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Volumn 2, Issue OCT, 2011, Pages

Conformational dynamics of insulin

Author keywords

Amide proton exchange; Diabetes mellitus; Hydrogen bond; NMR spectroscopy; Protein Dynamics; Protein Engineering; Protein structure; Protein Therapeutics

Indexed keywords


EID: 84874384424     PISSN: None     EISSN: 16642392     Source Type: Journal    
DOI: 10.3389/fendo.2011.00048     Document Type: Article
Times cited : (27)

References (91)
  • 2
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Bai, Y., Milne, J. S., Mayne, L., and Eng-lander, S. W. (1993). Primary structure effects on peptide group hydrogen exchange. Proteins 17, 75-86.
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Eng-lander, S.W.4
  • 3
    • 0030479856 scopus 로고    scopus 로고
    • Physicochemical basis for the rapid time-action of LysB28ProB29-insulin: dissociation of a protein-ligand complex
    • Bakaysa, D. L., Radziuk, J., Havel, H. A., Brader, M. L., Li, S., Dodd, S. W., Beals, J. M., Pekar, A. H., and Brems, D. N. (1996). Physicochemical basis for the rapid time-action of LysB28ProB29-insulin: dissociation of a protein-ligand complex. Protein Sci. 5, 2521-2531.
    • (1996) Protein Sci , vol.5 , pp. 2521-2531
    • Bakaysa, D.L.1    Radziuk, J.2    Havel, H.A.3    Brader, M.L.4    Li, S.5    Dodd, S.W.6    Beals, J.M.7    Pekar, A.H.8    Brems, D.N.9
  • 7
    • 0026659078 scopus 로고
    • Chemical stability of insulin
    • Brange, J., Havelund, S., and Hougaard, P. (1992b). Chemical stability of insulin. 2. Formation of higher molecular weight transformation products during storage of pharmaceutical preparations. Pharm. Res. 9, 727-734.
    • (1992) Pharm. Res. , vol.9 , pp. 727-734
    • Brange, J.1    Havelund, S.2    Hougaard, P.3
  • 8
    • 0027863980 scopus 로고
    • Insulin structure and stability
    • Brange, J., and Langkjoer, L. (1993). Insulin structure and stability. Pharm. Biotechnol. 5, 315-350.
    • (1993) Pharm. Biotechnol. , vol.5 , pp. 315-350
    • Brange, J.1    Langkjoer, L.2
  • 13
    • 0029913517 scopus 로고    scopus 로고
    • Insulin lispro: its role in the treatment of dia-betes mellitus
    • Campbell, R. K., Campbell, L. K., and White, J. R. (1996). Insulin lispro: its role in the treatment of dia-betes mellitus. Ann. Pharmacother. 30, 1263-1271.
    • (1996) Ann. Pharmacother. , vol.30 , pp. 1263-1271
    • Campbell, R.K.1    Campbell, L.K.2    White, J.R.3
  • 14
  • 15
    • 0020614069 scopus 로고
    • Transmission of conforma-tional change in insulin
    • Chothia, C., Lesk, A. M., Dod-son, G. G., and Hodgkin, D. C. (1983). Transmission of conforma-tional change in insulin. Nature 302, 500-505.
    • (1983) Nature , vol.302 , pp. 500-505
    • Chothia, C.1    Lesk, A.M.2    Dod-son, G.G.3    Hodgkin, D.C.4
  • 16
    • 0026489072 scopus 로고
    • The A14 position of insulin tolerates con-siderable structural alterations with modest effects on the biological behavior of the hormone
    • Chu, Y. C., Zong, L., Burke, G. T., and Katsoyannis, P. G. (1992). The A14 position of insulin tolerates con-siderable structural alterations with modest effects on the biological behavior of the hormone. J. Protein Chem. 11, 571-577.
    • (1992) J. Protein Chem. , vol.11 , pp. 571-577
    • Chu, Y.C.1    Zong, L.2    Burke, G.T.3    Katsoyannis, P.G.4
  • 17
    • 0029644942 scopus 로고
    • Role of C-terminal B-chain residues in insulin assembly: the structure of hexam-eric LysB28ProB29-human insulin
    • Ciszak, E., Beals, J. M., Frank, B. H., Baker, J. C., Carter, N. D., and Smith, G. D. (1995). Role of C-terminal B-chain residues in insulin assembly: the structure of hexam-eric LysB28ProB29-human insulin. Structure 3, 615-622.
