SEARCH

SEARCH BY CITATION

References

  • Arai, M., Ikura, T., Semitsonov, G.V., Kihara, H., Amemiya, Y., and Kuwajima, K. 1998. Kinetic refolding of β-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy. J. Mol. Biol. 275: 149162.
  • Bauer, R., Carrotta, R., Rischel, C., Øgendal, L. 2000. Characterization and isolation of intermediates in β-lactolobulin heat aggregation. Biophys. J. 79: 10301038.
  • Bellare, J.R., Davis, H.T., Scriven, L.E., and Talmon, Y. 1988. Controlled environment vitrification system: An improved sample preparation technique. J. Electron Microsc. Technol. 10: 87111
  • Booth, D.R., Sunde, M., Bellotti, V., Robinson, C.V., Hutchinson, W.L., Fraser, P.E., Hawkins, P.N., Dobson, C.M., Radford, S.E., Blake, C.C.F., et al. 1997. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature 385: 787793.
  • Brownlow, S., Cabral, J.H.M., Cooper, R., Flower, D.R., Yewdall, S.J., Polikarpov, I., North, A.C.T., and Sawyer, L. 1997. Bovine β-lactolobulin at 1.8 Å resolution—Still an enigmatic lipocalin. Structure 5: 481495.
  • Dobson, C.M. 1999. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24: 329332.
  • Dobson, C.M. 2000. Protein folding, evolution and disease. Eur. Biophys. J. 29: 233.
  • Fasman, G.D. 1996. Circular dichroism and conformational analysis of biomolecules. Plenum Press, New York.
  • Fersht, A. 1999. Structure and mechanism in protein science. Freeman, New York.
  • Fink, A.L. 1998. Protein aggregation: Folding aggregates, inclusion bodies and amyloid. Folding & Design 3: R9R23.
  • Forge, V., Hoshino, M., Kuwata, K., Arai, M., Kuwajima, K., Batt, C.A., and Goto, Y. 2000. Is folding of β-lactoglobulin non-hierachic? Intermediate with native-like β-sheet and non-native α-helix. J. Mol. Biol. 296: 10391051.
  • Fujiwara, K., Arai, M., Shimizu, A., Ikeguchi, M., Kuwajima, K., and Sugai, S. 1999. Folding–unfolding equilibrium and kinetics of equine β-lactolobulin: Equivalence between the equilibrium molten globule state and a burst-phase folding intermediate. Biochemistry 38: 44554463.
  • Hamada, D. and Goto, Y. 1997. The equilibrium intermediate of b-lactoglobulin with non-native α-helical structure. J. Mol. Biol. 269: 479487.
  • Hamada, D., Segawa, S., and Goto, Y. 1996. Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein. Nat. Struct. Biol. 3: 868873.
  • Hashimoto, M., Hsu, L.J., Sisk, A., Xia, Y., Takeda, A., Sundsmo, M., and Masliah, E. 1998. Human recombinant NACP/α-synuclein is aggregated and fibrillated in vitro: Relevance for Lewy body disease. Brain Research 799: 301306.
  • Ikeguchi, M., Kato, S., Shimizu, A., and Sugai, S. 1997. Molten globule state of equine β-lactoglobulin. Proteins: Struct. Funct. Genet. 27: 567575.
  • Ionescu-Zanetti, C., Khurana, R., Gillespie, J.R., Petrick, J.S., Trabachino, L.C., Minert, L.J., Carter, S.A., and Fink, A.L. 1999. Monitoring the assembly of Ig light-chain amyloid fibrils by atomic force microscopy. Proc. Natl. Acad. Sci. USA 96: 1317513179.
  • Johnson, W.G. 2000. Late-onset neurodegenerative diseases—The role of protein insolubility. J. Anat. 196: 609616.
  • Kayed, R., Bernhagen, J., Greenfield, N., Sweimeh, K., Brunner, H., Voelter, W., and Kapurniotu, A. 1999. Conformational transitions of Islet amyloid polypeptide (IAPP) in amyloid formation in vitro. J. Mol. Biol. 287: 781796.
