메뉴 건너뛰기




Volumn 46, Issue 1, 2007, Pages 218-224

The sequence determinant causing different folding behaviors of insulin and insulin-like growth factor-1

Author keywords

[No Author keywords available]

Indexed keywords

B-CHAIN; INSULIN-LIKE PEPTIDES; PEPTIDES; TERTIARY STRUCTURES;

EID: 33846094025     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0616798     Document Type: Article
Times cited : (11)

References (29)
  • 2
    • 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, Biochemistry. 31, 1749-1756.
    • (1992) Biochemistry , vol.31 , pp. 1749-1756
    • Hober, S.1    Forsberg, G.2    Palm, G.3    Hartmanis, M.4    Nilsson, B.5
  • 3
    • 0033036635 scopus 로고    scopus 로고
    • Insulin-like growth factors I and II are unable to form and maintain their native disulfides under in vivo redox conditions
    • Hober, S., Lundstrom Ljung, J., Uhlen, M., and Nilsson, B. (1999) Insulin-like growth factors I and II are unable to form and maintain their native disulfides under in vivo redox conditions, FEBS Lett. 443, 271-276.
    • (1999) FEBS Lett , vol.443 , pp. 271-276
    • Hober, S.1    Lundstrom Ljung, J.2    Uhlen, M.3    Nilsson, B.4
  • 4
    • 0025700681 scopus 로고
    • Insulin-like growth factors I and II
    • Humbel, R. E. (1990) Insulin-like growth factors I and II, Eur. J. Biochem. 190, 445-462.
    • (1990) Eur. J. Biochem , vol.190 , pp. 445-462
    • Humbel, R.E.1
  • 6
    • 0025822851 scopus 로고
    • Solution structure of human insulin-like growth factor 1: A nuclear magnetic resonance and restrained molecular dynamics study
    • Cook, R. M., Harvey, T. S., and Campbell, I. D. (1991) Solution structure of human insulin-like growth factor 1: a nuclear magnetic resonance and restrained molecular dynamics study, Biochemistry 30, 5484-5491.
    • (1991) Biochemistry , vol.30 , pp. 5484-5491
    • Cook, R.M.1    Harvey, T.S.2    Campbell, I.D.3
  • 8
    • 0035814878 scopus 로고    scopus 로고
    • Putative disulfide-forming pathway of porcine insulin precursor during its refolding in vitro
    • Qiao, Z. S., Guo, Z. Y., and Feng, Y. M. (2001) Putative disulfide-forming pathway of porcine insulin precursor during its refolding in vitro, Biochemistry 40, 2662-2668.
    • (2001) Biochemistry , vol.40 , pp. 2662-2668
    • Qiao, Z.S.1    Guo, Z.Y.2    Feng, Y.M.3
  • 9
    • 0027311222 scopus 로고
    • Role of native disulfide bonds in the structure and activity of insulin-like growth factor 1: Genetic models of protein-folding intermediates
    • Narhi, L. O., Hua, Q. X., Arakawa, T., Fox, G. M., Tsai L, Rosenfeld, R., Holst, P., Miller, J. A., Weiss, M. A. (1993) Role of native disulfide bonds in the structure and activity of insulin-like growth factor 1: genetic models of protein-folding intermediates, Biochemistry 18, 5214-5221.
    • (1993) Biochemistry , vol.18 , 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
  • 11
    • 0037377495 scopus 로고    scopus 로고
    • A peptide model of insulin folding intermediate with one disulfide
    • Yan, H., Guo, Z. Y., Gong, X. W., Xi, D., and Feng, Y. M. (2003) A peptide model of insulin folding intermediate with one disulfide, Protein Sci. 4, 768-775.
    • (2003) Protein Sci , vol.4 , pp. 768-775
