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Volumn 277, Issue 1, 1998, Pages 103-118

Mini-proinsulin and Mini-IGF-I: Homologous protein sequences encoding non-homologous structures

Author keywords

Insulin; Insulin receptor; NMR; Protein folding; Transmembrane signaling

Indexed keywords

INSULIN RECEPTOR; PROINSULIN; SOMATOMEDIN C;

EID: 0032549666     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1574     Document Type: Article
Times cited : (52)

References (85)
  • 1
    • 0016809148 scopus 로고
    • Nonenzymic reactivation of reduced bovine pancreatic ribonuclease by air oxidation and by glutathione oxidoreduction buffers
    • Ahmed A.K., Schaffer S.W., Wetlaufer D.B. Nonenzymic reactivation of reduced bovine pancreatic ribonuclease by air oxidation and by glutathione oxidoreduction buffers. J. Biol. Chem. 250:1975;8477-8482
    • (1975) J. Biol. Chem. , vol.250 , pp. 8477-8482
    • Ahmed, A.K.1    Schaffer, S.W.2    Wetlaufer, D.B.3
  • 2
    • 0026577226 scopus 로고
    • Flexibility in crystalline insulins
    • Badger J. Flexibility in crystalline insulins. Biophys. J. 61:1992;816-819
    • (1992) Biophys. J. , vol.61 , pp. 816-819
    • Badger, J.1
  • 4
    • 0001926444 scopus 로고
    • E. Gross, Meienhofer J. New York: Academic Press Ltd
    • Barany G., Merrifield R.B. Gross E., Meienhofer J. The Peptides. vol. 2:1979;3-284 Academic Press Ltd, New York
    • (1979) The Peptides , vol.2 , pp. 3-284
    • Barany, G.1    Merrifield, R.B.2
  • 5
    • 0018233390 scopus 로고
    • The rhombohedral insulin crystal transformation
    • Bentley G., Dodson G., Lewitova A. The rhombohedral insulin crystal transformation. J. Mol. Biol. 126:1978;871-875
    • (1978) J. Mol. Biol. , vol.126 , pp. 871-875
    • Bentley, G.1    Dodson, G.2    Lewitova, A.3
  • 6
    • 77956751025 scopus 로고
    • Insulin: The structure in the crystal and its reflection in chemistry and biology
    • Blundell T.L., Dodson G.G., Hodgkin D.C., Mercola D.A. Insulin the structure in the crystal and its reflection in chemistry and biology. Advan. Protein Chem. 26:1972;279-402
    • (1972) Advan. Protein Chem. , vol.26 , pp. 279-402
    • Blundell, T.L.1    Dodson, G.G.2    Hodgkin, D.C.3    Mercola, D.A.4
  • 7
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three-dimensional structure
    • Bowie J.U., Luthy R., Eisenberg D. A method to identify protein sequences that fold into a known three-dimensional structure. Science. 253:1990;164-170
    • (1990) Science , vol.253 , pp. 164-170
    • Bowie, J.U.1    Luthy, R.2    Eisenberg, D.3
  • 11
    • 0025978597 scopus 로고
    • The conformational stability and flexibility of insulin with an additional intramolecular cross-link
    • Brems D.N., Brown P.L., Nakagawa S.H., Tager H.S. The conformational stability and flexibility of insulin with an additional intramolecular cross-link. J. Biol. Chem. 266:1991;1611-1615
    • (1991) J. Biol. Chem. , vol.266 , pp. 1611-1615
    • Brems, D.N.1    Brown, P.L.2    Nakagawa, S.H.3    Tager, H.S.4
  • 13
    • 0004283184 scopus 로고
    • New Haven, CT: Yale University Press
    • Brünger A.T. X-PLOR. 1992;Yale University Press, New Haven, CT
    • (1992) X-PLOR
    • Brünger, A.T.1
  • 16
    • 0020614069 scopus 로고
    • Transmission of conformational change in insulin
    • Chothia C., Lesk A.M., Dodson G.G., Hodskin D.C. Transmission of conformational change in insulin. Nature. 302:1983;500-505
    • (1983) Nature , vol.302 , pp. 500-505
    • Chothia, C.1    Lesk, A.M.2    Dodson, G.G.3    Hodskin, D.C.4
  • 18
    • 0018242265 scopus 로고
    • The chemical synthesis and biological evaluation of [1-L-alanine-A]-and 1-D-alanine-A]-insulins
