-
1
-
-
43549085062
-
We find them here, we find them there: functional bacterial amyloid
-
Otzen D., and Nielsen P.H. We find them here, we find them there: functional bacterial amyloid. Cell Mol. Life Sci. 65 (2008) 910-927
-
(2008)
Cell Mol. Life Sci.
, vol.65
, pp. 910-927
-
-
Otzen, D.1
Nielsen, P.H.2
-
2
-
-
34249782573
-
Similarities in the thermodynamics and kinetics of aggregation of disease-related Abeta(1-40) peptides
-
Meinhardt J., Tartaglia G.G., Pawar A., Christopeit T., Hortschansky P., Schroeckh V., Dobson C.M., Vendruscolo M., and Fandrich M. Similarities in the thermodynamics and kinetics of aggregation of disease-related Abeta(1-40) peptides. Protein Sci. 16 (2007) 1214-1222
-
(2007)
Protein Sci.
, vol.16
, pp. 1214-1222
-
-
Meinhardt, J.1
Tartaglia, G.G.2
Pawar, A.3
Christopeit, T.4
Hortschansky, P.5
Schroeckh, V.6
Dobson, C.M.7
Vendruscolo, M.8
Fandrich, M.9
-
3
-
-
0037076539
-
Growth of beta-amyloid(1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy
-
Nichols M.R., Moss M.A., Reed D.K., Lin W.L., Mukhopadhyay R., Hoh J.H., and Rosenberry T.L. Growth of beta-amyloid(1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy. Biochemistry 41 (2002) 6115-6127
-
(2002)
Biochemistry
, vol.41
, pp. 6115-6127
-
-
Nichols, M.R.1
Moss, M.A.2
Reed, D.K.3
Lin, W.L.4
Mukhopadhyay, R.5
Hoh, J.H.6
Rosenberry, T.L.7
-
4
-
-
34249028643
-
A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils
-
Vestergaard B., Groenning M., Roessle M., Kastrup J.S., van de W.M., Flink J.M., Frokjaer S., Gajhede M., and Svergun D.I. A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils. PLoS. Biol. 5 (2007) e134
-
(2007)
PLoS. Biol.
, vol.5
-
-
Vestergaard, B.1
Groenning, M.2
Roessle, M.3
Kastrup, J.S.4
van de, W.M.5
Flink, J.M.6
Frokjaer, S.7
Gajhede, M.8
Svergun, D.I.9
-
5
-
-
0037041420
-
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
-
Bucciantini M., Giannoni E., Chiti F., Baroni F., Formigli L., Zurdo J., Taddei N., Ramponi G., Dobson C.M., and Stefani M. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416 (2002) 507-511
-
(2002)
Nature
, vol.416
, pp. 507-511
-
-
Bucciantini, M.1
Giannoni, E.2
Chiti, F.3
Baroni, F.4
Formigli, L.5
Zurdo, J.6
Taddei, N.7
Ramponi, G.8
Dobson, C.M.9
Stefani, M.10
-
6
-
-
0034681163
-
Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy
-
Conway K.A., Lee S.J., Rochet J.C., Ding T.T., Williamson R.E., and Lansbury Jr. P.T. Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc. Natl. Acad. Sci. USA 97 (2000) 571-576
-
(2000)
Proc. Natl. Acad. Sci. USA
, vol.97
, pp. 571-576
-
-
Conway, K.A.1
Lee, S.J.2
Rochet, J.C.3
Ding, T.T.4
Williamson, R.E.5
Lansbury Jr., P.T.6
-
7
-
-
56349095198
-
Prefibrillar transthyretin oligomers and cold stored native tetrameric transthyretin are cytotoxic in cell culture
-
Sorgjerd K., Klingstedt T., Lindgren M., Kagedal K., and Hammarstrom P. Prefibrillar transthyretin oligomers and cold stored native tetrameric transthyretin are cytotoxic in cell culture. Biochem. Biophys. Res. Commun. 377 (2008) 1072-1078
-
(2008)
Biochem. Biophys. Res. Commun.
, vol.377
, pp. 1072-1078
-
-
Sorgjerd, K.1
Klingstedt, T.2
Lindgren, M.3
Kagedal, K.4
Hammarstrom, P.5
-
8
-
-
0347357617
-
Protein folding and misfolding
-
Dobson C.M. Protein folding and misfolding. Nature 426 (2003) 884-890
-
(2003)
Nature
, vol.426
, pp. 884-890
-
-
Dobson, C.M.1
-
9
-
-
0000464103
-
Fluorescent stains, with special reference to amyloid and connective tissues
-
Vassar P., and Culling C. Fluorescent stains, with special reference to amyloid and connective tissues. Arch. Pathol. 68 (1959) 487-498
-
(1959)
Arch. Pathol.
, vol.68
, pp. 487-498
-
-
Vassar, P.1
Culling, C.2
-
10
-
-
0014351967
-
X-ray diffraction studies on amyloid filaments
-
Eanes E.D., and Glenner G.G. X-ray diffraction studies on amyloid filaments. J. Histochem. Cytochem. 16 (1968) 673-677
-
(1968)
