-
1
-
-
0037168655
-
A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR
-
DOI 10.1073/pnas.262663499
-
Petkova, A. T., Ishii, Y., Balbach, J. J., Antzutkin, O. N., Leapman, R. D., Delaglio, F., and Tycko, R. (2002) A structural model for Alzheimer β-amyloid fibrils based on experimental constraints from solid-state NMR. Proc. Natl. Acad. Sci. U.S.A. 99, 16742-16747 (Pubitemid 36034043)
-
(2002)
Proceedings of the National Academy of Sciences of the United States of America
, vol.99
, Issue.26
, pp. 16742-16747
-
-
Petkova, A.T.1
Ishii, Y.2
Balbach, J.J.3
Antzutkin, O.N.4
Leapman, R.D.5
Delaglio, F.6
Tycko, R.7
-
2
-
-
12244249201
-
Self-propagating, molecular level polymorphism in Alzheimer β-amyloid fibrils
-
Petkova, A. T., Leapman, R. D., Guo, Z., Yau, W. M., Mattson, M. P., and Tycko, R. (2005) Self-propagating, molecular level polymorphism in Alzheimer β-amyloid fibrils. Science 307, 262-265
-
(2005)
Science
, vol.307
, pp. 262-265
-
-
Petkova, A.T.1
Leapman, R.D.2
Guo, Z.3
Yau, W.M.4
Mattson, M.P.5
Tycko, R.6
-
3
-
-
57449091884
-
Molecular structural basis for polymorphism in Alzheimer β-amyloid fibrils
-
Paravastu, A. K., Leapman, R. D., Yau, W. M., and Tycko, R. (2008) Molecular structural basis for polymorphism in Alzheimer β-amyloid fibrils. Proc. Natl. Acad. Sci. U.S.A. 105, 18349-18354
-
(2008)
Proc. Natl. Acad. Sci. U.S.A.
, vol.105
, pp. 18349-18354
-
-
Paravastu, A.K.1
Leapman, R.D.2
Yau, W.M.3
Tycko, R.4
-
4
-
-
66149140617
-
Seeded growth of β-amyloid fibrils from Alzheimer brain-derived fibrils produces a distinct fibril structure
-
Paravastu, A. K., Qahwash, I., Leapman, R. D., Meredith, S. C., and Tycko, R. (2009) Seeded growth of β-amyloid fibrils from Alzheimer brain-derived fibrils produces a distinct fibril structure. Proc. Natl. Acad. Sci. U.S.A. 106, 7443-7448
-
(2009)
Proc. Natl. Acad. Sci. U.S.A.
, vol.106
, pp. 7443-7448
-
-
Paravastu, A.K.1
Qahwash, I.2
Leapman, R.D.3
Meredith, S.C.4
Tycko, R.5
-
5
-
-
80053554845
-
A new structural model of Aβ40 fibrils
-
Bertini, I., Gonnelli, L., Luchinat, C., Mao, J., and Nesi, A. (2011) A new structural model of Aβ40 fibrils. J. Am. Chem. Soc. 133, 16013-16022
-
(2011)
J. Am. Chem. Soc.
, vol.133
, pp. 16013-16022
-
-
Bertini, I.1
Gonnelli, L.2
Luchinat, C.3
Mao, J.4
Nesi, A.5
-
6
-
-
28444442999
-
Three-dimensional structure of Alzheimer amyloid β(1-42) fibrils
-
Lührs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Döbeli, H., Schubert, D., and Riek, R. (2005) Three-dimensional structure of Alzheimer amyloid β(1-42) fibrils. Proc. Natl. Acad. Sci. U.S.A. 102, 17342-17347
-
(2005)
Proc. Natl. Acad. Sci. U.S.A.
