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Volumn 331, Issue 1, 2003, Pages 21-28

Effects of salt concentration on association of the amyloid protofilaments of Hen egg white lysozyme studied by time-resolved neutron scattering

Author keywords

Amyloid; Kinetics; Lysozyme; Neutron scattering; Protein aggregation

Indexed keywords

AMYLOID PROTEIN; HYPERTONIC SOLUTION; LYSOZYME;

EID: 0038161262     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00722-8     Document Type: Article
Times cited : (47)

References (35)
  • 2
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and X-ray diffraction
    • Sunde M., Blake C.C.F. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Advan. Protein Chem. 50:1997;123-159.
    • (1997) Advan. Protein Chem. , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.C.F.2
  • 5
    • 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. A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. Proc. Natl Acad. Sci. USA. 97:2000;8979-8984.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 8979-8984
    • Ramirez-Alvarado, M.1    Merkel, J.S.2    Regan, L.3
  • 7
    • 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. Amyloid protofilament formation of hen egg white lysozyme in highly concentrated ethanol solution. Protein Sci. 9:2000;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
  • 8
    • 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. Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the β-domain. J. Mol. Biol. 300:2000;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
  • 9
    • 0034646397 scopus 로고    scopus 로고
    • The process of amyloid-like fibril formation by methionine aminopeptidase from a hyperthermophile, Pyrococcus furiosus
    • Yutani K., Takayama G., Goda S., Yamagata Y., Maki S., Namba K., et al. The process of amyloid-like fibril formation by methionine aminopeptidase from a hyperthermophile, Pyrococcus furiosus. Biochemistry. 39:2000;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
  • 10
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • Fändrich M., Fletcher M.A., Dobson C.M. Amyloid fibrils from muscle myoglobin. Nature. 410:2001;165-166.
    • (2001) Nature , vol.410 , pp. 165-166
    • Fändrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 11
    • 0036404245 scopus 로고    scopus 로고
    • 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
    • Yonezawa Y., Tanaka S., Kubota T., Wakabayashi K., Yutani K., Fujiwara S. 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. J. Mol. Biol. 323:2002;237-251.
    • (2002) J. Mol. Biol. , vol.323 , pp. 237-251
    • Yonezawa, Y.1    Tanaka, S.2    Kubota, T.3    Wakabayashi, K.4    Yutani, K.5    Fujiwara, S.6
  • 14
    • 0035839035 scopus 로고    scopus 로고
    • Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain
    • Zurdo J., Guijarro J.I., Jiménez J.L., Saibil H.R., Dobson C.M. Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain. J. Mol. Biol. 311:2001;325-340.
    • (2001) J. Mol. Biol. , vol.311 , pp. 325-340
    • Zurdo, J.1    Guijarro, J.I.2    Jiménez, J.L.3    Saibil, H.R.4    Dobson, C.M.5
  • 15
    • 0035955555 scopus 로고    scopus 로고
    • 2-Microgloblin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro
    • 2-Microgloblin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro. J. Mol. Biol. 313:2001;559-571.
    • (2001) J. Mol. Biol. , vol.313 , pp. 559-571
    • Kad, N.M.1    Thomson, N.H.2    Smith, D.P.3    Smith, D.A.4    Radford, S.E.5
  • 17
    • 0036304350 scopus 로고    scopus 로고
    • Insulin at pH 2: Structural analysis of the conditions promoting insulin fibre formation
    • Whittingham J.L., Scott D.J., Chance K., Wilson A., Finch J., Brange J., et al. Insulin at pH 2: structural analysis of the conditions promoting insulin fibre formation. J. Mol. Biol. 318:2002;479-490.
    • (2002) J. Mol. Biol. , vol.318 , pp. 479-490
    • Whittingham, J.L.1    Scott, D.J.2    Chance, K.3    Wilson, A.4    Finch, J.5    Brange, J.6
  • 18
    • 0036951939 scopus 로고    scopus 로고
    • PH-dependent aggregate forms and conformation of Alzheimer amyloid β-peptide (12-24)
    • Abe H., Kawasaki K., Nakanishi H. pH-dependent aggregate forms and conformation of Alzheimer amyloid β-peptide (12-24). J. Biochem. 132:2002;863-874.
    • (2002) J. Biochem. , vol.132 , pp. 863-874
    • Abe, H.1    Kawasaki, K.2    Nakanishi, H.3
  • 19
    • 0016959784 scopus 로고
    • Advantages of neutron scattering for biological structure analysis