  • Kobayashi, T., Ikeguchi, M., and Sugai, S. 2000. Molten globule structure of equine β-lactoglobulin probed by hydrogen exchange. J. Mol. Biol. 299: 757770.
  • Koradi, R., Billeter, M., and Wütrich, K. 1996 MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graphics 14: 5155.
  • Kuwata, K., Hoshino, M., Era, S., Batt, C.A., and Goto, Y. 1998. α [RIGHTWARDS ARROW] β transition of β-lactoglobulin as evidenced by heteronuclear NMR. J. Mol. Biol. 283: 731739.
  • Kuwata, K., Shastry, R., Cheng, H., Hoshino, M., Batt, C.A., Goto, Y., and Roder, H. 2001. Structural and kinetic characterization of early folding events in β-lactoglobulin. Nat. Struct. Biol. 8: 151155.
  • Le Vine, H., III 1995. Thioflavine T interaction with amyloid β-sheet structures. Amyloid: Int. J. Exp. Clin. Invest. 2: 16.
  • Manavalan, P. and Johnson, W.C., Jr. 1987. Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Anal. Biochem. 167: 7685.
  • Manderson, G.A., Hardman, M.J., and Creamer, L.K. 1998. Effect of heat treatment on the conformation and aggregation of β-lactoglobulin A, B and C. J. Agricul. Food Chem. 46: 50525061.
  • Matulis, D. and Lovrien, R. 1998 1-Anilino-8-naphthalene sulfonate anion–protein binding depends primarily on ion pair formation. Biophys. J. 74: 422429.
  • McParland, V.J., Kad, N.M., Kalverda, A.P., Brown, A., Kirwin-Jones, P., Hunter, M.G., Sunde, M., and Radford, S.E. 2000. Partially unfolded states of β2-microglobulin and amyloid formation in vitro. Biochemistry 39: 87358746.
  • Qi, X.L., Holt, C., McNulty, D., Clarke, D.T., Brownlow, S., and Jones, G.R. 1997. Effect of temperature on the secondary structure of β-lactoglobulin at pH 6.7 as determined by CD and IR spectroscopy: A test of the molten globule hypothesis. Biochem. J. 324: 341346.
  • Qin, B.Y., Bewley, M.C., Creamer, L.K., Baker, H.M., Baker, E.N., Geoffrey, B., and Jameson, G.B. 1999. Structural basis of the Tanford transition of bovine β-lactoglobulin. Biochemistry 37: 1401414023.
  • Rochet, J.C. and Lansbury, P.T. 2000. Amyloid fibrilloenesis: Themes and variations. Curr. Opin. Struct. Biol. 10: 6068.
  • Schweers, O., Mandelkow, E.-M., Biernat, J., and Mandelkow, E. 1995. Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein τ controls the in vitro assembly of paired helical filaments. Proc. Natl. Acad. Sci. USA 92: 84638467.
  • Shimada, K. and Cheftel, J.C. 1989. Sulfhydryl group/disulfide bond interchange reactions during heat-induced gelation of whey protein isolate. J. Agricul. Food Chem. 37: 161168.
  • von Bergen, M., Friedhoff, J., Heberle, J., Mandelkow, E.-M., and Mandelkow, E. 2000. Assembly of τ protein into Alzheimer paired helical filaments depends on a local sequence motif (306VQIVYK311) forming β structure. Proc. Natl. Acad. Sci. USA 97: 51295134.
  • Walsh, D.M., Lomakin, A., Benedek, G.B., Condron, M.M., and Teplow, D.B. 1997. Amyloid β-protein fibrillogenesis. Detection of a protofibrillar intermediate. J. Biol. Chem. 272: 2236422372.
  • Wilkins, D.K., Dobson, C.M., and Groβ, M. 2000. Biophysical studies of the development of amyloid fibrils from a peptide fragment of cold shock protein B. Eur. J. Biochem. 267: 26092616.