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Volumn , Issue , 2007, Pages 21-31

An infrared study of fibril formation in insulin from different sources

Author keywords

Amyloid; Fibrils; Infrared spectroscopy; Insulin; Protein structure

Indexed keywords


EID: 84892087247     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-1-4020-6466-1_2     Document Type: Chapter
Times cited : (2)

References (20)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern folding of protein chains
    • Anfinsen, C. B. (1973) Principles That Govern Folding of Protein Chains. Science 181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 2
    • 0344672542 scopus 로고    scopus 로고
    • Structure and dynamics of membrane proteins as studied by infrared spectroscopy
    • Arrondo, J. L. R. and Goñi, F. M. (1999) Structure and dynamics of membrane proteins as studied by infrared spectroscopy. Prog. Biophys. Mol. Biol. 72:367-405.
    • (1999) Prog. Biophys. Mol. Biol. , vol.72 , pp. 367-405
    • Arrondo, J.L.R.1    Goñi, F.M.2
  • 3
    • 0027354020 scopus 로고
    • Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy
    • Arrondo, J. L. R., Muga, A., Castresana, J., and Goñi, F. M. (1993) Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy. Prog. Biophys. Mol. Biol. 59:23-56.
    • (1993) Prog. Biophys. Mol. Biol. , vol.59 , pp. 23-56
    • Arrondo, J.L.R.1    Muga, A.2    Castresana, J.3    Goñi, F.M.4
  • 4
    • 0033777523 scopus 로고    scopus 로고
    • Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy
    • Bouchard, M., Zurdo, J., Nettleton, E. J., Dobson, C. M., and Robinson, C. V. (2000) Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy. Protein Sci. 9:1960-1967.
    • (2000) Protein Sci. , vol.9 , pp. 1960-1967
    • Bouchard, M.1    Zurdo, J.2    Nettleton, E.J.3    Dobson, C.M.4    Robinson, C.V.5
  • 5
    • 0025944507 scopus 로고
    • Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy [published erratum appears in Biochemistry 1991 Oct. 29;30(43):10600]
    • Caughey, B. W., Dong, A., Bhat, K. S., Ernst, D., Hayes, S. F., and Caughey, W. S. (1991) Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy [published erratum appears in Biochemistry 1991 Oct. 29;30(43):10600]. Biochemistry 30:7672-7680.
    • (1991) Biochemistry , vol.30 , pp. 7672-7680
    • Caughey, B.W.1    Dong, A.2    Bhat, K.S.3    Ernst, D.4    Hayes, S.F.5    Caughey, W.S.6
  • 6
    • 0141530970 scopus 로고    scopus 로고
    • Deacylated pulmonary surfactant protein SP-C transforms from alpha-helical to amyloid fibril structure via a pH-dependent mechanism: An infrared structural investigation
    • Dluhy, R. A., Shanmukh, S., Leapard, J. B., Kruger, P., and Baatz, J. E. (2003) Deacylated Pulmonary Surfactant Protein SP-C Transforms From alpha-Helical to Amyloid Fibril Structure via a pH-Dependent Mechanism: An Infrared Structural Investigation. Biophys. J. 85:2417-2429.
    • (2003) Biophys. J. , vol.85 , pp. 2417-2429
    • Dluhy, R.A.1    Shanmukh, S.2    Leapard, J.B.3    Kruger, P.4    Baatz, J.E.5
  • 7
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C. M. (2003) Protein folding and misfolding. Nature 426:884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 8
    • 0027249811 scopus 로고
    • Comparative analysis of human and Dutch-type Alzheimer β-amyloid peptides by infrared spectroscopy and circular dichroism
    • Fabian, H., Szendrei, G. I., Mantsch, H. H., and Otvos, L., Jr. (1993) Comparative analysis of human and Dutch-type Alzheimer β-amyloid peptides by infrared spectroscopy and circular dichroism. Biochem. Biophys. Res. Commun. 191:232-239.