    • B. Schoenborn. Upton, NY: Brookhaven National Laboratory
    • Schoenborn B. Advantages of neutron scattering for biological structure analysis. Schoenborn B. Neutron Scattering for the Analysis of Biological Structures. 1975;110-117 Brookhaven National Laboratory, Upton, NY.
    • (1975) Neutron Scattering for the Analysis of Biological Structures , pp. 110-117
    • Schoenborn, B.1
  • 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. Denaturation and aggregation of hen egg lysozyme in aqueous ethanol solution studied by dynamic light scattering. Biopolymers. 59:2001;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
  • 21
    • 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. An NMR investigation of solution aggregation reactions preceding the misassembly of acid-denatured cold shock protein A into fibrils. J. Mol. Biol. 291:1999;1191-1206.
    • (1999) J. Mol. Biol. , vol.291 , pp. 1191-1206
    • Alexandrescu, A.T.1    Rathgeb-Szabo, K.2
  • 22
    • 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. Prion domain initiation of amyloid formation in vitro from native Ure2p. Science. 283:1999;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
  • 24
    • 0021103482 scopus 로고
    • Stages of tubulin assembly and disassembly studied by time-resolved synchrotron X-ray scattering
    • Bordas J., Mandelkow E.M., Mandelkow E. Stages of tubulin assembly and disassembly studied by time-resolved synchrotron X-ray scattering. J. Mol. Biol. 164:1983;89-135.
    • (1983) J. Mol. Biol. , vol.164 , pp. 89-135
    • Bordas, J.1    Mandelkow, E.M.2    Mandelkow, E.3
  • 27
    • 0033849915 scopus 로고    scopus 로고
    • Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants
    • Morozova-Roche L.A., Zurdo J., Spencer A., Noppe W., Receveur V., Archer D.B., et al. Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants. J. Struct. Biol. 130:2000;339-351.
    • (2000) J. Struct. Biol. , vol.130 , pp. 339-351
    • Morozova-Roche, L.A.1    Zurdo, J.2    Spencer, A.3    Noppe, W.4    Receveur, V.5    Archer, D.B.6
  • 29
    • 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. Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy. J. Mol. Biol. 311:2001;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
  • 30
    • 0029996091 scopus 로고    scopus 로고
    • Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Aβ
    • Wood S.J., Maleeff B., Hart T., Wetzel R. Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Aβ J. Mol. Biol. 256:1996;870-877.
    • (1996) J. Mol. Biol. , vol.256 , pp. 870-877
    • Wood, S.J.1    Maleeff, B.2    Hart, T.3    Wetzel, R.4
  • 32
    • 0033777523 scopus 로고    scopus 로고
    • Formation of insulin amyloid fibrils followed by FTIR simulatenouly with CD and electron microscopy
    • Bouchard M., Zurdo J., Nettleton E.J., Dobson C.M., Robinson C.V. Formation of insulin amyloid fibrils followed by FTIR simulatenouly 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
  • 33
    • 0035957228 scopus 로고    scopus 로고
    • Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates
    • Khurana R., Gillespie J.R., Talapatra A., Minert L.J., Ionescu-Zanetti C., Millett I., et al. Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates. Biochemistry. 40:2001;3525-3535.
    • (2001) Biochemistry , vol.40 , pp. 3525-3535
    • Khurana, R.1    Gillespie, J.R.2    Talapatra, A.3    Minert, L.J.4    Ionescu-Zanetti, C.5    Millett, I.6
  • 34
    • 0035804936 scopus 로고    scopus 로고
    • Identification of a novel human islet amyloid polypeptide β-sheet domain and factors influencing fibrillogenesis
    • Jaikaran E.T.A., Higham C.E., Serpell L.C., Zurdo J., Gross M., Clark A., et al. Identification of a novel human islet amyloid polypeptide β-sheet domain and factors influencing fibrillogenesis. J. Mol. Biol. 308:2001;515-525.
    • (2001) J. Mol. Biol. , vol.308 , pp. 515-525
    • Jaikaran, E.T.A.1    Higham, C.E.2    Serpell, L.C.3    Zurdo, J.4    Gross, M.5    Clark, A.6
  • 35
    • 0037059069 scopus 로고    scopus 로고
    • Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases
    • Chiti F., Calamai M., Taddei N., Stefani M., Ramponi G., Dobson C.M. Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases. Proc. Natl Acad. Sci. USA. 99:2002;16419-16426.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 16419-16426
    • Chiti, F.1    Calamai, M.2    Taddei, N.3    Stefani, M.4    Ramponi, G.5    Dobson, C.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.