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Volumn 39, Issue 1, 2006, Pages 1-55

Molecular structure of amyloid fibrils: Insights from solid-state NMR

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; AMINO ACID; AMYLIN; AMYLOID; AMYLOID BETA PROTEIN; CALCITONIN; POLYPEPTIDE; PRION PROTEIN;

EID: 33750017513     PISSN: 00335835     EISSN: 14698994     Source Type: Journal    
DOI: 10.1017/S0033583506004173     Document Type: Review
Times cited : (460)

References (222)
  • 1
    • 0001264601 scopus 로고
    • Selective determination of anisotropic magnetic interactions from high resolution NMR spectra of powdered samples
    • ALLA, M. A., KUNDLA, E. I. & LIPPMAA, E. T. (1978). Selective determination of anisotropic magnetic interactions from high resolution NMR spectra of powdered samples. JETP Letters 27, 194-197.
    • (1978) JETP Letters , vol.27 , pp. 194-197
    • Alla, M.A.1    Kundla, E.I.2    Lippmaa, E.T.3
  • 3
    • 4043165350 scopus 로고
    • Removal of dipolar broadening of nuclear magnetic resonance spectra of solids by specimen rotation
    • ANDREW, E. R., BRADBURY, A. & EADES, R. G. (1959). Removal of dipolar broadening of nuclear magnetic resonance spectra of solids by specimen rotation. Nature 183, 1802-1803.
    • (1959) Nature , vol.183 , pp. 1802-1803
    • Andrew, E.R.1    Bradbury, A.2    Eades, R.G.3
  • 5
  • 6
    • 0037960361 scopus 로고    scopus 로고
    • Site-specific identification of non-β-strand conformations in Alzheimer's β-amyloid fibrils by solid state NMR
    • ANTZUTKIN, O. N., BALBACH, J. J. & TYCKO, R. (2003). Site-specific identification of non-β-strand conformations in Alzheimer's β-amyloid fibrils by solid state NMR. Biophysical Journal 84, 3326-3335.
    • (2003) Biophysical Journal , vol.84 , pp. 3326-3335
    • Antzutkin, O.N.1    Balbach, J.J.2    Tycko, R.3
  • 7
    • 0037168446 scopus 로고    scopus 로고
    • Supramolecular structural constraints on Alzheimer's β-amyloid fibrils from electron microscopy and solid state nuclear magnetic resonance
    • ANTZUTKIN, O. N., LEAPMAN, R. D., BALBACH, J. J. & TYCKO, R. (2002). Supramolecular structural constraints on Alzheimer's β-amyloid fibrils from electron microscopy and solid state nuclear magnetic resonance. Biochemistry 41, 15436-15450.
    • (2002) Biochemistry , vol.41 , pp. 15436-15450
    • Antzutkin, O.N.1    Leapman, R.D.2    Balbach, J.J.3    Tycko, R.4
  • 8
    • 4644296906 scopus 로고    scopus 로고
    • Anatomy of an amyloidogenic intermediate: Conversion of β-sheet to α-sheet structure in transthyretin at acidic pH
    • ARMEN, R. S., ALONSO, D. O. V. & DAGGETT, V. (2004a). Anatomy of an amyloidogenic intermediate: conversion of β-sheet to α-sheet structure in transthyretin at acidic pH. Structure 12, 1847-1863.
    • (2004) Structure , vol.12 , pp. 1847-1863
    • Armen, R.S.1    Alonso, D.O.V.2    Daggett, V.3
  • 9
    • 4143067019 scopus 로고    scopus 로고
    • Pauling and Corey's α-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease
    • ARMEN, R. S., DEMARCO, M. L., ALONSO, D. O. V. & DAGGETT, V. (2004b). Pauling and Corey's α-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease. Proceedings of the National Academy of Sciences USA 101, 11622-11627.
    • (2004) Proceedings of the National Academy of Sciences USA , vol.101 , pp. 11622-11627
    • Armen, R.S.1    Demarco, M.L.2    Alonso, D.O.V.3    Daggett, V.4
  • 11
    • 0001419932 scopus 로고
    • The x-ray interpretation of denaturation and the structure of the seed globulins
    • ASTBURY, W. T., DICKINSON, S. & BAILEY, K. (1935). The x-ray interpretation of denaturation and the structure of the seed globulins. Biochemica Journal 29, 2351.
    • (1935) Biochemica Journal , vol.29 , pp. 2351
    • Astbury, W.T.1    Dickinson, S.2    Bailey, K.3
  • 13
    • 0035997080 scopus 로고    scopus 로고
    • Supramolecular structure in full-length Alzheimer's β-amyloid fibrils: Evidence for a parallel β-sheet organization from solid state nuclear magnetic resonance
    • BALBACH, J. J., PETKOVA, A. T., OYLER, N. A., ANTZUTKIN, O. N., GORDON, D. J., MEREDITH, S. C. & TYCKO, R. (2002). Supramolecular structure in full-length Alzheimer's β-amyloid fibrils: evidence for a parallel β-sheet organization from solid state nuclear magnetic resonance. Biophysical Journal 83, 1205-1216.
    • (2002) Biophysical Journal , vol.83 , pp. 1205-1216
    • Balbach, J.J.1    Petkova, A.T.2    Oyler, N.A.3    Antzutkin, O.N.4    Gordon, D.J.5    Meredith, S.C.6    Tycko, R.7
  • 21
    • 0026583834 scopus 로고
    • Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent
    • BESSEN, R. A. & MARSH, R. F. (1992). Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent. Journal of Virology 66, 2096-2101.
    • (1992) Journal of Virology , vol.66 , pp. 2096-2101
    • Bessen, R.A.1    Marsh, R.F.2
  • 22
    • 0035833997 scopus 로고    scopus 로고
    • An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates parallel β-fibrils
    • BEVIVINO, A. E. & LOLL, P. J. (2001). An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates parallel β-fibrils. Proceedings of the National Academy of Sciences USA 98, 11955-11960.
    • (2001) Proceedings of the National Academy of Sciences USA , vol.98 , pp. 11955-11960
    • Bevivino, A.E.1    Loll, P.J.2
  • 23
    • 0035798396 scopus 로고    scopus 로고
    • Solid-state NMR data support a helix-loop-helix structural model for the N-terminal half of HIV-1 Rev in fibrillar form
    • BLANCO, F. J., HESS, S., PANNELL, L. K., RIZZO, N. W. & TYCKO, R. (2001). Solid-state NMR data support a helix-loop-helix structural model for the N-terminal half of HIV-1 Rev in fibrillar form. Journal of Molecular Biology 313, 845-859.
    • (2001) Journal of Molecular Biology , vol.313 , pp. 845-859
    • Blanco, F.J.1    Hess, S.2    Pannell, L.K.3    Rizzo, N.W.4    Tycko, R.5
  • 27
    • 26844435756 scopus 로고    scopus 로고
    • Molecular dynamics simulations of Alzheimer's β-amyloid protofilaments
    • BUCHETE, N. V., TYCKO, R. & HUMMER, G. (2005). Molecular dynamics simulations of Alzheimer's β-amyloid protofilaments. Journal of Molecular Biology 353, 804-821.
    • (2005) Journal of Molecular Biology , vol.353 , pp. 804-821
    • Buchete, N.V.1    Tycko, R.2    Hummer, G.3
  • 30
    • 0041327067 scopus 로고    scopus 로고
    • Symmetry principles for the design of radiofrequency pulse sequences in the nuclear magnetic resonance of rotating solids
    • CARRAVETTA, M., EDEN, M., ZHAO, X., BRINKMANN, A. & LEVITT, M. H. (2000). Symmetry principles for the design of radiofrequency pulse sequences in the nuclear magnetic resonance of rotating solids. Chemical Physics Letters 321, 205-215.
