-
1
-
-
0037102362
-
Getting out of shape
-
Dobson C.M. Getting out of shape. Nature 418 (2002) 729-730
-
(2002)
Nature
, vol.418
, pp. 729-730
-
-
Dobson, C.M.1
-
2
-
-
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
-
3
-
-
0033616575
-
Designing conditions for in vitro formation of amyloid protofilaments and fibrils
-
Chiti F., Webster P., Taddei N., Clark A., Stefani M., Ramponi G., and Dobson C.M. Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc. Natl Acad. Sci. USA 96 (1999) 3590-3594
-
(1999)
Proc. Natl Acad. Sci. USA
, vol.96
, pp. 3590-3594
-
-
Chiti, F.1
Webster, P.2
Taddei, N.3
Clark, A.4
Stefani, M.5
Ramponi, G.6
Dobson, C.M.7
-
4
-
-
0034656947
-
Conversion of yeast phosphoglycerate kinase into amyloid-like structure
-
Damaschun G., Damaschun H., Fabian H., Gast K., Krober R., Wieske M., and Zirwer D. Conversion of yeast phosphoglycerate kinase into amyloid-like structure. Proteins 39 (2000) 204-211
-
(2000)
Proteins
, vol.39
, pp. 204-211
-
-
Damaschun, G.1
Damaschun, H.2
Fabian, H.3
Gast, K.4
Krober, R.5
Wieske, M.6
Zirwer, D.7
-
5
-
-
0035826234
-
Amyloid fibrils from muscle myoglobin
-
Fandrich M., Fletcher M.A., and Dobson C.M. Amyloid fibrils from muscle myoglobin. Nature 410 (2001) 165-166
-
(2001)
Nature
, vol.410
, pp. 165-166
-
-
Fandrich, M.1
Fletcher, M.A.2
Dobson, C.M.3
-
6
-
-
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
-
7
-
-
0034718157
-
Alzheimer's amyloid fibrils: structure and assembly
-
Serpell L.C. Alzheimer's amyloid fibrils: structure and assembly. Biochim. Biophys. Acta 1502 (2000) 16-30
-
(2000)
Biochim. Biophys. Acta
, vol.1502
, pp. 16-30
-
-
Serpell, L.C.1
-
8
-
-
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., et al. 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
-
9
-
-
0030908095
-
Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
-
Harper J.D., and Lansbury Jr. P.T. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem. 66 (1997) 385-407
-
(1997)
Annu. Rev. Biochem.
, vol.66
, pp. 385-407
-
-
Harper, J.D.1
Lansbury Jr., P.T.2
-
10
-
-
0022799567
-
Cooperative polymerization reactions. Analytical approximations, numerical examples, and experimental strategy
-
Goldstein R.F., and Stryer L. Cooperative polymerization reactions. Analytical approximations, numerical examples, and experimental strategy. Biophys. J. 50 (1986) 583-599
-
(1986)
Biophys. J.
, vol.50
, pp. 583-599
-
-
Goldstein, R.F.1
Stryer, L.2
-
11
-
-
23444445907
-
Competing pathways determine fibril morphology in the self-assembly of beta2-microglobulin into amyloid
-
Gosal W.S., Morten I.J., Hewitt E.W., Smith D.A., Thomson N.H., and Radford S.E. Competing pathways determine fibril morphology in the self-assembly of beta2-microglobulin into amyloid. J. Mol. Biol. 351 (2005) 850-864
-
(2005)
