메뉴 건너뛰기




Volumn 579, Issue 18, 2005, Pages 3927-3931

Unfolding and breakdown of insulin in the presence of endogenous thiols

Author keywords

Insulin; Isomerization of insulin; Stability of insulin; Structure of denatured insulin; Thermal denaturation of insulin; Unfolding of insulin

Indexed keywords

CYSTEINE; DISULFIDE; GUANIDINE; INSULIN; THIOL DERIVATIVE; UREA;

EID: 21844479265     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.06.010     Document Type: Article
Times cited : (22)

References (35)
  • 1
    • 0023916658 scopus 로고
    • Sequences, sequences and sequences
    • F. Sanger Sequences, sequences and sequences Annu. Rev. Biochem. 57 1988 1 28
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 1-28
    • Sanger, F.1
  • 2
    • 0014146156 scopus 로고
    • Evidence for a precursor in the biosynthesis of insulin
    • D.F. Steiner Evidence for a precursor in the biosynthesis of insulin Trans. N. Y. Acad. Sci. 30 1967 60 68
    • (1967) Trans. N. Y. Acad. Sci. , vol.30 , pp. 60-68
    • Steiner, D.F.1
  • 4
    • 0020684912 scopus 로고
    • Human insulin form recombinant DNA technology
    • I.S. Johnson Human insulin form recombinant DNA technology Science 219 1983 632 637
    • (1983) Science , vol.219 , pp. 632-637
    • Johnson, I.S.1
  • 5
  • 6
    • 0026703427 scopus 로고
    • Chemical stability of insulin. 1. Hydrolytic degradation during storage of pharmaceutical preparations
    • J. Brange, L. Langkjaer, S. Havelund, and A. Volund Chemical stability of insulin. 1. Hydrolytic degradation during storage of pharmaceutical preparations Pharm. Res. 9 1992 715 726
    • (1992) Pharm. Res. , vol.9 , pp. 715-726
    • Brange, J.1    Langkjaer, L.2    Havelund, S.3    Volund, A.4
  • 7
    • 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
    • J. Markussen, I. Diers, P. Hougaard, L. Langkjaer, K. Norris, L. Snel, A.R. Sorensen, E. Sorensen, and H.O. Voigt 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
  • 10
    • 0021067853 scopus 로고
    • Minimizing the aggregation of neutral insulin solutions
    • R. Quinn, and J.D. Andrade Minimizing the aggregation of neutral insulin solutions J. Pharm. Sci. 72 1983 1472 1473
    • (1983) J. Pharm. Sci. , vol.72 , pp. 1472-1473
    • Quinn, R.1    Andrade, J.D.2
  • 12
    • 0035902492 scopus 로고    scopus 로고
    • Probing the mechanism of insulin fibril formation with insulin mutants
    • L. Nielsen, S. Frokjaer, J. Brange, V.N. Uversky, and A.L. Fink Probing the mechanism of insulin fibril formation with insulin mutants Biochemistry 40 2001 8397 8409
    • (2001) Biochemistry , vol.40 , pp. 8397-8409
    • Nielsen, L.1    Frokjaer, S.2    Brange, J.3    Uversky, V.N.4    Fink, A.L.5
  • 13
    • 0142241163 scopus 로고    scopus 로고
    • Chemical modification of insulin in amyloid fibrils
    • M.R. Nilsson, and C.M. Dobson Chemical modification of insulin in amyloid fibrils Protein Sci. 12 2003 2637 2641
    • (2003) Protein Sci. , vol.12 , pp. 2637-2641
    • Nilsson, M.R.1    Dobson, C.M.2
  • 19
    • 0028344969 scopus 로고
    • Equilibrium intermediates in the denaturation of human insulin and two monomeric insulin analogs
    • R.L. Millican, and D.N. Brems Equilibrium intermediates in the denaturation of human insulin and two monomeric insulin analogs Biochemistry 33 1994 1116 1124
    • (1994) Biochemistry , vol.33 , pp. 1116-1124
    • Millican, R.L.1    Brems, D.N.2
  • 20
    • 0037126725 scopus 로고    scopus 로고
    • A protein caught in a kinetic trap: Structures and stabilities of insulin disulfide isomers
    • Q.X. Hua, W. Jia, B.H. Frank, N.F. Phillips, and M.A. Weiss A protein caught in a kinetic trap: structures and stabilities of insulin disulfide isomers Biochemistry 41 2002 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
  • 21
    • 11244272777 scopus 로고    scopus 로고
    • In vitro refolding/unfolding pathways of amphioxus insulin-like peptide: Implications for folding behavior of insulin family proteins
    • Y. Chen, R. Jin, H.Y. Dong, and Y.M. Feng In vitro refolding/unfolding pathways of amphioxus insulin-like peptide: implications for folding behavior of insulin family proteins J. Biol. Chem. 279 2004 55224 55233
    • (2004) J. Biol. Chem. , vol.279 , pp. 55224-55233
    • Chen, Y.1    Jin, R.2    Dong, H.Y.3    Feng, Y.M.4
  • 22
    • 1242292281 scopus 로고    scopus 로고
    • 2. a novel concept in evaluating the contribution of 'Native-framework' of disulfides to the global conformational stability of proteins
    • 2. A novel concept in evaluating the contribution of 'Native-framework' of disulfides to the global conformational stability of proteins Biochem. J. 377 2004 685 692
