메뉴 건너뛰기




Volumn 23, Issue 2, 2005, Pages 97-110

The role of disulfide bonds in the structure and function of murine epidermal growth factor (mEGF)

Author keywords

Disulfide bond; EGF; EGF receptor; Mitogenic activity; NMR; Structure function

Indexed keywords

2 AMINOBUTYRIC ACID; CYSTEINE; DIMETHYL SULFOXIDE; DISULFIDE; EPIDERMAL GROWTH FACTOR; AMINOBUTYRIC ACID DERIVATIVE; OXYGEN; PEPTIDE;

EID: 24944478764     PISSN: 08977194     EISSN: None     Source Type: Journal    
DOI: 10.1080/08977190500096061     Document Type: Article
Times cited : (14)

References (89)
  • 1
    • 0030795612 scopus 로고    scopus 로고
    • The ErbB signaling network in embryogenesis and oncogenesis: Signal diversification through combinatorial ligand-receptor interactions
    • Alroy, I, Yarden, Y. The ErbB signaling network in embryogenesis and oncogenesis: Signal diversification through combinatorial ligand-receptor interactions FEBS Lett, 1997; 410: 83-86
    • (1997) FEBS Lett , vol.410 , pp. 83-86
    • Alroy, I.1    Yarden, Y.2
  • 5
    • 5144233105 scopus 로고
    • MILEV-17 based two dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A, Davis, DG. MILEV-17 based two dimensional homonuclear magnetization transfer spectroscopy J Magn Reson, 1985; 65: 355-360
    • (1985) J Magn Reson , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 6
    • 0014620599 scopus 로고
    • Human pituitary growth hormone. Physicochemical investigations of the native and reduced-alkylated protein
    • Bewley, TA, Brovetto-Cruz, J, Li, CH. Human pituitary growth hormone. Physicochemical investigations of the native and reduced-alkylated protein Biochemistry, 1969; 8: 4701-4708
    • (1969) Biochemistry , vol.8 , pp. 4701-4708
    • Bewley, T.A.1    Brovetto-Cruz, J.2    Li, C.H.3
  • 7
    • 0025215889 scopus 로고
    • Equilibrium denaturation of human growth hormone and its cysteine-modified forms
    • Brems, DN, Brown, PL, Becker, GW. Equilibrium denaturation of human growth hormone and its cysteine-modified forms J Biol Chem, 1990; 265: 5504-5511
    • (1990) J Biol Chem , vol.265 , pp. 5504-5511
    • Brems, D.N.1    Brown, P.L.2    Becker, G.W.3
  • 9
    • 0020464160 scopus 로고
    • Two forms of murine epidermal growth factor: Rapid separation by using reverse-phase high performance liquid chromatography
    • Burgess, AW, Knesel, J, Sparrow, LG, Nicola, NA, Nice, EC. Two forms of murine epidermal growth factor: Rapid separation by using reverse-phase high performance liquid chromatography Proc Natl Acad Sci USA, 1982; 79: 5753-5757
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 5753-5757
    • Burgess, A.W.1    Knesel, J.2    Sparrow, L.G.3    Nicola, N.A.4    Nice, E.C.5
  • 10
    • 0021008434 scopus 로고
    • Murine epidermal growth factor: Heterogeneity on high resolution ion-exchange chromatography
    • Burgess, AW, Lloyd, CJ, Nice, EC. Murine epidermal growth factor: Heterogeneity on high resolution ion-exchange chromatography EMBO J, 1983; 2: 2065-2069
    • (1983) EMBO J , vol.2 , pp. 2065-2069
    • Burgess, A.W.1    Lloyd, C.J.2    Nice, E.C.3
  • 14
    • 0022557470 scopus 로고
    • A high resolution 1H NMR study of the solution structure of human epidermal growth factor
    • Carver, JA, Cooke, RM, Esposito, G, Campbell, D, Gregory, H, Sheard, B. A high resolution 1H NMR study of the solution structure of human epidermal growth factor FEBS Lett, 1986; 205: 77-81
