SEARCH

SEARCH BY CITATION

References

  • Allen, F.H. and Johnson, O. 1991. Automated conformational analysis from crystallographic data. IV. Statistical descriptors for a distribution of torsion angles. Acta Crystallogr. B47: 6267.
  • Bax, A. and Davis, D.G. 1985. MLEV-17 based two dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65: 355360.
  • Becker, J.W. and Reeke, G.N. Jr. 1985. Three-dimensional structure of β2-microglobulin. Proc. Nat. Acad. Sci. 82: 42254229.
  • Bellotti, V., Stoppini, M., Mangione, P., Sunde, M., Robinson, C.V., Asti, L., Brancaccio, D., and Ferri, G. 1998. β2-microglobulin can be refolded into a native state from ex vivo amyloid fibrils. Eur. J. Biochem. 258: 6167.
  • Bjorkman, P.J., Saper, M.A., Samaroui, B., Bennet, W.S., Strominger, J.L., and Wiley, D.C. 1987. Structure of the human class I histocompatibility antigen, HLA-A2. Nature 329: 506512.
  • Braunschweiler, L. and Ernst, R.R. 1983. Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy. J. Magn. Reson. 53: 521528.
  • Capeiller-Blandin, C., Delaveau, T., and Descamps-Latscha, B. 1991. Structural modifications of human β2-microglobulin treated with oxygen-derived radicals. Biochem. J. 277: 175182.
  • Cheng, Y.K. and Rossky, P.J. 1998. Surface topography dependence of biomolecular hydrophobic hydration. Nature 392: 696699.
  • Chiti, F., Mangione, P., Andreola, A., Giorgetti, S., Stefani, M., Dobson, C.M., Bellotti, V., and Taddei, N. 2001. Detection of two partially structured species in the folding process of the amyloidogenic protein β2-microglobulin. microglobulin 307: 379391
  • Connors, L.H., Shirahama, T., Skinner, M., Fenves, A., and Cohen, A.S. 1985. In vitro formation of amyloid fibrils from intact β2-microglobulin Biochem. Biophys. Res. Commun. 131: 10631068.
  • Dayringer, H.E., Tramontano, A., Sprang, S.R., and Fletterick, R.J. 1986. Interactive program for visualization and modelling of proteins, nucleic acids and small molecules. J. Mol. Graphics 6: 8287.
  • De Lorenzi, E., Grossi, S., Massolini, G., Giorgetti, S., Mangione, P., Andreola, A., Chiti, F., Bellotti, V., and Caccialanza, G. 2001. Capillary electrophoresis investigation of a partially unfolded conformation of β2-microglobulin. Electophoresis (in press).
  • Doreleijers, J.F., Rullmann, J.A.C., and Kaptein, R. 1998. Quality assessment of NMR structures: A statistical survey. J. Mol. Biol. 281: 149164.
  • Esposito, G., Carver, J.A., Boyd, J., and Campbell, I.D. 1987. High resolution 1H NMR study of the solution structure of alamethicin. Biochemistry 26: 10431050.
  • Esposito, G., Fogolari, F., Damante, G., Formisano, S., Tell, G., Leonardi, A., Di Lauro, R., and Viglino, P. 1996. Analysis of the solution structure of the homeodomain of rat thyroid transcription factor 1 by 1H-NMR spectroscopy and restrained molecular mechanics. Eur. J. Biochem. 241: 101113.
  • Esposito, G., Michelutti, R., Verdone, G., Viglino, P., Hernández, H., Robonson, C.V., Amoresano, A., Dal Piaz, F., Monti, M., Pucci, P., Mangione, P., Stoppini, M., Merlini, G., Ferri, G., and Bellotti, V. 2000. Removal of the N-terminal hexapeptide from human β2-microglobulin facilitates protein aggregation and fibril formation. Protein Sci. 9: 831845.
  • Gejyo, F., Yamada, T., Odani, S., Nakagawa, Y., Arakawa, M., Kunitomo, T., Kataoka, H., Suzuki, M., Hirasawa, Y., Shirahama, T., Cohen, A.S., and Schmid, K. 1985. A new form of amyloid protein associated with hemodialysis was identified as β2-microglobulin. Biochem. Biophys. Res. Commun. 129: 701706.
  • Güntert, P., Braun, W., and Wüthrich, K. 1991. Efficient computation of three-dimensional protein structure in solution from nuclear magnetic resonance data using the program DIANA and supporting programs CALIBA, HABAS and GLOMSA. J. Mol. Biol. 217: 517530.
  • Güntert, P., Mumenthaler, C., and Wüthrich, K. 1997. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273: 283298.
  • Hurle, M.R., Helms, L.R., Li, L., Chan, W., and Wetzel, R. 1994. A role for destabilizing amino acid replacement in light-chain amyloidosis. Proc. Natl. Acad. Sci. 91: 54465450.
  • Hwang, T.L. and Shaka, A.J. 1995. Water suppression that works. Excitation sculpting using arbitrary waveforms and pulsed field gradients. J. Mag. Reson. 112: 275279.