    • (2000) Chemical Physics Letters , vol.321 , pp. 205-215
    • Carravetta, M.1    Eden, M.2    Zhao, X.3    Brinkmann, A.4    Levitt, M.H.5
  • 32
    • 17444413067 scopus 로고    scopus 로고
    • In vitro generation of infectious scrapie prions
    • CASTILLA, J., SAA, P., HETZ, C. & SOTO, C. (2005). In vitro generation of infectious scrapie prions. Cell 121, 195-206.
    • (2005) Cell , vol.121 , pp. 195-206
    • Castilla, J.1    Saa, P.2    Hetz, C.3    Soto, C.4
  • 33
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • CAUGHEY, B. & LANSBURY, P. T. (2003). Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annual Review of Neuroscience 26, 267-298.
    • (2003) Annual Review of Neuroscience , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 34
    • 0033610870 scopus 로고    scopus 로고
    • Strain-dependent differences in β-sheet conformations of abnormal prion protein
    • CAUGHEY, B., RAYMOND, G. J. & BESSEN, R. A. (1998). Strain-dependent differences in β-sheet conformations of abnormal prion protein. Journal of Biological Chemistry 273, 32230-32235.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 32230-32235
    • Caughey, B.1    Raymond, G.J.2    Bessen, R.A.3
  • 35
    • 0001228293 scopus 로고    scopus 로고
    • R sequences for the scalar-coupling mediated homonuclear correlation spectroscopy under fast magic-angle spinning
    • CHAN, J. C. C. & BRUNKLAUS, G. (2001). R sequences for the scalar-coupling mediated homonuclear correlation spectroscopy under fast magic-angle spinning. Chemical Physics Letters 349, 104-112.
    • (2001) Chemical Physics Letters , vol.349 , pp. 104-112
    • Chan, J.C.C.1    Brunklaus, G.2
  • 36
    • 23244449092 scopus 로고    scopus 로고
    • Parallel β-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p
    • CHAN, J. C. C., OYLER, N. A., YAU, W. M. & TYCKO, R. (2005). Parallel β-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p. Biochemistry 44, 10669-10680.
    • (2005) Biochemistry , vol.44 , pp. 10669-10680
    • Chan, J.C.C.1    Oyler, N.A.2    Yau, W.M.3    Tycko, R.4
  • 38
    • 0141620310 scopus 로고    scopus 로고
    • Solid state NMR spectroscopy method for determination of the backbone torsion angle ψ in peptides with isolated uniformly labeled residues
    • CHAN, J. C. C. & TYCKO, R. (2003b). Solid state NMR spectroscopy method for determination of the backbone torsion angle ψ in peptides with isolated uniformly labeled residues. Journal of the American Chemical Society 125, 11828-11829.
    • (2003) Journal of the American Chemical Society , vol.125 , pp. 11828-11829
    • Chan, J.C.C.1    Tycko, R.2
  • 39
    • 2542464085 scopus 로고    scopus 로고
    • Broadband rotational resonance in solid state NMR spectroscopy
    • CHAN, J. C. C. & TYCKO, R. (2004). Broadband rotational resonance in solid state NMR spectroscopy. Journal of Chemical Physics 120, 8349-8352.
    • (2004) Journal of Chemical Physics , vol.120 , pp. 8349-8352
    • Chan, J.C.C.1    Tycko, R.2
  • 40
    • 0031593854 scopus 로고    scopus 로고
    • Molecular modeling of the Aβ1-42 peptide from Alzheimer's disease
    • CHANEY, M. O., WEBSTER, S. D., KUO, Y. M. & ROHER, A. E. (1998). Molecular modeling of the Aβ1-42 peptide from Alzheimer's disease. Protein Engineering 11, 761-767.
    • (1998) Protein Engineering , vol.11 , pp. 761-767
    • Chaney, M.O.1    Webster, S.D.2    Kuo, Y.M.3    Roher, A.E.4
  • 42
    • 0034646391 scopus 로고    scopus 로고
    • Fibrils formed in vitro from α-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid
    • CONWAY, K. A., HARPER, J. D. & LANSBURY, P. T. (2000). Fibrils formed in vitro from α-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid. Biochemistry 39, 2552-2563.
    • (2000) Biochemistry , vol.39 , pp. 2552-2563
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 43
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • CORNILESCU, G., DELAGLIO, F. & BAX, A. (1999). Protein backbone angle restraints from searching a database for chemical shift and sequence homology. Journal of Biomolecular NMR 13, 289-302.
    • (1999) Journal of Biomolecular NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 44
    • 0002084355 scopus 로고    scopus 로고
    • Solid-state NMR measurement of ψ in peptides: A NCCN 2Q-heteronuclear local field experiment
    • COSTA, P. R., GROSS, J. D., HONG, M. & GRIFFIN, R. G. (1997). Solid-state NMR measurement of ψ in peptides: a NCCN 2Q-heteronuclear local field experiment. Chemical Physics Letters 280, 95-103.
    • (1997) Chemical Physics Letters , vol.280 , pp. 95-103
    • Costa, P.R.1    Gross, J.D.2    Hong, M.3    Griffin, R.G.4
  • 45
    • 0030885650 scopus 로고    scopus 로고
    • The protein product of the HET-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog
    • COUSTOU, V., DELEU, C., SAUPE, S. & BEGUERET, J. (1997). The protein product of the HET-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proceedings of the National Academy of Sciences USA 94, 9773-9778.
    • (1997) Proceedings of the National Academy of Sciences USA , vol.94 , pp. 9773-9778
    • Coustou, V.1    Deleu, C.2    Saupe, S.3    Begueret, J.4
  • 47
    • 0025977281 scopus 로고
    • Straight and paired helical filaments in Alzheimer's disease have a common structural unit
    • CROWTHER, R. A. (1991). Straight and paired helical filaments in Alzheimer's disease have a common structural unit. Proceedings of the National Academy of Sciences USA 88, 2288-2292.
    • (1991) Proceedings of the National Academy of Sciences USA , vol.88 , pp. 2288-2292
    • Crowther, R.A.1
  • 48
    • 0030464914 scopus 로고    scopus 로고
    • Amyloid deposition and other measures of neuropathology predict cognitive status in Alzheimer's disease
    • CUMMINGS, B. J., PIKE, C. J., SHANKLE, R. & COTMAN, C. W. (1996). β-Amyloid deposition and other measures of neuropathology predict cognitive status in Alzheimer's disease. Neurobiology of Aging 17, 921-933.
    • (1996) Neurobiology of Aging , vol.17 , pp. 921-933
    • Cummings, B.J.1    Pike, C.J.2    Shankle, R.3    Cotman, C.W.4
  • 50
    • 0028188303 scopus 로고
    • Chemical shifts of carbonyl carbons in peptides and proteins
    • DEDIOS, A. C. & OLDFIELD, E. (1994). Chemical shifts of carbonyl carbons in peptides and proteins. Journal of the American Chemical Society 116, 11485-11488.
    • (1994) Journal of the American Chemical Society , vol.116 , pp. 11485-11488
    • Dedios, A.C.1    Oldfield, E.2
  • 51
    • 0027308278 scopus 로고
    • Secondary and tertiary structural effects on protein NMR chemical shifts: An ab initio approach
    • DEDIOS, A. C., PEARSON, J.G. & OLDFIELD, E. (1993). Secondary and tertiary structural effects on protein NMR chemical shifts: an ab initio approach. Science 260, 1491-1496.