    • (1986) FEBS Lett , vol.205 , pp. 77-81
    • Carver, J.A.1    Cooke, R.M.2    Esposito, G.3    Campbell, D.4    Gregory, H.5    Sheard, B.6
  • 15
    • 0028911697 scopus 로고
    • The disulfide folding pathway of human epidermal growth factor
    • Chang, JY, Schindler, P, Ramseier, U, Lai, PH. The disulfide folding pathway of human epidermal growth factor J Biol Chem, 1995; 270: 9207-9216
    • (1995) J Biol Chem , vol.270 , pp. 9207-9216
    • Chang, J.Y.1    Schindler, P.2    Ramseier, U.3    Lai, P.H.4
  • 16
    • 0035895917 scopus 로고    scopus 로고
    • A major kinetic trap for the oxidative folding of human epidermal growth factor
    • Chang, JY, Li, L, Lai, PH. A major kinetic trap for the oxidative folding of human epidermal growth factor J Biol Chem, 2001; 276: 4845-4852
    • (2001) J Biol Chem , vol.276 , pp. 4845-4852
    • Chang, J.Y.1    Li, L.2    Lai, P.H.3
  • 17
    • 0037162799 scopus 로고    scopus 로고
    • Structure of the extracellular region of HER3 reveals an interdomain tether
    • Cho, HS, Leahy, DJ. Structure of the extracellular region of HER3 reveals an interdomain tether Science, 2002; 297: 1330-1333
    • (2002) Science , vol.297 , pp. 1330-1333
    • Cho, H.S.1    Leahy, D.J.2
  • 19
    • 0023258054 scopus 로고
    • The solution structure of human epidermal growth factor
    • Cooke, RM, Wilkinson, AJ, Baron, M. The solution structure of human epidermal growth factor Nature, 1987; 327: 339-341 et al.
    • (1987) Nature , vol.327 , pp. 339-341
    • Cooke, R.M.1    Wilkinson, A.J.2    Baron, M.3
  • 22
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman, GL. Tissue sulfhydryl groups Arch Biochem Biophys, 1959; 82: 70-77
    • (1959) Arch Biochem Biophys , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 23
    • 0037291769 scopus 로고    scopus 로고
    • EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization
    • Ferguson, KM, Berger, MB, Mendrola, JM, Cho, HS, Leahy, DJ, Lemmon, MA. EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization Mol Cell, 2003; 11: 507-517
    • (2003) Mol Cell , vol.11 , pp. 507-517
    • Ferguson, K.M.1    Berger, M.B.2    Mendrola, J.M.3    Cho, H.S.4    Leahy, D.J.5    Lemmon, M.A.6
  • 24
    • 0026483350 scopus 로고
    • Solid-phase synthesis of bovine pancreatic trypsin inhibitor (BPTI) and two analogues. A chemical approach for evaluating the role of disulfide bridges in protein folding and stability
    • Ferrer, M, Woodward, C, Barany, G. Solid-phase synthesis of bovine pancreatic trypsin inhibitor (BPTI) and two analogues. A chemical approach for evaluating the role of disulfide bridges in protein folding and stability Int J Pept Protein Res, 1992; 40: 94-207
    • (1992) Int J Pept Protein Res , vol.40 , pp. 94-207
    • Ferrer, M.1    Woodward, C.2    Barany, G.3
  • 25
    • 0028966372 scopus 로고
    • Partially folded, molten globule and molten coil states of bovine pancreatic trypsin inhibitor
    • Ferrer, M, Barany, G, Woodward, C. Partially folded, molten globule and molten coil states of bovine pancreatic trypsin inhibitor Nat Struct Biol, 1995; 2: 211-217
    • (1995) Nat Struct Biol , vol.2 , pp. 211-217
    • Ferrer, M.1    Barany, G.2    Woodward, C.3
  • 28
    • 0023706804 scopus 로고
    • The contribution of the C-terminal undecapeptide sequence of urogastron-epidermal growth factor to its biological action