J. Histochem. Cytochem.
, vol.16
, pp. 673-677
-
-
Eanes, E.D.1
Glenner, G.G.2
-
11
-
-
65249169320
-
Cross-beta spine architecture of fibrils formed by the amyloidogenic segment NFGSVQFV of medin from solid-state NMR and X-ray fibre diffraction measurements
-
Madine J., Copland A., Serpell L., and Middleton D. Cross-beta spine architecture of fibrils formed by the amyloidogenic segment NFGSVQFV of medin from solid-state NMR and X-ray fibre diffraction measurements. Biochemistry 48 (2009) 3089-3099
-
(2009)
Biochemistry
, vol.48
, pp. 3089-3099
-
-
Madine, J.1
Copland, A.2
Serpell, L.3
Middleton, D.4
-
12
-
-
57349120654
-
Structural insights into the polymorphism of amyloid-like fibrils formed by region 20-29 of amylin revealed by solid-state NMR and X-ray fiber diffraction
-
Madine J., Jack E., Stockley P.G., Radford S.E., Serpell L.C., and Middleton D.A. Structural insights into the polymorphism of amyloid-like fibrils formed by region 20-29 of amylin revealed by solid-state NMR and X-ray fiber diffraction. J. Am. Chem. Soc. 130 (2008) 14990-15001
-
(2008)
J. Am. Chem. Soc.
, vol.130
, pp. 14990-15001
-
-
Madine, J.1
Jack, E.2
Stockley, P.G.3
Radford, S.E.4
Serpell, L.C.5
Middleton, D.A.6
-
13
-
-
33845334180
-
3D structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state NMR
-
Iwata K., Fujiwara T., Matsuki Y., Akutsu H., Takahashi S., Naiki H., and Goto Y. 3D structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state NMR. Proc. Natl. Acad. Sci. USA 103 (2006) 18119-18124
-
(2006)
Proc. Natl. Acad. Sci. USA
, vol.103
, pp. 18119-18124
-
-
Iwata, K.1
Fujiwara, T.2
Matsuki, Y.3
Akutsu, H.4
Takahashi, S.5
Naiki, H.6
Goto, Y.7
-
14
-
-
33745757474
-
The kinetics of nucleated polymerizations at high concentrations: amyloid fibril formation near and above the "supercritical concentration"
-
Powers E.T., and Powers D.L. The kinetics of nucleated polymerizations at high concentrations: amyloid fibril formation near and above the "supercritical concentration". Biophys. J. 91 (2006) 122-132
-
(2006)
Biophys. J.
, vol.91
, pp. 122-132
-
-
Powers, E.T.1
Powers, D.L.2
-
15
-
-
51349098137
-
Evidence for stepwise formation of amyloid fibrils by the mouse prion protein
-
Jain S., and Udgaonkar J.B. Evidence for stepwise formation of amyloid fibrils by the mouse prion protein. J. Mol. Biol. 382 (2008) 1228-1241
-
(2008)
J. Mol. Biol.
, vol.382
, pp. 1228-1241
-
-
Jain, S.1
Udgaonkar, J.B.2
-
16
-
-
34247862247
-
A three-stage kinetic model of amyloid fibrillation
-
Lee C.C., Nayak A., Sethuraman A., Belfort G., and McRae G.J. A three-stage kinetic model of amyloid fibrillation. Biophys. J. 92 (2007) 3448-3458
-
(2007)
Biophys. J.
, vol.92
, pp. 3448-3458
-
-
Lee, C.C.1
Nayak, A.2
Sethuraman, A.3
Belfort, G.4
McRae, G.J.5
-
17
-
-
0037047118
-
The protofilament structure of insulin amyloid fibrils
-
Jimenez J.L., Nettleton E.J., Bouchard M., Robinson C.V., Dobson C.M., and Saibil H.R. The protofilament structure of insulin amyloid fibrils. Proc. Natl. Acad. Sci. USA 99 (2002) 9196-9201
-
(2002)
Proc. Natl. Acad. Sci. USA
, vol.99
, pp. 9196-9201
-
-
Jimenez, J.L.1
Nettleton, E.J.2
Bouchard, M.3
Robinson, C.V.4
Dobson, C.M.5
Saibil, H.R.6
-
18
-
-
62649173217
-
Branching in amyloid fibril growth
-
Andersen C.B., Yagi H., Manno M., Martorana V., Ban T., Christiansen G., Otzen D.E., Goto Y., and Rischel C. Branching in amyloid fibril growth. Biophys. J. 96 (2009) 1529-1536
-
(2009)
Biophys. J.
, vol.96
, pp. 1529-1536
-
-
Andersen, C.B.1
Yagi, H.2
Manno, M.3
Martorana, V.4
Ban, T.5
Christiansen, G.6
Otzen, D.E.7
Goto, Y.8
Rischel, C.9
-
19
-
-
34250872212
-
Glucagon amyloid-like fibril morphology is selected via morphology-dependent growth inhibition
-
Andersen C.B., Otzen D., Christiansen G., and Rischel C. Glucagon amyloid-like fibril morphology is selected via morphology-dependent growth inhibition. Biochemistry 46 (2007) 7314-7324
-
(2007)
Biochemistry
, vol.46
, pp. 7314-7324
-
-
Andersen, C.B.1
Otzen, D.2
Christiansen, G.3
Rischel, C.4
-
20
-
-
44949250850
-
Paired beta-sheet structure of an Abeta(1-40) amyloid fibril revealed by electron microscopy
-
Sachse C., Fandrich M., and Grigorieff N. Paired beta-sheet structure of an Abeta(1-40) amyloid fibril revealed by electron microscopy. Proc. Natl. Acad. Sci. USA 105 (2008) 7462-7466
-
(2008)
Proc. Natl. Acad. Sci. USA
, vol.105
, pp. 7462-7466
-
-
Sachse, C.1
Fandrich, M.2
Grigorieff, N.3
-
21
-
-
58049204808
-
SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs
-
Shaikh T.R., Gao H., Baxter W.T., Asturias F.J., Boisset N., Leith A., and Frank J. SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs. Nat. Protoc. 3 (2008) 1941-1974
-
(2008)
Nat. Protoc.