    • (1993) Science , vol.260 , pp. 1491-1496
    • Dedios, A.C.1    Pearson, J.G.2    Oldfield, E.3
  • 52
    • 0032568793 scopus 로고    scopus 로고
    • A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion
    • DEPACE, A. H., SANTOSO, A., HILLNER, P. & WEISSMAN, J. S. (1998). A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion. Cell 93, 1241-1252.
    • (1998) Cell , vol.93 , pp. 1241-1252
    • Depace, A.H.1    Santoso, A.2    Hillner, P.3    Weissman, J.S.4
  • 53
    • 0141733169 scopus 로고    scopus 로고
    • Structural organization of α-synuclein fibrils studied by site-directed spin labeling
    • DER-SARKISSIAN, A., JAO, C. C., CHEN, J. & LANGEN, R. (2003). Structural organization of α-synuclein fibrils studied by site-directed spin labeling. Journal of Biological Chemistry 278, 37530-37535.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 37530-37535
    • Der-Sarkissian, A.1    Jao, C.C.2    Chen, J.3    Langen, R.4
  • 54
    • 0346106076 scopus 로고    scopus 로고
    • Metal binding and oxidation of amyloid-β within isolated senile plaque cores: Raman microscopic evidence
    • DONG, J., ATWOOD, C. S., ANDERSON, V. E., SIEDLAK, S. L., SMITH, M. A., PERRY, G. & CAREY, P. R. (2003). Metal binding and oxidation of amyloid-β within isolated senile plaque cores: Raman microscopic evidence. Biochemistry 42, 2768-2773.
    • (2003) Biochemistry , vol.42 , pp. 2768-2773
    • Dong, J.1    Atwood, C.S.2    Anderson, V.E.3    Siedlak, S.L.4    Smith, M.A.5    Perry, G.6    Carey, P.R.7
  • 56
    • 0037058949 scopus 로고    scopus 로고
    • Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein
    • EDSKES, H. K. & WICKNER, R. B. (2002). Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein. Proceedings of the National Academy of Sciences USA 99, 16384-16391.
    • (2002) Proceedings of the National Academy of Sciences USA , vol.99 , pp. 16384-16391
    • Edskes, H.K.1    Wickner, R.B.2
  • 57
    • 2542561209 scopus 로고    scopus 로고
    • A DECODER NMR study of backbone orientation in Nephila clavipes dragline silk under varying strain and draw rate
    • ELES, P. T. & MICHAL, C. A. (2004). A DECODER NMR study of backbone orientation in Nephila clavipes dragline silk under varying strain and draw rate. Biomacromolecules 5, 661-665.
    • (2004) Biomacromolecules , vol.5 , pp. 661-665
    • Eles, P.T.1    Michal, C.A.2
  • 58
    • 0036845354 scopus 로고    scopus 로고
    • The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation
    • FANDRICH, M. & DOBSON, C. M. (2002). The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation. EMBO Journal 21, 5682-5690.
    • (2002) EMBO Journal , vol.21 , pp. 5682-5690
    • Fandrich, M.1    Dobson, C.M.2
  • 61
    • 0032729982 scopus 로고    scopus 로고
    • Computationally derived structural models of the β-amyloid found in Alzheimer's disease plaques and the interaction with possible aggregation inhibitors
    • GEORGE, A. R. & HOWLETT, D. R. (1999). Computationally derived structural models of the β-amyloid found in Alzheimer's disease plaques and the interaction with possible aggregation inhibitors. Biopolymers 50, 733-741.
    • (1999) Biopolymers , vol.50 , pp. 733-741
    • George, A.R.1    Howlett, D.R.2
  • 65
    • 0033849965 scopus 로고    scopus 로고
    • Studies on the in vitro assembly of Aβ1-40 colon; implications for the search for Aβ fibril formation inhibitors
    • GOLDSBURY, C. S., WIRTZ, S., MULLER, S. A., SUNDERJI, S., WICKI, P., AEBI, U. & FREY, P. (2000b). Studies on the in vitro assembly of Aβ1-40 colon; implications for the search for Aβ fibril formation inhibitors. Journal of Structural Biology 130, 217-231.
    • (2000) Journal of Structural Biology , vol.130 , pp. 217-231
    • Goldsbury, C.S.1    Wirtz, S.2    Muller, S.A.3    Sunderji, S.4    Wicki, P.5    Aebi, U.6    Frey, P.7
  • 67
    • 0036299470 scopus 로고    scopus 로고
    • Improved narrowband dipolar recoupling for homonuclear distance measurements in rotating solids
    • GOOBES, G. & VEGA, S. (2002). Improved narrowband dipolar recoupling for homonuclear distance measurements in rotating solids. Journal of Magnetic Resonance 154, 236-251.
    • (2002) Journal of Magnetic Resonance , vol.154 , pp. 236-251
    • Goobes, G.1    Vega, S.2
  • 68
    • 0346057932 scopus 로고    scopus 로고
    • Increasing the amphiphilicity of an amyloidogenic peptide changes the β-sheet structure in the fibrils from antiparallel to parallel
    • GORDON, D. J., BALBACH, J. J., TYCKO, R. & MEREDITH, S. C. (2004). Increasing the amphiphilicity of an amyloidogenic peptide changes the β-sheet structure in the fibrils from antiparallel to parallel. Biophysical Journal 86, 428-434.
    • (2004) Biophysical Journal , vol.86 , pp. 428-434
    • Gordon, D.J.1    Balbach, J.J.2    Tycko, R.3    Meredith, S.C.4
  • 69
    • 0035902507 scopus 로고    scopus 로고
    • Inhibition of β-amyloid(40) fibrillogenesis and disassembly of β-amyloid(40) fibrils by short β-amyloid congeners containing N-methyl amino acids at alternate residues
    • GORDON, D. J., SCIARRETTA, K. L. & MEREDITH, S. C. (2001). Inhibition of β-amyloid(40) fibrillogenesis and disassembly of β-amyloid(40) fibrils by short β-amyloid congeners containing N-methyl amino acids at alternate residues. Biochemistry 40, 8237-8245.
    • (2001) Biochemistry , vol.40 , pp. 8237-8245
    • Gordon, D.J.1    Sciarretta, K.L.2    Meredith, S.C.3
  • 72
  • 75
    • 0000277622 scopus 로고
    • A simple magic angle spinning NMR experiment for the dephasing of rotational echoes of dipolar coupled homonuclear spin pairs
    • GULLION, T. & VEGA, S. (1992). A simple magic angle spinning NMR experiment for the dephasing of rotational echoes of dipolar coupled homonuclear spin pairs. Chemical Physics Letters 194, 423-428.
    • (1992) Chemical Physics Letters , vol.194 , pp. 423-428
    • Gullion, T.1    Vega, S.2
  • 77
    • 36049055838 scopus 로고
    • Coherent averaging effects in magnetic resonance
    • HAEBERLEN, U. & WAUGH, J. S. (1968). Coherent averaging effects in magnetic resonance. Physics Review 175, 453-467.
    • (1968) Physics Review , vol.175 , pp. 453-467
    • Haeberlen, U.1    Waugh, J.S.2
  • 78
    • 0025275241 scopus 로고
    • Molecular determinants of amyloid deposition in Alzheimer's disease: Conformational studies of synthetic β-protein fragments
    • HALVERSON, K., FRASER, P. E., KIRSCHNER, D. A. & LANSBURY, P. T. (1990). Molecular determinants of amyloid deposition in Alzheimer's disease: conformational studies of synthetic β-protein fragments. Biochemistry 29, 2639-2644.
