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Volumn 323, Issue 2, 2002, Pages 237-251

An insight into the pathway of the amyloid fibril formation of hen egg white lysozyme obtained from a small-angle X-ray and neutron scattering study

Author keywords

Amyloid; Circular dichroism; Lysozyme; Neutron scattering; X ray scattering

Indexed keywords

ALCOHOL; AMYLOID PROTEIN; DIMER; EGG WHITE; LYSOZYME; MONOMER; PROTEIN; WATER;

EID: 0036404245     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00941-5     Document Type: Article
Times cited : (81)

References (58)
  • 2
    • 0030841343 scopus 로고    scopus 로고
    • Conformatinal disease
    • Carrell, R. W. & Lomas, D. A. (1997). Conformatinal disease. Lancet, 350, 134-138.
    • (1997) Lancet , vol.350 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 3
    • 0031825554 scopus 로고    scopus 로고
    • From the globular to the fibrous state: Protein structure and structural conversion in amyloid formation
    • Sunde, M. & Blake, C. C. F. (1998). From the globular to the fibrous state: Protein structure and structural conversion in amyloid formation. Quart. Rev. Biophys. 31, 1-39.
    • (1998) Quart. Rev. Biophys. , vol.31 , pp. 1-39
    • Sunde, M.1    Blake, C.C.F.2
  • 4
    • 0033977086 scopus 로고    scopus 로고
    • Amyloid fibrillogenesis: Themes and variations
    • Rochet, J.-C. & Lansbury, P. T. (2000). Amyloid fibrillogenesis: Themes and variations. Curr. Opin. Struct. Biol. 10, 60-68.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 60-68
    • Rochet, J.-C.1    Lansbury, P.T.2
  • 5
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and X-ray diffraction
    • Sunde, M. & Blake, C. C. F. (1997). The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Advan. Protein Chem. 50, 123-159.
    • (1997) Advan. Protein Chem. , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.C.F.2
  • 6
    • 0033849738 scopus 로고    scopus 로고
    • Review: History of the amyloid fibril
    • Sipe, J. D. & Cohen, A. S. (2000). Review: History of the amyloid fibril. J. Struct. Biol. 130, 88-98.
    • (2000) J. Struct. Biol. , vol.130 , pp. 88-98
    • Sipe, J.D.1    Cohen, A.S.2
  • 7
    • 0024352110 scopus 로고
    • Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet conformation
    • Klunk, W. E., Pettegrew, J. W. & Abraham, D. J. (1989). Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet conformation. J. Histochem. Cytochem. 37, 1273-1281.
    • (1989) J. Histochem. Cytochem. , vol.37 , pp. 1273-1281
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 8
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson, C. M. (1999). Protein misfolding, evolution and disease. Trends Biochem. Sci. 9, 329-332.
    • (1999) Trends Biochem. Sci. , vol.9 , pp. 329-332
    • Dobson, C.M.1
  • 11
    • 0034255027 scopus 로고    scopus 로고
    • A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro
    • Ramirez-Alvarado, M., Merkel, J. S. & Regan, L. (2000). A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. Proc. Natl Acad. Sci. USA, 97, 8979-8984.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 8979-8984
    • Ramirez-Alvarado, M.1    Merkel, J.S.2    Regan, L.3
  • 13
    • 0034005357 scopus 로고    scopus 로고
    • Amyloid protofilament formation of hen egg white lysozyme in highly concentrated ethanol solution
    • Goda, S., Takano, K., Yamagata, Y., Nagata, R., Akutsu, H., Maki, S. et al. (2000). Amyloid protofilament formation of hen egg white lysozyme in highly concentrated ethanol solution. Protein Sci. 9, 369-375.