  • Hyberts, S.G., Goldberg, M.S., Havel, T.F., and Wagner, G. 1992. The solution structure of eglin c based on measurements of many NOE and coupling constants. Protein Sci. 1: 736751.
  • Jeener, J., Meier, B.H., Bachmann, P., and Ernst, R.R. 1979. Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71: 286292.
  • Kabsh, W. and Sander, C. 1983. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 25772637.
  • Keeler, J., Clowes, R.T., Davis, A.L., and Laue, E.D. 1994. Pulsed field gradients: Theory and practice. Meth. Enzymol. 239: 145207.
  • Koradi, R., Billeter, M., and Wüthrich, K. 1996. MOLMOL: A program for display and analysis of macromolecular structure. J. Mol. Graphics 14: 5155.
  • Laskowski, R.A., Rullmann, J.A.C., MacArthur, M.W., Kaptein, R., and Thornton, J.M. 1996. AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8: 477486.
  • Linke, R.P., Hampl, H., Bartel-Schwarze, S., and Eulitz, M. 1987. β2-microglobulin, different fragments and polymers thereof in synovial amyloid in long-term hemodialysis. Biol. Chem. Hoppe Seyler 368: 137144.
  • Linke, R.P., Hampl, H., Lobeck, H., Ritz, E., Bommer, J., Waldherr, R., and Eulitz, M. 1989. Lysine-specific cleavage of β2-microglobulin in amyloid deposits associated with haemodialysis. Kidney Int. 36: 675681.
  • Marion, D. and Wüthrich, K. 1983. Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of proton–proton spin–spin coupling constants in proteins. Biochem. Biophys. Res. Commun. 113: 967974.
  • 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.
  • Miyata, T., Oda, O., Iinagi, R., Iida, Y., Araki, N., Yamada, N., Horiuchi, S., Taniguchi, N., Maeda, K., and Kinoshita, T. 1993. β2-microglobulin modified with advanced glycation end products is a major component of haemodialysis-associated amyloidosis. J. Clin. Invest. 92: 12431252.
  • Morgan, C.J., Gelfand, M., Atreya, C., and Miranker, A.D. 2001. Kidney dialysis-associated amyloidosis: A molecular role for copper in fiber formation. J. Mol. Biol. 309: 339345.
  • Okon, M., Bray, P., and Vucelic, D. 1992. 1H NMR assignments and secondary structure of human β2-microglobulin in solution. Biochemistry 31: 89068915.
  • Piantini, U., Sørensen, O.W., and Ernst, R.R. 1982. Multiple quantum filters for elucidating NMR coupling networks. J. Am. Chem. Soc. 104: 68006801.
  • Piotto, M., Saudek, V., and Sklenar, V. 1992. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2: 661665.
  • Saper, M.A., Bjorkman, P.J., and Wiley, D.C. 1991. Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution. J. Mol. Biol. 219: 277319.
  • Shaka, A.J., Lee, C.J., and Pines, A. 1988. Iterative schemes for bilinear operators: Application to spin decoupling. J. Magn. Reson. 77: 274293.
  • States, D.J., Haberkorn, R.A., and Ruben, D.J. 1982. A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants. J. Magn. Reson. 48: 286292.
  • Stoppini, M., Bellotti, V., Mangione, P., Merlini, G., and Ferri, G. 1997. Use of anti-β2 microglobulin mAb to study formation of amyloid fibrils. Eur. J. Biochem. 249: 2126.
  • Sunde, M., Serpell, L.C., Bartlam, M., Fraser, P.E., Pepys, M.B., and Blake, C.C.F. 1997. Common core structure of amyloid fibrils by sinchrotron X-ray diffraction. J. Mol. Biol. 273: 729739.
  • Wang, A.C. and Bax, A. 1996. Determination of the backbone dihedral angles φ in human ubiquitin from reparametrized empirical Karplus equations. J. Amer. Chem. Soc. 118: 24832494.
  • Wang, Y., Nip, A.M., and Wishart, D.S. 1997. A simple method to quantitatively measure polypeptide JHNHα coupling constants from TOCSY or NOESY spectra. J. Biomol. NMR 10: 373382.
  • Weiner, S.J., Kollman, P.A., Case, D.A., Singh, U.C., Ghio, C., Alagona, G., Profeta, S. Jr., and Weiner, P. 1984. A new force field for molecular mechanical simulation of nucleic acids and proteins. J. Am. Chem. Soc. 106: 765784.
  • Wüthrich, K. 1986. NMR spectroscopy of proteins and nucleic acids. Wiley & Sons, NY.
  • Wüthrich, K., Billeter, M., and Braun, W. 1983. Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton–proton distance constraints with nuclear magnetic resonance. J. Mol. Biol. 169: 949961.