    • (1995) Structure , vol.3 , pp. 615-622
    • Ciszak, E.1    Beals, J.M.2    Frank, B.H.3    Baker, J.C.4    Carter, N.D.5    Smith, G.D.6
  • 18
    • 84892598945 scopus 로고    scopus 로고
    • Protein Struc-ture: A Practical Approach. Oxford: IRL Press at Oxford University Press. De Meyts, P., and Whittaker, J. (2002). Structural biology of insulin and IGF1 receptors: implications for drug design
    • Creighton, T. E. (1997). Protein Struc-ture: A Practical Approach. Oxford: IRL Press at Oxford University Press. 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.
    • (1997) Nat. Rev. Drug Discov. , vol.1 , pp. 769-783
    • Creighton, T.E.1
  • 19
    • 0035032976 scopus 로고    scopus 로고
    • Insulin self-association and the relationship to pharmacokinetics and pharmacody-namics
    • DeFelippis, M. R., Chance, R. E., and Frank, B. H. (2001). Insulin self-association and the relationship to pharmacokinetics and pharmacody-namics. Crit. Rev. Ther. Drug Carrier Syst. 18, 201-264.
    • (2001) Crit. Rev. Ther. Drug Carrier Syst. , vol.18 , pp. 201-264
    • DeFelippis, M.R.1    Chance, R.E.2    Frank, B.H.3
  • 20
    • 0032054714 scopus 로고    scopus 로고
    • The role of assembly in insulin's biosyn-thesis
    • Dodson, G., and Steiner, D. (1998). The role of assembly in insulin's biosyn-thesis. Curr. Opin. Struct. Biol. 8, 189-194.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 189-194
    • Dodson, G.1    Steiner, D.2
  • 23
    • 18144365198 scopus 로고    scopus 로고
    • Insulin glulisine: a new rapid-acting insulin analogue for the treatment of diabetes
    • Garg, S. K., Ellis, S. L., and Ulrich, H. (2005). Insulin glulisine: a new rapid-acting insulin analogue for the treatment of diabetes. Expert Opin. Pharmacother. 6, 643-651.
    • (2005) Expert Opin. Pharmacother. , vol.6 , pp. 643-651
    • Garg, S.K.1    Ellis, S.L.2    Ulrich, H.3
  • 25
    • 27744560042 scopus 로고    scopus 로고
    • Muta-tional analysis of the absolutely con-served B8Gly: consequence on fold-ability and activity of insulin
    • Guo, Z. Y., Zhang, Z., Jia, X. Y., Tang, Y. H., and Feng, Y. M. (2005). Muta-tional analysis of the absolutely con-served B8Gly: consequence on fold-ability and activity of insulin. Acta Biochim. Biophys. Sin. (Shanghai) 10, 673-679.
    • (2005) Acta Biochim. Biophys. Sin. (Shanghai) , vol.10 , pp. 673-679
    • Guo, Z.Y.1    Zhang, Z.2    Jia, X.Y.3    Tang, Y.H.4    Feng, Y.M.5
  • 27
    • 0037303597 scopus 로고    scopus 로고
    • Functional intensified insulin therapy with short-acting insulin analog: effects on HbA1c and frequency of severe hypoglycemia
    • Hartemann-Heurtier, A., Sachon, C., Masseboeuf, N., Corset, E., and Grimaldi, A. (2003). Functional intensified insulin therapy with short-acting insulin analog: effects on HbA1c and frequency of severe hypoglycemia. An observational cohort study. Diabetes Metab. 29, 53-57.
    • (2003) Diabetes Metab , vol.29 , pp. 53-57
    • Hartemann-Heurtier, A.1    Sachon, C.2    Masseboeuf, N.3    Corset, E.4    Grimaldi, A.5
  • 28
    • 58149165212 scopus 로고    scopus 로고
    • Insulin analogs: impact on treatment, success, satis-faction,quality of life and adherence
    • Hartman, I. (2008). Insulin analogs: impact on treatment, success, satis-faction,quality of life and adherence. Clin. Med. Res. 6, 54-67.
    • (2008) Clin. Med. Res. , vol.6 , pp. 54-67
    • Hartman, I.1
  • 29
    • 0026018780 scopus 로고
    • A new method for building protein conformations from sequence align-ments with homologues of known structure
    • Havel, T. F., and Snow, M. E. (1991). A new method for building protein conformations from sequence align-ments with homologues of known structure. J. Mol. Biol. 217, 1-7.