    • (2000) Protein Sci. , vol.9 , pp. 369-375
    • Goda, S.1    Takano, K.2    Yamagata, Y.3    Nagata, R.4    Akutsu, H.5    Maki, S.6
  • 14
    • 0034647438 scopus 로고    scopus 로고
    • Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the β-domain
    • Krebs, M. R. H., Wilkins, D. K., Chung, E. W., Pitkeathly, M. C., Chamberlain, A. K., Zurdo, J. et al. (2000). Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the β-domain. J. Mol. Biol. 300, 541-549.
    • (2000) J. Mol. Biol. , vol.300 , pp. 541-549
    • Krebs, M.R.H.1    Wilkins, D.K.2    Chung, E.W.3    Pitkeathly, M.C.4    Chamberlain, A.K.5    Zurdo, J.6
  • 15
    • 0034646397 scopus 로고    scopus 로고
    • The process of amyloid-like fibril formation by methionine amino-peptidase from a hyperthermophile, Pyrococcus furiosus
    • Yutani, K., Takayama, G., Goda, S., Yamagata, Y., Maki, S., Namba, K. et al. (2000). The process of amyloid-like fibril formation by methionine amino-peptidase from a hyperthermophile, Pyrococcus furiosus. Biochemistry, 39, 2769-2777.
    • (2000) Biochemistry , vol.39 , pp. 2769-2777
    • Yutani, K.1    Takayama, G.2    Goda, S.3    Yamagata, Y.4    Maki, S.5    Namba, K.6
  • 16
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • Fändrich, M., Fletcher, M. A. & Dobson, C. M. (2001). Amyloid fibrils from muscle myoglobin. Nature, 410, 165-166.
    • (2001) Nature , vol.410 , pp. 165-166
    • Fändrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 18
    • 0031056829 scopus 로고    scopus 로고
    • Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
    • Booth, D. R., Sunde, M., Bellotti, V., Robinson, C. V., Hutchinson, W. L., Fraser, P. E. et al. (1997). Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature, 385, 787-793.
    • (1997) Nature , vol.385 , pp. 787-793
    • Booth, D.R.1    Sunde, M.2    Bellotti, V.3    Robinson, C.V.4    Hutchinson, W.L.5    Fraser, P.E.6
  • 19
    • 0030565979 scopus 로고    scopus 로고
    • Protein interactions as seen by solution X-ray scattering prior to crystallogenesis
    • Ducruix, A., Guilloteau, J. P., Riès-Kautt, M. & Tardieu, A. (1996). Protein interactions as seen by solution X-ray scattering prior to crystallogenesis. J. Crystal Growth, 168, 28-39.
    • (1996) J. Crystal Growth , vol.168 , pp. 28-39
    • Ducruix, A.1    Guilloteau, J.P.2    Riès-Kautt, M.3    Tardieu, A.4
  • 20
    • 0035888118 scopus 로고    scopus 로고
    • Denaturation and aggregation of hen egg lysozyme in aqueous ethanol solution studied by dynamic light scattering
    • Tanaka, S., Oda, Y., Ataka, M., Onuma, K., Fujiwara, S. & Yonezawa, Y. (2001). Denaturation and aggregation of hen egg lysozyme in aqueous ethanol solution studied by dynamic light scattering. Biopolymers, 59, 370-379.
    • (2001) Biopolymers , vol.59 , pp. 370-379
    • Tanaka, S.1    Oda, Y.2    Ataka, M.3    Onuma, K.4    Fujiwara, S.5    Yonezawa, Y.6
  • 23
    • 0015994218 scopus 로고
    • Real-space refinement of the structure of hen egg-white lysozyme
    • Diamond, R. (1974). Real-space refinement of the structure of hen egg-white lysozyme. J. Mol. Biol. 82, 371-391.
    • (1974) J. Mol. Biol. , vol.82 , pp. 371-391
    • Diamond, R.1
  • 25
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun, D. I., Barberato, C. & Koch, M. H. J. (1995). CRYSOL-A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallog. 28, 768-773.
    • (1995) J. Appl. Crystallog. , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 26
    • 0037117502 scopus 로고    scopus 로고
    • Is the first hydration shell of lysozyme of higher density than bulk water?