    • Gregory, H, Thomas, CE, Young, JA, Willshire, IR, Garner, A. The contribution of the C-terminal undecapeptide sequence of urogastron-epidermal growth factor to its biological action Regul Peptides, 1988; 22: 217-226
    • (1988) Regul Peptides , vol.22 , pp. 217-226
    • Gregory, H.1    Thomas, C.E.2    Young, J.A.3    Willshire, I.R.4    Garner, A.5
  • 29
    • 0028618937 scopus 로고
    • Structure-function relationships for the EGF/TGF-alpha family of mitogens
    • Groenen, LC, Nice, EC, Burgess, AW. Structure-function relationships for the EGF/TGF-alpha family of mitogens Growth Factors, 1994; 11: 235-257
    • (1994) Growth Factors , vol.11 , pp. 235-257
    • Groenen, L.C.1    Nice, E.C.2    Burgess, A.W.3
  • 30
    • 0024020582 scopus 로고
    • Conformational and receptor binding properties of human EGF and TGF-alpha second loop fragments
    • Han, KH, Ferretti, JA, Niu, CH, Lokeshwar, V, Clarke, R, Katz, D. Conformational and receptor binding properties of human EGF and TGF-alpha second loop fragments J Mol Recognit, 1988; 1: 116-123
    • (1988) J Mol Recognit , vol.1 , pp. 116-123
    • Han, K.H.1    Ferretti, J.A.2    Niu, C.H.3    Lokeshwar, V.4    Clarke, R.5    Katz, D.6
  • 31
    • 0012115649 scopus 로고
    • A synthetic approach to structure-function relationships in the murine epidermal growth factor molecule
    • Heath, WF, Merrifield, RB. A synthetic approach to structure-function relationships in the murine epidermal growth factor molecule Proc Natl Acad Sci USA, 1986; 83: 6367-6371
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 6367-6371
    • Heath, W.F.1    Merrifield, R.B.2
  • 32
    • 0017083620 scopus 로고
    • Conformation and unfolding thermodynamics of epidermal growth factor and derivatives
    • Holladay, LA, Savage, CR, Cohen, S, Puett, D. Conformation and unfolding thermodynamics of epidermal growth factor and derivatives Biochemistry, 1976; 15: 2624-2633
    • (1976) Biochemistry , vol.15 , pp. 2624-2633
    • Holladay, L.A.1    Savage, C.R.2    Cohen, S.3    Puett, D.4
  • 33
    • 0030735422 scopus 로고    scopus 로고
    • Peptides corresponding to the second epidermal growth factor-like domain of human blood coagulation factor VII: Synthesis, folding and biological activity
    • Husbyn, M, Orning, L, Sakariassen, KS, Fischer, PM. Peptides corresponding to the second epidermal growth factor-like domain of human blood coagulation factor VII: Synthesis, folding and biological activity J Pept Res, 1997; 50: 475-482
    • (1997) J Pept Res , vol.50 , pp. 475-482
    • Husbyn, M.1    Orning, L.2    Sakariassen, K.S.3    Fischer, P.M.4
  • 34
    • 0028670125 scopus 로고
    • The biology of erbB-2/neu/HER-2 and its role in cancer
    • Hynes, NE, Stern, DF. The biology of erbB-2/neu/HER-2 and its role in cancer Biochim Biophys Acta, 1994; 1198: 165-184
    • (1994) Biochim Biophys Acta , vol.1198 , pp. 165-184
    • Hynes, N.E.1    Stern, D.F.2
  • 36
    • 0343359244 scopus 로고
    • Investigation of chemical exchange processes by two dimensional NMR spectroscopy
    • Jenner, J, Meier, BH, Bachmann, P, Ernst, RR. Investigation of chemical exchange processes by two dimensional NMR spectroscopy J Chem Phys, 1979; 71: 4546-4553
    • (1979) J Chem Phys , vol.71 , pp. 4546-4553
    • Jenner, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 37
    • 0035914315 scopus 로고    scopus 로고
