-
1
-
-
0034578389
-
Aggresomes, inclusion bodies and protein aggregation
-
Kopito, R. R. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 10, 524-530 (2000).
-
(2000)
Trends Cell Biol.
, vol.10
, pp. 524-530
-
-
Kopito, R.R.1
-
2
-
-
0032006678
-
The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
-
Kelly, J. W. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 8, 101-106 (1998).
-
(1998)
Curr. Opin. Struct. Biol.
, vol.8
, pp. 101-106
-
-
Kelly, J.W.1
-
4
-
-
0037071906
-
Construction and deconstruction of bacterial inclusion bodies
-
Carriò, M. M. & Villaverde, A. Construction and deconstruction of bacterial inclusion bodies. J. Biotech. 96, 3-12 (2002).
-
(2002)
J. Biotech.
, vol.96
, pp. 3-12
-
-
Carriò, M.M.1
Villaverde, A.2
-
5
-
-
0033200063
-
Protein misfolding, evolution and disease
-
Dobson, C. M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24, 329-332 (1999).
-
(1999)
Trends Biochem. Sci.
, vol.24
, pp. 329-332
-
-
Dobson, C.M.1
-
6
-
-
0030801746
-
The structure of amyloid fibrils by electron microscopy and X-ray diffraction
-
Sunde, M. & Blake, C. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv. Protein Chem. 50, 123-159 (1997).
-
(1997)
Adv. Protein Chem.
, vol.50
, pp. 123-159
-
-
Sunde, M.1
Blake, C.2
-
7
-
-
0033574161
-
Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein
-
Liemann, S. & Glockshuber, R. Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein. Biochemistry 38, 3258-3267 (1999).
-
(1999)
Biochemistry
, vol.38
, pp. 3258-3267
-
-
Liemann, S.1
Glockshuber, R.2
-
8
-
-
0037473750
-
Prevention of transthyretin amyloid disease by changing protein misfolding energetics
-
Hammarstrom, P., Wiseman, R. L., Powers, E. T. & Kelly, J. W. Prevention of transthyretin amyloid disease by changing protein misfolding energetics. Science 299, 713-716 (2003).
-
(2003)
Science
, vol.299
, pp. 713-716
-
-
Hammarstrom, P.1
Wiseman, R.L.2
Powers, E.T.3
Kelly, J.W.4
-
9
-
-
0036166319
-
Kinetic partitioning of protein folding and aggregation
-
Chiti, F. et al. Kinetic partitioning of protein folding and aggregation. Nature Struct. Biol. 9, 137-143 (2002).
-
(2002)
Nature Struct. Biol.
, vol.9
, pp. 137-143
-
-
Chiti, F.1
-
10
-
-
0037059069
-
Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases
-
Chiti, F. et al. Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases. Proc. Natl Acad. Sci. USA 99, 16419-16426 (2002).
-
(2002)
Proc. Natl. Acad. Sci. USA
, vol.99
, pp. 16419-16426
-
-
Chiti, F.1
-
11
-
-
0037102362
-
Getting out of shape
-
Dobson, C. M. Getting out of shape. Nature 418, 729-730 (2002).
-
(2002)
Nature
, vol.418
, pp. 729-730
-
-
Dobson, C.M.1
-
12
-
-
0035951869
-
A hydrophobic stretch of 12 amino acid residues in the middle of α-synuclein is essential for filament assembly
-
Giasson, B. I., Murray, I. V., Trojanowski, J. Q. & Lee, V. M. A hydrophobic stretch of 12 amino acid residues in the middle of α-synuclein is essential for filament assembly. J. Biol. Chem. 276, 2380-2386 (2001).
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 2380-2386
-
-
Giasson, B.I.1
Murray, I.V.2
Trojanowski, J.Q.3
Lee, V.M.4
-
13
-
-
0035823520
-
Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide. An experimental support for the key role of the phenylalanine residue in amyloid formation
-
Azriel, R. & Gazit, E. Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide. An experimental support for the key role of the phenylalanine residue in amyloid formation. J. Biol. Chem. 276, 34156-34161 (2001).