    • (1990) Biochemistry , vol.29 , pp. 2639-2644
    • Halverson, K.1    Fraser, P.E.2    Kirschner, D.A.3    Lansbury, P.T.4
  • 79
  • 80
    • 27644518721 scopus 로고    scopus 로고
    • Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid state NMR
    • HEISE, H., HOYER, W., BECKER, S., ANDRONESI, O. C., RIEDEL, D. & BALDUS, M. (2005). Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid state NMR. Proceedings of the National Academy of Sciences USA 102, 15871-15876.
    • (2005) Proceedings of the National Academy of Sciences USA , vol.102 , pp. 15871-15876
    • Heise, H.1    Hoyer, W.2    Becker, S.3    Andronesi, O.C.4    Riedel, D.5    Baldus, M.6
  • 81
    • 48549109765 scopus 로고
    • 13C spin diffusion in the determination of intermolecular structure in solids
    • 13C spin diffusion in the determination of intermolecular structure in solids. Journal of Magnetic Resonance 58, 458-461.
    • (1984) Journal of Magnetic Resonance , vol.58 , pp. 458-461
    • Henrichs, P.M.1    Linder, M.2
  • 82
    • 0031189051 scopus 로고    scopus 로고
    • Site-resolved determination of peptide torsion angle φ from the relative orientations of backbone N-H and C-H bonds by solid state NMR
    • HONG, M., GROSS, J. D. & GRIFFIN, R. G. (1997). Site-resolved determination of peptide torsion angle φ from the relative orientations of backbone N-H and C-H bonds by solid state NMR. Journal of Physical Chemistry B 101, 5869-5874.
    • (1997) Journal of Physical Chemistry B , vol.101 , pp. 5869-5874
    • Hong, M.1    Gross, J.D.2    Griffin, R.G.3
  • 85
  • 87
    • 0035872678 scopus 로고    scopus 로고
    • 13C dipolar recoupling under very fast magic-angle spinning in solid state nuclear magnetic resonance: Applications to distance measurements, spectral assignments, and high-throughput secondary-structure determination
    • 13C dipolar recoupling under very fast magic-angle spinning in solid state nuclear magnetic resonance: applications to distance measurements, spectral assignments, and high-throughput secondary-structure determination. Journal of Chemical Physics 114, 8473-8483.
    • (2001) Journal of Chemical Physics , vol.114 , pp. 8473-8483
    • Ishii, Y.1
  • 88
    • 0035873018 scopus 로고    scopus 로고
    • Measurement of dipole-coupled lineshapes in a many-spin system by constant-time two-dimensional solid state NMR with high-speed magic-angle spinning
    • ISHII, Y., BALBACH, J. J. & TYCKO, R. (2001a). Measurement of dipole-coupled lineshapes in a many-spin system by constant-time two-dimensional solid state NMR with high-speed magic-angle spinning. Chemical Physics 266, 231-236.
    • (2001) Chemical Physics , vol.266 , pp. 231-236
    • Ishii, Y.1    Balbach, J.J.2    Tycko, R.3
  • 89
    • 0030167114 scopus 로고    scopus 로고
    • Relayed anisotropy correlation NMR: Determination of dihedral angles in solids
    • ISHII, Y., TERAO, T. & KAINOSHO, M. (1996). Relayed anisotropy correlation NMR: determination of dihedral angles in solids. Chemical Physics Letters 256, 133-140.
    • (1996) Chemical Physics Letters , vol.256 , pp. 133-140
    • Ishii, Y.1    Terao, T.2    Kainosho, M.3
  • 91
    • 0033064395 scopus 로고    scopus 로고
    • Cα and Cβ carbon-13 chemical shifts in proteins from an empirical database
    • IWADATE, M., ASAKURA, T. & WILLIAMSON, M. P. (1999). Cα and Cβ carbon-13 chemical shifts in proteins from an empirical database. Journal of Biomolecular NMR 13, 199-211.
    • (1999) Journal of Biomolecular NMR , vol.13 , pp. 199-211
    • Iwadate, M.1    Asakura, T.2    Williamson, M.P.3
  • 98
    • 9144267018 scopus 로고    scopus 로고
    • Identifying structural features of fibrillar islet amyloid polypeptide using site-directed spin labeling
    • JAYASINGHE, S. A. & LANGEN, R. (2004). Identifying structural features of fibrillar islet amyloid polypeptide using site-directed spin labeling. Journal of Biological Chemistry 279, 48420-48425.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 48420-48425
    • Jayasinghe, S.A.1    Langen, R.2
  • 100
    • 0042847751 scopus 로고    scopus 로고
    • Cryoelectron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
    • JIMENEZ, J. L., GUIJARRO, J. L., ORLOVA, E., ZURDO, J., DOBSON, C. M., SUNDE, M. & SAIBIL, H. R. (1999). Cryoelectron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO Journal 18, 815-821.
    • (1999) EMBO Journal , vol.18 , pp. 815-821
    • Jimenez, J.L.1    Guijarro, J.L.2    Orlova, E.3    Zurdo, J.4    Dobson, C.M.5    Sunde, M.6    Saibil, H.R.7
  • 102
    • 16244376187 scopus 로고    scopus 로고
    • The parallel superpleated β-structure as a model for amyloid fibrils of human amylin
    • KAJAVA, A. V., AEBI, U. & STEVEN, A. C. (2005). The parallel superpleated β-structure as a model for amyloid fibrils of human amylin. Journal of Molecular Biology 348, 247-252.
    • (2005) Journal of Molecular Biology , vol.348 , pp. 247-252
    • Kajava, A.V.1    Aebi, U.2    Steven, A.C.3
  • 107
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • KAYED, R., HEAD, E., THOMPSON, J. L., MCINTIRE, T. M., MILTON, S. C., COTMAN, C.W. & GLABE, C. G. (2003). Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486-489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    Mcintire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 108
    • 0027360175 scopus 로고
    • High-resolution conformation of gramicidin-A in a lipid bilayer by solid state NMR
    • KETCHEM, R. R., HU, W. & CROSS, T. A. (1993). High-resolution conformation of gramicidin-A in a lipid bilayer by solid state NMR. Science 261, 1457-1460.
    • (1993) Science , vol.261 , pp. 1457-1460
    • Ketchem, R.R.1    Hu, W.2    Cross, T.A.3
  • 109
    • 0035797795 scopus 로고    scopus 로고
    • Structural features of the Aβ amyloid fibril elucidated by limited proteolysis
    • KHETERPAL, I., WILLIAMS, A., MURPHY, C., BLEDSOE, B. & WETZEL, R. (2001). Structural features of the Aβ amyloid fibril elucidated by limited proteolysis. Biochemistry 40, 11757-11767.
    • (2001) Biochemistry , vol.40 , pp. 11757-11767
    • Kheterpal, I.1    Williams, A.2    Murphy, C.3    Bledsoe, B.4    Wetzel, R.5
  • 111
    • 0036708168 scopus 로고    scopus 로고
    • Paradigm shifts in Alzheimer's disease and other neuro-degenerative disorders: The emerging role of oligomeric assemblies
    • KIRKITADZE, M. D., BITAN, G. & TEPLOW, D. B. (2002). Paradigm shifts in Alzheimer's disease and other neuro-degenerative disorders: the emerging role of oligomeric assemblies. Journal of Neuroscience Research 69, 567-577.
