-
1
-
-
0037135111
-
The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
-
Hardy J., and Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics Science 297 2002 353 356
-
(2002)
Science
, vol.297
, pp. 353-356
-
-
Hardy, J.1
Selkoe, D.J.2
-
2
-
-
0037264120
-
Unfolding the role of protein misfolding in neurodegenerative diseases
-
Soto C. Unfolding the role of protein misfolding in neurodegenerative diseases Nat. Rev. Neurosci. 4 2003 49 60
-
(2003)
Nat. Rev. Neurosci.
, vol.4
, pp. 49-60
-
-
Soto, C.1
-
3
-
-
33746377894
-
Protein misfolding, functional amyloid, and human disease
-
Chiti F., and Dobson C.M. Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366
-
(2006)
Annu. Rev. Biochem.
, vol.75
, pp. 333-366
-
-
Chiti, F.1
Dobson, C.M.2
-
4
-
-
70349923038
-
Alzheimer's disease: From pathology to therapeutic approaches
-
Jakob-Roetne R., and Jacobsen H. Alzheimer's disease: from pathology to therapeutic approaches Angew. Chem. Int. Ed. 48 2009 3030 3059
-
(2009)
Angew. Chem. Int. Ed.
, vol.48
, pp. 3030-3059
-
-
Jakob-Roetne, R.1
Jacobsen, H.2
-
6
-
-
75349097530
-
A causative link between the structure of aberrant protein oligomers and their toxicity
-
Campioni S., Mannini B., Zampagni M., Pensalfini A., Parrini C., and Evangelisti E. A causative link between the structure of aberrant protein oligomers and their toxicity Nat. Chem. Biol. 6 2010 140 147
-
(2010)
Nat. Chem. Biol.
, vol.6
, pp. 140-147
-
-
Campioni, S.1
Mannini, B.2
Zampagni, M.3
Pensalfini, A.4
Parrini, C.5
Evangelisti, E.6
-
7
-
-
78751644048
-
Amyloid-β and tau - A toxic pas de deux in Alzheimer's disease
-
Ittner L.M., and Gotz J. Amyloid-β and tau - a toxic pas de deux in Alzheimer's disease Nat. Rev. Neurosci. 12 2011 67 72
-
(2011)
Nat. Rev. Neurosci.
, vol.12
, pp. 67-72
-
-
Ittner, L.M.1
Gotz, J.2
-
8
-
-
0026646604
-
Amyloid β-peptide is produced by cultured cells during normal metabolism
-
Haass C., Schlossmacher M.G., Hung A.Y., Vigo-Pelfrey C., Mellon A., and Ostaszewski B.L. Amyloid β-peptide is produced by cultured cells during normal metabolism Nature 359 1992 322 325
-
(1992)
Nature
, vol.359
, pp. 322-325
-
-
Haass, C.1
Schlossmacher, M.G.2
Hung, A.Y.3
Vigo-Pelfrey, C.4
Mellon, A.5
Ostaszewski, B.L.6
-
9
-
-
0026646605
-
Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids
-
Seubert P., Vigo-Pelfrey C., Esch F., Lee M., Dovey H., and Davis D. Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids Nature 359 1992 325 327
-
(1992)
Nature
, vol.359
, pp. 325-327
-
-
Seubert, P.1
Vigo-Pelfrey, C.2
Esch, F.3
Lee, M.4
Dovey, H.5
Davis, D.6
-
10
-
-
0026760261
-
Production of the Alzheimer amyloid β protein by normal proteolytic processing
-
Shoji M., Golde T.E., Ghiso J., Cheung T.T., Estus S., and Shaffer L.M. Production of the Alzheimer amyloid β protein by normal proteolytic processing Science 258 1992 126 129
-
(1992)
Science
, vol.258
, pp. 126-129
-
-
Shoji, M.1
Golde, T.E.2
Ghiso, J.3
Cheung, T.T.4
Estus, S.5
Shaffer, L.M.6
-
11
-
-
0037041426
-
Naturally secreted oligomers of amyloid-β protein potently inhibit hippocampal long-term potentiation in vivo
-
Walsh D.M., Klyubin I., Fadeeva J.V., Cullen W.K., Anwyl R., and Wolfe M.S. Naturally secreted oligomers of amyloid-β protein potently inhibit hippocampal long-term potentiation in vivo Nature 416 2002 535 539
-
(2002)
Nature
, vol.416
, pp. 535-539
-
-
Walsh, D.M.1
Klyubin, I.2
Fadeeva, J.V.3
Cullen, W.K.4
Anwyl, R.5
Wolfe, M.S.6
-
12
-
-
34248190279
-
Aβ oligomers - A decade of discovery
-
Walsh D.M., and Selkoe D.J. Aβ oligomers - a decade of discovery J. Neurochem. 101 2007 1172 1184
-
(2007)