    • (1991) J. Mol. Biol. , vol.217 , pp. 1-7
    • Havel, T.F.1    Snow, M.E.2
  • 30
    • 0026572081 scopus 로고
    • Disulfide exchange folding of insulin-like growth factor I
    • Hober, S., Forsberg, G., Palm, G., Hartmanis, M., and Nilsson, B. (1992). Disulfide exchange folding of insulin-like growth factor I. Bio-chemistry 31, 1749-1756.
    • (1992) Bio-chemistry , vol.31 , pp. 1749-1756
    • Hober, S.1    Forsberg, G.2    Palm, G.3    Hartmanis, M.4    Nilsson, B.5
  • 31
    • 0028332083 scopus 로고
    • Fold-ing of insulin-like growth fac-tor I is thermodynamically con-trolled by insulin-like growth fac-tor binding protein
    • Hober, S., Hansson, A., Uhlen, M., and Nilsson, B. (1994). Fold-ing of insulin-like growth fac-tor I is thermodynamically con-trolled by insulin-like growth fac-tor binding protein. Biochemistry 33, 6758-6761.
    • (1994) Biochemistry , vol.33 , pp. 6758-6761
    • Hober, S.1    Hansson, A.2    Uhlen, M.3    Nilsson, B.4
  • 34
    • 79953185744 scopus 로고    scopus 로고
    • Insulin: a small protein with a long journey
    • Hua, Q. (2010). Insulin: a small protein with a long journey. Protein Cell 1, 537-551.
    • (2010) Protein Cell , vol.1 , pp. 537-551
    • Hua, Q.1
  • 35
    • 0037044828 scopus 로고    scopus 로고
    • Mech-anism of insulin chain combination Asymmetric roles of A-chain alpha-helices in disulfide pairing
    • Hua, Q. X., Chu, Y. C., Jia, W., Phillips, N. B., Wang, R. Y., Katsoyannis, P. G., and Weiss, M. A. (2002a). Mech-anism 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.B.4    Wang, R.Y.5    Katsoyannis, P.G.6    Weiss, M.A.7
  • 36
    • 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. B., 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.B.4    Weiss, M.A.5
  • 39
    • 0029991679 scopus 로고    scopus 로고
    • Native and non-native structure in a protein-folding intermediate: spec-troscopic 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: spec-troscopic 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
  • 41
    • 0027162763 scopus 로고
    • Comparison of the dynamics of an engineered insulin monomer and dimer by acid-quenched amide proton exchange Non-local stabilization of interchain hydrogen bonds by dimerization
    • Hua, Q. X., Jia, W., Frank, B. H., and Weiss, M. A. (1993). Comparison of the dynamics of an engineered insulin monomer and dimer by acid-quenched amide proton exchange. Non-local stabilization of interchain hydrogen bonds by dimerization. J. Mol. Biol. 230, 387-394.
    • (1993) J. Mol. Biol. , vol.230 , pp. 387-394
    • Hua, Q.X.1    Jia, W.2    Frank, B.H.3    Weiss, M.A.4
  • 42
    • 33747641643 scopus 로고    scopus 로고
    • A conserved histidine in insulin is required for the foldability of human proinsulin Structure and function of an AlaB5 analog
    • Hua, Q. X., Liu, M., Hu, S. Q., Jia, W., Arvan, P., and Weiss, M. A. (2006a). A conserved histidine in insulin is required for the foldability of human proinsulin. Structure and function of an AlaB5 analog. J. Biol. Chem. 281, 24889-24899.
    • (2006) J. Biol. Chem. , vol.281 , pp. 24889-24899
    • Hua, Q.X.1    Liu, M.2    Hu, S.Q.3    Jia, W.4    Arvan, P.5    Weiss, M.A.6
  • 43
    • 33748785712 scopus 로고    scopus 로고
    • The folding nucleus of the insulin super-family: a flexible peptide model fore-shadows the native state
    • Hua, Q. X., Mayer, J., Jia, W., Zhang, J., and Weiss, M. A. (2006b). The folding nucleus of the insulin super-family: a flexible peptide model fore-shadows the native state. J. Biol. Chem. 281, 28131-28142.