    • Role of cysteine residues in structural stability and function of a transmembrane helix bundle
    • Karim, CB, Paterlini, MG, Reddy, LG, Hunter, GW, Barany, DD, Thomas, DD. Role of cysteine residues in structural stability and function of a transmembrane helix bundle J Biol Chem, 2001; 276: 38814-38819
    • (2001) J Biol Chem , vol.276 , pp. 38814-38819
    • Karim, C.B.1    Paterlini, M.G.2    Reddy, L.G.3    Hunter, G.W.4    Barany, D.D.5    Thomas, D.D.6
  • 38
    • 0021364168 scopus 로고
    • Biologically active synthetic fragments of epidermal growth factor: Localization of a major receptor-binding region
    • Komoriya, A, Hortsch, M, Meyers, C, Smith, M, Kanety, H, Schlessinger, J. Biologically active synthetic fragments of epidermal growth factor: Localization of a major receptor-binding region Proc Natl Acad Sci USA, 1984; 81: 1351-1355
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 1351-1355
    • Komoriya, A.1    Hortsch, M.2    Meyers, C.3    Smith, M.4    Kanety, H.5    Schlessinger, J.6
  • 39
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar, A, Ernst, RR, Wuthrich, K. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules Biochem Biophys Res Commun, 1980; 95: 1-6
    • (1980) Biochem Biophys Res Commun , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wuthrich, K.3
  • 42
    • 0031305240 scopus 로고    scopus 로고
    • Crystal structure of the complex of diphtheria toxin with an extracellular fragment of its receptor
    • Louie, GV, Yang, W, Bowman, ME, Choe, S. Crystal structure of the complex of diphtheria toxin with an extracellular fragment of its receptor Mol Cell, 1997; 1: 67-78
    • (1997) Mol Cell , vol.1 , pp. 67-78
    • Louie, G.V.1    Yang, W.2    Bowman, M.E.3    Choe, S.4
  • 43
    • 0035860766 scopus 로고    scopus 로고
    • Crystal structure of human epidermal growth factor and its dimerization
    • Lu, HS, Chai, JJ, Li, M, Huang, BR, He, CH, Bi, RC. Crystal structure of human epidermal growth factor and its dimerization J Biol Chem, 2001; 276: 34913-34917
    • (2001) J Biol Chem , vol.276 , pp. 34913-34917
    • Lu, H.S.1    Chai, J.J.2    Li, M.3    Huang, B.R.4    He, C.H.5    Bi, R.C.6
  • 45
    • 0029776587 scopus 로고    scopus 로고
    • NMR study of the transforming growth factor-alpha (TGF-alpha)-epidermal growth factor receptor complex. Visualization of human TGF-alpha binding determinants through nuclear Overhauser enhancement analysis
    • McInnes, C, Hoyt, DW, Harkins, RN, Pagila, RN, Debanne, MT, O'Connor-McCourt, M, Sykes, BD. NMR study of the transforming growth factor-alpha (TGF-alpha)-epidermal growth factor receptor complex. Visualization of human TGF-alpha binding determinants through nuclear Overhauser enhancement analysis J Biol Chem, 1996; 271: 32204-32211
    • (1996) J Biol Chem , vol.271 , pp. 32204-32211
    • McInnes, C.1    Hoyt, DW.2    Harkins, R.N.3    Pagila, R.N.4    Debanne, M.T.5    O'Connor-McCourt, M.6    Sykes, B.D.7
  • 46
    • 0032538437 scopus 로고    scopus 로고
    • Minimization of transforming growth factor-alpha (TGF-alpha) through NMR analysis of the receptor-bound ligand. Design, solution structure, and activity of TGF-alpha 8-50
    • McInnes, C, Wang, J, Al Moustafa, AE, Yansouni, C, O'Connor-McCourt, M, Sykes, BD. Minimization of transforming growth factor-alpha (TGF-alpha) through NMR analysis of the receptor-bound ligand. Design, solution structure, and activity of TGF-alpha 8-50 J Biol Chem, 1998; 273: 27357-27363