J. Neurochem.
, vol.101
, pp. 1172-1184
-
-
Walsh, D.M.1
Selkoe, D.J.2
-
13
-
-
0037041420
-
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
-
Bucciantini M., Giannoni E., Chiti F., Baroni F., Formigli L., and Zurdo J. 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
-
14
-
-
0242668337
-
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., and Glabe C.G. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis Science 300 2003 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
-
15
-
-
77951975748
-
Structural conversion of neurotoxic amyloid-β(1-42) oligomers to fibrils
-
Ahmed M., Davis J., Aucoin D., Sato T., Ahuja S., and Aimoto S. Structural conversion of neurotoxic amyloid-β(1-42) oligomers to fibrils Nat. Struct. Mol. Biol. 17 2010 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
-
16
-
-
0033793872
-
Mechanisms of amyloidogenicity
-
Kelly J. Mechanisms of amyloidogenicity Nat. Struct. Biol. 7 2000 824 826
-
(2000)
Nat. Struct. Biol.
, vol.7
, pp. 824-826
-
-
Kelly, J.1
-
17
-
-
36048941372
-
Peptide fibrillization
-
Hamley I.W. Peptide fibrillization Angew. Chem. Int. Ed. 46 2007 8128 8147
-
(2007)
Angew. Chem. Int. Ed.
, vol.46
, pp. 8128-8147
-
-
Hamley, I.W.1
-
18
-
-
78751675430
-
Probing aromatic, hydrophobic and steric effects on the self-assembly of an amyloid-β fragment peptide
-
Senguen F.T., Lee N.R., Gu X., Ryan D.M., Doran T.M., Anderson E.A., and Nilsson B.L. Probing aromatic, hydrophobic and steric effects on the self-assembly of an amyloid-β fragment peptide Mol. BioSyst. 7 2011 486 496
-
(2011)
Mol. BioSyst.
, vol.7
, pp. 486-496
-
-
Senguen, F.T.1
Lee, N.R.2
Gu, X.3
Ryan, D.M.4
Doran, T.M.5
Anderson, E.A.6
Nilsson, B.L.7
-
19
-
-
78751674190
-
Clarifying the influence of core amino acid hydrophobicity, secondary structure propensity, and molecular volume on amyloid-β 16-22 self-assembly
-
Senguen F.T., Doran T.M., Anderson E.A., and Nilsson B.L. Clarifying the influence of core amino acid hydrophobicity, secondary structure propensity, and molecular volume on amyloid-β 16-22 self-assembly Mol. BioSyst. 7 2011 497 510
-
(2011)
Mol. BioSyst.
, vol.7
, pp. 497-510
-
-
Senguen, F.T.1
Doran, T.M.2
Anderson, E.A.3
Nilsson, B.L.4
-
20
-
-
0033855845
-
The Alzheimer's peptide Aβ adopts a collapsed coil structure in water
-
Zhang S., Iwata K., Lachenmann M.J., Peng J.W., Li S., and Stimson E.R. The Alzheimer's peptide Aβ adopts a collapsed coil structure in water J. Struct. Biol. 130 2000 130 141
-
(2000)
J. Struct. Biol.
, vol.130
, pp. 130-141
-
-
Zhang, S.1
Iwata, K.2
Lachenmann, M.J.3
Peng, J.W.4
Li, S.5
Stimson, E.R.6
-
21
-
-
0035997080
-
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., and Tycko R. Supramolecular structure in full-length Alzheimer's β-amyloid fibrils: evidence for a parallel β-sheet organization from solid-state nuclear magnetic resonance Biophys. J. 83 2002 1205 1216
-
(2002)
Biophys. J.