    • (2002) Journal of Neuroscience Research , vol.69 , pp. 567-577
    • Kirkitadze, M.D.1    Bitan, G.2    Teplow, D.B.3
  • 112
    • 0035812658 scopus 로고    scopus 로고
    • Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis
    • KIRKITADZE, M. D., CONDRON, M. M. & TEPLOW, D. B. (2001). Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis. Journal of Molecular Biology 312, 1103-1119.
    • (2001) Journal of Molecular Biology , vol.312 , pp. 1103-1119
    • Kirkitadze, M.D.1    Condron, M.M.2    Teplow, D.B.3
  • 114
    • 20444474976 scopus 로고    scopus 로고
    • Structural insights into a yeast prion illuminate nucleation and strain diversity
    • KRISHNAN, R. & LINDQUIST, S. L. (2005). Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature 435, 765-772.
    • (2005) Nature , vol.435 , pp. 765-772
    • Krishnan, R.1    Lindquist, S.L.2
  • 118
    • 0032539573 scopus 로고    scopus 로고
    • Amyloid fibrils may be assembled from β-helical protofibrils
    • LAZO, N. D. & DOWNING, D. T. (1998). Amyloid fibrils may be assembled from β-helical protofibrils. Biochemistry 37, 1731-1735.
    • (1998) Biochemistry , vol.37 , pp. 1731-1735
    • Lazo, N.D.1    Downing, D.T.2
  • 121
    • 0033040551 scopus 로고    scopus 로고
    • An atomic model for the pleated β-sheet structure of Aβ amyloid protofilaments
    • LI, L. P., DARDEN, T. A., BARTOLOTTI, L., KOMINOS, D. & PEDERSEN, L. G. (1999). An atomic model for the pleated β-sheet structure of Aβ amyloid protofilaments. Biophysical Journal 76, 2871-2878.
    • (1999) Biophysical Journal , vol.76 , pp. 2871-2878
    • Li, L.P.1    Darden, T.A.2    Bartolotti, L.3    Kominos, D.4    Pedersen, L.G.5
  • 122
    • 0036298936 scopus 로고    scopus 로고
    • A robust technique for two-dimensional separation of undistorted chemical shift anisotropy powder patterns in magic-angle spinning NMR
    • LIU, S. F., MAO, J. D. & SCHMIDT-ROHR, K. (2002). A robust technique for two-dimensional separation of undistorted chemical shift anisotropy powder patterns in magic-angle spinning NMR. Journal of Magnetic Resonance 155, 15-28.
    • (2002) Journal of Magnetic Resonance , vol.155 , pp. 15-28
    • Liu, S.F.1    Mao, J.D.2    Schmidt-Rohr, K.3
  • 123
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: As domains continue to swap
    • LIU, Y. & EISENBERG, D. (2002). 3D domain swapping: as domains continue to swap. Protein Science 11, 1285-1299.
    • (2002) Protein Science , vol.11 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 125
    • 17144382523 scopus 로고    scopus 로고
    • The GB1 amyloid fibril: Recruitment of the peripheral β-strands of the domain swapped dimer into the polymeric interface
    • LOUIS, J. M., BYEON, I. J. L., BAXAL, U. & GRONENBORN, A. M. (2005). The GB1 amyloid fibril: Recruitment of the peripheral β-strands of the domain swapped dimer into the polymeric interface. Journal of Molecular Biology 348, 687-698.
    • (2005) Journal of Molecular Biology , vol.348 , pp. 687-698
    • Louis, J.M.1    Byeon, I.J.L.2    Baxal, U.3    Gronenborn, A.M.4
  • 126
    • 36149028286 scopus 로고
    • Free induction decays of rotating solids
    • LOWE, I. J. (1959). Free induction decays of rotating solids. Physical Review Letters 2, 285-287.
    • (1959) Physical Review Letters , vol.2 , pp. 285-287
    • Lowe, I.J.1
  • 130
    • 0034722985 scopus 로고    scopus 로고
    • Formation of mixed fibrils demonstrates the generic nature and potential utility of amyloid nanostructures
    • MACPHEE, C. E. & DOBSON, C. M. (2000). Formation of mixed fibrils demonstrates the generic nature and potential utility of amyloid nanostructures. Journal of the American Chemical Society 122, 12707-12713.
    • (2000) Journal of the American Chemical Society , vol.122 , pp. 12707-12713
    • Macphee, C.E.1    Dobson, C.M.2
  • 132
    • 0031962158 scopus 로고    scopus 로고
    • Structural analysis of Alzheimer's β(1-40) amyloid: Protofilament assembly of tubular fibrils
    • MALINCHIK, S. B., INOUYE, H., SZUMOWSKI, K. E. & KIRSCHNER, D. A. (1998). Structural analysis of Alzheimer's β(1-40) amyloid: Protofilament assembly of tubular fibrils. Biophysical Journal 74, 537-545.
    • (1998) Biophysical Journal , vol.74 , pp. 537-545
    • Malinchik, S.B.1    Inouye, H.2    Szumowski, K.E.3    Kirschner, D.A.4
  • 135
    • 36549095702 scopus 로고
    • Excitation of multiple quantum transitions under magic-angle spinning conditions: Adamantane
    • MEIER, B.H. & EARL, W. L. (1986). Excitation of multiple quantum transitions under magic-angle spinning conditions: adamantane. Journal of Chemical Physics 85, 4905-4911.
    • (1986) Journal of Chemical Physics , vol.85 , pp. 4905-4911
    • Meier, B.H.1    Earl, W.L.2
  • 138
    • 0031127043 scopus 로고    scopus 로고
    • Development of the multiple sequence approximation within the Agadir model of α-helix formation: Comparison with Zimm-Bragg and Lifson-Roig formalisms
    • MUNOZ, V. & SERRANO, L. (1997). Development of the multiple sequence approximation within the Agadir model of α-helix formation: comparison with Zimm-Bragg and Lifson-Roig formalisms. Biopolymers 41, 495-509.
    • (1997) Biopolymers , vol.41 , pp. 495-509
    • Munoz, V.1    Serrano, L.2
  • 140
    • 17144398382 scopus 로고    scopus 로고
    • Probing the structure of the infectious amyloid form of the prion-forming domain of HET-s using high resolution hydrogen/deuterium exchange monitored by mass spectrometry
    • NAZABAL, A., MADDELEIN, M. L., BONNEU, M., SAUPE, S. J. & SCHMITTER, J. M. (2005). Probing the structure of the infectious amyloid form of the prion-forming domain of HET-s using high resolution hydrogen/deuterium exchange monitored by mass spectrometry. Journal of Biological Chemistry 280, 13220-13228.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 13220-13228
    • Nazabal, A.1    Maddelein, M.L.2    Bonneu, M.3    Saupe, S.J.4    Schmitter, J.M.5
  • 142
    • 0033939451 scopus 로고    scopus 로고
    • Three-dimensional structure determination of a uniformly labeled molecule by frequency-selective dipolar recoupling under magic-angle spinning
    • NOMURA, K., TAKEGOSHI, K., TERAO, T., UCHIDA, K. & KAINOSHO, M. (2000). Three-dimensional structure determination of a uniformly labeled molecule by frequency-selective dipolar recoupling under magic-angle spinning. Journal of Biomolecular NMR 17, 111-123.