    • (1993) Biochem. Biophys. Res. Commun. , vol.191 , pp. 232-239
    • Fabian, H.1    Szendrei, G.I.2    Mantsch, H.H.3    Otvos Jr., L.4
  • 9
    • 0027388993 scopus 로고
    • Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity
    • Gasset, M., Baldwin, M. A., Fletterick, R. J., and Prusiner, S. B. (1993) Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity. Proc. Natl. Acad. Sci. USA 90:1-5.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1-5
    • Gasset, M.1    Baldwin, M.A.2    Fletterick, R.J.3    Prusiner, S.B.4
  • 11
    • 28244437028 scopus 로고    scopus 로고
    • The Yin and Yang of protein folding
    • Jahn, T. R. and Radford, S. E. (2005) The Yin and Yang of protein folding. FEBSD J. 272:5962-5970.
    • (2005) FEBSD J. , vol.272 , pp. 5962-5970
    • Jahn, T.R.1    Radford, S.E.2
  • 12
    • 28244484729 scopus 로고    scopus 로고
    • Structures for amyloid fibrils
    • Makin, O. S. and Serpell, L. C. (2005) Structures for amyloid fibrils. FEBS J. 272:5950-5961.
    • (2005) FEBS J. , vol.272 , pp. 5950-5961
    • Makin, O.S.1    Serpell, L.C.2
  • 13
    • 0035158241 scopus 로고    scopus 로고
    • Studies of the structure of insulin fibrils by Fourier transform infrared (FTIR) spectroscopy and electron microscopy
    • Nielsen, L., Frokjaer, S., Carpenter, J. F., and Brange, J. (2001) Studies of the structure of insulin fibrils by Fourier transform infrared (FTIR) spectroscopy and electron microscopy. J. Pharm. Sci. 90:29-37.
    • (2001) J. Pharm. Sci. , vol.90 , pp. 29-37
    • Nielsen, L.1    Frokjaer, S.2    Carpenter, J.F.3    Brange, J.4
  • 14
    • 0013812532 scopus 로고
    • Congo red as a stain for fluorescence microscopy of amyloid
    • Puchtler, H. and Sweat, F. (1965) Congo Red as a Stain for Fluorescence Microscopy of Amyloid. J. of Histochem. Cytochem. 13:693-694.
    • (1965) J. of Histochem. Cytochem. , vol.13 , pp. 693-694
    • Puchtler, H.1    Sweat, F.2
  • 15
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • Stefani, M. and Dobson, C. M. (2003) Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 81:678-699.
    • (2003) J. Mol. Med. , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 16
    • 1342324027 scopus 로고    scopus 로고
    • Progress towards a molecular-level structural understanding of amyloid fibrils
    • Tycko, R. (2004) Progress towards a molecular-level structural understanding of amyloid fibrils. Curr. Opin. Struct. Biol. 14:96-103.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 96-103
    • Tycko, R.1
  • 17
    • 0001451739 scopus 로고
    • Zur Celluslose-Frage
    • Virchow, R. (1854) Zur Celluslose-Frage. Virchows Arch. 6:415-426.
    • (1854) Virchows Arch. , vol.6 , pp. 415-426
    • Virchow, R.1
  • 18
    • 28244446220 scopus 로고    scopus 로고
    • Aspects on human amyloid forms and their fibril polypeptides
    • Westermark, P. (2005) Aspects on human amyloid forms and their fibril polypeptides. FEBS J. 272:5942-5949.
    • (2005) FEBS J. , vol.272 , pp. 5942-5949
    • Westermark, P.1
  • 20
    • 0035839035 scopus 로고    scopus 로고
    • Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain
    • Zurdo, J., Guijarro, J. I., Jimenez, J. L., Saibil, H. R., and Dobson, C. M. (2001) Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain. J. Mol. Biol. 311:325-340.
    • (2001) J. Mol. Biol. , vol.311 , pp. 325-340
    • Zurdo, J.1    Guijarro, J.I.2    Jimenez, J.L.3    Saibil, H.R.4    Dobson, C.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.