    • Merzel, F. & Smith, J. C. (2002). Is the first hydration shell of lysozyme of higher density than bulk water? Proc. Natl Acad. Sci. USA, 99, 5378-5383.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 5378-5383
    • Merzel, F.1    Smith, J.C.2
  • 28
    • 0011109945 scopus 로고
    • Structure of muramidase (lysozyme). III. Effect of 2-chloroethanol, ethanol and dioxane on the stability of muramidase
    • Hamaguchi, K. & Kurono, A. (1963). Structure of muramidase (lysozyme). III. Effect of 2-chloroethanol, ethanol and dioxane on the stability of muramidase. J. Biochem. 54, 497-505.
    • (1963) J. Biochem. , vol.54 , pp. 497-505
    • Hamaguchi, K.1    Kurono, A.2
  • 29
    • 0011118150 scopus 로고
    • Structure of muramidase (lysozyme). VII. Effect of alcohols and the related compounds on the stability of muramidase
    • Kurono, A. & Hamaguchi, K. (1964). Structure of muramidase (lysozyme). VII. Effect of alcohols and the related compounds on the stability of muramidase. J. Biochem. 56, 432-440.
    • (1964) J. Biochem. , vol.56 , pp. 432-440
    • Kurono, A.1    Hamaguchi, K.2
  • 30
    • 0014901114 scopus 로고
    • Interaction of alcohols with lysozyme. I. Studies on circular dichroism
    • Ikeda, K. & Hamaguchi, K. (1970). Interaction of alcohols with lysozyme. I. Studies on circular dichroism. J. Biochem. 68, 785-794.
    • (1970) J. Biochem. , vol.68 , pp. 785-794
    • Ikeda, K.1    Hamaguchi, K.2
  • 31
    • 0030828611 scopus 로고    scopus 로고
    • Trifluoroethanol-induced conformational transition of hen egg-white lysozyme studied by small-angle X-ray scattering
    • Hoshino, M., Hagihara, Y., Hamada, D., Kataoka, M. & Goto, Y. (1997). Trifluoroethanol-induced conformational transition of hen egg-white lysozyme studied by small-angle X-ray scattering. FEBS Letters, 416, 72-76.
    • (1997) FEBS Letters , vol.416 , pp. 72-76
    • Hoshino, M.1    Hagihara, Y.2    Hamada, D.3    Kataoka, M.4    Goto, Y.5
  • 32
    • 0031936293 scopus 로고    scopus 로고
    • The methanol-induced transition and the expanded helical conformation in hen lysozyme
    • Kamatari, Y. O., Konno, T., Kataoka, M. & Akasaka, K. (1998). The methanol-induced transition and the expanded helical conformation in hen lysozyme. Protein Sci. 7, 681-688.
    • (1998) Protein Sci. , vol.7 , pp. 681-688
    • Kamatari, Y.O.1    Konno, T.2    Kataoka, M.3    Akasaka, K.4
  • 33
    • 0022349985 scopus 로고
    • Study of ethanol-lysozyme interactions using neutron diffraction
    • Lehman, M. S., Mason, S. A. & McIntyre, G. J. (1985). Study of ethanol-lysozyme interactions using neutron diffraction. Biochemistry, 24, 5862-5869
    • (1985) Biochemistry , vol.24 , pp. 5862-5869
    • Lehman, M.S.1    Mason, S.A.2    McIntyre, G.J.3
  • 34
    • 0002905623 scopus 로고
    • A neutron small-angle scattering study of hen egg-white lysozyme
    • Stuhrmann, H. B. & Fuess, H. (1976). A neutron small-angle scattering study of hen egg-white lysozyme. Acta Crystallog. Sect. A, 32, 67-74.
    • (1976) Acta Crystallog. Sect. A , vol.32 , pp. 67-74
    • Stuhrmann, H.B.1    Fuess, H.2
  • 35
    • 0013852463 scopus 로고
    • Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Å resolution
    • Blake, C. C. F., Koenig, D. F., Mair, G. A., North, A. C. T., Phillips, D. C. & Sarma, V. R. (1965). Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Å resolution. Nature, 206, 757-761.