    • (2006) J. Biol. Chem. , vol.281 , pp. 28131-28142
    • Hua, Q.X.1    Mayer, J.2    Jia, W.3    Zhang, J.4    Weiss, M.A.5
  • 44
    • 33747670241 scopus 로고    scopus 로고
    • Toward the active con-formation 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 con-formation 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
  • 45
    • 0035899983 scopus 로고    scopus 로고
    • Katsoyan-nis, P. G., and Weiss, M. A
    • Hua, Q. X., Nakagawa, S. H., Jia, W., Hu, S. Q., Chu, Y. C., Katsoyan-nis, P. G., and Weiss, M. A. (2001). Hierarchical protein folding: asym-metric unfolding of an insulin ana-logue 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
  • 46
    • 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
  • 47
    • 0025996911 scopus 로고
    • Recep-tor binding redefined by a structural switch in a mutant human insulin
    • Hua, Q. X., Shoelson, S. E., Kochoyan, M., and Weiss, M. A. (1991). Recep-tor 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
  • 48
    • 0025251933 scopus 로고
    • Toward the solution struc-ture of human insulin: sequential 2D 1H NMR assignment of a des-pentapeptide analogue and compar-ison with crystal structure
    • Hua, Q. X., and Weiss, M. A. (1990). Toward the solution struc-ture of human insulin: sequential 2D 1H NMR assignment of a des-pentapeptide analogue and compar-ison with crystal structure. Biochem-istry 29, 10545-10555.
    • (1990) Biochem-istry , vol.29 , pp. 10545-10555
    • Hua, Q.X.1    Weiss, M.A.2
  • 49
    • 0025778802 scopus 로고
    • Comparative 2D NMR studies of human insulin and des-pentapeptide insulin: sequential resonance assignment and impli-cations 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 impli-cations 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
  • 50
    • 33744834546 scopus 로고    scopus 로고
    • The relationship between the con-necting peptide of recombined sin-gle chain insulin and its biological function
    • Huang,Y., Liang, Z., and Feng,Y. (2001). The relationship between the con-necting peptide of recombined sin-gle chain insulin and its biological function. Sci. China C Life Sci. 44, 593-600.
    • (2001) Sci. China C Life Sci. , vol.44 , pp. 593-600
    • Huang, Y.1    Liang, Z.2    Feng, Y.3
  • 51
    • 79955394050 scopus 로고    scopus 로고
    • Individualizing glycemic targets in type 2 diabetes mellitus: implications of recent clin-ical trials
    • Ismail-Beigi, F., Moghissi, E., Tiktin, M., Hirsch, I. B., Inzucchi, S. E., and Genuth, S. (2011). Individualizing glycemic targets in type 2 diabetes mellitus: implications of recent clin-ical trials. Ann. Intern. Med. 154, 554-559.
    • (2011) Ann. Intern. Med. , vol.154 , pp. 554-559
    • Ismail-Beigi, F.1    Moghissi, E.2    Tiktin, M.3    Hirsch, I.B.4    Inzucchi, S.E.5    Genuth, S.6
  • 52
    • 0142241183 scopus 로고    scopus 로고
    • Peptide models of four pos-sible 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 pos-sible 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
  • 54
    • 0014026175 scopus 로고
    • Synthesis of insulin
    • Katsoyannis, P. G. (1966). Synthesis of insulin. Science 154, 1509-1514.
    • (1966) Science , vol.154 , pp. 1509-1514
    • Katsoyannis, P.G.1
  • 56
  • 58
    • 0030614323 scopus 로고    scopus 로고
    • ASPB10 insulin induction of increased mitogenic responses and phenotypic changes in human breast epithelial
    • Milazzo, G., Sciacca, L., Papa, V., Goldfine, I. D., and Vigneri, R. (1997). ASPB10 insulin induction of increased mitogenic responses and phenotypic changes in human breast epithelial. Mol. Carcinog. 18, 19-25.
    • (1997) Mol. Carcinog. , vol.18 , pp. 19-25
    • Milazzo, G.1    Sciacca, L.2    Papa, V.3    Goldfine, I.D.4    Vigneri, R.5
  • 59
  • 60
    • 0033586410 scopus 로고    scopus 로고
    • Prob-ing the disulfide folding pathway of insulin-like growth factor-I
    • Milner, S. J., Carver, J. A., Ballard, F. J., and Francis, G. L. (1999). Prob-ing the disulfide folding pathway of insulin-like growth factor-I. Biotech-nol. Bioeng. 62, 693-703.