    • (1998) J Biol Chem , vol.273 , pp. 27357-27363
    • McInnes, C.1    Wang, J.2    Al Moustafa, A.E.3    Yansouni, C.4    O'Connor-McCourt, M.5    Sykes, B.D.6
  • 47
    • 0034016522 scopus 로고    scopus 로고
    • NMR study of the differential contributions of residues of transforming growth factor alpha to association with its receptor
    • McInnes, C, Grothe, S, O'Connor-McCourt, M, Sykes, BD. NMR study of the differential contributions of residues of transforming growth factor alpha to association with its receptor Protein Eng, 2000; 13: 143-147
    • (2000) Protein Eng , vol.13 , pp. 143-147
    • McInnes, C.1    Grothe, S.2    O'Connor-McCourt, M.3    Sykes, B.D.4
  • 49
    • 0343386901 scopus 로고
    • Indentification of two anti-parallel β-sheet conformations in the solution structure of murine epidermal growth factor by proton magnetic resonance
    • Montelione, GT, Wuthrich, K, Nice, EC, Burgess, AW, Scheraga, HA. Indentification of two anti-parallel β-sheet conformations in the solution structure of murine epidermal growth factor by proton magnetic resonance Proc Natl Acad Sci USA, 1986; 83: 8594-8598
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 8594-8598
    • Montelione, G.T.1    Wuthrich, K.2    Nice, E.C.3    Burgess, A.W.4    Scheraga, H.A.5
  • 50
    • 0023394258 scopus 로고
    • Solution structure of murine epidermal growth factor: Determination of the polypeptide backbone chain-fold by nuclear magnetic resonance and distance geometry
    • Montelione, GT, Wuthrich, K, Nice, EC, Burgess, AW, Scheraga, HA. Solution structure of murine epidermal growth factor: Determination of the polypeptide backbone chain-fold by nuclear magnetic resonance and distance geometry Proc Natl Acad Sci USA, 1987; 84: 5226-5230
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5226-5230
    • Montelione, G.T.1    Wuthrich, K.2    Nice, E.C.3    Burgess, A.W.4    Scheraga, H.A.5
  • 51
    • 0026508986 scopus 로고
    • Solution structure of murine epidermal growth factor determined by NMR spectroscopy and refined by energy minimization with restraints
    • Montelione, GT, Wuthrich, K, Burgess, AW, Nice, EC, Wagner, G, Gibson, KD, Scheraga, HA. Solution structure of murine epidermal growth factor determined by NMR spectroscopy and refined by energy minimization with restraints Biochemistry, 1992; 31: 236-249
    • (1992) Biochemistry , vol.31 , pp. 236-249
    • Montelione, G.T.1    Wuthrich, K.2    Burgess, A.W.3    Nice, E.C.4    Wagner, G.5    Gibson, K.D.6    Scheraga, H.A.7
  • 52
    • 0028146248 scopus 로고
    • Solution structure of the epidermal growth factor-like domain of heregulin-alpha, a ligand for p180erbB-4
    • Nagata, K, Kohda, D, Hatanaka, H, Ichikawa, S, Matsuda, S, Yamamoto, T, Suzuki, A, Inagaki, F. Solution structure of the epidermal growth factor-like domain of heregulin-alpha, a ligand for p180erbB-4 EMBO J, 1994; 13: 3517-3523
    • (1994) EMBO J , vol.13 , pp. 3517-3523
    • Nagata, K.1    Kohda, D.2    Hatanaka, H.3    Ichikawa, S.4    Matsuda, S.5    Yamamoto, T.6    Suzuki, A.7    Inagaki, F.8
  • 54
    • 0000928917 scopus 로고
    • Micropreparative LC of proteins
    • Nice, EC. Micropreparative LC of proteins Nature, 1990; 348: 462-463
    • (1990) Nature , vol.348 , pp. 462-463
    • Nice, E.C.1
  • 55
