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Volumn 362, Issue 2, 2006, Pages 327-333

A Microbeam X-ray Diffraction Study of Insulin Spherulites

Author keywords

insulin amyloid; micro x ray diffraction; spherulite; synchrotron radiation

Indexed keywords

INSULIN;

EID: 33747755522     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.07.041     Document Type: Article
Times cited : (11)

References (24)
  • 2
    • 0000335935 scopus 로고
    • A fibrous modification of insulin. I. The heat precipitate of insulin
    • Waugh D.F. A fibrous modification of insulin. I. The heat precipitate of insulin. J. Amer. Chem. Soc. 68 (1946) 247-250
    • (1946) J. Amer. Chem. Soc. , vol.68 , pp. 247-250
    • Waugh, D.F.1
  • 4
    • 0001005525 scopus 로고
    • Regeneration of insulin from insulin fibrils by the action of alkali
    • Waugh D.F. Regeneration of insulin from insulin fibrils by the action of alkali. J. Amer. Chem. Soc. 70 (1948) 1850-1857
    • (1948) J. Amer. Chem. Soc. , vol.70 , pp. 1850-1857
    • Waugh, D.F.1
  • 6
    • 0002228831 scopus 로고    scopus 로고
    • Relation between the phase separation and the crystallization in protein solutions
    • Tanaka S., Yamamoto M., Ito K., and Hayakawa R. Relation between the phase separation and the crystallization in protein solutions. Phys. Rev. E 56 (1997) R67-R69
    • (1997) Phys. Rev. E , vol.56
    • Tanaka, S.1    Yamamoto, M.2    Ito, K.3    Hayakawa, R.4
  • 7
    • 12344272183 scopus 로고    scopus 로고
    • Aggregation across the length scales in β-lactoglobulin
    • Bromley E.H.C., Krebs M.R.H., and Donald A.M. Aggregation across the length scales in β-lactoglobulin. Faraday Discuss 128 (2005) 13-27
    • (2005) Faraday Discuss , vol.128 , pp. 13-27
    • Bromley, E.H.C.1    Krebs, M.R.H.2    Donald, A.M.3
  • 10
    • 16844368271 scopus 로고    scopus 로고
    • Structural analysis of cell membrane complex of a hair fibre by micro-beam X-ray diffraction
    • Ohta N., Oka T., Inoue K., Yagi N., Kato S., and Hatta I. Structural analysis of cell membrane complex of a hair fibre by micro-beam X-ray diffraction. J. Appl. Crystallog. 38 (2005) 274-279
    • (2005) J. Appl. Crystallog. , vol.38 , pp. 274-279
    • Ohta, N.1    Oka, T.2    Inoue, K.3    Yagi, N.4    Kato, S.5    Hatta, I.6
  • 11
    • 0029249356 scopus 로고
    • Large-aperture TV detector with a beryllium-windowed image intensifier for X-ray diffraction
    • Amemiya Y., Ito K., Yagi N., Asano Y., Wakabayashi K., Ueki T., and Endo T. Large-aperture TV detector with a beryllium-windowed image intensifier for X-ray diffraction. Rev. Sci. Instrum. 66 (1995) 2290-2294
    • (1995) Rev. Sci. Instrum. , vol.66 , pp. 2290-2294
    • Amemiya, Y.1    Ito, K.2    Yagi, N.3    Asano, Y.4    Wakabayashi, K.5    Ueki, T.6    Endo, T.7
  • 12
    • 21244483188 scopus 로고    scopus 로고
    • The mechanism of amyloid spherulite formation by bovine insulin
    • Krebs M.R.H., Bromley E.H.C., Rogers S.S., and Donald A.M. The mechanism of amyloid spherulite formation by bovine insulin. Biophys. J. 88 (2005) 2013-2021
    • (2005) Biophys. J. , vol.88 , pp. 2013-2021
    • Krebs, M.R.H.1    Bromley, E.H.C.2    Rogers, S.S.3    Donald, A.M.4
  • 13
    • 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. Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy. Protein Sci. 9 (2000) 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
  • 14
    • 0030586945 scopus 로고    scopus 로고
    • Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibrilis a continuous β-sheet helix
    • Blake C.C.F., and Serpell L.C. Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibrilis a continuous β-sheet helix. Structure 4 (1996) 989-998
    • (1996) Structure , vol.4 , pp. 989-998
    • Blake, C.C.F.1    Serpell, L.C.2
  • 16
    • 0034712918 scopus 로고    scopus 로고
    • Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformation
    • Serpell L.C., Berriman J., Jakes R., Goedert M., and Crowther R.A. Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformation. Proc. Natl Acad.Sci. USA 97 (2000) 4897-4902
    • (2000) Proc. Natl Acad.Sci. USA , vol.97 , pp. 4897-4902
    • Serpell, L.C.1    Berriman, J.2    Jakes, R.3    Goedert, M.4    Crowther, R.A.5
  • 18
    • 0015987644 scopus 로고
    • Structural studies of P-filaments produced from Salmonella Flagellins
    • Wakabayashi K., Yamaguchi T., and Kagawa H. Structural studies of P-filaments produced from Salmonella Flagellins. J. Mol. Biol. 83 (1974) 545-549
    • (1974) J. Mol. Biol. , vol.83 , pp. 545-549
    • Wakabayashi, K.1    Yamaguchi, T.2    Kagawa, H.3
  • 19
    • 0022547855 scopus 로고
    • X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-β conformation
    • Kirschner D.A., Abraham C., and Selkoe D.J. X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-β conformation. Proc. Natl Acad. Sci. USA 83 (1986) 503-507
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 503-507
    • Kirschner, D.A.1    Abraham, C.2    Selkoe, D.J.3
  • 20
    • 33646155955 scopus 로고    scopus 로고
    • Structure of core domain of fibril-forming PHF/Tau fragments
    • Inouye H., Dharma D., Goux W.J., and Kirschner D.A. Structure of core domain of fibril-forming PHF/Tau fragments. Biophys. J. 90 (2006) 1774-1789
    • (2006) Biophys. J. , vol.90 , pp. 1774-1789
    • Inouye, H.1    Dharma, D.2    Goux, W.J.3    Kirschner, D.A.4
  • 21
    • 26844435756 scopus 로고    scopus 로고
    • Molecular dynamics simulations of Alzheimer's β-amyloid protofilaments
    • Buchete N.-V., Tycko R., and Hummer G. Molecular dynamics simulations of Alzheimer's β-amyloid protofilaments. J. Mol. Biol. 353 (2005) 804-821
    • (2005) J. Mol. Biol. , vol.353 , pp. 804-821
    • Buchete, N.-V.1    Tycko, R.2    Hummer, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.