, 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
-
22
-
-
12244249201
-
Self-propagating, molecular-level polymorphism in Alzheimer's β-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 β-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
-
23
-
-
30744433878
-
Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils
-
Petkova A.T., Yau W.M., and Tycko R. Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils Biochemistry 45 2006 498 512
-
(2006)
Biochemistry
, vol.45
, pp. 498-512
-
-
Petkova, A.T.1
Yau, W.M.2
Tycko, R.3
-
24
-
-
57449091884
-
Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils
-
Paravastu A.K., Leapman R.D., Yau W.M., and Tycko R. Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils Proc. Natl Acad. Sci. USA 105 2008 18349 18354
-
(2008)
Proc. Natl Acad. Sci. USA
, vol.105
, pp. 18349-18354
-
-
Paravastu, A.K.1
Leapman, R.D.2
Yau, W.M.3
Tycko, R.4
-
25
-
-
67650022104
-
Evidence for novel β-sheet structures in Iowa mutant β-amyloid fibrils
-
Tycko R., Sciaretta K.L., Orgel J.P.R.O., and Meredith S.C. Evidence for novel β-sheet structures in Iowa mutant β-amyloid fibrils Biochemistry 48 2009 6072 6084
-
(2009)
Biochemistry
, vol.48
, pp. 6072-6084
-
-
Tycko, R.1
Sciaretta, K.L.2
Orgel, J.P.R.O.3
Meredith, S.C.4
-
26
-
-
79953765150
-
Solid-state NMR studies of amyloid fibril structure
-
Tycko R. Solid-state NMR studies of amyloid fibril structure Annu. Rev. Phys. Chem. 62 2011 279 299
-
(2011)
Annu. Rev. Phys. Chem.
, vol.62
, pp. 279-299
-
-
Tycko, R.1
-
27
-
-
22444449900
-
On the nucleation of amyloid β-protein monomer folding
-
Lazo N.D., Grant M.A., Condron M.C., Rigby A.C., and Teplow D.B. On the nucleation of amyloid β-protein monomer folding Protein Sci. 14 2005 1581 1596
-
(2005)
Protein Sci.
, vol.14
, pp. 1581-1596
-
-
Lazo, N.D.1
Grant, M.A.2
Condron, M.C.3
Rigby, A.C.4
Teplow, D.B.5
-
28
-
-
28444442999
-
3D structure of Alzheimer's amyloid-β(1-42) fibrils
-
Lührs T., Ritter C., Adrian M., Riek-Loher D., Bohrmann B., and Döbeli H. 3D structure of Alzheimer's amyloid-β(1-42) fibrils Proc. Natl Acad. Sci. USA 102 2005 17342 17347
-
(2005)
Proc. Natl Acad. Sci. USA
, vol.102
, pp. 17342-17347
-
-
Lührs, T.1
Ritter, C.2
Adrian, M.3
Riek-Loher, D.4
Bohrmann, B.5
Döbeli, H.6
-
29
-
-
15544388942
-
Hydrogen-deuterium (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., and Serpersu E.H. Hydrogen-deuterium (H/D) exchange mapping of Aβ(1-40) amyloid fibril secondary structure using nuclear magnetic resonance spectroscopy Biochemistry 44 2005 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
-
30
-
-
37649019187
-
Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Aβ protofibrils
-
Habicht G., Haupt C., Friedrich R.P., Hortschansky P., Sachse C., and Meinhardt J. Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Aβ protofibrils Proc. Natl Acad. Sci. USA 104 2007 19232 19237
-
(2007)
Proc. Natl Acad. Sci. USA
, vol.104
, pp. 19232-19237
-
-
Habicht, G.1
Haupt, C.2
Friedrich, R.P.3
Hortschansky, P.4
Sachse, C.5
Meinhardt, J.6
-
31
-
-
34247234602
-
The Alzheimer's peptides Aβ40 and 42 adopt distinct conformations in water: A combined MD/NMR study
-
Sgourakis N.G., Yan Y., McCallum S.A., Wang C., and Garcia A.E. The Alzheimer's peptides Aβ40 and 42 adopt distinct conformations in water: a combined MD/NMR study J. Mol. Biol. 368 2007 1448 1457
-
(2007)
