Rev , vol.40 , pp. 11-16
    • Peking, I.R.G.1
  • 88
    • 0035814878 scopus 로고    scopus 로고
    • Putative disulfide-forming pathway of porcine insulin precursor during its refolding in vitro
    • Qiao, Z. S., Guo, Z. Y., and Feng, Y. M. (2001). Putative disulfide-forming pathway of porcine insulin precursor during its refolding in vitro. Biochemistry 40, 2662-2668.
    • (2001) Biochemistry , vol.40 , pp. 2662-2668
    • Qiao, Z.S.1    Guo, Z.Y.2    Feng, Y.M.3
  • 89
    • 33646429254 scopus 로고    scopus 로고
    • In vitro folding/unfolding of insulin/single-chain insulin
    • Qiao, Z. S., Guo, Z. Y., and Feng, Y. M. (2006). In vitro folding/unfolding of insulin/single-chain insulin. Protein Pept Lett 13, 423-429.
    • (2006) Protein Pept Lett , vol.13 , pp. 423-429
    • Qiao, Z.S.1    Guo, Z.Y.2    Feng, Y.M.3
  • 90
    • 0038043253 scopus 로고    scopus 로고
    • In vitro refolding of human proinsulin. Kinetic intermediates, putative disulfide-forming pathway folding initiation site, and potential role of C-peptide in folding process
    • Qiao, Z. S., Min, C. Y., Hua, Q. X., Weiss, M. A., and Feng, Y. M. (2003). In vitro refolding of human proinsulin. Kinetic intermediates, putative disulfide-forming pathway folding initiation site, and potential role of C-peptide in folding process. J Biol Chem 278, 17800-17809.
    • (2003) J Biol Chem , vol.278 , pp. 17800-17809
    • Qiao, Z.S.1    Min, C.Y.2    Hua, Q.X.3    Weiss, M.A.4    Feng, Y.M.5
  • 91
    • 0036175125 scopus 로고    scopus 로고
    • Proteotoxicity in the endoplasmic reticulum: lessons from the Akita diabetic mouse
    • Ron, D. (2002). Proteotoxicity in the endoplasmic reticulum: lessons from the Akita diabetic mouse. J Clin Invest 109, 443-445.
    • (2002) J Clin Invest , vol.109 , pp. 443-445
    • Ron, D.1
  • 94
    • 0028268592 scopus 로고
    • A model for insulin binding to the insulin receptor
    • Schäffer, L. (1994). A model for insulin binding to the insulin receptor. Eur J Biochem 221, 1127-1132.
    • (1994) Eur J Biochem , vol.221 , pp. 1127-1132
    • Schäffer, L.1
  • 95
    • 0026548864 scopus 로고
    • Mutations at the dimer, hexamer, and receptor-binding surfaces of insulin independently affect insulin-insulin and insulin-receptor interactions
    • Shoelson, S. E., Lu, Z. X., Parlautan, L., Lynch, C. S., and Weiss, M. A. (1992). Mutations at the dimer, hexamer, and receptor-binding surfaces of insulin independently affect insulin-insulin and insulin-receptor interactions. Biochemistry 31, 1757-1767.
    • (1992) Biochemistry , vol.31 , pp. 1757-1767
    • Shoelson, S.E.1    Lu, Z.X.2    Parlautan, L.3    Lynch, C.S.4    Weiss, M.A.5
  • 96
    • 0018133234 scopus 로고
    • 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)
    • Sieber, P. S., Eisler, K., Kamber, B., Riniker, B., Rittel, W., Märki, F., and de Gasparo, M. (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). Hoppe Seylers Z Physiol Chem 359, 113-123.
    • (1978) Hoppe Seylers Z Physiol Chem , vol.359 , pp. 113-123
    • Sieber, P.S.1    Eisler, K.2    Kamber, B.3    Riniker, B.4    Rittel, W.5    Märki, F.6    de Gasparo, M.7
  • 97
    • 0014146156 scopus 로고
    • Evidence for a precursor in the biosynthesis of insulin
    • Steiner, D. F. (1967). Evidence for a precursor in the biosynthesis of insulin. Trans N Y Acad Sci 30, 60-68.
    • (1967) Trans N Y Acad Sci , vol.30 , pp. 60-68
    • Steiner, D.F.1
  • 98
    • 0031995477 scopus 로고    scopus 로고
    • The proprotein convertases
    • Steiner, D. F. (1998). The proprotein convertases. Curr Opin Chem Biol 2, 31-39.
    • (1998) Curr Opin Chem Biol , vol.2 , pp. 31-39
    • Steiner, D.F.1
  • 101
    • 0025372089 scopus 로고
    • The insulin A and B-chains contain structural information for the formation of the native molecule. Studies with protein disulphide-isomerase
    • Tang, J. G., and Tsou, C. L. (1990). The insulin A and B-chains contain structural information for the formation of the native molecule. Studies with protein disulphide-isomerase. Biochem J 268, 429-435.