    • (1999) Biotech-nol. Bioeng. , vol.62 , pp. 693-703
    • Milner, S.J.1    Carver, J.A.2    Ballard, F.J.3    Francis, G.L.4
  • 61
    • 16344376210 scopus 로고    scopus 로고
    • Chi-ral mutagenesis of insulin
    • Nakagawa, S. H., Zhao, M., Hua, Q. X., Hu, S. Q., Wan, Z. L., Jia, W., and Weiss, M. A. (2005). Chi-ral mutagenesis of insulin. Fold-ability 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
  • 62
    • 29144453326 scopus 로고    scopus 로고
    • Intensive diabetes treatment and cardiovas-cular disease in patients with type 1 diabetes
    • DCCT/EDIC Study Research Group
    • Nathan, D. M., Cleary, P. A., Back-lund, J. Y., Genuth, S. M., Lachin, J. M., Orchard, T. J., Raskin, P., Zin-man, B., and DCCT/EDIC Study Research Group. (2005). Intensive diabetes treatment and cardiovas-cular disease in patients with type 1 diabetes. N. Engl. J. Med. 353, 2643-2653.
    • (2005) N. Engl. J. Med. , vol.353 , pp. 2643-2653
    • Nathan, D.M.1    Cleary, P.A.2    Back-lund, J.Y.3    Genuth, S.M.4    Lachin, J.M.5    Orchard, T.J.6    Raskin, P.7    Zin-man, B.8
  • 63
    • 0034334566 scopus 로고    scopus 로고
    • Implications of the United Kingdom Prospective Diabetes Study (UKPDS) results on patient management
    • Nicollerat, J. A. (2000). Implications of the United Kingdom Prospective Diabetes Study (UKPDS) results on patient management. Diabetes Educ. 26(Suppl.), 8-10.
    • (2000) Diabetes Educ , vol.26 , Issue.SUPPL. , pp. 8-10
    • Nicollerat, J.A.1
  • 64
    • 0042528355 scopus 로고    scopus 로고
    • Global epidemic of type 2 diabetes: implications for develop-ing countries
    • Osei, K. (2003). Global epidemic of type 2 diabetes: implications for develop-ing countries. Ethn. Dis. 13, S102-S106.
    • (2003) Ethn. Dis. , vol.13
    • Osei, K.1
  • 65
    • 0035814878 scopus 로고    scopus 로고
    • Putative disulfide-forming pathway of porcine insulin precur-sor during its refolding in vitro
    • Qiao, Z. S., Guo, Z. Y., and Feng, Y. M. (2001). Putative disulfide-forming pathway of porcine insulin precur-sor 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
  • 66
    • 0038043253 scopus 로고    scopus 로고
    • In vitro refolding of human proinsulin. Kinetic inter-mediates, putative disulfide-forming pathway, folding initiation site, and protential role of C-peptide in fold-ing 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 inter-mediates, putative disulfide-forming pathway, folding initiation site, and protential role of C-peptide in fold-ing 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
  • 67
    • 66649123653 scopus 로고    scopus 로고
    • Single-chain insulins as receptor agonists
    • Rajpal,G.,Liu,M.,Zhang,Y.,and Arvan, P. (2009). Single-chain insulins as receptor agonists. Mol. Endocrinol. 23, 679-688.
    • (2009) Mol. Endocrinol. , vol.23 , pp. 679-688
    • Rajpal, G.1    Liu, M.2    Zhang, Y.3    Arvan, P.4
  • 68
    • 0345711504 scopus 로고    scopus 로고
    • Use of insulin lispro in continuous subcutaneous insulin infusion treatment. Results of a mul-ticenter trial. German Humalog-CSII Study Group
    • Renner, R., Pfutzner,A., Trautmann, M., Harzer, O., Sauter, K., and Land-graf, R. (1999). Use of insulin lispro in continuous subcutaneous insulin infusion treatment. Results of a mul-ticenter trial. German Humalog-CSII Study Group. Diabetes Care 22, 784-788.