J. Mol. Biol.
, vol.368
, pp. 1448-1457
-
-
Sgourakis, N.G.1
Yan, Y.2
McCallum, S.A.3
Wang, C.4
Garcia, A.E.5
-
32
-
-
66149189211
-
Thermodynamics and dynamics of amyloid peptide oligomerization are sequence dependent
-
Lu Y., Derreumaux P., Guo Z., Mousseau N., and Wei G. Thermodynamics and dynamics of amyloid peptide oligomerization are sequence dependent Proteins 75 2008 954 963
-
(2008)
Proteins
, vol.75
, pp. 954-963
-
-
Lu, Y.1
Derreumaux, P.2
Guo, Z.3
Mousseau, N.4
Wei, G.5
-
33
-
-
69249239132
-
Antiparallel β-sheet: A signature structure of the oligomeric amyloid β-peptide
-
Cerf E., Sarroukh R., Tamamizu-Kato S., Breydo L., Derclaye S., and Dufrene Y.F. Antiparallel β-sheet: a signature structure of the oligomeric amyloid β-peptide Biochem. J. 421 2009 415 423
-
(2009)
Biochem. J.
, vol.421
, pp. 415-423
-
-
Cerf, E.1
Sarroukh, R.2
Tamamizu-Kato, S.3
Breydo, L.4
Derclaye, S.5
Dufrene, Y.F.6
-
34
-
-
64549140676
-
Structural characterization of a soluble amyloid β-peptide oligomer
-
Yu L., Edalji R., Harlan J.E., Holzman T.F., Lopez A.P., and Labkovsky B. Structural characterization of a soluble amyloid β-peptide oligomer Biochemistry 48 2009 1870 1877
-
(2009)
Biochemistry
, vol.48
, pp. 1870-1877
-
-
Yu, L.1
Edalji, R.2
Harlan, J.E.3
Holzman, T.F.4
Lopez, A.P.5
Labkovsky, B.6
-
35
-
-
77955790562
-
Comparing the folding free-energy landscapes of Aβ42 variants with different aggregation properties
-
Mitternacht S., Staneva I., Härd T., and Irbäck A. Comparing the folding free-energy landscapes of Aβ42 variants with different aggregation properties Proteins 78 2010 2600 2608
-
(2010)
Proteins
, vol.78
, pp. 2600-2608
-
-
Mitternacht, S.1
Staneva, I.2
Härd, T.3
Irbäck, A.4
-
36
-
-
80053554845
-
A new structural model of Aβ40 fibrils
-
Bertini I., Gonelli L., Luchinat C., Mao J., and Nesi A. A new structural model of Aβ40 fibrils J. Am. Chem. Soc. 133 2011 16013 16022
-
(2011)
J. Am. Chem. Soc.
, vol.133
, pp. 16013-16022
-
-
Bertini, I.1
Gonelli, L.2
Luchinat, C.3
Mao, J.4
Nesi, A.5
-
37
-
-
0036438914
-
Solution structure of the Alzheimer amyloid β-peptide (1-42) in an apolar microenvironment
-
Crescenzi O., Tomaselli S., Guerrini R., Salvadori S., D'Ursi A.M., Temussi P.A., and Picone D. Solution structure of the Alzheimer amyloid β-peptide (1-42) in an apolar microenvironment Eur. J. Biochem. 269 2002 5642 5648
-
(2002)
Eur. J. Biochem.