    • 0342683748 scopus 로고    scopus 로고
    • Micropreparative HPLC of proteins and peptides: Principles and applications
    • Nice, EC. Micropreparative HPLC of proteins and peptides: Principles and applications Biopolymers (Peptide Science), 1996; 40: 319-341
    • (1996) Biopolymers (Peptide Science) , vol.40 , pp. 319-341
    • Nice, E.C.1
  • 58
    • 1642421130 scopus 로고    scopus 로고
    • Target-based agents against ErbB receptors and their ligands: A novel approach to cancer treatment
    • Normanno, N, Bianco, C, De Luca, A, Maiello, MR, Salomon, DS. Target-based agents against ErbB receptors and their ligands: A novel approach to cancer treatment Endocr Relat Cancer, 2003; 10: 1-21
    • (2003) Endocr Relat Cancer , vol.10 , pp. 1-21
    • Normanno, N.1    Bianco, C.2    De Luca, A.3    Maiello, M.R.4    Salomon, D.S.5
  • 59
    • 0030737618 scopus 로고    scopus 로고
    • Ligand-binding enhances the affinity of dimerization of the extracellular domain of the epidermal growth factor receptor
    • Odaka, M, Kohda, D, Lax, I, Schlessinger, J, Inagaki, F. Ligand-binding enhances the affinity of dimerization of the extracellular domain of the epidermal growth factor receptor J Biochem (Tokyo), 1997; 122: 116-121
    • (1997) J Biochem (Tokyo) , vol.122 , pp. 116-121
    • Odaka, M.1    Kohda, D.2    Lax, I.3    Schlessinger, J.4    Inagaki, F.5
  • 62
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M, Saudek, V, Sklenar, V. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions J Biomol NMR, 1992; 2: 661-665
    • (1992) J Biomol NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 63
    • 0030900908 scopus 로고    scopus 로고
    • Insertion of Argos sequences into the B-loop of epidermal growth factor results in a low-affinity ligand with strong agonistic activity
    • van de Poll, ML, van Vugt, MJ, Lenferink, AE, van Zoelen, EJ. Insertion of Argos sequences into the B-loop of epidermal growth factor results in a low-affinity ligand with strong agonistic activity Biochemistry, 1997; 36: 7425-7431
    • (1997) Biochemistry , vol.36 , pp. 7425-7431
    • van de Poll, M.L.1    van Vugt, M.J.2    Lenferink, A.E.3    van Zoelen, E.J.4
  • 64
    • 0032568939 scopus 로고    scopus 로고
    • Identification of the minimal requirements for binding to the human epidermal growth factor (EGF) receptor using chimeras of human EGF and an EGF repeat of Drosophila Notch
    • van de Poll, ML, van Vugt, MJ, Lenferink, AE, van Zoelen, EJ. Identification of the minimal requirements for binding to the human epidermal growth factor (EGF) receptor using chimeras of human EGF and an EGF repeat of Drosophila Notch J Biol Chem, 1998; 273: 16075-16081
    • (1998) J Biol Chem , vol.273 , pp. 16075-16081
    • van de Poll, M.L.1    van Vugt, M.J.2    Lenferink, A.E.3    van Zoelen, E.J.4
  • 65
    • 0026487597 scopus 로고
    • The type 1 (EGFR-related) family of growth factor receptors and their ligands
    • Prigent, SA, Lemoine, NR. The type 1 (EGFR-related) family of growth factor receptors and their ligands Prog Growth Factor Res, 1992; 4: 1-24
    • (1992) Prog Growth Factor Res , vol.4 , pp. 1-24
    • Prigent, S.A.1    Lemoine, N.R.2
  • 67
    • 0031936410 scopus 로고    scopus 로고
    • Specificity within the EGF family/ErbB receptor family signaling network
    • Riese, DJ, Stern, DF. Specificity within the EGF family/ErbB receptor family signaling network Bioessays, 1998; 20: 41-48