, vol.102
, pp. 17342-17347
-
-
Lührs, T.1
Ritter, C.2
Adrian, M.3
Riek-Loher, D.4
Bohrmann, B.5
Döbeli, H.6
Schubert, D.7
Riek, R.8
-
7
-
-
34249051698
-
Amide solvent protection analysis demonstrates that amyloid-β(1-40) and amyloid-β(1-42) form different fibrillar structures under identical conditions
-
DOI 10.1042/BJ20061561
-
Olofsson, A., Lindhagen-Persson, M., Sauer-Eriksson, A. E., and Ohman, A. (2007) Amide solvent protection analysis demonstrates that amyloid β(1-40) and amyloid β(1-42) form different fibrillar structures under identical conditions. Biochem. J. 404, 63-70 (Pubitemid 46788085)
-
(2007)
Biochemical Journal
, vol.404
, Issue.1
, pp. 63-70
-
-
Olofsson, A.1
Lindhagen-Persson, M.2
Sauer-Eriksson, A.E.3
Ohman, A.4
-
8
-
-
44949250850
-
Paired β-sheet structure of an Aβ(1-40) amyloid fibril revealed by electron microscopy
-
DOI 10.1073/pnas.0712290105
-
Sachse, C., Fändrich, M., and Grigorieff, N. (2008) Paired β-sheet structure of an Aβ(1-40) amyloid fibril revealed by electron microscopy. Proc. Natl. Acad. Sci. U.S.A. 105, 7462-7466 (Pubitemid 351830040)
-
(2008)
Proceedings of the National Academy of Sciences of the United States of America
, vol.105
, Issue.21
, pp. 7462-7466
-
-
Sachse, C.1
Fandrich, M.2
Grigorieff, N.3
-
9
-
-
73949117777
-
Comparison of Alzheimer Aβ(1-40) and Aβ(1-42) amyloid fibrils reveals similar protofilament structures
-
Schmidt, M., Sachse, C., Richter, W., Xu, C., Fändrich, M., and Grigorieff, N. (2009) Comparison of Alzheimer Aβ(1-40) and Aβ(1-42) amyloid fibrils reveals similar protofilament structures. Proc. Natl. Acad. Sci. U.S.A. 106, 19813-19818
-
(2009)
Proc. Natl. Acad. Sci. U.S.A.
, vol.106
, pp. 19813-19818
-
-
Schmidt, M.1
Sachse, C.2
Richter, W.3
Xu, C.4
Fändrich, M.5
Grigorieff, N.6
-
10
-
-
34249290108
-
Atomic structures of amyloid cross-β spines reveal varied steric zippers
-
DOI 10.1038/nature05695, PII NATURE05695
-
Sawaya, M. R., Sambashivan, S., Nelson, R., Ivanova, M. I., Sievers, S. A., Apostol, M. I., Thompson, M. J., Balbirnie, M., Wiltzius, J. J., McFarlane, H. T., Madsen, A. Ø., Riekel, C., and Eisenberg, D. (2007) Atomic structures of amyloid cross-β spines reveal varied steric zippers. Nature 447, 453-457 (Pubitemid 46816731)
-
(2007)
Nature
, vol.447
, Issue.7143
, pp. 453-457
-
-
Sawaya, M.R.1
Sambashivan, S.2
Nelson, R.3
Ivanova, M.I.4
Sievers, S.A.5
Apostol, M.I.6
Thompson, M.J.7
Balbirnie, M.8
Wiltzius, J.J.W.9
McFarlane, H.T.10
Madsen, A.O.11
Riekel, C.12
Eisenberg, D.13
-
11
-
-
77955273305
-
Aβ(1-40) forms five distinct amyloid structures whose β-sheet contents and fibril stabilities are correlated
-
Kodali, R., Williams, A. D., Chemuru, S., and Wetzel, R. (2010) Aβ(1-40) forms five distinct amyloid structures whose β-sheet contents and fibril stabilities are correlated. J. Mol. Biol. 401, 503-517
-
(2010)
J. Mol. Biol.
, vol.401
, pp. 503-517
-
-
Kodali, R.1
Williams, A.D.2
Chemuru, S.3
Wetzel, R.4
-
12
-
-
80054752317
-
Molecular basis for amyloid β polymorphism
-
Colletier, J. P., Laganowsky, A., Landau, M., Zhao, M., Soriaga, A. B., Goldschmidt, L., Flot, D., Cascio, D., Sawaya, M. R., and Eisenberg, D. (2011) Molecular basis for amyloid β polymorphism. Proc. Natl. Acad. Sci. U.S.A. 108, 16938-16943
-
(2011)
Proc. Natl. Acad. Sci. U.S.A.
, vol.108
, pp. 16938-16943
-
-
Colletier, J.P.1
Laganowsky, A.2
Landau, M.3
Zhao, M.4
Soriaga, A.B.5
Goldschmidt, L.6
Flot, D.7
Cascio, D.8
Sawaya, M.R.9
Eisenberg, D.10
-
13
-
-
79958058969
-
Recent progress in understanding Alzheimer β-amyloid structures
-
Fändrich, M., Schmidt, M., and Grigorieff, N. (2011) Recent progress in understanding Alzheimer β-amyloid structures. Trends Biochem. Sci. 36, 338-345
-
(2011)
Trends Biochem. Sci.