    • Yan, H.1    Guo, Z.Y.2    Gong, X.W.3    Xi, D.4    Feng, Y.M.5
  • 12
    • 33748785712 scopus 로고    scopus 로고
    • The folding nucleus of the insulin superfamily: A flexible peptide model foreshadows the native state
    • Hua, Q. X., Mayer, J. P., Jia, W., Zhang, J., Weiss, M. A. (2006) The folding nucleus of the insulin superfamily: a flexible peptide model foreshadows the native state, J. Biol. Chem. 2, 28131-28142.
    • (2006) J. Biol. Chem , vol.2 , pp. 28131-28142
    • Hua, Q.X.1    Mayer, J.P.2    Jia, W.3    Zhang, J.4    Weiss, M.A.5
  • 15
    • 0025880180 scopus 로고
    • X-ray analysis of the single chain B29-A1 peptide-linked insulin molecule. A completely inactive analogue
    • Derewenda, U., Derewenda, Z., Dodson, E. J., Dodson, G. G., Bing, X. G., and Markussen, J. (1991) X-ray analysis of the single chain B29-A1 peptide-linked insulin molecule. A completely inactive analogue, J. Mol. Biol. 220, 425-433.
    • (1991) J. Mol. Biol , vol.220 , pp. 425-433
    • Derewenda, U.1    Derewenda, Z.2    Dodson, E.J.3    Dodson, G.G.4    Bing, X.G.5    Markussen, J.6
  • 17
    • 0037022177 scopus 로고    scopus 로고
    • The different folding behavior of insulin and insulin-like growth factor 1 is mainly controlled by their B-chain/domain
    • Guo, Z. Y., Shen, L., and Feng, Y. M. (2002) The different folding behavior of insulin and insulin-like growth factor 1 is mainly controlled by their B-chain/domain, Biochemistry 41, 1556-1567.
    • (2002) Biochemistry , vol.41 , pp. 1556-1567
    • Guo, Z.Y.1    Shen, L.2    Feng, Y.M.3
  • 20
    • 0037183471 scopus 로고    scopus 로고
    • The different energetic state of the intra A-chain/domain disulfide of insulin and insulin-like growth factor 1 is mainly controlled by their B-chain/domain
    • Guo, Z. Y., Shen, L., and Feng, Y. M. (2002) The different energetic state of the intra A-chain/domain disulfide of insulin and insulin-like growth factor 1 is mainly controlled by their B-chain/domain, Biochemistry 41, 10585-10592.
    • (2002) Biochemistry , vol.41 , pp. 10585-10592
    • Guo, Z.Y.1    Shen, L.2    Feng, Y.M.3
  • 21
    • 3142751249 scopus 로고    scopus 로고
    • Sequences of B-chain/domain 1-10/1-9 of insulin and insulin-like growth factor 1 determine their different folding behavior
    • Chen, Y., You, Y., Jin, R., Guo, Z. Y., and Feng, Y. M. (2004) Sequences of B-chain/domain 1-10/1-9 of insulin and insulin-like growth factor 1 determine their different folding behavior, Biochemistry 43, 9225-9233.
    • (2004) Biochemistry , vol.43 , pp. 9225-9233
    • Chen, Y.1    You, Y.2    Jin, R.3    Guo, Z.Y.4    Feng, Y.M.5
  • 22
    • 33646794618 scopus 로고    scopus 로고
    • The thermodynamic stability of insulin disulfides is not affected by the C-domain of insulin-like growth factor 1
    • Guo, Z. Y., and Feng, Y. M. (2002) The thermodynamic stability of insulin disulfides is not affected by the C-domain of insulin-like growth factor 1, Sci. China (Series C) 45, 245-250.
    • (2002) Sci. China (Series C) , vol.45 , pp. 245-250
    • Guo, Z.Y.1    Feng, Y.M.2
  • 23
    • 9644275348 scopus 로고    scopus 로고