    • (1998) Bioessays , vol.20 , pp. 41-48
    • Riese, D.J.1    Stern, D.F.2
  • 68
    • 0028302118 scopus 로고
    • Roles of disulfide bonds in recombinant human interleukin 6 conformation
    • Rock, FL, Li, X, Chong, P, Ida, N, Klein, M. Roles of disulfide bonds in recombinant human interleukin 6 conformation Biochemistry, 1994; 5146-5154
    • (1994) Biochemistry , pp. 5146-5154
    • Rock, F.L.1    Li, X.2    Chong, P.3    Ida, N.4    Klein, M.5
  • 71
    • 0023110220 scopus 로고
    • Synthesis of biologically-active human transforming growth factor-alpha by fluorenylmethoxycarbonyl solid phase peptide chemistry
    • Scanlon, DB, Eefting, M, Lloyd, CJ, Burgess, AW, Simpson, RJ. Synthesis of biologically-active human transforming growth factor-alpha by fluorenylmethoxycarbonyl solid phase peptide chemistry J Chem Soc: Chem Commun, 1987; 25: 516-518
    • (1987) J Chem Soc: Chem Commun , vol.25 , pp. 516-518
    • Scanlon, D.B.1    Eefting, M.2    Lloyd, C.J.3    Burgess, A.W.4    Simpson, R.J.5
  • 72
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger, J. Cell signaling by receptor tyrosine kinases Cell, 2000; 103: 211-225
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 73
    • 0037145061 scopus 로고    scopus 로고
    • Ligand-induced, receptor-mediated dimerization and activation of EGF receptor
    • Schlessinger, J. Ligand-induced, receptor-mediated dimerization and activation of EGF receptor Cell, 2002; 110: 669-672
    • (2002) Cell , vol.110 , pp. 669-672
    • Schlessinger, J.1
  • 74
    • 0026486811 scopus 로고
    • Situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences
    • Schnolzer, M, Alewood, P, Jones, A, Alewood, D, Kent, SB. In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences Int J Pept Protein Res, 1992; 40: 180-193
    • (1992) Int J Pept Protein Res , vol.40 , pp. 180-193
    • Schnolzer, M.1    Alewood, P.2    Jones, A.3    Alewood, D.4    Kent, S.B.5
  • 75
    • 0028945946 scopus 로고
    • Synthesis and biological activity of N-terminal-truncated derivatives of human epidermal growth factor (h-EGF)
    • Shin, SY, Shimizu, M, Ohtaki, T, Munekata, E. Synthesis and biological activity of N-terminal-truncated derivatives of human epidermal growth factor (h-EGF) Peptides, 1995; 16: 205-210
    • (1995) Peptides , vol.16 , pp. 205-210
    • Shin, S.Y.1    Shimizu, M.2    Ohtaki, T.3    Munekata, E.4
  • 77
    • 0028314332 scopus 로고
    • A novel strategy for the synthesis of the cysteine-rich protective antigen of the malaria merozoite surface protein (MSP-1). Knowledge-based strategy for disulfide formation
    • Spetzler, JC, Rao, C, Tam, JP. A novel strategy for the synthesis of the cysteine-rich protective antigen of the malaria merozoite surface protein (MSP-1). Knowledge-based strategy for disulfide formation Int J Pept Protein Res, 1994; 43: 351-358
    • (1994) Int J Pept Protein Res , vol.43 , pp. 351-358
    • Spetzler, J.C.1    Rao, C.2    Tam, J.P.3
  • 78
    • 0023139996 scopus 로고
    • Synthesis of biologically active transforming growth factor alpha
    • Tam, JP. Synthesis of biologically active transforming growth factor alpha Int J Pept Protein Res, 1987; 29: 421-431
    • (1987) Int J Pept Protein Res , vol.29 , pp. 421-431
    • Tam, J.P.1
  • 79
    • 0021324338 scopus 로고
    • Synthesis of biologically active rat transforming growth factor I