    • Cosmatos A., Cheng K., Okada H., Katsoyannis P.G. The chemical synthesis and biological evaluation of [1-L-alanine-A]-and 1-D-alanine-A]-insulins. J. Biol. Chem. 253:1978;6586-6590
    • (1978) J. Biol. Chem. , vol.253 , pp. 6586-6590
    • Cosmatos, A.1    Cheng, K.2    Okada, H.3    Katsoyannis, P.G.4
  • 19
    • 0018569823 scopus 로고
    • Chemical synthesis of [des(tetrapeptide B27-30), Tyr(NH2)26-B] and [des(pentapeptide B26-30), Phe(NH2)25-B] bovine insulins
    • Cosmatos A., Ferderigos N., Katsoyannis P.G. Chemical synthesis of [des(tetrapeptide B27-30), Tyr(NH2)26-B] and [des(pentapeptide B26-30), Phe(NH2)25-B] bovine insulins. Int. J. Pep. Protein Res. 14:1979;457-471
    • (1979) Int. J. Pep. Protein Res. , vol.14 , pp. 457-471
    • Cosmatos, A.1    Ferderigos, N.2    Katsoyannis, P.G.3
  • 20
    • 0003139548 scopus 로고
    • Refinement of the structure of despentapetide (B26-B30) insulin at 1.5 Å resolution
    • Dai J.-B., Lou M.-Z., You J.-M., Liang D.-C. Refinement of the structure of despentapetide (B26-B30) insulin at 1.5 Å resolution. Sci. Sin. 30:1988;55-65
    • (1988) Sci. Sin. , vol.30 , pp. 55-65
    • Dai, J.-B.1    Lou, M.-Z.2    You, J.-M.3    Liang, D.-C.4
  • 23
    • 0025880180 scopus 로고
    • The 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.G., Markussen J. The X-ray analysis of the single chain B29-A1 peptide-linked insulin molecule a completely inactive analogue. J. Mol. Biol. 220:1991;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.G.5    Markussen, J.6
  • 26
    • 0019390868 scopus 로고
    • NA1, NA1, NA1-trimethylinsulin: An insulin analogue with a quaternary amino group at the A1 terminus
    • Drewes S.E., Magojo H.E., Gliemann J. NA1, NA1, NA1-trimethylinsulin an insulin analogue with a quaternary amino group at the A1 terminus. Hoppe-Seylers Z. Physiol. Chem. 362:1981;745-753
    • (1981) Hoppe-Seylers Z. Physiol. Chem. , vol.362 , pp. 745-753
    • Drewes, S.E.1    Magojo, H.E.2    Gliemann, J.3
  • 27
    • 0020628130 scopus 로고
    • Two routes for producing human insulin utilizing recombinant DNA technology
    • Frank B.H., Chance R.E. Two routes for producing human insulin utilizing recombinant DNA technology. MMW: Munchener Medizinische Wochenschrift. (Suppl. 1):1993;S14-S20
    • (1993) MMW: Munchener Medizinische Wochenschrift , Issue.SUPPL. 1
    • Frank, B.H.1    Chance, R.E.2
  • 28
    • 0028092036 scopus 로고
    • Improving insulin therapy: Achievements and challenges
    • Galloway J.A., Chance R.E. Improving insulin therapy achievements and challenges. Hormone Metabol. Res. 26:1994;591-598
    • (1994) Hormone Metabol. Res. , vol.26 , pp. 591-598
    • Galloway, J.A.1    Chance, R.E.2
  • 29
    • 10544225385 scopus 로고    scopus 로고
    • Engineering the C-region of human insulin-like growth factor-1: Implications for receptor binding
    • Gill R., Wallach B., Verma C., Urso B., De Wolf E., Grotzinger J. Engineering the C-region of human insulin-like growth factor-1 implications for receptor binding. Protein Eng. 9:1996;1011-1019
    • (1996) Protein Eng. , vol.9 , pp. 1011-1019
    • Gill, R.1    Wallach, B.2    Verma, C.3    Urso, B.4    De Wolf, E.5    Grotzinger, J.6
  • 30
    • 0016167531 scopus 로고
    • Zinc binding, circular dichroism, and equilibrium sedimentation studies of insulin (bovine) and several of its derivatives
    • Goldman J., Carpenter F.H. Zinc binding, circular dichroism, and equilibrium sedimentation studies of insulin (bovine) and several of its derivatives. Biochemistry. 13:1974;4566-4574
    • (1974) Biochemistry , vol.13 , pp. 4566-4574
    • Goldman, J.1    Carpenter, F.H.2
  • 31
    • 0015442509 scopus 로고
    • Increased coupling yields in solid-phase peptide synthesis with a modified carbodiimide coupling procedure