    • (2000) Journal of Biomolecular NMR , vol.17 , pp. 111-123
    • Nomura, K.1    Takegoshi, K.2    Terao, T.3    Uchida, K.4    Kainosho, M.5
  • 143
    • 0000785903 scopus 로고
    • Rotary resonance recoupling of dipolar interactions in solid state nuclear magnetic resonance spectroscopy
    • OAS, T. G., GRIFFIN, R. G. & LEVITT, M. H. (1988). Rotary resonance recoupling of dipolar interactions in solid state nuclear magnetic resonance spectroscopy. Journal of Chemical Physics 89, 692-695.
    • (1988) Journal of Chemical Physics , vol.89 , pp. 692-695
    • Oas, T.G.1    Griffin, R.G.2    Levitt, M.H.3
  • 144
    • 1842637853 scopus 로고    scopus 로고
    • Absolute structural constraints on amyloid fibrils from solid state NMR spectroscopy of partially oriented samples
    • OYLER, N. A. & TYCKO, R. (2004). Absolute structural constraints on amyloid fibrils from solid state NMR spectroscopy of partially oriented samples. Journal of the American Chemical Society 126, 4478-4479.
    • (2004) Journal of the American Chemical Society , vol.126 , pp. 4478-4479
    • Oyler, N.A.1    Tycko, R.2
  • 145
    • 0034977531 scopus 로고    scopus 로고
    • Islet amyloid polypeptide: Identification of long-range contacts and local order on the fibrillogenesis pathway
    • PADRICK, S. B. & MIRANKER, A. D. (2001). Islet amyloid polypeptide: identification of long-range contacts and local order on the fibrillogenesis pathway. Journal of Molecular Biology 308, 783-794.
    • (2001) Journal of Molecular Biology , vol.308 , pp. 783-794
    • Padrick, S.B.1    Miranker, A.D.2
  • 146
    • 33744831968 scopus 로고    scopus 로고
    • Polymorphic fibril formation by residues 10-40 of the Alzheimer's β-amyloid peptide
    • in press
    • PARAVASTU, A. K., PETKOVA, A. T. & TYCKO, R. (in press). Polymorphic fibril formation by residues 10-40 of the Alzheimer's β-amyloid peptide. Biophysical Journal.
    • Biophysical Journal
    • Paravastu, A.K.1    Petkova, A.T.2    Tycko, R.3
  • 147
    • 34547926330 scopus 로고    scopus 로고
    • Frequency-selective homonuclear dipolar recoupling in solid state NMR
    • in press
    • PARAVASTU, A. K. & TYCKO, R. (in press). Frequency-selective homonuclear dipolar recoupling in solid state NMR. Journal of Chemical Physics.
    • Journal of Chemical Physics
    • Paravastu, A.K.1    Tycko, R.2
  • 153
    • 0344255649 scopus 로고    scopus 로고
    • Solid state NMR reveals a pH-dependent antiparallel β-sheet registry in fibrils formed by a β-amyloid peptide
    • PETKOVA, A. T., BUNTKOWSKY, G., DYDA, F., LEAPMAN, R. D., YAU, W. M. & TYCKO, R. (2004). Solid state NMR reveals a pH-dependent antiparallel β-sheet registry in fibrils formed by a β-amyloid peptide. Journal of Molecular Biology 335, 247-260.
    • (2004) Journal of Molecular Biology , vol.335 , pp. 247-260
    • Petkova, A.T.1    Buntkowsky, G.2    Dyda, F.3    Leapman, R.D.4    Yau, W.M.5    Tycko, R.6
  • 155
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils
    • PETKOVA, A. T., LEAPMAN, R. D., GUO, Z. H., YAU, W. M., MATTSON, M. P. & TYCKO, R. (2005). Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils. Science 307, 262-265.
    • (2005) Science , vol.307 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.H.3    Yau, W.M.4    Mattson, M.P.5    Tycko, R.6
  • 156
    • 1842631726 scopus 로고    scopus 로고
    • 13C-labeled solids: Effects on high-resolution magic-angle spinning NMR spectra and applications in structural studies of biomolecular systems
    • 13C-labeled solids: effects on high-resolution magic-angle spinning NMR spectra and applications in structural studies of biomolecular systems. Journal of Magnetic Resonance 168, 137-146.
    • (2004) Journal of Magnetic Resonance , vol.168 , pp. 137-146
    • Petkova, A.T.1    Tycko, R.2
  • 157
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils
    • PETKOVA, A. T., YAU, W. M. & TYCKO, R. (2006). Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils. Biochemistry 45, 498-512.
    • (2006) Biochemistry , vol.45 , pp. 498-512
    • Petkova, A.T.1    Yau, W.M.2    Tycko, R.3
  • 158
    • 0035125001 scopus 로고    scopus 로고
    • β-cell dysfunction and failure in type 2 diabetes: Potential mechanisms
    • PORTE, D. & KAHN, S. E. (2001). β-Cell dysfunction and failure in type 2 diabetes: potential mechanisms. Diabetes 50, S160-S163.
    • (2001) Diabetes , vol.50
    • Porte, D.1    Kahn, S.E.2
  • 160
    • 0037466613 scopus 로고    scopus 로고
    • Casting metal nanowires within discrete self-assembled peptide nanotubes
    • RECHES, M. & GAZIT, E. (2003). Casting metal nanowires within discrete self-assembled peptide nanotubes. Science 300, 625-627.
    • (2003) Science , vol.300 , pp. 625-627
    • Reches, M.1    Gazit, E.2
  • 164
  • 171
    • 24644510813 scopus 로고    scopus 로고
    • Amyloid-like fibrils of ribonuclease a with three-dimensional domain-swapped and native-like structure
    • SAMBASHIVAN, S., LIU, Y. S., SAWAYA, M. R., GINGERY, M. & EISENBERG, D. (2005). Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure. Nature 437, 266-269.
    • (2005) Nature , vol.437 , pp. 266-269
    • Sambashivan, S.1    Liu, Y.S.2    Sawaya, M.R.3    Gingery, M.4    Eisenberg, D.5
  • 174
    • 0029766182 scopus 로고    scopus 로고
    • 13C-labeled amino acids and peptides by separated-local-field double-quantum NMR
    • 13C-labeled amino acids and peptides by separated-local-field double-quantum NMR. Journal of the American Chemical Society 118, 7601-7603.
    • (1996) Journal of the American Chemical Society , vol.118 , pp. 7601-7603
    • Schmidt-Rohr, K.1
  • 175
    • 17644397372 scopus 로고    scopus 로고
    • Aβ 40-lactam(D23/K28) models a conformation highly favorable for nucleation of amyloid
    • SCIARRETTA, K. L., GORDON, D. J., PETKOVA, A. T., TYCKO, R. & MEREDITH, S. C. (2005). Aβ 40-lactam(D23/K28) models a conformation highly favorable for nucleation of amyloid. Biochemistry 44, 6003-6014.
    • (2005) Biochemistry , vol.44 , pp. 6003-6014
    • Sciarretta, K.L.1    Gordon, D.J.2    Petkova, A.T.3    Tycko, R.4    Meredith, S.C.5
  • 177
    • 0034716942 scopus 로고    scopus 로고
    • Direct visualisation of the β-sheet structure of synthetic Alzheimer's amyloid
    • SERPELL, L. C. & SMITH, J. M. (2000). Direct visualisation of the β-sheet structure of synthetic Alzheimer's amyloid. Journal of Molecular Biology 299, 225-231.