    • (1990) Biochem J , vol.268 , pp. 429-435
    • Tang, J.G.1    Tsou, C.L.2
  • 102
    • 0029059589 scopus 로고
    • Solution structure of human insulin-like growth factor II. Relationship to receptor and binding protein interactions
    • Torres, A. M., Forbes, B. E., Aplin, S. E., Wallace, J. C., Francis, G. L., and Norton, R. S. (1995). Solution structure of human insulin-like growth factor II. Relationship to receptor and binding protein interactions. J Mol Biol 248, 385-401.
    • (1995) J Mol Biol , vol.248 , pp. 385-401
    • Torres, A.M.1    Forbes, B.E.2    Aplin, S.E.3    Wallace, J.C.4    Francis, G.L.5    Norton, R.S.6
  • 103
    • 0034048940 scopus 로고    scopus 로고
    • Genetically engineered insulin analogs: diabetes in the new millenium
    • Vajo, Z., and Duckworth, W. C. (2000). Genetically engineered insulin analogs: diabetes in the new millenium. Pharmacol Rev 52, 1-9.
    • (2000) Pharmacol Rev , vol.52 , pp. 1-9
    • Vajo, Z.1    Duckworth, W.C.2
  • 104
    • 48149093031 scopus 로고    scopus 로고
    • The structure of a mutant insulin uncouples receptor binding from protein allostery. An electrostatic block to the TR transition
    • Wan, Z. L., Huang, K., Hu, S. Q., Whittaker, J., and Weiss, M. A. (2008). The structure of a mutant insulin uncouples receptor binding from protein allostery. An electrostatic block to the TR transition. J Biol Chem 283, 21198-21210.
    • (2008) J Biol Chem , vol.283 , pp. 21198-21210
    • Wan, Z.L.1    Huang, K.2    Hu, S.Q.3    Whittaker, J.4    Weiss, M.A.5
  • 105
    • 0025777247 scopus 로고
    • The insulin A and B-chains contain sufficient structural information to form the native molecule
    • Wang, C. C., and Tsou, C. L. (1991). The insulin A and B-chains contain sufficient structural information to form the native molecule. Trends Biochem Sci 16, 279-281.
    • (1991) Trends Biochem Sci , vol.16 , pp. 279-281
    • Wang, C.C.1    Tsou, C.L.2
  • 106
    • 76649144177 scopus 로고    scopus 로고
    • A brief account on the study of the insulin crystal structure
    • Wang, D. C. G., and Gu, X. C. (2010). A brief account on the study of the insulin crystal structure. Sin China Series C 53, 13-15.
    • (2010) Sin China Series C , vol.53 , pp. 13-15
    • Wang, D.C.G.1    Gu, X.C.2
  • 107
    • 0032918044 scopus 로고    scopus 로고
    • A mutation in the insulin 2 gene induces diabetes with severe pancreatic beta-cell dysfunction in the Mody mouse
    • Wang, J., Takeuchi, T., Tanaka, S., Kubo, S. K., Kayo, T., Lu, D., Takata, K., Koizumi, A., and Izumi, T. (1999). A mutation in the insulin 2 gene induces diabetes with severe pancreatic beta-cell dysfunction in the Mody mouse. J Clin Invest 103, 27-37.
    • (1999) J Clin Invest , vol.103 , pp. 27-37
    • Wang, J.1    Takeuchi, T.2    Tanaka, S.3    Kubo, S.K.4    Kayo, T.5    Lu, D.6    Takata, K.7    Koizumi, A.8    Izumi, T.9
  • 109
    • 1642468519 scopus 로고
    • The properties of protein fibers produced. Reversibly from soluble protein molecules
    • Waugh, D. F. (1941). The properties of protein fibers produced. Reversibly from soluble protein molecules. Am J Physiol 133, 484-P485.
    • (1941) Am J Physiol , vol.133
    • Waugh, D.F.1
  • 110
    • 0006567078 scopus 로고
    • The linkage of corpuscular protein molecules. I. A fibrous modification on insulin
    • Waugh, D. F. (1944). The linkage of corpuscular protein molecules. I. A fibrous modification on insulin. J Am Chem Soc 66, 663.
    • (1944) J Am Chem Soc , vol.66 , pp. 663
    • Waugh, D.F.1
  • 112
    • 0000335935 scopus 로고
    • A fibrous modification of insulin. I. The heat precipitate of insulin
    • Waugh, D. F. (1946b). A fibrous modification of insulin. I. The heat precipitate of insulin. J Am Chem Soc 68, 247-250.
    • (1946) J Am Chem Soc , vol.68 , pp. 247-250
    • Waugh, D.F.1
  • 113
    • 0034687669 scopus 로고    scopus 로고
    • Hierarchical protein "un-design": insulin's intrachain disulfide bridge tethers a recognition alpha-helix
    • Weiss, M. A., Hua, Q. X., Jia, W., Chu, Y. C., Wang, R. Y., and Katsoyannis, P. G. (2000). Hierarchical protein "un-design": insulin's intrachain disulfide bridge tethers a recognition alpha-helix. Biochemistry 39, 15429-15440.