    • 1.42 Å crystal structure of mini-IGF-1(2): An analysis of the disulfide isomerization property and receptor binding property of IGF-1 based on the three-dimensional structure
    • Yun, C. H., Tang, Y. H., Feng, Y. M., An, X. M., Chang, W. R., Liang, D. C. (2005) 1.42 Å crystal structure of mini-IGF-1(2): an analysis of the disulfide isomerization property and receptor binding property of IGF-1 based on the three-dimensional structure, Biochem. Biophys. Res. Commun. 326, 52-59.
    • (2005) Biochem. Biophys. Res. Commun , vol.326 , pp. 52-59
    • Yun, C.H.1    Tang, Y.H.2    Feng, Y.M.3    An, X.M.4    Chang, W.R.5    Liang, D.C.6
  • 25
    • 0025634026 scopus 로고
    • Evolution of the insulin superfamily: Cloning of a hybrid insulin/insulin-like growth factor cDNA from amphioxus
    • Chan, S. J., Cao, Q. P., and Steiner, F. D. (1990) Evolution of the insulin superfamily: cloning of a hybrid insulin/insulin-like growth factor cDNA from amphioxus, Proc. Natl. Acad. Sci. U.S.A. 87, 9319-9323.
    • (1990) Proc. Natl. Acad. Sci. U.S.A , vol.87 , pp. 9319-9323
    • Chan, S.J.1    Cao, Q.P.2    Steiner, F.D.3
  • 26
    • 0037183522 scopus 로고    scopus 로고
    • In vitro evolution of amphioxus insulin-like peptide to mammalian insulin
    • Guo, Z. Y., Shen, L., Gu, W., Wu, A. Z., Ma, J. G., and Feng, Y. M. (2002) In vitro evolution of amphioxus insulin-like peptide to mammalian insulin, Biochemistry 41, 10603-10607.
    • (2002) Biochemistry , vol.41 , pp. 10603-10607
    • Guo, Z.Y.1    Shen, L.2    Gu, W.3    Wu, A.Z.4    Ma, J.G.5    Feng, Y.M.6
  • 27
    • 11244272777 scopus 로고    scopus 로고
    • In vitro refolding/unfolding pathways of amphioxus insulin-like peptide: Implications for folding behavior of insulin family proteins
    • Chen, Y., Jin, R., Dong, H. Y., and Feng, Y. M. (2004) In vitro refolding/unfolding pathways of amphioxus insulin-like peptide: implications for folding behavior of insulin family proteins, J. Biol. Chem. 279, 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
  • 28
    • 0042527408 scopus 로고    scopus 로고
    • Refolding of amphioxus insulin-like peptide: Implications of a bifurcating evolution of the different folding behavior of insulin and insulin-like growth factor 1
    • Wang, S., Guo, Z. Y., Shen, L., Zhang, Y. J., and Feng, Y. M. (2003) Refolding of amphioxus insulin-like peptide: implications of a bifurcating evolution of the different folding behavior of insulin and insulin-like growth factor 1, Biochemistry 42, 9687-9693.
    • (2003) Biochemistry , vol.42 , pp. 9687-9693
    • Wang, S.1    Guo, Z.Y.2    Shen, L.3    Zhang, Y.J.4    Feng, Y.M.5
  • 29
    • 0033772185 scopus 로고    scopus 로고
    • Direct identification of a novel disulfide bond linkage system of new isolated isomer (isomer V) in recombinantly produced h-IGF-1
    • Iwai, M., Yokoyama, H., Yamada, H., Niwa, M., Kobayashi, M. (2000) Direct identification of a novel disulfide bond linkage system of new isolated isomer (isomer V) in recombinantly produced h-IGF-1, Chem. Pham. Bull. (Tokyo) 48, 1304-1309.
    • (2000) Chem. Pham. Bull. (Tokyo) , vol.48 , pp. 1304-1309
    • Iwai, M.1    Yokoyama, H.2    Yamada, H.3    Niwa, M.4    Kobayashi, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.