    • (1999) Diabetes Care , vol.22 , pp. 784-788
    • Renner, R.1    Pfutzner, A.2    Trautmann, M.3    Harzer, O.4    Sauter, K.5    Land-graf, R.6
  • 69
    • 77956640139 scopus 로고    scopus 로고
    • Effects of inten-sive glucose lowering in the man-agement of patients with type 2 dia-betes mellitus in the Action to Con-trol Cardiovascular Risk in Diabetes (ACCORD) trial
    • Riddle, M. C. (2010). Effects of inten-sive glucose lowering in the man-agement of patients with type 2 dia-betes mellitus in the Action to Con-trol Cardiovascular Risk in Diabetes (ACCORD) trial. Circulation 122, 844-846.
    • (2010) Circulation , vol.122 , pp. 844-846
    • Riddle, M.C.1
  • 70
    • 0024331090 scopus 로고
    • Structural charac-terization of protein folding inter-mediates by proton magnetic reso-nance and hydrogen exchange
    • Roder, H. (1989). Structural charac-terization of protein folding inter-mediates by proton magnetic reso-nance and hydrogen exchange. Meth. Enzymol. 176, 446-473.
    • (1989) Meth. Enzymol. , vol.176 , pp. 446-473
    • Roder, H.1
  • 71
    • 0022399120 scopus 로고
    • Amide proton exchange in proteins by EX1 kinetics: studies of the basic pancreatic trypsin inhibitor at variable p2H and temperature
    • Roder, H., Wagner, G., and Wüthrich, K. (1985). Amide proton exchange in proteins by EX1 kinetics: studies of the basic pancreatic trypsin inhibitor at variable p2H and temperature. Biochemistry 24, 7396-7407.
    • (1985) Biochemistry , vol.24 , pp. 7396-7407
    • Roder, H.1    Wagner, G.2    Wüthrich, K.3
  • 72
    • 0035936763 scopus 로고    scopus 로고
    • New perspectives into the molecular pathogenesis and treatment of type-2 diabetes
    • Saltiel, A. R. (2001). New perspectives into the molecular pathogenesis and treatment of type-2 diabetes. Cell 104, 517-529.
    • (2001) Cell , vol.104 , pp. 517-529
    • Saltiel, A.R.1
  • 74
  • 75
    • 0026548864 scopus 로고
    • Mutations at the dimer, hexamer, and receptor-binding, sur-faces 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, sur-faces 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
  • 76
    • 0034045782 scopus 로고    scopus 로고
    • Application of circu-lar dichroism to study RNA fold-ing transitions
    • Sosnick, T. R., Fang, X., and Shelton, V. M. (2000). Application of circu-lar dichroism to study RNA fold-ing transitions. Meth. Enzymol. 317, 393-409.
    • (2000) Meth. Enzymol. , vol.317 , pp. 393-409
    • Sosnick, T.R.1    Fang, X.2    Shelton, V.M.3
  • 77
    • 0014146156 scopus 로고
    • Evidence for a pre-cursor in the biosynthesis of insulin
    • Steiner, D. F. (1967). Evidence for a pre-cursor 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
  • 79
    • 0025372089 scopus 로고
    • The insulin A and B chains contain struc-tural information for the forma-tion of the native molecule
    • Tang, J. G., and Tsou, C. L. (1990). The insulin A and B chains contain struc-tural information for the forma-tion of the native molecule. Studies with protein disulphide-isomerase. Biochem. J. 268, 429-435.
    • (1990) Studies with protein disulphide-isomerase. Biochem. J. , vol.268 , pp. 429-435
    • Tang, J.G.1    Tsou, C.L.2
  • 80
    • 0027370108 scopus 로고
    • The effect of intensive treatment of diabetes on the development and progres-sion of long-term complications in insulin-dependent diabetes mellitus
    • The Diabetes Control Group and Complications Trial Research Group
    • The Diabetes Control Group and Complications Trial Research Group. (1993). The effect of intensive treatment of diabetes on the development and progres-sion of long-term complications in insulin-dependent diabetes mellitus. N.Engl.J.Med.329, 977-986.
    • (1993) N. Engl. J. Med. , vol.329 , pp. 977-986
  • 81
    • 33745844324 scopus 로고    scopus 로고
    • Diabetes mellitus: compli-cations and therapeutics
    • Tripathi, B. K., and Srivastava, A. K. (2006). Diabetes mellitus: compli-cations and therapeutics. Med. Sci. Monit. 12, RA130-RA147.
    • (2006) Med. Sci. Monit. , vol.12
    • Tripathi, B.K.1    Srivastava, A.K.2
  • 82
    • 0022555889 scopus 로고
    • Observation of internal motility of proteins by nuclear magnetic reso-nance in solution
    • Wagner, G., and Wüthrich, K. (1986). Observation of internal motility of proteins by nuclear magnetic reso-nance in solution. Meth. Enzymol. 131, 307-326.