    • (1965) Nature , vol.206 , pp. 757-761
    • Blake, C.C.F.1    Koenig, D.F.2    Mair, G.A.3    North, A.C.T.4    Phillips, D.C.5    Sarma, V.R.6
  • 37
    • 0030586945 scopus 로고    scopus 로고
    • Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix
    • Blake, C. & Serpell, L. (1996). Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix. Structure, 4, 989-998.
    • (1996) Structure , vol.4 , pp. 989-998
    • Blake, C.1    Serpell, L.2
  • 39
    • 0042847751 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
    • Jiménez, J. L., Guijarro, J. I., Orlova, E., Zurdo, J., Dobson, C. M., Sunde, M. & Saibil, H. R. (1999). Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J. 18, 815-821.
    • (1999) EMBO J. , vol.18 , pp. 815-821
    • Jiménez, J.L.1    Guijarro, J.I.2    Orlova, E.3    Zurdo, J.4    Dobson, C.M.5    Sunde, M.6    Saibil, H.R.7
  • 40
    • 0033520495 scopus 로고    scopus 로고
    • An NMR investigation of solution aggregation reactions preceding the misassembly of acid-denatured cold shock protein A into fibrils
    • Alexandrescu, A. T. & Rathgeb-Szabo, K. (1999). An NMR investigation of solution aggregation reactions preceding the misassembly of acid-denatured cold shock protein A into fibrils. J. Mol. Biol. 291, 1191-1206.
    • (1999) J. Mol. Biol. , vol.291 , pp. 1191-1206
    • Alexandrescu, A.T.1    Rathgeb-Szabo, K.2
  • 41
    • 0033605278 scopus 로고    scopus 로고
    • Prion domain initiation of amyloid formation in vitro from native Ure2p
    • Taylor, K. L., Cheng, N., Williams, R. W., Steven, A. C. & Wickner, R. B. (1999). Prion domain initiation of amyloid formation in vitro from native Ure2p. Science, 283, 1339-1343.
    • (1999) Science , vol.283 , pp. 1339-1343
    • Taylor, K.L.1    Cheng, N.2    Williams, R.W.3    Steven, A.C.4    Wickner, R.B.5
  • 44
    • 0035839046 scopus 로고    scopus 로고
    • Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy
    • Jiménez, J. L., Tennent, G., Pepys, M. & Saibil, H. R. (2001). Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy. J. Mol. Biol. 311, 241-247.
    • (2001) J. Mol. Biol. , vol.311 , pp. 241-247
    • Jiménez, J.L.1    Tennent, G.2    Pepys, M.3    Saibil, H.R.4
  • 45
    • 0030004644 scopus 로고    scopus 로고
    • The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid
    • Lai, Z., Colón, W. & Kelly, J. W. (1996). The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid. Biochemistry, 35, 6470-6482.
    • (1996) Biochemistry , vol.35 , pp. 6470-6482
    • Lai, Z.1    Colón, W.2    Kelly, J.W.3
  • 46
    • 0027332116 scopus 로고
    • Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins
    • Pan, K.-M., Baldwin, M., Nguyen, J., Gasset, M., Serban, A., Groth, D. et al. (1993). Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc. Natl Acad. Sci. USA, 90, 10962-10966.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 10962-10966
    • Pan, K.-M.1    Baldwin, M.2    Nguyen, J.3    Gasset, M.4    Serban, A.5    Groth, D.6
  • 47
    • 0028980362 scopus 로고
    • The α-helical to β-strand transition in the amino-terminal fragment of the amyloid β-peptide modulates amyloid formation
    • Soto, C., Castaño, E. M., Frangione, B. & Inestrosa, N. C. (1995). The α-helical to β-strand transition in the amino-terminal fragment of the amyloid β-peptide modulates amyloid formation. J. Biol. Chem. 270, 3063-3067.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3063-3067
    • Soto, C.1    Castaño, E.M.2    Frangione, B.3    Inestrosa, N.C.4
  • 48
    • 0033520461 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates
    • Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A. et al. (1999). Amyloid β-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. J. Biol. Chem. 274, 25945-25952.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25945-25952
    • Walsh, D.M.1    Hartley, D.M.2    Kusumoto, Y.3    Fezoui, Y.4    Condron, M.M.5    Lomakin, A.6
  • 49
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated conformational conversion and the replication of conformational information by a prion determinant
    • Serio, T. R., Cashikar, A. G., Kowal, A. S., Sawicki, G. J., Moslehi, J. J., Serpell, L. et al. (2000). Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science, 289, 1317-1321.