J. Mol. Biol.
, vol.351
, pp. 850-864
-
-
Gosal, W.S.1
Morten, I.J.2
Hewitt, E.W.3
Smith, D.A.4
Thomson, N.H.5
Radford, S.E.6
-
12
-
-
2942593931
-
Transthyretin aggregation under partially denaturing conditions is a downhill polymerization
-
Hurshman A.R., White J.T., Powers E.T., and Kelly J.W. Transthyretin aggregation under partially denaturing conditions is a downhill polymerization. Biochemistry 43 (2004) 7365-7381
-
(2004)
Biochemistry
, vol.43
, pp. 7365-7381
-
-
Hurshman, A.R.1
White, J.T.2
Powers, E.T.3
Kelly, J.W.4
-
13
-
-
0034733023
-
Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism
-
Esler W.P., Stimson E.R., Jennings J.M., Vinters H.V., Ghilardi J.R., Lee J.P., et al. Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism. Biochemistry 39 (2000) 6288-6295
-
(2000)
Biochemistry
, vol.39
, pp. 6288-6295
-
-
Esler, W.P.1
Stimson, E.R.2
Jennings, J.M.3
Vinters, H.V.4
Ghilardi, J.R.5
Lee, J.P.6
-
14
-
-
23144459082
-
Molecular recycling within amyloid fibrils
-
Carulla N., Caddy G.L., Hall D.R., Zurdo J., Gairi M., Feliz M., et al. Molecular recycling within amyloid fibrils. Nature 436 (2005) 554-558
-
(2005)
Nature
, vol.436
, pp. 554-558
-
-
Carulla, N.1
Caddy, G.L.2
Hall, D.R.3
Zurdo, J.4
Gairi, M.5
Feliz, M.6
-
16
-
-
0041817542
-
The amyloid beta peptide (Abeta(1-40)) is thermodynamically soluble at physiological concentrations
-
Sengupta P., Garai K., Sahoo B., Shi Y., Callaway D.J., and Maiti S. The amyloid beta peptide (Abeta(1-40)) is thermodynamically soluble at physiological concentrations. Biochemistry 42 (2003) 10506-10513
-
(2003)
Biochemistry
, vol.42
, pp. 10506-10513
-
-
Sengupta, P.1
Garai, K.2
Sahoo, B.3
Shi, Y.4
Callaway, D.J.5
Maiti, S.6
-
17
-
-
0035125904
-
Apolipoprotein A-I-derived amyloid in atherosclerosis. Its association with plasma levels of apolipoprotein A-I and cholesterol
-
Mucchiano G.I., Jonasson L., Haggqvist B., Einarsson E., and Westermark P. Apolipoprotein A-I-derived amyloid in atherosclerosis. Its association with plasma levels of apolipoprotein A-I and cholesterol. Am. J. Clin. Pathol. 115 (2001) 298-303
-
(2001)
Am. J. Clin. Pathol.
, vol.115
, pp. 298-303
-
-
Mucchiano, G.I.1
Jonasson, L.2
Haggqvist, B.3
Einarsson, E.4
Westermark, P.5
-
18
-
-
0033587677
-
Medin: an integral fragment of aortic smooth muscle cell-produced lactadherin forms the most common human amyloid
-
Haggqvist B., Naslund J., Sletten K., Westermark G.T., Mucchiano G., Tjernberg L.O., et al. Medin: an integral fragment of aortic smooth muscle cell-produced lactadherin forms the most common human amyloid. Proc. Natl Acad. Sci. USA 96 (1999) 8669-8674
-
(1999)
Proc. Natl Acad. Sci. USA
, vol.96
, pp. 8669-8674
-
-
Haggqvist, B.1
Naslund, J.2
Sletten, K.3
Westermark, G.T.4
Mucchiano, G.5
Tjernberg, L.O.6
-
19
-
-
0036520326
-
The structural basis for amyloid formation by plasma apolipoproteins: a review
-
Hatters D.M., and Howlett G.J. The structural basis for amyloid formation by plasma apolipoproteins: a review. Eur. Biophys. J. 31 (2002) 2-8
-
(2002)
Eur. Biophys. J.