    • Hagenmaier H., Frank H. Increased coupling yields in solid-phase peptide synthesis with a modified carbodiimide coupling procedure. Hoppe-Seylers Z. Physiolo. Chem. 353:1972;1973-1976
    • (1972) Hoppe-Seylers Z. Physiolo. Chem. , vol.353 , pp. 1973-1976
    • Hagenmaier, H.1    Frank, H.2
  • 32
    • 0025932859 scopus 로고
    • An evaluation of computational strategies for use in the determination of protein structure from distance constraints obtained by nuclear magnetic resonance
    • Havel T.F. An evaluation of computational strategies for use in the determination of protein structure from distance constraints obtained by nuclear magnetic resonance. Prog. Biophys. Mol. Biol. 56:1991;43-78
    • (1991) Prog. Biophys. Mol. Biol. , vol.56 , pp. 43-78
    • Havel, T.F.1
  • 34
    • 0028332083 scopus 로고
    • Folding of insulin-like growth factor I is thermodynamically controlled by insulin-like growth factor binding protein
    • Hober S., Hansson A., Uhlen M., Nilsson B. Folding of insulin-like growth factor I is thermodynamically controlled by insulin-like growth factor binding protein. Biochemistry. 33:1994;6758-6761
    • (1994) Biochemistry , vol.33 , pp. 6758-6761
    • Hober, S.1    Hansson, A.2    Uhlen, M.3    Nilsson, B.4
  • 36
    • 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., Weiss M.A. Comparative 2D NMR studies of human insulin and des-pentapeptide insulin sequential resonance assignment and implications for protein dynamics and receptor recognition. Biochemistry. 30:1991;5505-5515
    • (1991) Biochemistry , vol.30 , pp. 5505-5515
    • Hua, Q.-X.1    Weiss, M.A.2
  • 37
    • 0025996911 scopus 로고
    • Receptor binding redefined by a structural switch in a mutant human insulin
    • Hua Q.-X., Shoelson S.E., Kochoyan M., Weiss M.A. Receptor binding redefined by a structural switch in a mutant human insulin. Nature. 354:1991;238-241
    • (1991) Nature , vol.354 , pp. 238-241
    • Hua, Q.-X.1    Shoelson, S.E.2    Kochoyan, M.3    Weiss, M.A.4
  • 38
    • 0027458937 scopus 로고
    • Paradoxial structure and function in a mutant human insulin associated with diabetes mellitus
    • Hua Q.-X., Shoelson S.E., Inouye K., Weiss M.A. Paradoxial structure and function in a mutant human insulin associated with diabetes mellitus. Proc. Natl. Acad. Sci. USA. 90:1993;582-586
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 582-586
    • Hua, Q.-X.1    Shoelson, S.E.2    Inouye, K.3    Weiss, M.A.4
  • 39
    • 0027162763 scopus 로고
    • Comparison of the dynamics of an engineered insulin monomer and dimer by acid-quenched amide proton exchange: Non-local stabilization of the interchain hydrogen bonds by dimerization
    • Hua Q.-X., Jia W., Frank B.H., Weiss M.A. Comparison of the dynamics of an engineered insulin monomer and dimer by acid-quenched amide proton exchange Non-local stabilization of the interchain hydrogen bonds by dimerization. J. Mol. Biol. 230:1993;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
  • 41
    • 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., Weiss M.A. 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. 259:1996;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
  • 43
    • 0026492003 scopus 로고
    • Three-dimensional solution structure of an insulin dimer. A study of the B9(Asp) mutant of an human insulin using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics
    • Jørgensen A.M.M., Kristensen S.M., Led J.J., Balschmidt P. Three-dimensional solution structure of an insulin dimer. A study of the B9(Asp) mutant of an human insulin using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics. J. Mol. Biol. 227:1992;1146-1163
    • (1992) J. Mol. Biol. , vol.227 , pp. 1146-1163