    • (2000) Science , vol.289 , pp. 1317-1321
    • Serio, T.R.1    Cashikar, A.G.2    Kowal, A.S.3    Sawicki, G.J.4    Moslehi, J.J.5    Serpell, L.6
  • 50
    • 0035796475 scopus 로고    scopus 로고
    • Three-dimensional structure of the lithostathine protofibril, a protein involved in Alzheimer's disease
    • Grégoire, C., Marco, S., Thimonier, J., Duplan, L., Laurine, E., Chauvin, J.-P. et al. (2001). Three-dimensional structure of the lithostathine protofibril, a protein involved in Alzheimer's disease. EMBO J. 20, 3313-3321.
    • (2001) EMBO J. , vol.20 , pp. 3313-3321
    • Grégoire, C.1    Marco, S.2    Thimonier, J.3    Duplan, L.4    Laurine, E.5    Chauvin, J.-P.6
  • 52
    • 0032558978 scopus 로고    scopus 로고
    • Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: Implications for wild-type, V30M, and L55P amyloid fibril formation
    • Lashuel, H. A., Lai, Z. & Kelly, J. W. (1998). Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: Implications for wild-type, V30M, and L55P amyloid fibril formation. Biochemistry, 37, 17851-17864.
    • (1998) Biochemistry , vol.37 , pp. 17851-17864
    • Lashuel, H.A.1    Lai, Z.2    Kelly, J.W.3
  • 53
    • 0028845988 scopus 로고
    • Examination of the structure of the transthyretin amyloid fibril by image reconstruction from electron micrographs
    • Serpell, L. C., Sunde, M., Fraser, P. E., Luther, P. K., Morris, E. P., Sangren, O. et al. (1995). Examination of the structure of the transthyretin amyloid fibril by image reconstruction from electron micrographs. J. Mol. Biol. 254, 113-118.
    • (1995) J. Mol. Biol. , vol.254 , pp. 113-118
    • Serpell, L.C.1    Sunde, M.2    Fraser, P.E.3    Luther, P.K.4    Morris, E.P.5    Sangren, O.6
  • 54
    • 0014595905 scopus 로고
    • Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. I. Dependence on pH at 25 degrees
    • Aune, K. C. & Tanford, C. (1969). Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. I. Dependence on pH at 25 degrees. Biochemistry, 8, 4579-4585.
    • (1969) Biochemistry , vol.8 , pp. 4579-4585
    • Aune, K.C.1    Tanford, C.2
  • 56
    • 0002327557 scopus 로고
    • Progress in X-ray synchrotron diffraction studies of muscle contraction
    • Ebashi, S., Koch, M. & Rubenstein, E., eds. North-Holland, Amsterdam
    • Wakabayashi, K. & Amemiya, Y. (1991). Progress in X-ray synchrotron diffraction studies of muscle contraction. In Handbook on Synchrotron Radiation (Ebashi, S., Koch, M. & Rubenstein, E., eds), pp. 597-678, North-Holland, Amsterdam.
    • (1991) Handbook on Synchrotron Radiation , pp. 597-678
    • Wakabayashi, K.1    Amemiya, Y.2


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