    • Tam, JP, Marquardt, H, Rosberger, DF, Wong, TW, Todaro, GJ. Synthesis of biologically active rat transforming growth factor I Nature, 1984; 309: 376-378
    • (1984) Nature , vol.309 , pp. 376-378
    • Tam, J.P.1    Marquardt, H.2    Rosberger, D.F.3    Wong, T.W.4    Todaro, G.J.5
  • 80
    • 0009042981 scopus 로고
    • Efficient synthesis of human type alpha transforming growth factor: Its physical and biological characterization
    • Tam, JP, Sheikh, MA, Solomon, DS, Ossowski, L. Efficient synthesis of human type alpha transforming growth factor: Its physical and biological characterization Proc Natl Acad Sci USA, 1986; 83: 8082-8086
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 8082-8086
    • Tam, J.P.1    Sheikh, M.A.2    Solomon, D.S.3    Ossowski, L.4
  • 81
    • 32144447178 scopus 로고
    • Disulfide bond formation in peptides by dimethylsulphoxide. Scope and aapplication
    • Tam, JP, Wu, C-R, Liu, W, Zhang, J-W. Disulfide bond formation in peptides by dimethylsulphoxide. Scope and aapplication J Am Chem Soc, 1991; 86: 4099-4103
    • (1991) J Am Chem Soc , vol.86 , pp. 4099-4103
    • Tam, J.P.1    Wu, C.-R.2    Liu, W.3    Zhang, J.-W.4
  • 83
    • 0037112617 scopus 로고    scopus 로고
    • Renaturation of human proinsulin-a study on refolding and conversion to insulin
    • Winter, J, Lilie, H, Rudolph, R. Renaturation of human proinsulin-a study on refolding and conversion to insulin Anal Biochem, 2002; 310: 148-155
    • (2002) Anal Biochem , vol.310 , pp. 148-155
    • Winter, J.1    Lilie, H.2    Rudolph, R.3
  • 84
    • 0025943469 scopus 로고
    • Simple techniques for the quantification of protein secondary structure by 1H NMR spectroscopy
    • Wishart, DS, Sykes, BD, Richards, FM. Simple techniques for the quantification of protein secondary structure by 1H NMR spectroscopy FEBS Lett, 1991; 293: 72-80
    • (1991) FEBS Lett , vol.293 , pp. 72-80
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 85
    • 0024421799 scopus 로고
    • Chemical synthesis in protein engineering: Total synthesis, purification and covalent structural characterization of a mitogenic protein, human transforming growth factor-alpha
    • Woo, DD, Clark-Lewis, I, Chait, BT, Kent, SB. Chemical synthesis in protein engineering: Total synthesis, purification and covalent structural characterization of a mitogenic protein, human transforming growth factor-alpha Protein Eng, 1989; 3: 29-37
    • (1989) Protein Eng , vol.3 , pp. 29-37
    • Woo, D.D.1    Clark-Lewis, I.2    Chait, B.T.3    Kent, S.B.4
  • 86
    • 0020648375 scopus 로고
    • Sequential individual resonance assignments in the 1H-NMR spectra of polypeptides and proteins
    • Wuthrich, K. Sequential individual resonance assignments in the 1H-NMR spectra of polypeptides and proteins Biopolymers, 1983; 22: 131-138
    • (1983) Biopolymers , vol.22 , pp. 131-138
    • Wuthrich, K.1
  • 88
    • 0029122867 scopus 로고
    • Kinetic analysis of the folding of human growth hormone. Influence of disulfide bonds
    • Youngman, KM, Spencer, DB, Brems, DN, DeFelippis, MR. Kinetic analysis of the folding of human growth hormone. Influence of disulfide bonds J Biol Chem, 1995; 270: 19816-19822
    • (1995) J Biol Chem , vol.270 , pp. 19816-19822
    • Youngman, K.M.1    Spencer, D.B.2    Brems, D.N.3    DeFelippis, M.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.