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 34156-34161
-
-
Azriel, R.1
Gazit, E.2
-
14
-
-
0033638450
-
S20G mutant amylin exhibits increased in vitro amyloidogenicity and increased intracellular cytotoxicity compared to wild-type amylin
-
Sakagashira, S. et al. S20G mutant amylin exhibits increased in vitro amyloidogenicity and increased intracellular cytotoxicity compared to wild-type amylin. Am. J. Pathol. 157, 2101-2109 (2000).
-
(2000)
Am. J. Pathol.
, vol.157
, pp. 2101-2109
-
-
Sakagashira, S.1
-
15
-
-
0033567401
-
Molecular determinants of the physicochemical properties of a critical prion protein region comprising residues 106-126
-
Salmona, M. et al. Molecular determinants of the physicochemical properties of a critical prion protein region comprising residues 106-126. Biochem. J. 342, 207-214 (1999).
-
(1999)
Biochem. J.
, vol.342
, pp. 207-214
-
-
Salmona, M.1
-
16
-
-
0035847063
-
The Val-210-Ile pathogenic Creutzfeldt-Jakob disease mutation increases both the helical and aggregation propensities of a sequence corresponding to helix-3 of PrP(C)
-
Thompson, A. J., Barnham, K. J., Norton, R. S. & Barrow, C. J. The Val-210-Ile pathogenic Creutzfeldt-Jakob disease mutation increases both the helical and aggregation propensities of a sequence corresponding to helix-3 of PrP(C). Biochim. Biophys. Acta 1544, 242-254 (2001).
-
(2001)
Biochim. Biophys. Acta
, vol.1544
, pp. 242-254
-
-
Thompson, A.J.1
Barnham, K.J.2
Norton, R.S.3
Barrow, C.J.4
-
17
-
-
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. et al. 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, 571-576 (2000).
-
(2000)
Proc. Natl. Acad. Sci. USA
, vol.97
, pp. 571-576
-
-
Conway, K.A.1
-
18
-
-
0035980088
-
Pathogenic effects of D23N Iowa mutant amyloid β-protein
-
Van Nostrand, W. E., Melchor, J. P., Cho, H. S., Greenberg, S. M. & Rebeck, G. W. Pathogenic effects of D23N Iowa mutant amyloid β-protein. J. Biol. Chem. 276, 32860-32866 (2001).
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 32860-32866
-
-
Van Nostrand, W.E.1
Melchor, J.P.2
Cho, H.S.3
Greenberg, S.M.4
Rebeck, G.W.5
-
19
-
-
0034282630
-
Substitutions at codon 22 of Alzheimer's abeta peptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells
-
Miravalle, L. et al. Substitutions at codon 22 of Alzheimer's abeta peptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells. J. Biol. Chem. 275, 27110-27116 (2000).
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 27110-27116
-
-
Miravalle, L.1
-
20
-
-
17944368176
-
The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation
-
Nilsberth, C. et al. The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation. Nature Neurosci. 4, 887-893 (2001).
-
(2001)
Nature Neurosci.
, vol.4
, pp. 887-893
-
-
Nilsberth, C.1
-
21
-
-
0029854533
-
Point substitution in the central hydrophobic cluster of a human β-amyloid congener disrupts peptide folding and abolishes plaque competence
-
Esler, W. P. et al. Point substitution in the central hydrophobic cluster of a human β-amyloid congener disrupts peptide folding and abolishes plaque competence. Biochemistry 35, 13914-13921 (1996).
-
(1996)
Biochemistry
, vol.35
, pp. 13914-13921
-
-
Esler, W.P.1
-
22
-
-
0037465354
-
Tau polymerization: Role of the amino terminus
-
Gamblin, T. C., Berry, R. W. & Binder, L. I. Tau polymerization: Role of the amino terminus. Biochemistry 42, 2252-2257 (2003).