, vol.269
, pp. 5642-5648
-
-
Crescenzi, O.1
Tomaselli, S.2
Guerrini, R.3
Salvadori, S.4
D'Ursi, A.M.5
Temussi, P.A.6
Picone, D.7
-
38
-
-
32344451179
-
The α-to-β conformational transition of Alzheimer's Aβ-(1-42) peptide in aqueous media is reversible: A step by step conformational analysis suggests the location of β conformation seeding
-
Tomaselli S., Esposito V., Vangone P., Nuland N.A.J.V., Bonvin A.M.J.J., and Guerrini R. The α-to-β conformational transition of Alzheimer's Aβ-(1-42) peptide in aqueous media is reversible: a step by step conformational analysis suggests the location of β conformation seeding ChemBioChem 7 2006 257 267
-
(2006)
ChemBioChem
, vol.7
, pp. 257-267
-
-
Tomaselli, S.1
Esposito, V.2
Vangone, P.3
Nuland, N.A.J.V.4
Bonvin, A.M.J.J.5
Guerrini, R.6
-
39
-
-
17644397372
-
Aβ40-lactam (D23/K28) models a conformation highly favorable for nucleation of amyloid
-
Sciarretta K.L., Gordon D.J., Petkova A.T., Tycko R., and Meredith S.C. Aβ40-lactam (D23/K28) models a conformation highly favorable for nucleation of amyloid Biochemistry 44 2005 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
-
40
-
-
42449111198
-
Stabilization of a β-hairpin in monomeric Alzheimer's amyloid-β peptide inhibits amyloid formation
-
Hoyer W., Grönwall C., Jonsson A., Ståhl S., and Härd T. Stabilization of a β-hairpin in monomeric Alzheimer's amyloid-β peptide inhibits amyloid formation Proc. Natl. Acad. Sci. USA 105 2008 5099 5104
-
(2008)
Proc. Natl. Acad. Sci. USA
, vol.105
, pp. 5099-5104
-
-
Hoyer, W.1
Grönwall, C.2
Jonsson, A.3
Ståhl, S.4
Härd, T.5
-
41
-
-
17944368176
-
The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation
-
Nilsberth C., Westlind-Danielsson A., Eckman C.B., Condron M.M., Axelman K., and Forsell C. The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation Nat. Neurosci. 4 2001 887 893
-
(2001)
Nat. Neurosci.
, vol.4
, pp. 887-893
-
-
Nilsberth, C.1
Westlind-Danielsson, A.2
Eckman, C.B.3
Condron, M.M.4
Axelman, K.5
Forsell, C.6
-
43
-
-
0001561813
-
Rules for antiparallel β-sheet design: D-Pro-Gly is superior to l-Asn-Gly for β-hairpin nucleation
-
Stanger H.E., and Gellman S.H. Rules for antiparallel β-sheet design: d-Pro-Gly is superior to l-Asn-Gly for β-hairpin nucleation J. Am. Chem. Soc. 120 1998 4236 4237
-
(1998)
J. Am. Chem. Soc.
, vol.120
, pp. 4236-4237
-
-
Stanger, H.E.1
Gellman, S.H.2
-
44
-
-
58149333149
-
A new amyloid-like β-aggregate with amyloid characteristics, except fibril morphology
-
Chang E.S.H., Liao T.Y., Lim T.S., Fann W., and Chen R.P.Y. A new amyloid-like β-aggregate with amyloid characteristics, except fibril morphology J. Mol. Biol. 385 2009 1257 1265
-
(2009)
J. Mol. Biol.
, vol.385
, pp. 1257-1265
-
-
Chang, E.S.H.1
Liao, T.Y.2
Lim, T.S.3
Fann, W.4
Chen, R.P.Y.5
-
45
-
-
0000291574
-
Mirror image reverse turns promote β-hairpin formation
-
Haque T.S., Little J.C., and Gellman S.H. Mirror image reverse turns promote β-hairpin formation J. Am. Chem. Soc. 116 1994 4105 4106
-
(1994)
J. Am. Chem. Soc.
, vol.116
, pp. 4105-4106
-
-
Haque, T.S.1
Little, J.C.2
Gellman, S.H.3
-
46
-
-
0030992473
-
Insights on β-hairpin stability in aqueous solution from peptides with enforced type I′ and type II′ β-turns
-
Haque T.S., and Gellman S.H. Insights on β-hairpin stability in aqueous solution from peptides with enforced type I′ and type II′ β-turns J. Am. Chem. Soc. 119 1997 2303 2304
-
(1997)
J. Am. Chem. Soc.
, vol.119
, pp. 2303-2304
-
-
Haque, T.S.1
Gellman, S.H.2
-
47
-
-
0032849874
-
Quantification of β-sheet amyloid fibril structures with thioflavin T
-
LeVine H. Quantification of β-sheet amyloid fibril structures with thioflavin T Methods Enzymol. 309 1999 274 284
-
(1999)
Methods Enzymol.