, vol.3
, pp. 1941-1974
-
-
Shaikh, T.R.1
Gao, H.2
Baxter, W.T.3
Asturias, F.J.4
Boisset, N.5
Leith, A.6
Frank, J.7
-
22
-
-
59649110455
-
Abeta(1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils
-
Meinhardt J., Sachse C., Hortschansky P., Grigorieff N., and Fandrich M. Abeta(1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils. J. Mol. Biol. 386 (2009) 869-877
-
(2009)
J. Mol. Biol.
, vol.386
, pp. 869-877
-
-
Meinhardt, J.1
Sachse, C.2
Hortschansky, P.3
Grigorieff, N.4
Fandrich, M.5
-
23
-
-
0036415838
-
Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils
-
Lashuel H.A., Petre B.M., Wall J., Simon M., Nowak R.J., Walz T., and Lansbury Jr. P.T. Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils. J. Mol. Biol. 322 (2002) 1089-1102
-
(2002)
J. Mol. Biol.
, vol.322
, pp. 1089-1102
-
-
Lashuel, H.A.1
Petre, B.M.2
Wall, J.3
Simon, M.4
Nowak, R.J.5
Walz, T.6
Lansbury Jr., P.T.7
-
24
-
-
33744966120
-
High resolution scanning tunnelling microscopy of the beta-amyloid protein (Abeta1-40) of Alzheimer's disease suggests a novel mechanism of oligomer assembly
-
Losic D., Martin L.L., Mechler A., Aguilar M.I., and Small D.H. High resolution scanning tunnelling microscopy of the beta-amyloid protein (Abeta1-40) of Alzheimer's disease suggests a novel mechanism of oligomer assembly. J. Struct. Biol. 155 (2006) 104-110
-
(2006)
J. Struct. Biol.
, vol.155
, pp. 104-110
-
-
Losic, D.1
Martin, L.L.2
Mechler, A.3
Aguilar, M.I.4
Small, D.H.5
-
25
-
-
0037072284
-
Annular alpha-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes
-
Ding T.T., Lee S.J., Rochet J.C., and Lansbury Jr. P.T. Annular alpha-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes. Biochemistry 41 (2002) 10209-10217
-
(2002)
Biochemistry
, vol.41
, pp. 10209-10217
-
-
Ding, T.T.1
Lee, S.J.2
Rochet, J.C.3
Lansbury Jr., P.T.4
-
26
-
-
33845358566
-
Quantitative morphological analysis reveals ultrastructural diversity of amyloid fibrils from alpha-synuclein mutants
-
van Raaij M.E., Segers-Nolten I.M., and Subramaniam V. Quantitative morphological analysis reveals ultrastructural diversity of amyloid fibrils from alpha-synuclein mutants. Biophys. J. 91 (2006) L96-L98
-
(2006)
Biophys. J.
, vol.91
-
-
van Raaij, M.E.1
Segers-Nolten, I.M.2
Subramaniam, V.3
-
27
-
-
58149277410
-
Concentration dependence of alpha-synuclein fibril length assessed by quantitative atomic force microscopy and statistical-mechanical theory
-
van Raaij M.E., van G.J., Segers-Nolten I.M., de Leeuw S.W., and Subramaniam V. Concentration dependence of alpha-synuclein fibril length assessed by quantitative atomic force microscopy and statistical-mechanical theory. Biophys. J. 95 (2008) 4871-4878
-
(2008)
Biophys. J.
, vol.95
, pp. 4871-4878
-
-
van Raaij, M.E.1
van, G.J.2
Segers-Nolten, I.M.3
de Leeuw, S.W.4
Subramaniam, V.5
-
28
-
-
34249674524
-
Cytotoxicity of insulin within its self-assembly and amyloidogenic pathways
-
Grudzielanek S., Velkova A., Shukla A., Smirnovas V., Tatarek-Nossol M., Rehage H., Kapurniotu A., and Winter R. Cytotoxicity of insulin within its self-assembly and amyloidogenic pathways. J. Mol. Biol. 370 (2007) 372-384
-
(2007)
J. Mol. Biol.
, vol.370
, pp. 372-384
-
-
Grudzielanek, S.1
Velkova, A.2
Shukla, A.3
Smirnovas, V.4
Tatarek-Nossol, M.5
Rehage, H.6
Kapurniotu, A.7
Winter, R.8
-
29
-
-
58549104760
-
Inhibition of Alzheimer's amyloid toxicity with a tricyclic pyrone molecule in vitro and in vivo
-
Hong H.S., Rana S., Barrigan L., Shi A., Zhang Y., Zhou F., Jin L.W., and Hua D.H. Inhibition of Alzheimer's amyloid toxicity with a tricyclic pyrone molecule in vitro and in vivo. J. Neurochem. 108 (2009) 1097-1108
-
(2009)
J. Neurochem.
, vol.108
, pp. 1097-1108
-
-
Hong, H.S.1
Rana, S.2
Barrigan, L.3
Shi, A.4
Zhang, Y.5
Zhou, F.6
Jin, L.W.7
Hua, D.H.8
-
30
-
-
59349111854
-
Nano-scale imaging and dynamics of amylin-membrane interactions and its implication in type II diabetes mellitus
-
Cho W.J., Jena B.P., and Jeremic A.M. Nano-scale imaging and dynamics of amylin-membrane interactions and its implication in type II diabetes mellitus. Meth. Cell Biol. 90 (2008) 267-286
-
(2008)
Meth. Cell Biol.