    • (2000) Journal of Molecular Biology , vol.299 , pp. 225-231
    • Serpell, L.C.1    Smith, J.M.2
  • 179
    • 1842862922 scopus 로고    scopus 로고
    • Solid-state NMR yields structural constraints on the V3 loop from HIV-1 gp120 bound to the 447-52D antibody Fv fragment
    • SHARPE, S., KESSLER, N., ANGLISTER, J. A., YAU, W. M. & TYCKO, R. (2004). Solid-state NMR yields structural constraints on the V3 loop from HIV-1 gp120 bound to the 447-52D antibody Fv fragment. Journal of the American Chemical Society 126, 4979-4990.
    • (2004) Journal of the American Chemical Society , vol.126 , pp. 4979-4990
    • Sharpe, S.1    Kessler, N.2    Anglister, J.A.3    Yau, W.M.4    Tycko, R.5
  • 180
    • 20444372360 scopus 로고    scopus 로고
    • Expression and purification of a recombinant peptide from the Alzheimer's β-amyloid protein for solid state NMR
    • SHARPE, S., YAU, W. M. & TYCKO, R. (2005). Expression and purification of a recombinant peptide from the Alzheimer's β-amyloid protein for solid state NMR. Protein Expression and Purification 42, 200-210.
    • (2005) Protein Expression and Purification , vol.42 , pp. 200-210
    • Sharpe, S.1    Yau, W.M.2    Tycko, R.3
  • 181
    • 31044432820 scopus 로고    scopus 로고
    • Structure and dynamics of the HIV-1 Vpu transmembrane domain revealed by solid state NMR with magic-angle spinning
    • SHARPE, S., YAU, W. M. & TYCKO, R. (2006). Structure and dynamics of the HIV-1 Vpu transmembrane domain revealed by solid state NMR with magic-angle spinning. Biochemistry 45, 918-933.
    • (2006) Biochemistry , vol.45 , pp. 918-933
    • Sharpe, S.1    Yau, W.M.2    Tycko, R.3
  • 182
    • 10644252759 scopus 로고    scopus 로고
    • An intersheet packing interaction in Aβ fibrils mapped by disulfide cross-linking
    • SHIVAPRASAD, S. & WETZEL, R. (2004). An intersheet packing interaction in Aβ fibrils mapped by disulfide cross-linking. Biochemistry 43, 15310-15317.
    • (2004) Biochemistry , vol.43 , pp. 15310-15317
    • Shivaprasad, S.1    Wetzel, R.2
  • 183
    • 18044391103 scopus 로고    scopus 로고
    • High-resolution solid state NMR spectroscopy of the prion protein HET-s in its amyloid conformation
    • SIEMER, A. B., RITTER, C., ERNST, M., RIEK, R. & MEIER, B. H. (2005). High-resolution solid state NMR spectroscopy of the prion protein HET-s in its amyloid conformation. Angewandte Chemie - International Edition 44, 2441-2444.
    • (2005) Angewandte Chemie - International Edition , vol.44 , pp. 2441-2444
    • Siemer, A.B.1    Ritter, C.2    Ernst, M.3    Riek, R.4    Meier, B.H.5
  • 184
    • 0041630890 scopus 로고    scopus 로고
    • Structure and texture of fibrous crystals formed by Alzheimer's Aβ(11-25) peptide fragment
    • SIKORSKI, P., ATKINS, E. D. T. & SERPELL, L. C. (2003). Structure and texture of fibrous crystals formed by Alzheimer's Aβ(11-25) peptide fragment. Structure 11, 915-926.
    • (2003) Structure , vol.11 , pp. 915-926
    • Sikorski, P.1    Atkins, E.D.T.2    Serpell, L.C.3
  • 189
    • 0026320119 scopus 로고
    • An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: Application of solid state NMR to the determination of protein secondary structure
    • SPENCER, R. G. S., HALVERSON, K. J., AUGER, M., MCDERMOTT, A. E., GRIFFIN, R. G. & LANSBURY, P. T. (1991). An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: application of solid state NMR to the determination of protein secondary structure. Biochemistry 30, 10382-10387.
    • (1991) Biochemistry , vol.30 , pp. 10382-10387
    • Spencer, R.G.S.1    Halverson, K.J.2    Auger, M.3    Mcdermott, A.E.4    Griffin, R.G.5    Lansbury, P.T.6
  • 191
    • 13844267500 scopus 로고    scopus 로고
    • The HPr proteins from the thermophile Bacillus stearothermophilus can form domain-swapped dimers
    • SRIDHARAN, S., RAZVI, A., SCHOLTZ, J. M. & SACCHETTINI, J. C. (2005). The HPr proteins from the thermophile Bacillus stearothermophilus can form domain-swapped dimers. Journal of Molecular Biology 346, 919-931.
    • (2005) Journal of Molecular Biology , vol.346 , pp. 919-931
    • Sridharan, S.1    Razvi, A.2    Scholtz, J.M.3    Sacchettini, J.C.4
  • 192
    • 0035801540 scopus 로고    scopus 로고
    • Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily
    • STANIFORTH, R. A., GIANNINI, S., HIGGINS, L. D., CONROY, M. J., HOUNSLOW, A. M., JERALA, R., CRAVEN, C. J. & WALTHO, J. P. (2001). Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily. EMBO Journal 20, 4774-4781.
    • (2001) EMBO Journal , vol.20 , pp. 4774-4781
    • Staniforth, R.A.1    Giannini, S.2    Higgins, L.D.3    Conroy, M.J.4    Hounslow, A.M.5    Jerala, R.6    Craven, C.J.7    Waltho, J.P.8
  • 193
    • 0036681397 scopus 로고    scopus 로고
    • Prediction of strand pairing in antiparallel and parallel β-sheets using information theory
    • STEWARD, R. E. & THORNTON, J. M. (2002). Prediction of strand pairing in antiparallel and parallel β-sheets using information theory. Proteins - Structure Function and Genetics 48, 178-191.
    • (2002) Proteins - Structure Function and Genetics , vol.48 , pp. 178-191
    • Steward, R.E.1    Thornton, J.M.2
  • 194
    • 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. Quarterly Reviews of Biophysics 31, 1-39.
    • (1998) Quarterly Reviews of Biophysics , vol.31 , pp. 1-39
    • Sunde, M.1    Blake, C.C.F.2
  • 196
    • 0031201794 scopus 로고    scopus 로고
    • Selective homonuclear polarization transfer in the tilted rotating frame under magic angle spinning in solids
    • TAKEGOSHI, K., NOMURA, K. & TERAO, T. (1997). Selective homonuclear polarization transfer in the tilted rotating frame under magic angle spinning in solids. Journal of Magnetic Resonance 127, 206-216.
    • (1997) Journal of Magnetic Resonance , vol.127 , pp. 206-216
    • Takegoshi, K.1    Nomura, K.2    Terao, T.3
  • 197
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • TANAKA, M., CHIEN, P., NABER, N., COOKE, R. & WEISSMAN, J. S. (2004). Conformational variations in an infectious protein determine prion strain differences. Nature 428, 323-328.
    • (2004) Nature , vol.428 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 198
    • 0033605278 scopus 로고    scopus 로고
    • Prion domain initiation of amyloid formation in vitro from native Ure2p
    • TAYLOR, K. L., CHENG, N. Q., 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.Q.2    Williams, R.W.3    Steven, A.C.4    Wickner, R.B.5
  • 202
    • 0037174998 scopus 로고    scopus 로고
    • Structural and dynamic features of Alzheimer's Aβ peptide in amyloid fibrils studied by site-directed spin labeling
    • TOROK, M., MILTON, S., KAYED, R., WU, P., MCINTIRE, T., GLABE, C.G. & LANGEN, R. (2002). Structural and dynamic features of Alzheimer's Aβ peptide in amyloid fibrils studied by site-directed spin labeling. Journal of Biological Chemistry 277, 40810-40815.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 40810-40815
    • Torok, M.1    Milton, S.2    Kayed, R.3    Wu, P.4    Mcintire, T.5    Glabe, C.G.6    Langen, R.7
  • 203
    • 0030253417 scopus 로고    scopus 로고
    • Prospects for resonance assignments in multidimensional solid state NMR spectra of uniformly labeled proteins
    • TYCKO, R. (1996). Prospects for resonance assignments in multidimensional solid state NMR spectra of uniformly labeled proteins. Journal of Biomolecular NMR 8, 239-251.