, vol.36
, pp. 338-345
-
-
Fändrich, M.1
Schmidt, M.2
Grigorieff, N.3
-
14
-
-
33750017513
-
Molecular structure of amyloid fibrils: Insights from solid- State NMR
-
Tycko, R. (2006) Molecular structure of amyloid fibrils: insights from solid- state NMR. Q. Rev. Biophys. 39, 1-55
-
(2006)
Q. Rev. Biophys.
, vol.39
, pp. 1-55
-
-
Tycko, R.1
-
15
-
-
79952498441
-
Solid-state NMR spectroscopic investigation of Aβ protofibrils: Implication of a β-sheet remodeling upon maturation into terminal amyloid fibrils
-
Scheidt, H. A., Morgado, I., Rothemund, S., Huster, D., and Fändrich, M. (2011) Solid-state NMR spectroscopic investigation of Aβ protofibrils: implication of a β-sheet remodeling upon maturation into terminal amyloid fibrils. Angew. Chem. Int. Ed. Engl. 50, 2837-2840
-
(2011)
Angew. Chem. Int. Ed. Engl.
, vol.50
, pp. 2837-2840
-
-
Scheidt, H.A.1
Morgado, I.2
Rothemund, S.3
Huster, D.4
Fändrich, M.5
-
16
-
-
36849084640
-
Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid
-
DOI 10.1038/nsmb1345, PII NSMB1345
-
Chimon, S., Shaibat, M. A., Jones, C. R., Calero, D. C., Aizezi, B., and Ishii, Y. (2007) Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer β-amyloid. Nat. Struct. Mol. Biol. 14, 1157-1164 (Pubitemid 350223342)
-
(2007)
Nature Structural and Molecular Biology
, vol.14
, Issue.12
, pp. 1157-1164
-
-
Chimon, S.1
Shaibat, M.A.2
Jones, C.R.3
Calero, D.C.4
Aizezi, B.5
Ishii, Y.6
-
17
-
-
77951975748
-
Structural conversion of neurotoxic amyloid β(1-42) oligomers to fibrils
-
Ahmed, M., Davis, J., Aucoin, D., Sato, T., Ahuja, S., Aimoto, S., Elliott, J. I., Van Nostrand, W. E., and Smith, S. O. (2010) Structural conversion of neurotoxic amyloid β(1-42) oligomers to fibrils. Nat. Struct. Mol. Biol. 17, 561-567
-
(2010)
Nat. Struct. Mol. Biol.
, vol.17
, pp. 561-567
-
-
Ahmed, M.1
Davis, J.2
Aucoin, D.3
Sato, T.4
Ahuja, S.5
Aimoto, S.6
Elliott, J.I.7
Van Nostrand, W.E.8
Smith, S.O.9
-
18
-
-
42449111198
-
Stabilization of a β-hairpin in monomeric Alzheimer's amyloid-β peptide inhibits amyloid formation
-
DOI 10.1073/pnas.0711731105
-
Hoyer, W., Grönwall, C., Jonsson, A., Ståhl, S., and Härd, T. (2008) Stabilization of a β-hairpin in monomeric Alzheimer amyloid β peptide inhibits amyloid formation. Proc. Natl. Acad. Sci. U.S.A. 105, 5099-5104 (Pubitemid 351738516)
-
(2008)
Proceedings of the National Academy of Sciences of the United States of America
, vol.105
, Issue.13
, pp. 5099-5104
-
-
Hoyer, W.1
Gronwall, C.2
Jonsson, A.3
Stahl, S.4
Hard, T.5
-
19
-
-
44949250971
-
Structural and dynamical characterization of fibrils from a disease-associated alanine expansion domain using proteolysis and solid-state NMR spectroscopy
-
DOI 10.1021/ja800120s
-
Sackewitz, M., Scheidt, H. A., Lodderstedt, G., Schierhorn, A., Schwarz, E., and Huster, D. (2008) Structural and dynamical characterization of fibrils from a disease-associated alanine expansion domain using proteolysis and solid-state NMR spectroscopy. J. Am. Chem. Soc. 130, 7172-7173 (Pubitemid 351813179)
-
(2008)
Journal of the American Chemical Society
, vol.130
, Issue.23
, pp. 7172-7173
-
-
Sackewitz, M.1
Scheidt, H.A.2
Lodderstedt, G.3
Schierhorn, A.4
Schwarz, E.5
Huster, D.6
-
20
-
-
77749237271
-
Conformational flexibility of Y145Stop human prion protein amyloid fibrils probed by solid-state nuclear magnetic resonance spectroscopy
-
Helmus, J. J., Surewicz, K., Surewicz, W. K., and Jaroniec, C. P. (2010) Conformational flexibility of Y145Stop human prion protein amyloid fibrils probed by solid-state nuclear magnetic resonance spectroscopy. J. Am. Chem. Soc. 132, 2393-2403
-
(2010)