, vol.90
, pp. 267-286
-
-
Cho, W.J.1
Jena, B.P.2
Jeremic, A.M.3
-
31
-
-
36049013172
-
Mechanism of islet amyloid polypeptide fibrillation at lipid interfaces studied by infrared reflection absorption spectroscopy
-
Lopes D.H., Meister A., Gohlke A., Hauser A., Blume A., and Winter R. Mechanism of islet amyloid polypeptide fibrillation at lipid interfaces studied by infrared reflection absorption spectroscopy. Biophys. J. 93 (2007) 3132-3141
-
(2007)
Biophys. J.
, vol.93
, pp. 3132-3141
-
-
Lopes, D.H.1
Meister, A.2
Gohlke, A.3
Hauser, A.4
Blume, A.5
Winter, R.6
-
32
-
-
62649147822
-
Surface charge of polyoxometalates modulates polymerization of the scrapie prion protein
-
Wille H., Shanmugam M., Murugesu M., Ollesch J., Stubbs G., Long J.R., Safar J.G., and Prusiner S.B. Surface charge of polyoxometalates modulates polymerization of the scrapie prion protein. Proc. Natl. Acad. Sci. USA 106 (2009) 3740-3745
-
(2009)
Proc. Natl. Acad. Sci. USA
, vol.106
, pp. 3740-3745
-
-
Wille, H.1
Shanmugam, M.2
Murugesu, M.3
Ollesch, J.4
Stubbs, G.5
Long, J.R.6
Safar, J.G.7
Prusiner, S.B.8
-
33
-
-
34547454920
-
Nucleation of protein fibrillation by nanoparticles
-
Linse S., Cabaleiro-Lago C., Xue W.F., Lynch I., Lindman S., Thulin E., Radford S.E., and Dawson K.A. Nucleation of protein fibrillation by nanoparticles. Proc. Natl. Acad. Sci. USA 104 (2007) 8691-8696
-
(2007)
Proc. Natl. Acad. Sci. USA
, vol.104
, pp. 8691-8696
-
-
Linse, S.1
Cabaleiro-Lago, C.2
Xue, W.F.3
Lynch, I.4
Lindman, S.5
Thulin, E.6
Radford, S.E.7
Dawson, K.A.8
-
34
-
-
0037592927
-
Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence
-
Ban T., Hamada D., Hasegawa K., Naiki H., and Goto Y. Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence. J. Biol. Chem. 278 (2003) 16462-16465
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 16462-16465
-
-
Ban, T.1
Hamada, D.2
Hasegawa, K.3
Naiki, H.4
Goto, Y.5
-
35
-
-
33645214738
-
ATSAS 2.1, a program package for small-angle scattering data analysis
-
Konarev P.V., Petoukhov M.V., Volkov V.V., and Svergun D.I. ATSAS 2.1, a program package for small-angle scattering data analysis. J. Appl. Cryst. 39 (2006) 277-286
-
(2006)
J. Appl. Cryst.
, vol.39
, pp. 277-286
-
-
Konarev, P.V.1
Petoukhov, M.V.2
Volkov, V.V.3
Svergun, D.I.4
-
36
-
-
0033001996
-
Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
-
Svergun D.I. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76 (1999) 2879-2886
-
(1999)
Biophys. J.
, vol.76
, pp. 2879-2886
-
-
Svergun, D.I.1
-
37
-
-
0026910457
-
Determination of the regularization parameter in indirect-transform methods using perceptual criteria
-
Svergun D.I. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Cryst. 25 (1992) 495-503
-
(1992)
J. Appl. Cryst.
, vol.25
, pp. 495-503
-
-
Svergun, D.I.1
-
38
-
-
0029185933
-
CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
-
Svergun D.I., Barberato B., and Koch M.H.J. CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Cryst. 28 (1995) 768-773
-
(1995)
J. Appl. Cryst.
, vol.28
, pp. 768-773
-
-
Svergun, D.I.1
Barberato, B.2
Koch, M.H.J.3
-
39
-
-
0034503624
-
A software system for rigid-body modelling of solution scattering data
-
Kozin M.B., and Svergun D.I. A software system for rigid-body modelling of solution scattering data. J. Appl. Cryst. 33 (2000) 775-777
-
(2000)
J. Appl. Cryst.
, vol.33
, pp. 775-777
-
-
Kozin, M.B.1
Svergun, D.I.2
-
40
-
-
30044446633
-
Early events in the fibrillation of monomeric insulin
-
Ahmad A., Uversky V.N., Hong D., and Fink A.L. Early events in the fibrillation of monomeric insulin. J. Biol. Chem. 280 (2005) 42669-42675
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 42669-42675
-
-
Ahmad, A.1
Uversky, V.N.2
Hong, D.3
Fink, A.L.4
-
41
-
-
59849109485
-
A universal pathway for amyloid nucleus and precursor formation for insulin
-
Nayak A., Sorci M., Krueger S., and Belfort G. A universal pathway for amyloid nucleus and precursor formation for insulin. Proteins 74 (2009) 556-565
-
(2009)
Proteins
, vol.74
, pp. 556-565
-
-
Nayak, A.1
Sorci, M.2
Krueger, S.3
Belfort, G.4
-
42
-
-
61349090415
-
A SAXS study of glucagon fibrillation
-
Oliveira C.L.P., Behrens M.A., Pedersen J.S., Erlacher K., Otzen D.E., and Pedersen J.S. A SAXS study of glucagon fibrillation. J. Mol. Biol. 387 (2009) 146-161
-
(2009)