, vol.309
, pp. 274-284
-
-
Levine, H.1
-
48
-
-
33749251222
-
Kinetics and thermodynamics of amyloid assembly using a high-performance liquid chromatography-based sedimentation assay
-
O'Nuallain B., Thakur A.K., Williams A.D., Bhattacharyya A.M., Chen S., Thiagarajan G., and Wetzel R. Kinetics and thermodynamics of amyloid assembly using a high-performance liquid chromatography-based sedimentation assay Methods Enzymol. 413 2006 34 74
-
(2006)
Methods Enzymol.
, vol.413
, pp. 34-74
-
-
O'Nuallain, B.1
Thakur, A.K.2
Williams, A.D.3
Bhattacharyya, A.M.4
Chen, S.5
Thiagarajan, G.6
Wetzel, R.7
-
49
-
-
0032877134
-
Analysis of protein aggregation kinetics
-
Ferrone F. Analysis of protein aggregation kinetics Methods Enzymol. 309 1999 256 274
-
(1999)
Methods Enzymol.
, vol.309
, pp. 256-274
-
-
Ferrone, F.1
-
50
-
-
72149118250
-
An analytical solution to the kinetics of breakable filament assembly
-
Knowles T.P.J., Waudby C.A., Devlin G.L., Cohen S.I.A., Aguzzi A., and Vendruscolo M. An analytical solution to the kinetics of breakable filament assembly Science 326 2009 1533 1537
-
(2009)
Science
, vol.326
, pp. 1533-1537
-
-
Knowles, T.P.J.1
Waudby, C.A.2
Devlin, G.L.3
Cohen, S.I.A.4
Aguzzi, A.5
Vendruscolo, M.6
-
52
-
-
1542600164
-
Mapping Aβ amyloid fibril secondary structure using scanning proline mutagenesis
-
Williams A.D., Portelius E., Kheterpal I., Guo J.T., Cook K.D., Xu Y., and Wetzel R. Mapping Aβ amyloid fibril secondary structure using scanning proline mutagenesis J. Mol. Biol. 335 2004 833 842
-
(2004)
J. Mol. Biol.
, vol.335
, pp. 833-842
-
-
Williams, A.D.1
Portelius, E.2
Kheterpal, I.3
Guo, J.T.4
Cook, K.D.5
Xu, Y.6
Wetzel, R.7
-
53
-
-
33644818046
-
Alanine scanning mutagenesis of Aβ(1-40) amyloid fibril stability
-
Williams A.D., Shivaprasad S., and Wetzel R. Alanine scanning mutagenesis of Aβ(1-40) amyloid fibril stability J. Mol. Biol. 357 2006 1283 1294
-
(2006)
J. Mol. Biol.
, vol.357
, pp. 1283-1294
-
-
Williams, A.D.1
Shivaprasad, S.2
Wetzel, R.3
-
54
-
-
17644397372
-
Aβ40-lactam (D23/K28) models a conformation highly favorable for nucleation of amyloid
-
Sciaretta K.L., Gordon D.J., Petkova A.T., Tycko R., and Meredith S.C. Aβ40-lactam (D23/K28) models a conformation highly favorable for nucleation of amyloid Biochemistry 44 2005 6003 6014
-
(2005)
Biochemistry
, vol.44
, pp. 6003-6014
-
-
Sciaretta, K.L.1
Gordon, D.J.2
Petkova, A.T.3
Tycko, R.4
Meredith, S.C.5
-
55
-
-
0031962158
-
Structural analysis of Alzheimer's β(1-40) amyloid: Protofilament assembly of tubular fibrils
-
Malinchik S.B., Inouye H., Szumowski K.E., and Kirschner D.A. Structural analysis of Alzheimer's β(1-40) amyloid: protofilament assembly of tubular fibrils Biophys. J. 74 1998 537 545
-
(1998)
Biophys. J.