-
(2003)
Biochemistry
, vol.42
, pp. 2252-2257
-
-
Gamblin, T.C.1
Berry, R.W.2
Binder, L.I.3
-
23
-
-
0034718571
-
Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias
-
Barghorn, S. et al. Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias. Biochemistry 39, 11714-11721 (2000).
-
(2000)
Biochemistry
, vol.39
, pp. 11714-11721
-
-
Barghorn, S.1
-
24
-
-
0034705192
-
In vitro polymerization of tau protein monitored by laser light scattering: Method and application to the study of FTDP-17 mutants
-
Gamblin, T. C. et al. In vitro polymerization of tau protein monitored by laser light scattering: Method and application to the study of FTDP-17 mutants. Biochemistry 39, 6136-6144 (2000).
-
(2000)
Biochemistry
, vol.39
, pp. 6136-6144
-
-
Gamblin, T.C.1
-
25
-
-
0033011181
-
Accelerated filament formation from tau protein with specific FTDP-17 missense mutations
-
Nacharaju, P. et al. Accelerated filament formation from tau protein with specific FTDP-17 missense mutations. FEBS Lett. 447, 195-199 (1999).
-
(1999)
FEBS Lett.
, vol.447
, pp. 195-199
-
-
Nacharaju, P.1
-
26
-
-
0036830506
-
Structure, stability, and aggregation of paired helical filaments from tau protein and FTDP-17 mutants probed by tryptophan scanning mutagenesis
-
Li, L., Von Bergen, M., Mandelkow, E. M. & Mandelkow, E. Structure, stability, and aggregation of paired helical filaments from tau protein and FTDP-17 mutants probed by tryptophan scanning mutagenesis. J. Biol. Chem. 277, 41390-41400 (2002).
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 41390-41400
-
-
Li, L.1
Von Bergen, M.2
Mandelkow, E.M.3
Mandelkow, E.4
-
27
-
-
0030744878
-
X-ray diffraction and far-UV CD studies of filaments formed by a leucine-rich repeat peptide: Structural similarity to the amyloid fibrils of prions and Alzheimer's disease β-protein
-
Symmons, M. F., Buchanan, S. G., Clarke, D. T., Jones, G. & Gay, N. J. X-ray diffraction and far-UV CD studies of filaments formed by a leucine-rich repeat peptide: Structural similarity to the amyloid fibrils of prions and Alzheimer's disease β-protein. FEBS Lett. 412, 397-403 (1997).
-
(1997)
FEBS Lett.
, vol.412
, pp. 397-403
-
-
Symmons, M.F.1
Buchanan, S.G.2
Clarke, D.T.3
Jones, G.4
Gay, N.J.5
-
28
-
-
0033522983
-
Induction of beta-sheet structure in amyloidogenic peptides by neutralization of aspartate: A model for amyloid nucleation
-
Orpiszewski, J. & Benson, M. D. Induction of beta-sheet structure in amyloidogenic peptides by neutralization of aspartate: A model for amyloid nucleation. J. Mol. Biol. 289, 413-428 (1999).
-
(1999)
J. Mol. Biol.
, vol.289
, pp. 413-428
-
-
Orpiszewski, J.1
Benson, M.D.2
-
29
-
-
0033529861
-
Intrinsic β-sheet propensities result from van der Waals interactions between side chains and the local backbone
-
Street, A. G. & Mayo, S. L. Intrinsic β-sheet propensities result from van der Waals interactions between side chains and the local backbone. Proc. Natl Acad. Sci. USA 96, 9074-9076 (1999).
-
(1999)
Proc. Natl. Acad. Sci. USA
, vol.96
, pp. 9074-9076
-
-
Street, A.G.1
Mayo, S.L.2
-
30
-
-
0037041420
-
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
-
Bucciantini, M. et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416, 507-511 (2002).
-
(2002)
Nature
, vol.416
, pp. 507-511
-
-
Bucciantini, M.1
|