J. Mol. Biol.
, vol.387
, pp. 146-161
-
-
Oliveira, C.L.P.1
Behrens, M.A.2
Pedersen, J.S.3
Erlacher, K.4
Otzen, D.E.5
Pedersen, J.S.6
-
43
-
-
58049215425
-
Silk fiber assembly studied by synchrotron radiation SAXS/WAXS and Raman spectroscopy
-
Martel A., Burghammer M., Davies R.J., Di C.E., Vendrely C., and Riekel C. Silk fiber assembly studied by synchrotron radiation SAXS/WAXS and Raman spectroscopy. J. Am. Chem. Soc. 130 (2008) 17070-17074
-
(2008)
J. Am. Chem. Soc.
, vol.130
, pp. 17070-17074
-
-
Martel, A.1
Burghammer, M.2
Davies, R.J.3
Di, C.E.4
Vendrely, C.5
Riekel, C.6
-
44
-
-
41149141255
-
Characterization of fibrillation process of alpha-synuclein at the initial stage
-
Tashiro M., Kojima M., Kihara H., Kasai K., Kamiyoshihara T., Ueda K., and Shimotakahara S. Characterization of fibrillation process of alpha-synuclein at the initial stage. Biochem. Biophys. Res. Commun. 369 (2008) 910-914
-
(2008)
Biochem. Biophys. Res. Commun.
, vol.369
, pp. 910-914
-
-
Tashiro, M.1
Kojima, M.2
Kihara, H.3
Kasai, K.4
Kamiyoshihara, T.5
Ueda, K.6
Shimotakahara, S.7
-
45
-
-
0038161262
-
Effects of salt concentration on association of the amyloid protofilaments of hen egg white lysozyme studied by time-resolved neutron scattering
-
Fujiwara S., Matsumoto F., and Yonezawa Y. Effects of salt concentration on association of the amyloid protofilaments of hen egg white lysozyme studied by time-resolved neutron scattering. J. Mol. Biol. 331 (2003) 21-28
-
(2003)
J. Mol. Biol.
, vol.331
, pp. 21-28
-
-
Fujiwara, S.1
Matsumoto, F.2
Yonezawa, Y.3
-
46
-
-
0036404245
-
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., and 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
-
47
-
-
52949123661
-
Domain conformation of tau protein studied by solution small-angle X-ray scattering
-
Mylonas E., Hascher A., Bernado P., Blackledge M., Mandelkow E., and Svergun D.I. Domain conformation of tau protein studied by solution small-angle X-ray scattering. Biochemistry 47 (2008) 10345-10353
-
(2008)
Biochemistry
, vol.47
, pp. 10345-10353
-
-
Mylonas, E.1
Hascher, A.2
Bernado, P.3
Blackledge, M.4
Mandelkow, E.5
Svergun, D.I.6
-
48
-
-
34247891557
-
Structural characterization of flexible proteins using small-angle X-ray scattering
-
Bernado P., Mylonas E., Petoukhov M.V., Blackledge M., and Svergun D.I. Structural characterization of flexible proteins using small-angle X-ray scattering. J. Am. Chem. Soc. 129 (2007) 5656-5664
-
(2007)
J. Am. Chem. Soc.
, vol.129
, pp. 5656-5664
-
-
Bernado, P.1
Mylonas, E.2
Petoukhov, M.V.3
Blackledge, M.4
Svergun, D.I.5
-
49
-
-
20444440728
-
Structure of the cross-beta spine of amyloid-like fibrils
-
Nelson R., Sawaya M.R., Balbirnie M., Madsen A.O., Riekel C., Grothe R., and Eisenberg D. Structure of the cross-beta spine of amyloid-like fibrils. Nature 435 (2005) 773-778
-
(2005)
Nature
, vol.435
, pp. 773-778
-
-
Nelson, R.1
Sawaya, M.R.2
Balbirnie, M.3
Madsen, A.O.4
Riekel, C.5
Grothe, R.6
Eisenberg, D.7
-
50
-
-
34249290108
-
Atomic structures of amyloid cross-beta spines reveal varied steric zippers
-
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.O., Riekel C., and Eisenberg D. Atomic structures of amyloid cross-beta spines reveal varied steric zippers. Nature 447 (2007) 453-457
-
(2007)
Nature
, vol.447
, 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.9
McFarlane, H.T.10
Madsen, A.O.11
Riekel, C.12
Eisenberg, D.13
-
51
-
-
50049095633
-
Atomic structure of the cross-beta spine of islet amyloid polypeptide (amylin)
-
Wiltzius J.J., Sievers S.A., Sawaya M.R., Cascio D., Popov D., Riekel C., and Eisenberg D. Atomic structure of the cross-beta spine of islet amyloid polypeptide (amylin). Protein Sci. 17 (2008) 1467-1474
-
(2008)
Protein Sci.
, vol.17
, pp. 1467-1474
-
-
Wiltzius, J.J.1
Sievers, S.A.2
Sawaya, M.R.3
Cascio, D.4
Popov, D.5
Riekel, C.6
Eisenberg, D.7
-
52
-
-
57849090528
-
A combined microRaman and microdiffraction set-up at the European Synchrotron Radiation Facility ID13 beamline
-
Davies R.J., Burghammer M., and Riekel C. A combined microRaman and microdiffraction set-up at the European Synchrotron Radiation Facility ID13 beamline. J. Synchrotron. Radiat. 16 (2009) 22-29
-
(2009)
J. Synchrotron. Radiat.
, vol.16
, pp. 22-29
-
-
Davies, R.J.1
Burghammer, M.2
Riekel, C.3
-
53
-
-
0031879388
-
Small is beautiful: protein micro-crystallography
-
Cusack S., Belrhali H., Bram A., Burghammer M., Perrakis A., and Riekel C. Small is beautiful: protein micro-crystallography. Nat. Struct. Biol. 5 Suppl. (1998) 634-637
-
(1998)
Nat. Struct. Biol.