, vol.74
, pp. 537-545
-
-
Malinchik, S.B.1
Inouye, H.2
Szumowski, K.E.3
Kirschner, D.A.4
-
56
-
-
0033584815
-
An FT-IR study of the β-amyloid conformation: Standardization of aggregation grade
-
Szabó Z., Klement É., Jost K., Zarándi M., Soós K., and Penke B. An FT-IR study of the β-amyloid conformation: standardization of aggregation grade Biochem. Biophys. Res. Commun. 265 1999 297 300
-
(1999)
Biochem. Biophys. Res. Commun.
, vol.265
, pp. 297-300
-
-
Szabó, Z.1
Klement, É.2
Jost, K.3
Zarándi, M.4
Soós, K.5
Penke, B.6
-
57
-
-
0035865539
-
Temperature-induced conformational changes in amyloid β(1-40) peptide investigated by simultaneous FT-IR microspectroscopy with thermal system
-
Chu H.L., and Lin C.Y. Temperature-induced conformational changes in amyloid β(1-40) peptide investigated by simultaneous FT-IR microspectroscopy with thermal system Biophys. Chem. 89 2001 173 180
-
(2001)
Biophys. Chem.
, vol.89
, pp. 173-180
-
-
Chu, H.L.1
Lin, C.Y.2
-
58
-
-
0014592230
-
Computed circular dichroism spectra for the evaluation of protein conformation
-
Greenfield N., and Fasman G.D. Computed circular dichroism spectra for the evaluation of protein conformation Biochemistry 8 1969 4108 4116
-
(1969)
Biochemistry
, vol.8
, pp. 4108-4116
-
-
Greenfield, N.1
Fasman, G.D.2
-
59
-
-
0037200117
-
Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability
-
Dahlgren K.N., Manelli A.M., Stine W.B., Baker L.K., Krafft G.A., and LaDu M.J. Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability J. Biol. Chem. 277 2002 32046 32053
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 32046-32053
-
-
Dahlgren, K.N.1
Manelli, A.M.2
Stine, W.B.3
Baker, L.K.4
Krafft, G.A.5
Ladu, M.J.6
-
60
-
-
0038176528
-
In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis
-
Stine W.B., Dahlgren K.N., Krafft G.A., and LaDu M.J. In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis J. Biol. Chem. 278 2003 11612 11622
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 11612-11622
-
-
Stine, W.B.1
Dahlgren, K.N.2
Krafft, G.A.3
Ladu, M.J.4
-
61
-
-
14944378094
-
Certain inhibitors of synthetic amyloid β-peptide (Aβ) fibrillogenesis block oligomerization of natural Aβ and thereby rescue long-term potentiation
-
Walsh D.M., Townsend M., Podlisny M.B., Shankar G.M., Fadeeva J.V., and Agnaf O.E. Certain inhibitors of synthetic amyloid β-peptide (Aβ) fibrillogenesis block oligomerization of natural Aβ and thereby rescue long-term potentiation J. Neurosci. 25 2005 2455 2462
-
(2005)
J. Neurosci.
, vol.25
, pp. 2455-2462
-
-
Walsh, D.M.1
Townsend, M.2
Podlisny, M.B.3
Shankar, G.M.4
Fadeeva, J.V.5
Agnaf, O.E.6
-
62
-
-
16644379264
-
Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
-
Cleary J.P., Walsh D.M., Hofmeister J.J., Shankar G.M., Kuskowski M.A., Selkoe D.J., and Ashe K.H. Natural oligomers of the amyloid-β protein specifically disrupt cognitive function Nat. Neurosci. 8 2005 79 84
-
(2005)
Nat. Neurosci.