    • (1996) Journal of Biomolecular NMR , vol.8 , pp. 239-251
    • Tycko, R.1
  • 204
    • 4244132605 scopus 로고
    • Measurement of nuclear magnetic dipole-dipole couplings in magic-angle spinning NMR
    • TYCKO, R. & DABBAGH, G. (1990). Measurement of nuclear magnetic dipole-dipole couplings in magic-angle spinning NMR. Chemical Physics Letters 173, 461-465.
    • (1990) Chemical Physics Letters , vol.173 , pp. 461-465
    • Tycko, R.1    Dabbagh, G.2
  • 205
    • 0000106305 scopus 로고
    • Nuclear magnetic resonance crystallography: Molecular orientational ordering in three forms of solid methanol
    • TYCKO, R. & DABBAGH, G. (1991). Nuclear magnetic resonance crystallography: molecular orientational ordering in three forms of solid methanol. Journal of the American Chemical Society 113, 3592-3593.
    • (1991) Journal of the American Chemical Society , vol.113 , pp. 3592-3593
    • Tycko, R.1    Dabbagh, G.2
  • 206
    • 0000782602 scopus 로고
    • Determination of chemical shift anisotropy lineshapes in a two-dimensional magic-angle spinning NMR experiment
    • TYCKO, R., DABBAGH, G. & MIRAU, P. A. (1989). Determination of chemical shift anisotropy lineshapes in a two-dimensional magic-angle spinning NMR experiment. Journal of Magnetic Resonance 85, 265-274.
    • (1989) Journal of Magnetic Resonance , vol.85 , pp. 265-274
    • Tycko, R.1    Dabbagh, G.2    Mirau, P.A.3
  • 207
    • 0038209242 scopus 로고    scopus 로고
    • Constraints on supramolecular structure in amyloid fibrils from two-dimensional solid state NMR spectroscopy with uniform isotopic labeling
    • TYCKO, R. & ISHII, Y. (2003). Constraints on supramolecular structure in amyloid fibrils from two-dimensional solid state NMR spectroscopy with uniform isotopic labeling. Journal of the American Chemical Society 125, 6606-6607.
    • (2003) Journal of the American Chemical Society , vol.125 , pp. 6606-6607
    • Tycko, R.1    Ishii, Y.2
  • 208
    • 0030575666 scopus 로고    scopus 로고
    • Investigation of molecular structure in solids by twodimensional NMR exchange spectroscopy with magic angle spinning
    • TYCKO, R., WELIKY, D.P. & BERGER, A. E. (1996). Investigation of molecular structure in solids by twodimensional NMR exchange spectroscopy with magic angle spinning. Journal of Chemical Physics 105, 7915-7930.
    • (1996) Journal of Chemical Physics , vol.105 , pp. 7915-7930
    • Tycko, R.1    Weliky, D.P.2    Berger, A.E.3
  • 209
    • 0035743161 scopus 로고    scopus 로고
    • Adiabatic dipolar recoupling in solid state NMR: The DREAM scheme
    • VEREL, R., ERNST, M. & MEIER, B. H. (2001). Adiabatic dipolar recoupling in solid state NMR: the DREAM scheme. Journal of Magnetic Resonance 150, 81-99.
    • (2001) Journal of Magnetic Resonance , vol.150 , pp. 81-99
    • Verel, R.1    Ernst, M.2    Meier, B.H.3
  • 210
    • 0042572518 scopus 로고    scopus 로고
    • Hydrogen exchange-mass spectrometry analysis of β-amyloid peptide structure
    • WANG, S. S. S., TOBLER, S. A., GOOD, T. A. & FERNANDEZ, E. J. (2003). Hydrogen exchange-mass spectrometry analysis of β-amyloid peptide structure. Biochemistry 42, 9507-9514.
    • (2003) Biochemistry , vol.42 , pp. 9507-9514
    • Wang, S.S.S.1    Tobler, S.A.2    Good, T.A.3    Fernandez, E.J.4
  • 212
    • 0001817565 scopus 로고
    • Correlation of chemical bond directions and functional group orientations in solids by two-dimensional NMR
    • WELIKY, D. P., DABBAGH, G. & TYCKO, R. (1993). Correlation of chemical bond directions and functional group orientations in solids by two-dimensional NMR. Journal of Magnetic Resonance Series A 104, 10-16.
    • (1993) Journal of Magnetic Resonance Series a , vol.104 , pp. 10-16
    • Weliky, D.P.1    Dabbagh, G.2    Tycko, R.3
  • 213
    • 0029831415 scopus 로고    scopus 로고
    • Determination of peptide conformations by two-dimensional magic angle spinning NMR exchange spectroscopy with rotor synchronization
    • WELIKY, D.P. & TYCKO, R. (1996). Determination of peptide conformations by two-dimensional magic angle spinning NMR exchange spectroscopy with rotor synchronization. Journal of the American Chemical Society 118, 8487-8488.
    • (1996) Journal of the American Chemical Society , vol.118 , pp. 8487-8488
    • Weliky, D.P.1    Tycko, R.2
  • 214
    • 15544388942 scopus 로고    scopus 로고
    • Hydrogendeuterium (H/D) exchange mapping of Aβ(1-40) amyloid fibril secondary structure using nuclear magnetic resonance spectroscopy
    • WHITTEMORE, N. A., MISHRA, R., KHETERPAL, I., WILLIAMS, A. D., WETZEL, R. & SERPERSU, E. H. (2005). Hydrogendeuterium (H/D) exchange mapping of Aβ(1-40) amyloid fibril secondary structure using nuclear magnetic resonance spectroscopy. Biochemistry 44, 4434-4441.
    • (2005) Biochemistry , vol.44 , pp. 4434-4441
    • Whittemore, N.A.1    Mishra, R.2    Kheterpal, I.3    Williams, A.D.4    Wetzel, R.5    Serpersu, E.H.6
  • 215
    • 0028308104 scopus 로고
    • Ure3 as an altered Ure2 protein: Evidence for a prion analog in Saccharomyces cerevisiae
    • WICKNER, R. B. (1994). Ure3 as an altered Ure2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 264, 566-569.
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1
  • 218
    • 0037420373 scopus 로고    scopus 로고
    • Determination of internuclear distances in uniformly labeled molecules by rotational resonance solid state NMR
    • WILLIAMSON, P. T. F., VERHOEVEN, A., ERNST, M. & MEIER, B. H. (2003). Determination of internuclear distances in uniformly labeled molecules by rotational resonance solid state NMR. Journal of the American Chemical Society 125, 2718-2722.
    • (2003) Journal of the American Chemical Society , vol.125 , pp. 2718-2722
    • Williamson, P.T.F.1    Verhoeven, A.2    Ernst, M.3    Meier, B.H.4
  • 221
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • WISHART, D. S., SYKES, B.D. & RICHARDS, F. M. (1991). Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. Journal of Molecular Biology 222, 311-333.
    • (1991) Journal of Molecular Biology , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3


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