, vol.5
, Issue.SUPPL
, pp. 634-637
-
-
Cusack, S.1
Belrhali, H.2
Bram, A.3
Burghammer, M.4
Perrakis, A.5
Riekel, C.6
-
54
-
-
34247504580
-
Solid-state NMR study of amyloid nanocrystals and fibrils formed by the peptide GNNQQNY from yeast prion protein Sup35p
-
van der Wel P.C., Lewandowski J.R., and Griffin R.G. Solid-state NMR study of amyloid nanocrystals and fibrils formed by the peptide GNNQQNY from yeast prion protein Sup35p. J. Am. Chem. Soc. 129 (2007) 5117-5130
-
(2007)
J. Am. Chem. Soc.
, vol.129
, pp. 5117-5130
-
-
van der Wel, P.C.1
Lewandowski, J.R.2
Griffin, R.G.3
-
55
-
-
57649128935
-
Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: molecular insights from electron paramagnetic resonance spectroscopy
-
Margittai M., and Langen R. Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: molecular insights from electron paramagnetic resonance spectroscopy. Q. Rev. Biophys. 41 (2008) 265-297
-
(2008)
Q. Rev. Biophys.
, vol.41
, pp. 265-297
-
-
Margittai, M.1
Langen, R.2
-
56
-
-
38849108169
-
Solid-state NMR spectroscopy of amyloid proteins
-
Heise H. Solid-state NMR spectroscopy of amyloid proteins. Chembiochem 9 (2008) 179-189
-
(2008)
Chembiochem
, vol.9
, pp. 179-189
-
-
Heise, H.1
-
57
-
-
54349103544
-
A sequential assignment procedure for proteins that have intermediate line widths in MAS NMR spectra: amyloid fibrils of human CA150.WW2
-
Becker J., Ferguson N., Flinders J., van Rossum B.J., Fersht A.R., and Oschkinat H. A sequential assignment procedure for proteins that have intermediate line widths in MAS NMR spectra: amyloid fibrils of human CA150.WW2. Chembiochem 9 (2008) 1946-1952
-
(2008)
Chembiochem
, vol.9
, pp. 1946-1952
-
-
Becker, J.1
Ferguson, N.2
Flinders, J.3
van Rossum, B.J.4
Fersht, A.R.5
Oschkinat, H.6
-
58
-
-
36749033116
-
Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR
-
Luca S., Yau W.M., Leapman R., and Tycko R. Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR. Biochemistry 46 (2007) 13505-13522
-
(2007)
Biochemistry
, vol.46
, pp. 13505-13522
-
-
Luca, S.1
Yau, W.M.2
Leapman, R.3
Tycko, R.4
-
59
-
-
51749125627
-
Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant alpha-synuclein
-
Heise H., Celej M.S., Becker S., Riedel D., Pelah A., Kumar A., Jovin T.M., and Baldus M. Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant alpha-synuclein. J. Mol. Biol. 380 (2008) 444-450
-
(2008)
J. Mol. Biol.
, vol.380
, pp. 444-450
-
-
Heise, H.1
Celej, M.S.2
Becker, S.3
Riedel, D.4
Pelah, A.5
Kumar, A.6
Jovin, T.M.7
Baldus, M.8
-
60
-
-
12244249201
-
Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils
-
Petkova A.T., Leapman R.D., Guo Z., Yau W.M., Mattson M.P., and Tycko R. Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science 307 (2005) 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
-
61
-
-
33144467755
-
Amyloid formation under physiological conditions proceeds via a native-like folding intermediate
-
Jahn T.R., Parker M.J., Homans S.W., and Radford S.E. Amyloid formation under physiological conditions proceeds via a native-like folding intermediate. Nat. Struct. Mol. Biol. 13 (2006) 195-201
-
(2006)
Nat. Struct. Mol. Biol.
, vol.13
, pp. 195-201
-
-
Jahn, T.R.1
Parker, M.J.2
Homans, S.W.3
Radford, S.E.4
-
62
-
-
28444442999
-
3D structure of Alzheimer's amyloid-beta(1-42) fibrils
-
Luhrs T., Ritter C., Adrian M., Riek-Loher D., Bohrmann B., Dobeli H., Schubert D., and Riek R. 3D structure of Alzheimer's amyloid-beta(1-42) fibrils. Proc. Natl. Acad. Sci. USA 102 (2005) 17342-17347
-
(2005)
Proc. Natl. Acad. Sci. USA
, vol.102
, pp. 17342-17347
-
-
Luhrs, T.1
Ritter, C.2
Adrian, M.3
Riek-Loher, D.4
Bohrmann, B.5
Dobeli, H.6
Schubert, D.7
Riek, R.8
-
63
-
-
33644851439
-
The solvent protection of alzheimer amyloid-beta-(1-42) fibrils as determined by solution NMR spectroscopy
-
Olofsson A., Sauer-Eriksson A.E., and Ohman A. The solvent protection of alzheimer amyloid-beta-(1-42) fibrils as determined by solution NMR spectroscopy. J. Biol. Chem. 281 (2006) 477-483
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 477-483
-
-
Olofsson, A.1
Sauer-Eriksson, A.E.2
Ohman, A.3
-
64
-
-
38649143194
-
Atomic models of de novo designed cc beta-Met amyloid-like fibrils
-
Steinmetz M.O., Gattin Z., Verel R., Ciani B., Stromer T., Green J.M., Tittmann P., Schulze-Briese C., Gross H., van Gunsteren W.F., Meier B.H., Serpell L.C., Muller S.A., and Kammerer R.A. Atomic models of de novo designed cc beta-Met amyloid-like fibrils. J. Mol. Biol. 376 (2008) 898-912
-
(2008)