    • Jørgensen, A.M.M.1    Kristensen, S.M.2    Led, J.J.3    Balschmidt, P.4
  • 44
    • 0014026175 scopus 로고
    • Synthesis of insulin
    • Katsoyannis P.G. Synthesis of insulin. Science. 154:1966;1509-1514
    • (1966) Science , vol.154 , pp. 1509-1514
    • Katsoyannis, P.G.1
  • 45
    • 0014127321 scopus 로고
    • Studies on the synthesis of insulin from natural and synthetic A and B chains. I. Splitting of insulin and isolation of the S-sulfonated derivatives of the A and B chains
    • Katsoyannis P.G., Tometsko A., Zalut C., Johnson S., Trakatellis A.C. Studies on the synthesis of insulin from natural and synthetic A and B chains. I. Splitting of insulin and isolation of the S-sulfonated derivatives of the A and B chains. Biochemistry. 6:1967;2635-2642
    • (1967) Biochemistry , vol.6 , pp. 2635-2642
    • Katsoyannis, P.G.1    Tometsko, A.2    Zalut, C.3    Johnson, S.4    Trakatellis, A.C.5
  • 47
    • 0025613125 scopus 로고
    • Refinement of the NMR structures for acyl carrier protein with scalar coupling data
    • Kim Y., Prestegard J.H. Refinement of the NMR structures for acyl carrier protein with scalar coupling data. Proteins: Struct. Funct. Genet. 8:1990;377-385
    • (1990) Proteins: Struct. Funct. Genet. , vol.8 , pp. 377-385
    • Kim, Y.1    Prestegard, J.H.2
  • 52
    • 0028024708 scopus 로고
    • Comparative studies on the dynamics of crosslinked insulin
    • Kruger P., Hahnen J., Wollmer A. Comparative studies on the dynamics of crosslinked insulin. Eur. Biophys. J. 23:1994;177-187
    • (1994) Eur. Biophys. J. , vol.23 , pp. 177-187
    • Kruger, P.1    Hahnen, J.2    Wollmer, A.3
  • 53
    • 0346565748 scopus 로고
    • The possible mechanism of binding interaction of insulin molecule with its receptor
    • Liang D.C., Chang W.R., Zhang J.P., Wan Z.L. The possible mechanism of binding interaction of insulin molecule with its receptor. Sci. China, ser. B. 35:1992;547-557
    • (1992) Sci. China, ser. B , vol.35 , pp. 547-557
    • Liang, D.C.1    Chang, W.R.2    Zhang, J.P.3    Wan, Z.L.4
  • 54
    • 0028241787 scopus 로고
    • High-resolution structure of an engineered biologically potent insulin monomer, B16 Tyr→His, as determined by nuclear magnetic resonance spectroscopy
    • Ludvigsen S., Roy M., Tørgersen H., Kaarsholm N.C. High-resolution structure of an engineered biologically potent insulin monomer, B16 Tyr→His, as determined by nuclear magnetic resonance spectroscopy. Biochemistry. 33:1994;7998-8006
    • (1994) Biochemistry , vol.33 , pp. 7998-8006
    • Ludvigsen, S.1    Roy, M.2    Tørgersen, H.3    Kaarsholm, N.C.4
  • 55
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy R., Bowie J.U., Eisenberg D. Assessment of protein models with three-dimensional profiles. Nature. 356:1991;83-85
    • (1991) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 56
    • 0022003687 scopus 로고
    • Comparative reduction/oxidation studies with single chain des-(B30) insulin and porcine proinsulin
    • Markussen J. Comparative reduction/oxidation studies with single chain des-(B30) insulin and porcine proinsulin. Int. J. Pept. Protein. Res. 25:1985;431-434
    • (1985) Int. J. Pept. Protein. Res. , vol.25 , pp. 431-434
    • Markussen, J.1
  • 58
    • 0001468029 scopus 로고
    • Soluble, prolonged-acting insulin derivatives. I. Degree of protraction and crystallizability of insulins substituted in the terminal of the B-chain
    • Markussen J., Hougaar P., Ribel U., Sorensen A.S., Sorensen E. Soluble, prolonged-acting insulin derivatives. I. Degree of protraction and crystallizability of insulins substituted in the terminal of the B-chain. Protein Eng. 1:1987;205-213
    • (1987) Protein Eng. , vol.1 , pp. 205-213