J. Am. Chem. Soc.
, vol.132
, pp. 2393-2403
-
-
Helmus, J.J.1
Surewicz, K.2
Surewicz, W.K.3
Jaroniec, C.P.4
-
22
-
-
33845557418
-
Two-dimensional rotational spin-echo nuclear magnetic resonance in solids: Correlation of chemical shift and dipolar interactions
-
Munowitz, M. G., Griffin, R. G., Bodenhausen, G., and Huang, T. H. (1981) Two-dimensional rotational spin-echo nuclear magnetic resonance in solids: correlation of chemical shift and dipolar interactions. J. Am. Chem. Soc. 103, 2529-2533
-
(1981)
J. Am. Chem. Soc.
, vol.103
, pp. 2529-2533
-
-
Munowitz, M.G.1
Griffin, R.G.2
Bodenhausen, G.3
Huang, T.H.4
-
23
-
-
19944375100
-
Investigations of the structure and dynamics of membrane- Associated peptides by magic angle spinning NMR
-
Huster, D. (2005) Investigations of the structure and dynamics of membrane- associated peptides by magic angle spinning NMR. Prog. Nucl. Magn. Reson. Spectrosc. 46, 79-107
-
(2005)
Prog. Nucl. Magn. Reson. Spectrosc.
, vol.46
, pp. 79-107
-
-
Huster, D.1
-
24
-
-
0037489349
-
Structural and dynamical changes of the bindin B18 peptide upon binding to lipid membranes. A solid-state NMR study
-
DOI 10.1021/bi034239e
-
Barré, P., Zschörnig, O., Arnold, K., and Huster, D. (2003) Structural and dynamical changes of the bindin B18 peptide upon binding to lipid membranes. A solid-state NMR study. Biochemistry 42, 8377-8386 (Pubitemid 36858999)
-
(2003)
Biochemistry
, vol.42
, Issue.27
, pp. 8377-8386
-
-
Barre, P.1
Zschornig, O.2
Arnold, K.3
Huster, D.4
-
25
-
-
0035954376
-
Solid-state NMR investigation of the dynamics of the soluble and membrane-bound colicin Ia channel-forming domain
-
Huster, D., Xiao, L., and Hong, M. (2001) Solid-stateNMRinvestigation of the dynamics of the soluble and membrane-bound colicin Ia channelforming domain. Biochemistry 40, 7662-7674 (Pubitemid 32578030)
-
(2001)
Biochemistry
, vol.40
, Issue.25
, pp. 7662-7674
-
-
Huster, D.1
Xiao, L.2
Hong, M.3
-
27
-
-
27644518721
-
Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR
-
DOI 10.1073/pnas.0506109102
-
Heise, H., Hoyer, W., Becker, S., Andronesi, O. C., Riedel, D., and Baldus, M. (2005) Molecular level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR. Proc. Natl. Acad. Sci. U.S.A. 102, 15871-15876 (Pubitemid 41552835)
-
(2005)
Proceedings of the National Academy of Sciences of the United States of America
, vol.102
, Issue.44
, pp. 15871-15876
-
-
Heise, H.1
Hoyer, W.2
Becker, S.3
Andronesi, O.C.4
Riedel, D.5
Baldus, M.6
-
28
-
-
79952258282
-
The unique Alzheimer β-amyloid triangular fibril has a cavity along the fibril axis under physiological conditions
-
Miller, Y., Ma, B., and Nussinov, R. (2011) The unique Alzheimer β-amyloid triangular fibril has a cavity along the fibril axis under physiological conditions. J. Am. Chem. Soc. 133, 2742-2748
-
(2011)
J. Am. Chem. Soc.
, vol.133
, pp. 2742-2748
-
-
Miller, Y.1
Ma, B.2
Nussinov, R.3
-
29
-
-
34247637243
-
Structure and dynamics of parallel β-sheets, hydrophobic core, and loops in Alzheimer Aβ fibrils
-
Buchete, N. V., and Hummer, G. (2007) Structure and dynamics of parallel β-sheets, hydrophobic core, and loops in Alzheimer Aβ fibrils. Biophys. J. 92, 3032-3039
-
(2007)
Biophys. J.
, vol.92
, pp. 3032-3039
-
-
Buchete, N.V.1
Hummer, G.2
-
30
-
-
33744831968
-
Polymorphic fibril formation by residues 10-40 of the Alzheimer's β-amyloid peptide
-
DOI 10.1529/biophysj.105.076927
-
Paravastu, A. K., Petkova, A. T., and Tycko, R. (2006) Polymorphic fibril formation by residues 10-40 of the Alzheimer β-amyloid peptide. Biophys. J. 90, 4618-4629 (Pubitemid 43830905)
-
(2006)
Biophysical Journal
, vol.90
, Issue.12
, pp. 4618-4629
-
-
Paravastu, A.K.1
Petkova, A.T.2
Tycko, R.3
|