, vol.31
, pp. 2-8
-
-
Hatters, D.M.1
Howlett, G.J.2
-
20
-
-
33746932145
-
Amino-terminal domain stability mediates apolipoprotein E aggregation into neurotoxic fibrils
-
Hatters D.M., Zhong N., Rutenber E., and Weisgraber K.H. Amino-terminal domain stability mediates apolipoprotein E aggregation into neurotoxic fibrils. J. Mol. Biol. 361 (2006) 932-944
-
(2006)
J. Mol. Biol.
, vol.361
, pp. 932-944
-
-
Hatters, D.M.1
Zhong, N.2
Rutenber, E.3
Weisgraber, K.H.4
-
21
-
-
27144480726
-
From hexamer to amyloid: marginal stability of apolipoprotein SAA2.2 leads to in vitro fibril formation at physiological temperature
-
Wang L., Lashuel H.A., and Colon W. From hexamer to amyloid: marginal stability of apolipoprotein SAA2.2 leads to in vitro fibril formation at physiological temperature. Amyloid 12 (2005) 139-148
-
(2005)
Amyloid
, vol.12
, pp. 139-148
-
-
Wang, L.1
Lashuel, H.A.2
Colon, W.3
-
22
-
-
0034682559
-
Human apolipoprotein C-II forms twisted amyloid ribbons and closed loops
-
Hatters D.M., MacPhee C.E., Lawrence L.J., Sawyer W.H., and Howlett G.J. Human apolipoprotein C-II forms twisted amyloid ribbons and closed loops. Biochemistry 39 (2000) 8276-8283
-
(2000)
Biochemistry
, vol.39
, pp. 8276-8283
-
-
Hatters, D.M.1
MacPhee, C.E.2
Lawrence, L.J.3
Sawyer, W.H.4
Howlett, G.J.5
-
23
-
-
2442642590
-
Non-fibrillar components of amyloid deposits mediate the self-association and tangling of amyloid fibrils
-
MacRaild C.A., Stewart C.R., Mok Y.F., Gunzburg M.J., Perugini M.A., Lawrence L.J., et al. Non-fibrillar components of amyloid deposits mediate the self-association and tangling of amyloid fibrils. J. Biol. Chem. 279 (2004) 21038-21045
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 21038-21045
-
-
MacRaild, C.A.1
Stewart, C.R.2
Mok, Y.F.3
Gunzburg, M.J.4
Perugini, M.A.5
Lawrence, L.J.6
-
24
-
-
1642264113
-
Fibrillar amyloid protein present in atheroma activates CD36 signal transduction
-
Medeiros L.A., Khan T., El Khoury J.B., Pham C.L., Hatters D.M., Howlett G.J., et al. Fibrillar amyloid protein present in atheroma activates CD36 signal transduction. J. Biol. Chem. 279 (2004) 10643-10648
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 10643-10648
-
-
Medeiros, L.A.1
Khan, T.2
El Khoury, J.B.3
Pham, C.L.4
Hatters, D.M.5
Howlett, G.J.6
-
25
-
-
34948863450
-
Serum amyloid P colocalizes with apolipoproteins in human atheroma: functional implications
-
Stewart C.R., Haw III A., Lopez R., McDonald T.O., Callaghan J.M., McConville M.J., et al. Serum amyloid P colocalizes with apolipoproteins in human atheroma: functional implications. J. Lipid Res. 48 (2007) 2162-2171
-
(2007)
J. Lipid Res.
, vol.48
, pp. 2162-2171
-
-
Stewart, C.R.1
Haw III, A.2
Lopez, R.3
McDonald, T.O.4
Callaghan, J.M.5
McConville, M.J.6
-
26
-
-
0037040878
-
Macromolecular crowding accelerates amyloid formation by human apolipoprotein C-II
-
Hatters D.M., Minton A.P., and Howlett G.J. Macromolecular crowding accelerates amyloid formation by human apolipoprotein C-II. J. Biol. Chem. 277 (2002) 7824-7830
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 7824-7830
-
-
Hatters, D.M.1
Minton, A.P.2
Howlett, G.J.3
-
27
-
-
0034009520
-
Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
-
Schuck P. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys. J. 78 (2000) 1606-1619
-
(2000)
Biophys. J.
, vol.78
, pp. 1606-1619
-
-
Schuck, P.1
-
28
-
-
10744229371
-
The circularization of amyloid fibrils formed by apolipoprotein C-II
-
Hatters D.M., MacRaild C.A., Daniels R., Gosal W.S., Thomson N.H., Jones J.A., et al. The circularization of amyloid fibrils formed by apolipoprotein C-II. Biophys. J. 85 (2003) 3979-3990
-
(2003)
Biophys. J.