    • Markussen, J.1    Hougaar, P.2    Ribel, U.3    Sorensen, A.S.4    Sorensen, E.5
  • 59
    • 0023918646 scopus 로고
    • Soluble, prolonged-acting insulin derivatives. III. Degree of protraction, crystallizability, and chemical stability of insulins substituted in positions A21, B13, B23, B27 and B30
    • Markussen J., Diers I., Hougaard P., Langkjaer L., Norris K., Snel L., Sorensen A.R., Sorensen E., Voigt H.O. Soluble, prolonged-acting insulin derivatives. III. Degree of protraction, crystallizability, and chemical stability of insulins substituted in positions A21, B13, B23, B27 and B30. Protein Eng. 2:1988;157-166
    • (1988) Protein Eng. , vol.2 , pp. 157-166
    • Markussen, J.1    Diers, I.2    Hougaard, P.3    Langkjaer, L.4    Norris, K.5    Snel, L.6    Sorensen, A.R.7    Sorensen, E.8    Voigt, H.O.9
  • 60
    • 0020395778 scopus 로고
    • Synthesis of the antibacterial peptide cecropin A (1-33)
    • Merrifield R.B., Vizioli L.D., Boman H.G. Synthesis of the antibacterial peptide cecropin A (1-33). Biochemistry. 21:1982;5020-5031
    • (1982) Biochemistry , vol.21 , pp. 5020-5031
    • Merrifield, R.B.1    Vizioli, L.D.2    Boman, H.G.3
  • 62
    • 0024553746 scopus 로고
    • Role of the phenylalanine B24 side-chain in directing insulin interaction with its receptor
    • Mirmira R., Tager H.S. Role of the phenylalanine B24 side-chain in directing insulin interaction with its receptor. J. Biol. Chem. 264:1989;6349-6354
    • (1989) J. Biol. Chem. , vol.264 , pp. 6349-6354
    • Mirmira, R.1    Tager, H.S.2
  • 63
    • 0024587180 scopus 로고
    • Perturbation of insulin-receptor interactions by intramolecular hormone cross-linking. Analysis of relative movement among residues A1, B1, and B29
    • Nakagawa S.H., Tager H.S. Perturbation of insulin-receptor interactions by intramolecular hormone cross-linking. Analysis of relative movement among residues A1, B1, and B29. J. Biol. Chem. 264:1989;272-279
    • (1989) J. Biol. Chem. , vol.264 , pp. 272-279
    • Nakagawa, S.H.1    Tager, H.S.2
  • 64
    • 0026634650 scopus 로고
    • Importance of aliphatic side-chain structure at positions 2 and 3 of the insulin A chain in insulin-receptor interactions
    • Nakagawa S.H., Tager H.S. Importance of aliphatic side-chain structure at positions 2 and 3 of the insulin A chain in insulin-receptor interactions. Biochemistry. 31:1992;3204-3214
    • (1992) Biochemistry , vol.31 , pp. 3204-3214
    • Nakagawa, S.H.1    Tager, H.S.2
  • 65
    • 0027311222 scopus 로고
    • Role of native disulfide bonds in the structure and activity of insulin-like growth factor I (IGF-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., Weiss M.A. Role of native disulfide bonds in the structure and activity of insulin-like growth factor I (IGF-1) genetic models of protein-folding intermediates. Biochemistry. 32:1993;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
  • 66
    • 0030015918 scopus 로고    scopus 로고
    • Solution structure of an engineered insulin monomer at neutral pH
    • Olsen H.B., Ludvigsen S., Kaarsholm N.C. Solution structure of an engineered insulin monomer at neutral pH. Biochemistry. 35:1996;8836-8845
    • (1996) Biochemistry , vol.35 , pp. 8836-8845
    • Olsen, H.B.1    Ludvigsen, S.2    Kaarsholm, N.C.3
  • 70
    • 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., Hua Q.-X., Lynch C.E., Weiss M.A. Mutations at the dimer, hexamer, and receptor-binding surfaces of insulin independently affect insulin-insulin and insulin-receptor interactions. Biochemistry. 31:1992;1757-1767
    • (1992) Biochemistry , vol.31 , pp. 1757-1767
    • Shoelson, S.E.1    Hua, Q.-X.2    Lynch, C.E.3    Weiss, M.A.4
  • 71