    • (1986) Meth. Enzymol. , vol.131 , pp. 307-326
    • Wagner, G.1    Wüthrich, K.2
  • 83
    • 0025777247 scopus 로고
    • The insulin A and B chains contain suffi-cient structural information to form the native molecule
    • Wang, C. C., and Tsou, C. L. (1991). The insulin A and B chains contain suffi-cient 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
  • 84
    • 67749096213 scopus 로고    scopus 로고
    • Proinsulin and the genetics of diabetes mellitus
    • Weiss, M. A. (2009). Proinsulin and the genetics of diabetes mellitus. J. Biol. Chem. 284, 19159-19163.
    • (2009) J. Biol. Chem. , vol.284 , pp. 19159-19163
    • Weiss, M.A.1
  • 85
    • 0024992662 scopus 로고
    • NMR and photo-CIDNP studies of human proinsulin and prohormone pro-cessing intermediates with applica-tion to endopeptidase recognition
    • Weiss, M. A., Frank, B. H., Khait, I., Pekar, A., Heiney, R., Shoelson, S. E., and Neuringer, L. J. (1990). NMR and photo-CIDNP studies of human proinsulin and prohormone pro-cessing intermediates with applica-tion to endopeptidase recognition. Biochemistry 29, 8389-8401.
    • (1990) Biochemistry , vol.29 , pp. 8389-8401
    • Weiss, M.A.1    Frank, B.H.2    Khait, I.3    Pekar, A.4    Heiney, R.5    Shoelson, S.E.6    Neuringer, L.J.7
  • 86
    • 0025718640 scopus 로고
    • Heteronuclear 2D NMR studies of an engineered insulin monomer: assignment and characterization of the receptor-binding surface by selective 2H and 13C labeling with application to protein design
    • Weiss, M. A., Hua, Q. X., Lynch, C. S., Frank, B. H., and Shoel-son, S. E. (1991). Heteronuclear 2D NMR studies of an engineered insulin monomer: assignment and characterization of the receptor-binding surface by selective 2H and 13C labeling with application to protein design. Biochemistry 30, 7373-7389.
    • (1991) Biochemistry , vol.30 , pp. 7373-7389
    • Weiss, M.A.1    Hua, Q.X.2    Lynch, C.S.3    Frank, B.H.4    Shoel-son, S.E.5
  • 87
    • 84874375822 scopus 로고
    • NMR of Proteins and Nucleic Acids.NewYork,NY: John Wiley & Sons
    • Wüthrich, K. (1986). NMR of Proteins and Nucleic Acids.NewYork,NY: John Wiley & Sons.
    • (1986)
    • Wüthrich, K.1
  • 88
    • 0018782084 scopus 로고
    • Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor
    • Wüthrich, K., and Wagner, G. (1979). Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor. J. Mol. Biol. 130, 1-18.
    • (1979) J. Mol. Biol. , vol.130 , pp. 1-18
    • Wüthrich, K.1    Wagner, G.2
  • 89
    • 77950915587 scopus 로고    scopus 로고
    • Solution structure of proinsulin: connecting domain flexibility and prohormone processing
    • Yang, Y., Hua, Q. X., Liu, J., Shimizu, E. H., Choquette, M. H., Mackin, R. B., and Weiss, M. A. (2010a). Solution structure of proinsulin: connecting domain flexibility and pro-hormone processing. J. Biol. Chem. 285, 7847-7851.
    • (2010) J. Biol. Chem. , vol.285 , pp. 7847-7851
    • Yang, Y.1    Hua, Q.X.2    Liu, J.3    Shimizu, E.H.4    Choquette, M.H.5    Mackin, R.B.6    Weiss, M.A.7
  • 91
    • 0031048313 scopus 로고    scopus 로고
    • Insulin lispro in CSII: results of a double-blind crossover study
    • Zinman, B., Tildesley, H., Chiasson, J. L., Tsui, E., and Strack, T. (1997). Insulin lispro in CSII: results of a double-blind crossover study. Dia-betes 46, 440-443
    • (1997) Dia-betes , vol.46 , pp. 440-443
    • Zinman, B.1    Tildesley, H.2    Chiasson, J.L.3    Tsui, E.4    Strack, T.5


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