, vol.85
, pp. 3979-3990
-
-
Hatters, D.M.1
MacRaild, C.A.2
Daniels, R.3
Gosal, W.S.4
Thomson, N.H.5
Jones, J.A.6
-
29
-
-
0037380769
-
Sedimentation velocity analysis of flexible macromolecules: self-association and tangling of amyloid fibrils
-
MacRaild C.A., Hatters D.M., Lawrence L.J., and Howlett G.J. Sedimentation velocity analysis of flexible macromolecules: self-association and tangling of amyloid fibrils. Biophys. J. 84 (2003) 2562-2569
-
(2003)
Biophys. J.
, vol.84
, pp. 2562-2569
-
-
MacRaild, C.A.1
Hatters, D.M.2
Lawrence, L.J.3
Howlett, G.J.4
-
30
-
-
0016369152
-
Kinetics and mechanism of deoxyhemoglobin S gelation: a new approach to understanding sickle cell disease
-
Hofrichter J., Ross P.D., and Eaton W.A. Kinetics and mechanism of deoxyhemoglobin S gelation: a new approach to understanding sickle cell disease. Proc. Natl Acad. Sci. USA 71 (1974) 4864-4868
-
(1974)
Proc. Natl Acad. Sci. USA
, vol.71
, pp. 4864-4868
-
-
Hofrichter, J.1
Ross, P.D.2
Eaton, W.A.3
-
31
-
-
33750480868
-
Characterization of the nanoscale properties of individual amyloid fibrils
-
Smith J.F., Knowles T.P., Dobson C.M., Macphee C.E., and Welland M.E. Characterization of the nanoscale properties of individual amyloid fibrils. Proc. Natl Acad. Sci. USA 103 (2006) 15806-15811
-
(2006)
Proc. Natl Acad. Sci. USA
, vol.103
, pp. 15806-15811
-
-
Smith, J.F.1
Knowles, T.P.2
Dobson, C.M.3
Macphee, C.E.4
Welland, M.E.5
-
32
-
-
0035965138
-
Kinetic mechanism of end-to-end annealing of actin filaments
-
Andrianantoandro E., Blanchoin L., Sept D., McCammon J.A., and Pollard T.D. Kinetic mechanism of end-to-end annealing of actin filaments. J. Mol. Biol. 312 (2001) 721-730
-
(2001)
J. Mol. Biol.
, vol.312
, pp. 721-730
-
-
Andrianantoandro, E.1
Blanchoin, L.2
Sept, D.3
McCammon, J.A.4
Pollard, T.D.5
-
33
-
-
0032796310
-
Annealing accounts for the length of actin filaments formed by spontaneous polymerization
-
Sept D., Xu J., Pollard T.D., and McCammon J.A. Annealing accounts for the length of actin filaments formed by spontaneous polymerization. Biophys. J. 77 (1999) 2911-2919
-
(1999)
Biophys. J.
, vol.77
, pp. 2911-2919
-
-
Sept, D.1
Xu, J.2
Pollard, T.D.3
McCammon, J.A.4
-
34
-
-
33746698975
-
The physical basis of how prion conformations determine strain phenotypes
-
Tanaka M., Collins S.R., Toyama B.H., and Weissman J.S. The physical basis of how prion conformations determine strain phenotypes. Nature 442 (2006) 585-589
-
(2006)
Nature
, vol.442
, pp. 585-589
-
-
Tanaka, M.1
Collins, S.R.2
Toyama, B.H.3
Weissman, J.S.4
-
35
-
-
0036233931
-
Origins and kinetic consequences of diversity in Sup35 yeast prion fibers
-
DePace A.H., and Weissman J.S. Origins and kinetic consequences of diversity in Sup35 yeast prion fibers. Nat. Struct. Biol. 9 (2002) 389-396
-
(2002)
Nat. Struct. Biol.