    • (2004) Biochem. J. , vol.377 , pp. 685-692
    • Singh, R.R.1    Chang, J.-Y.2
  • 23
    • 0032946292 scopus 로고    scopus 로고
    • Denatured states of tick anticoagulant peptide. Compositional analysis of unfolded scrambled isomers
    • J.-Y. Chang Denatured states of tick anticoagulant peptide. Compositional analysis of unfolded scrambled isomers J. Biol. Chem. 274 1999 123 128
    • (1999) J. Biol. Chem. , vol.274 , pp. 123-128
    • Chang, J.-Y.1
  • 24
    • 0035971117 scopus 로고    scopus 로고
    • The structure of denatured alpha-lactalbumin elucidated by the technique of disulfide scrambling: Fractionation of conformational isomers of alpha-lactalbumin
    • J.-Y. Chang, and L. Li The structure of denatured alpha-lactalbumin elucidated by the technique of disulfide scrambling: fractionation of conformational isomers of alpha-lactalbumin J. Biol. Chem. 276 2001 9705 9712
    • (2001) J. Biol. Chem. , vol.276 , pp. 9705-9712
    • Chang, J.-Y.1    Li, L.2
  • 25
    • 0033104213 scopus 로고    scopus 로고
    • Quantitative analysis of the native and scrambled ribonuclease a
    • J.-Y. Chang Quantitative analysis of the native and scrambled ribonuclease A Anal. Biochem. 268 1999 147 150
    • (1999) Anal. Biochem. , vol.268 , pp. 147-150
    • Chang, J.-Y.1
  • 26
    • 0025271463 scopus 로고
    • PH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease a and ribonuclease T1
    • C.N. Pace, D.V. Laurents, and J.A. Thomson pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1 Biochemistry 29 1990 2564 2572
    • (1990) Biochemistry , vol.29 , pp. 2564-2572
    • Pace, C.N.1    Laurents, D.V.2    Thomson, J.A.3
  • 27
    • 0033536627 scopus 로고    scopus 로고
    • The molten globule state of a chimera of human alpha-lactalbumin and equine lysozyme
    • M. Mizuguchi, K. Masaki, and K. Nitta The molten globule state of a chimera of human alpha-lactalbumin and equine lysozyme J. Mol. Biol. 292 1999 1137 1148
    • (1999) J. Mol. Biol. , vol.292 , pp. 1137-1148
    • Mizuguchi, M.1    Masaki, K.2    Nitta, K.3
  • 28
    • 0018133234 scopus 로고
    • Synthesis and biological activity of two disulfide bond isomers of human insulin: [A7-A11, A6-B7 Cystine] and [A6-A7, A11-B7 Cystine] insulin
    • P.S. Sieber, K. Eisler, B. Kamber, B. Riniker, W. Rittel, F. Marki, and M. DeGasparo Synthesis and biological activity of two disulfide bond isomers of human insulin: [A7-A11, A6-B7 Cystine] and [A6-A7, A11-B7 Cystine] insulin Hoppe-Zeyler's Z Physiol. Chem. 359 1978 113 123
    • (1978) Hoppe-Zeyler'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
  • 30
    • 0035007258 scopus 로고    scopus 로고
    • Novel approach for the determination of the redox status of homocysteine and other aminothiols in plasma from healthy subjects and patients with Ischemic stroke
    • R.H. Williams, J.A. Maggiore, R.D. Reynolds, and C.M. Helgason Novel approach for the determination of the redox status of homocysteine and other aminothiols in plasma from healthy subjects and patients with Ischemic stroke Clin. Chem. 47 2001 1031 1039
    • (2001) Clin. Chem. , vol.47 , pp. 1031-1039
    • Williams, R.H.1    Maggiore, J.A.2    Reynolds, R.D.3    Helgason, C.M.4
  • 31
    • 0037016695 scopus 로고    scopus 로고
    • The folding pathway of alpha-lactalbumin elucidated by the technique of disulfide scrambling
    • J.-Y. Chang The folding pathway of alpha-lactalbumin elucidated by the technique of disulfide scrambling J. Biol. Chem. 277 2002 120 126
    • (2002) J. Biol. Chem. , vol.277 , pp. 120-126
    • Chang, J.-Y.1
  • 32
    • 1242296243 scopus 로고    scopus 로고
    • Structural stability of human alpha-thrombin studied by disulfide reduction and scrambling
    • S.S. Singh, and J.-Y. Chang Structural stability of human alpha-thrombin studied by disulfide reduction and scrambling Biochim. Biophys. Acta 1651 2003 85 92
    • (2003) Biochim. Biophys. Acta , vol.1651 , pp. 85-92
    • Singh, S.S.1    Chang, J.-Y.2
  • 33
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • C. Hwang, A.J. Sinskey, and H.F. Lodish Oxidized redox state of glutathione in the endoplasmic reticulum Science 257 1992 1496 1502
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 35
    • 0019039677 scopus 로고
    • Half-life and hypoglycemic effect of intravenous insulin in patients with diabetic ketoacidosis
    • I. Mincu, and C. Ionescu-Tirgoviste Half-life and hypoglycemic effect of intravenous insulin in patients with diabetic ketoacidosis Med. Intern. 18 1980 287 292
    • (1980) Med. Intern. , vol.18 , pp. 287-292
    • Mincu, I.1    Ionescu-Tirgoviste, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.