    • (2000) Biochemistry , vol.39 , pp. 15429-15440
    • Weiss, M.A.1    Hua, Q.X.2    Jia, W.3    Chu, Y.C.4    Wang, R.Y.5    Katsoyannis, P.G.6
  • 115
    • 0003919736 scopus 로고
    • New York, NY: Higher Education Press and Springer-Verlag
    • Wuthrich, K. (1986). NMR of Proteins and Nucleic Acids (New York, NY: Higher Education Press and Springer-Verlag).
    • (1986) NMR of Proteins and Nucleic Acids
    • Wuthrich, K.1
  • 116
    • 3142579218 scopus 로고    scopus 로고
    • Diabetes-associated mutations in insulin: consecutive residues in the B-chain contact distinct domains of the insulin receptor
    • Xu, B., Hu, S. Q., Chu, Y. C., Huang, K., Nakagawa, S. H., Whittaker, J., Katsoyannis, P. G., and Weiss, M. A. (2004a). Diabetes-associated mutations in insulin: consecutive residues in the B-chain contact distinct domains of the insulin receptor. Biochemistry 43, 8356-8372.
    • (2004) Biochemistry , vol.43 , pp. 8356-8372
    • Xu, B.1    Hu, S.Q.2    Chu, Y.C.3    Huang, K.4    Nakagawa, S.H.5    Whittaker, J.6    Katsoyannis, P.G.7    Weiss, M.A.8
  • 118
    • 67649827251 scopus 로고    scopus 로고
    • Decoding the cryptic active conformation of a protein by synthetic photoscanning: insulin inserts a detachable arm between receptor domains
    • Xu, B., Huang, K., Chu, Y. C., Hu, S. Q., Nakagawa, S., Wang, S., Wang, R. Y., Whittaker, J., Katsoyannis, P. G., and Weiss, M. A. (2009). Decoding the cryptic active conformation of a protein by synthetic photoscanning: insulin inserts a detachable arm between receptor domains. J Biol Chem 284, 14597-14608.
    • (2009) J Biol Chem , vol.284 , pp. 14597-14608
    • Xu, B.1    Huang, K.2    Chu, Y.C.3    Hu, S.Q.4    Nakagawa, S.5    Wang, S.6    Wang, R.Y.7    Whittaker, J.8    Katsoyannis, P.G.9    Weiss, M.A.10
  • 119
    • 0037377495 scopus 로고    scopus 로고
    • A peptide model of insulin folding intermediate with one disulfide
    • Yan, H., Guo, Z. Y., Gong, X. W., Xi, D., and Feng, Y. M. (2003). A peptide model of insulin folding intermediate with one disulfide. Protein Sci 12, 768-775.
    • (2003) Protein Sci , vol.12 , pp. 768-775
    • Yan, H.1    Guo, Z.Y.2    Gong, X.W.3    Xi, D.4    Feng, Y.M.5
  • 120
    • 0030907296 scopus 로고    scopus 로고
    • A novel locus, Mody4, distal to D7Mit189 on chromosome 7 determines early-onset NIDDM in nonobese C57BL/6 (Akita) mutant mice
    • Yoshioka, M., Kayo, T., Ikeda, T., and Koizumi, A. (1997). A novel locus, Mody4, distal to D7Mit189 on chromosome 7 determines early-onset NIDDM in nonobese C57BL/6 (Akita) mutant mice. Diabetes 46, 887-894.
    • (1997) Diabetes , vol.46 , pp. 887-894
    • Yoshioka, M.1    Kayo, T.2    Ikeda, T.3    Koizumi, A.4
  • 121
    • 0014182530 scopus 로고
    • Synthesis of an insulin B-chain disulfide polymer
    • Zahn, H., and Schmidt, G. (1967). Synthesis of an insulin B-chain disulfide polymer. Tetrahedron Lett 50, 5095-5098.
    • (1967) Tetrahedron Lett , vol.50 , pp. 5095-5098
    • Zahn, H.1    Schmidt, G.2
  • 122
    • 0034660242 scopus 로고    scopus 로고
    • Conformational correlation and coupled motion between residue A21 and B25 side chain observed in crystal structures of insulin mutants at position A21
    • Zeng, Z. H., Liu, Y. S., Jin, L., Zhang, Y., Havelund, S., Markussen, J., and Wang, D. C. (2000). Conformational correlation and coupled motion between residue A21 and B25 side chain observed in crystal structures of insulin mutants at position A21. Biochim Biophys Acta 1479, 225-236.
    • (2000) Biochim Biophys Acta , vol.1479 , pp. 225-236
    • Zeng, Z.H.1    Liu, Y.S.2    Jin, L.3    Zhang, Y.4    Havelund, S.5    Markussen, J.6    Wang, D.C.7
  • 123
    • 76649103701 scopus 로고    scopus 로고
    • The first protein ever synthesized in vitro
    • Zhang, Y. S. (2010). The first protein ever synthesized in vitro. Sin China Series C 53, 16-18.
    • (2010) Sin China Series C , vol.53 , pp. 16-18
    • Zhang, Y.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.