, vol.9
, pp. 389-396
-
-
DePace, A.H.1
Weissman, J.S.2
-
36
-
-
33846328750
-
Dynamics of the nucleated polymerization model of prion replication
-
Rubenstein R., Gray P.C., Cleland T.J., Piltch M.S., Hlavacek W.S., Roberts R.M., et al. Dynamics of the nucleated polymerization model of prion replication. Biophys. Chem. 125 (2007) 360-367
-
(2007)
Biophys. Chem.
, vol.125
, pp. 360-367
-
-
Rubenstein, R.1
Gray, P.C.2
Cleland, T.J.3
Piltch, M.S.4
Hlavacek, W.S.5
Roberts, R.M.6
-
37
-
-
0021527508
-
Kinetics of nucleation-controlled polymerization. A perturbation treatment for use with a secondary pathway
-
Bishop M.F., and Ferrone F.A. Kinetics of nucleation-controlled polymerization. A perturbation treatment for use with a secondary pathway. Biophys. J. 46 (1984) 631-644
-
(1984)
Biophys. J.
, vol.46
, pp. 631-644
-
-
Bishop, M.F.1
Ferrone, F.A.2
-
39
-
-
25444512708
-
Ultrasonication-induced amyloid fibril formation of beta2-microglobulin
-
Ohhashi Y., Kihara M., Naiki H., and Goto Y. Ultrasonication-induced amyloid fibril formation of beta2-microglobulin. J. Biol. Chem. 280 (2005) 32843-32848
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 32843-32848
-
-
Ohhashi, Y.1
Kihara, M.2
Naiki, H.3
Goto, Y.4
-
40
-
-
8844247180
-
Mechanism of prion propagation: amyloid growth occurs by monomer addition
-
Collins S.R., Douglass A., Vale R.D., and Weissman J.S. Mechanism of prion propagation: amyloid growth occurs by monomer addition. PLoS Biol. 2 (2004) e321
-
(2004)
PLoS Biol.
, vol.2
-
-
Collins, S.R.1
Douglass, A.2
Vale, R.D.3
Weissman, J.S.4
-
41
-
-
31544445747
-
Shear flow induces amyloid fibril formation
-
Hill E.K., Krebs B., Goodall D.G., Howlett G.J., and Dunstan D.E. Shear flow induces amyloid fibril formation. Biomacromolecules 7 (2006) 10-13
-
(2006)
Biomacromolecules
, vol.7
, pp. 10-13
-
-
Hill, E.K.1
Krebs, B.2
Goodall, D.G.3
Howlett, G.J.4
Dunstan, D.E.5
-
42
-
-
0037041426
-
Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
-
Walsh D.M., Klyubin I., Fadeeva J.V., Cullen W.K., Anwyl R., Wolfe M.S., et al. Naturally secreted oligomers of amyloid beta 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
-
43
-
-
0036708168
-
Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: the emerging role of oligomeric assemblies
-
Kirkitadze M.D., Bitan G., and Teplow D.B. Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: the emerging role of oligomeric assemblies. J. Neurosci. Res. 69 (2002) 567-577
-
(2002)
J. Neurosci. Res.
, vol.69
, pp. 567-577
-
-
Kirkitadze, M.D.1
Bitan, G.2
Teplow, D.B.3
-
44
-
-
33749506729
-
Sedimentation velocity analysis of amyloid oligomers and fibrils
-
Mok Y.F., and Howlett G.J. Sedimentation velocity analysis of amyloid oligomers and fibrils. Methods Enzymol. 413 (2006) 199-217
-
(2006)
Methods Enzymol.
, vol.413
, pp. 199-217
-
-
Mok, Y.F.1
Howlett, G.J.2
-
46
-
-
0034668130
-
Determination of the sedimentation coefficient distribution by least-squares boundary modeling
-
Schuck P., and Rossmanith P. Determination of the sedimentation coefficient distribution by least-squares boundary modeling. Biopolymers 54 (2000) 328-341
-
(2000)
Biopolymers
, vol.54
, pp. 328-341
-
-
Schuck, P.1
Rossmanith, P.2
|