J. Mol. Biol.
, vol.376
, pp. 898-912
-
-
Steinmetz, M.O.1
Gattin, Z.2
Verel, R.3
Ciani, B.4
Stromer, T.5
Green, J.M.6
Tittmann, P.7
Schulze-Briese, C.8
Gross, H.9
van Gunsteren, W.F.10
Meier, B.H.11
Serpell, L.C.12
Muller, S.A.13
Kammerer, R.A.14
-
65
-
-
33750826280
-
General structural motifs of amyloid protofilaments
-
Ferguson N., Becker J., Tidow H., Tremmel S., Sharpe T.D., Krause G., Flinders J., Petrovich M., Berriman J., Oschkinat H., and Fersht A.R. General structural motifs of amyloid protofilaments. Proc. Natl. Acad. Sci. USA 103 (2006) 16248-16253
-
(2006)
Proc. Natl. Acad. Sci. USA
, vol.103
, pp. 16248-16253
-
-
Ferguson, N.1
Becker, J.2
Tidow, H.3
Tremmel, S.4
Sharpe, T.D.5
Krause, G.6
Flinders, J.7
Petrovich, M.8
Berriman, J.9
Oschkinat, H.10
Fersht, A.R.11
-
66
-
-
62449148425
-
The peculiar interaction between mammalian prion protein and RNA
-
Gomes M.P., Cordeiro Y., and Silva J.L. The peculiar interaction between mammalian prion protein and RNA. Prion 2 (2008) 64-66
-
(2008)
Prion
, vol.2
, pp. 64-66
-
-
Gomes, M.P.1
Cordeiro, Y.2
Silva, J.L.3
-
67
-
-
0035127031
-
A domain-swapped RNase A dimer with implications for amyloid formation
-
Liu Y., Gotte G., Libonati M., and Eisenberg D. A domain-swapped RNase A dimer with implications for amyloid formation. Nat. Struct. Biol. 8 (2001) 211-214
-
(2001)
Nat. Struct. Biol.
, vol.8
, pp. 211-214
-
-
Liu, Y.1
Gotte, G.2
Libonati, M.3
Eisenberg, D.4
-
68
-
-
61349120815
-
Structural polymorphism of 441-residue tau at single residue resolution
-
Mukrasch M.D., Bibow S., Korukottu J., Jeganathan S., Biernat J., Griesinger C., Mandelkow E., and Zweckstetter M. Structural polymorphism of 441-residue tau at single residue resolution. PLoS Biol. 7 (2009) e34
-
(2009)
PLoS Biol.
, vol.7
-
-
Mukrasch, M.D.1
Bibow, S.2
Korukottu, J.3
Jeganathan, S.4
Biernat, J.5
Griesinger, C.6
Mandelkow, E.7
Zweckstetter, M.8
-
69
-
-
33751002965
-
NMR solution structure of the acylphosphatase from Escherichia coli
-
Pagano K., Ramazzotti M., Viglino P., Esposito G., Degl'Innocenti D., Taddei N., and Corazza A. NMR solution structure of the acylphosphatase from Escherichia coli. J. Biomol. NMR 36 (2006) 199-204
-
(2006)
J. Biomol. NMR
, vol.36
, pp. 199-204
-
-
Pagano, K.1
Ramazzotti, M.2
Viglino, P.3
Esposito, G.4
Degl'Innocenti, D.5
Taddei, N.6
Corazza, A.7
-
70
-
-
33750686583
-
Amyloid fibrils formation and amorphous aggregation in concanavalin A
-
Vetri V., Canale C., Relini A., Librizzi F., Militello V., Gliozzi A., and Leone M. Amyloid fibrils formation and amorphous aggregation in concanavalin A. Biophys. Chem. 125 (2007) 184-190
-
(2007)
Biophys. Chem.
, vol.125
, pp. 184-190
-
-
Vetri, V.1
Canale, C.2
Relini, A.3
Librizzi, F.4
Militello, V.5
Gliozzi, A.6
Leone, M.7
-
71
-
-
27744577906
-
FT-IR approaches on amyloid fibril structure
-
Hiramatsu H., and Kitagawa T. FT-IR approaches on amyloid fibril structure. Biochim. Biophys. Acta 1753 (2005) 100-107
-
(2005)
Biochim. Biophys. Acta
, vol.1753
, pp. 100-107
-
-
Hiramatsu, H.1
Kitagawa, T.2
-
72
-
-
34249650790
-
Analysis of insulin amyloid fibrils by Raman spectroscopy
-
Ortiz C., Zhang D., Ribbe A.E., Xie Y., and Ben-Amotz D. Analysis of insulin amyloid fibrils by Raman spectroscopy. Biophys. Chem. 128 (2007) 150-155
-
(2007)
Biophys. Chem.
, vol.128
, pp. 150-155
-
-
Ortiz, C.1
Zhang, D.2
Ribbe, A.E.3
Xie, Y.4
Ben-Amotz, D.5
-
73
-
-
33646727439
-
Raman crystallography and other biochemical applications of Raman microscopy
-
Carey P.R. Raman crystallography and other biochemical applications of Raman microscopy. Annu. Rev. Phys. Chem. 57 (2006) 527-554
-
(2006)
Annu. Rev. Phys. Chem.