    • 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., Marki F., deGasparo M. 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-Seyler's Z. Physiol. Chem. 359:1978;113-123
    • (1978) Hoppe-Seyler's Z. Physiol. Chem. , vol.359 , pp. 113-123
    • Sieber, P.S.1    Eisler, K.2    Kamber, B.3    Riniker, B.4    Rittel, W.5    Marki, F.6    Degasparo, M.7
  • 74
    • 0026955771 scopus 로고
    • Structure of a rhombohedral R6 insulin/phenol complex
    • Smith G.D., Dodson G.G. Structure of a rhombohedral R6 insulin/phenol complex. Proteins: Struct. Funct. Genet. 14:1992;401-408
    • (1992) Proteins: Struct. Funct. Genet. , vol.14 , pp. 401-408
    • Smith, G.D.1    Dodson, G.G.2
  • 75
    • 0028557212 scopus 로고
    • The structure of a complex of hexameric insulin and 4′-hydroxyacetanilide
    • Smith G.D., Ciszak E. The structure of a complex of hexameric insulin and 4′-hydroxyacetanilide. Proc. Natl Acad. Sci. USA. 91:1994;8851-8855
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 8851-8855
    • Smith, G.D.1    Ciszak, E.2
  • 77
    • 0004188835 scopus 로고
    • L.J. DeGroot. Philadelphia, PA: W. S. Saunders Co
    • Steiner D.F., Bell G.I., Tager H.S. DeGroot L.J. Endocrinology. 1990;1263-1289 W. S. Saunders Co, Philadelphia, PA
    • (1990) Endocrinology , pp. 1263-1289
    • Steiner, D.F.1    Bell, G.I.2    Tager, H.S.3
  • 78
    • 45149137643 scopus 로고
    • Studies on the crystal structure of A1-(D-Tryptophan) insulin
    • Wan Z.L., Liang D.C. Studies on the crystal structure of A1-(D-Tryptophan) insulin. Sci. China. ser. B. 33:1990;810-820
    • (1990) Sci. China. ser. B , vol.33 , pp. 810-820
    • Wan, Z.L.1    Liang, D.C.2
  • 79
    • 0025777247 scopus 로고
    • The insulin A and B chains contain sufficient structural information to form the native molecule
    • Wang C.C., Tsou C.L. The insulin A and B chains contain sufficient structural information to form the native molecule. Trends Biochem. Sci. 16:1991;279-281
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 279-281
    • Wang, C.C.1    Tsou, C.L.2
  • 80
    • 0025876949 scopus 로고
    • Insulin analogues with modifications in the beta-turn of the B-chain
    • Wang S.H., Hu S.Q., Burke G.T., Katsoyannis P.G. Insulin analogues with modifications in the beta-turn of the B-chain. J. Protein Chem. 10:1991;313-324
    • (1991) J. Protein Chem. , vol.10 , pp. 313-324
    • Wang, S.H.1    Hu, S.Q.2    Burke, G.T.3    Katsoyannis, P.G.4
  • 82
    • 0024835166 scopus 로고
    • Two-dimensional NMR and photo-CIDNP studies of the insulin monomer: Assignment of aromatic resonances with application to protein folding, structure, and dynamics
    • Weiss M.A., Nguyen D.T., Khait I., Inouye K., Frank B.H., Beckage M., O'Shea E., Shoelson S.E., Karplus M., Neuringer L.J. Two-dimensional NMR and photo-CIDNP studies of the insulin monomer assignment of aromatic resonances with application to protein folding, structure, and dynamics. Biochemistry. 29:1989;9855-9873
    • (1989) Biochemistry , vol.29 , pp. 9855-9873
    • Weiss, M.A.1    Nguyen, D.T.2    Khait, I.3    Inouye, K.4    Frank, B.H.5    Beckage, M.6    O'shea, E.7    Shoelson, S.E.8    Karplus, M.9    Neuringer, L.J.10
  • 84
    • 0028849027 scopus 로고
    • X-ray crystallographic studies on hexameric insulins in the presence of helix-stabilizing agents, thiocyanate, methylparaben, and phenol
    • Whittingham J.L., Chaudhuri S., Dodson E.J., Moody P.C., Dodson G.G. X-ray crystallographic studies on hexameric insulins in the presence of helix-stabilizing agents, thiocyanate, methylparaben, and phenol. Biochemistry. 34:1994;15553-15563
    • (1994) Biochemistry , vol.34 , pp. 15553-15563
    • Whittingham, J.L.1    Chaudhuri, S.2    Dodson, E.J.3    Moody, P.C.4    Dodson, G.G.5


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