, vol.8
, pp. 79-84
-
-
Cleary, J.P.1
Walsh, D.M.2
Hofmeister, J.J.3
Shankar, G.M.4
Kuskowski, M.A.5
Selkoe, D.J.6
Ashe, K.H.7
-
64
-
-
77953067946
-
Direct observation of nucleation and growth in amyloid self-assembly
-
Liang Y., Lynn D.G., and Berland K.M. Direct observation of nucleation and growth in amyloid self-assembly J. Am. Chem. Soc. 132 2010 6306 6308
-
(2010)
J. Am. Chem. Soc.
, vol.132
, pp. 6306-6308
-
-
Liang, Y.1
Lynn, D.G.2
Berland, K.M.3
-
65
-
-
77957257176
-
Stabilization of neurotoxic Alzheimer amyloid-β oligomers by protein engineering
-
Sandberg A., Luheshi L.M., Söllvander S., Barros T.P.D., Macao B., and Knowles T.P.J. Stabilization of neurotoxic Alzheimer amyloid-β oligomers by protein engineering Proc. Natl. Acad. Sci. USA 107 2010 15595 15600
-
(2010)
Proc. Natl. Acad. Sci. USA
, vol.107
, pp. 15595-15600
-
-
Sandberg, A.1
Luheshi, L.M.2
Söllvander, S.3
Barros, T.P.D.4
MacAo, B.5
Knowles, T.P.J.6
-
66
-
-
79959351077
-
Amyloid-β Annular Protofibrils Evade Fibrillar Fate in Alzheimer's Disease Brain
-
C.A. Lasagna-Reeves, C.G. Glabe, and R. Kayed Amyloid-β Annular Protofibrils Evade Fibrillar Fate in Alzheimer's Disease Brain J. Biol. Chem. 286 2011 22122 22130
-
(2011)
J. Biol. Chem.
, vol.286
, pp. 22122-22130
-
-
Lasagna-Reeves, C.A.1
Glabe, C.G.2
Kayed, R.3
-
67
-
-
34249860495
-
Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct
-
Necula M., Kayed R., Milton S., and Glabe C.G. Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct J. Biol. Chem. 282 2007 10311 10324
-
(2007)
J. Biol. Chem.
, vol.282
, pp. 10311-10324
-
-
Necula, M.1
Kayed, R.2
Milton, S.3
Glabe, C.G.4
-
68
-
-
75749115887
-
A substructure combination strategy to create potent and selective transthyretin kinetic stabilizers that prevent amyloidogenesis and cytotoxicity
-
Choi S., Reixach N., Connelly S., Johnson S.M., Wilson I.A., and Kelly J.W. A substructure combination strategy to create potent and selective transthyretin kinetic stabilizers that prevent amyloidogenesis and cytotoxicity J. Am. Chem. Soc. 132 2010 1359 1370
-
(2010)
J. Am. Chem. Soc.
, vol.132
, pp. 1359-1370
-
-
Choi, S.1
Reixach, N.2
Connelly, S.3
Johnson, S.M.4
Wilson, I.A.5
Kelly, J.W.6
-
69
-
-
80052231359
-
Homogeneous and heterogeneous tertiary structure ensembles of amyloid-β peptides
-
Ball K.A., Phillips A.H., Nerenberg P.S., Fawzi N.L., Wemmer D.E., and Head-Gordon T. Homogeneous and heterogeneous tertiary structure ensembles of amyloid-β peptides Biochemistry 50 2011 7612 7628
-
(2011)
Biochemistry
, vol.50
, pp. 7612-7628
-
-
Ball, K.A.1
Phillips, A.H.2
Nerenberg, P.S.3
Fawzi, N.L.4
Wemmer, D.E.5
Head-Gordon, T.6
-
70
-
-
0035918550
-
Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism
-
Nielsen L., Khurana R., Coats A., Frokjaer S., Brange J., and Vyas S. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism Biochemistry 40 2001 6036 6046
-
(2001)
Biochemistry
, vol.40
, pp. 6036-6046
-
-
Nielsen, L.1
Khurana, R.2
Coats, A.3
Frokjaer, S.4
Brange, J.5
Vyas, S.6
-
72
-
-
48249106228
-
Facial symmetry in protein self-assembly
-
Mehta A.K., Lu K., Childers W.S., Liang Y., Dublin S.N., and Dong J. Facial symmetry in protein self-assembly J. Am. Chem. Soc. 130 2008 9829 9835
-
(2008)
J. Am. Chem. Soc.
, vol.130
, pp. 9829-9835
-
-
Mehta, A.K.1
Lu, K.2
Childers, W.S.3
Liang, Y.4
Dublin, S.N.5
Dong, J.6
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