, vol.57
, pp. 527-554
-
-
Carey, P.R.1
-
74
-
-
61549102154
-
Interaction of IAPP and insulin with model interfaces studied using neutron reflectometry
-
Jeworrek C., Hollmann O., Steitz R., Winter R., and Czeslik C. Interaction of IAPP and insulin with model interfaces studied using neutron reflectometry. Biophys. J. 96 (2009) 1115-1123
-
(2009)
Biophys. J.
, vol.96
, pp. 1115-1123
-
-
Jeworrek, C.1
Hollmann, O.2
Steitz, R.3
Winter, R.4
Czeslik, C.5
-
75
-
-
43149121814
-
Revealing different aggregation pathways of amyloidogenic proteins by ultrasound velocimetry
-
Smirnovas V., and Winter R. Revealing different aggregation pathways of amyloidogenic proteins by ultrasound velocimetry. Biophys. J. 94 (2008) 3241-3246
-
(2008)
Biophys. J.
, vol.94
, pp. 3241-3246
-
-
Smirnovas, V.1
Winter, R.2
-
77
-
-
33744973540
-
Interaction-based evaluation of the propensity for amyloid formation with cross-beta structure
-
Saiki M., Konakahara T., and Morii H. Interaction-based evaluation of the propensity for amyloid formation with cross-beta structure. Biochem. Biophys. Res. Commun. 343 (2006) 1262-1271
-
(2006)
Biochem. Biophys. Res. Commun.
, vol.343
, pp. 1262-1271
-
-
Saiki, M.1
Konakahara, T.2
Morii, H.3
-
78
-
-
33845978790
-
Insight into the structure of amyloid fibrils from the analysis of globular proteins
-
Trovato A., Chiti F., Maritan A., and Seno F. Insight into the structure of amyloid fibrils from the analysis of globular proteins. PLoS Comput. Biol. 2 (2006) e170
-
(2006)
PLoS Comput. Biol.
, vol.2
-
-
Trovato, A.1
Chiti, F.2
Maritan, A.3
Seno, F.4
-
79
-
-
63549101789
-
BETASCAN: probable beta-amyloids identified by pairwise probabilistic analysis
-
Bryan Jr. A.W., Menke M., Cowen L.J., Lindquist S.L., and Berger B. BETASCAN: probable beta-amyloids identified by pairwise probabilistic analysis. PLoS Comput. Biol. 5 (2009) e1000333
-
(2009)
PLoS Comput. Biol.
, vol.5
-
-
Bryan Jr., A.W.1
Menke, M.2
Cowen, L.J.3
Lindquist, S.L.4
Berger, B.5
-
80
-
-
58149360794
-
All-atom computer simulations of amyloid fibrils disaggregation
-
Wang J., Tan C., Chen H.F., and Luo R. All-atom computer simulations of amyloid fibrils disaggregation. Biophys. J. 95 (2008) 5037-5047
-
(2008)
Biophys. J.
, vol.95
, pp. 5037-5047
-
-
Wang, J.1
Tan, C.2
Chen, H.F.3
Luo, R.4
-
81
-
-
9244260521
-
Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides
-
Nguyen H.D., and Hall C.K. Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides. Proc. Natl. Acad. Sci. USA 101 (2004) 16180-16185
-
(2004)
Proc. Natl. Acad. Sci. USA
, vol.101
, pp. 16180-16185
-
-
Nguyen, H.D.1
Hall, C.K.2
-
82
-
-
50549084663
-
Characterizing the first steps of amyloid formation for the ccbeta peptide
-
Strodel B., Fitzpatrick A.W., Vendruscolo M., Dobson C.M., and Wales D.J. Characterizing the first steps of amyloid formation for the ccbeta peptide. J. Phys. Chem. B 112 (2008) 9998-10004
-
(2008)
J. Phys. Chem. B
, vol.112
, pp. 9998-10004
-
-
Strodel, B.1
Fitzpatrick, A.W.2
Vendruscolo, M.3
Dobson, C.M.4
Wales, D.J.5
-
83
-
-
53249113119
-
Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering
-
Cammarata M., Levantino M., Schotte F., Anfinrud P.A., Ewald F., Choi J., Cupane A., Wulff M., and Ihee H. Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering. Nat. Meth. 5 (2008) 881-886
-
(2008)
Nat. Meth.
, vol.5
, pp. 881-886
-
-
Cammarata, M.1
Levantino, M.2
Schotte, F.3
Anfinrud, P.A.4
Ewald, F.5
Choi, J.6
Cupane, A.7
Wulff, M.8
Ihee, H.9
-
84
-
-
61949315876
-
Protein structure determination in living cells by in-cell NMR spectroscopy
-
Sakakibara D., Sasaki A., Ikeya T., Hamatsu J., Hanashima T., Mishima M., Yoshimasu M., Hayashi N., Mikawa T., Walchli M., Smith B.O., Shirakawa M., Guntert P., and Ito Y. Protein structure determination in living cells by in-cell NMR spectroscopy. Nature 458 (2009) 102-105
-
(2009)
Nature
, vol.458
, pp. 102-105
-
-
Sakakibara, D.1
Sasaki, A.2
Ikeya, T.3
Hamatsu, J.4
Hanashima, T.5
Mishima, M.6
Yoshimasu, M.7
Hayashi, N.8
Mikawa, T.9
Walchli, M.10
Smith, B.O.11
Shirakawa, M.12
Guntert, P.13
Ito, Y.14
-
85
-
-
34447326955
-
Amyloid imaging in Alzheimer's disease
-
Nordberg A. Amyloid imaging in Alzheimer's disease. Curr. Opin. Neurol. 20 (2007) 398-402
-
(2007)
Curr. Opin. Neurol.
, vol.20
, pp. 398-402
-
-
Nordberg, A.1
|