-
1
-
-
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
-
2
-
-
0042467550
-
Rationalization of the effects of mutations on peptide and protein aggregation rates
-
Chiti, R, Stefani, M., Taddei, N., Ramponi, G. & Dobson, C.M. Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 424, 805-808 (2003).
-
(2003)
Nature
, vol.424
, pp. 805-808
-
-
Chiti, R.1
Stefani, M.2
Taddei, N.3
Ramponi, G.4
Dobson, C.M.5
-
3
-
-
0036166319
-
Kinetic partitioning of protein folding and aggregation
-
Chiti, F. et al. Kinetic partitioning of protein folding and aggregation. Nat. Struct. Biol. 9, 137-143 (2002).
-
(2002)
Nat. Struct. Biol.
, vol.9
, pp. 137-143
-
-
Chiti, F.1
-
4
-
-
0035961329
-
The structural basis of protein folding and its links with human disease
-
Dobson, C.M. The structural basis of protein folding and its links with human disease. Philos. Trans. R. Soc. Lond. 6356, 133-145 (2001).
-
(2001)
Philos. Trans. R. Soc. Lond.
, vol.6356
, pp. 133-145
-
-
Dobson, C.M.1
-
5
-
-
0037102362
-
Protein-misfolding diseases: Getting out of shape
-
Dobson, C.M. Protein-misfolding diseases: getting out of shape. Nature 418, 729-730 (2002).
-
(2002)
Nature
, vol.418
, pp. 729-730
-
-
Dobson, C.M.1
-
6
-
-
0345827608
-
Sequence determinants of amyloid fibril formation
-
de la Paz, M.L. & Serrano, L. Sequence determinants of amyloid fibril formation. Proc. Natl. Acad. Sci. USA 101, 87-92 (2004).
-
(2004)
Proc. Natl. Acad. Sci. USA
, vol.101
, pp. 87-92
-
-
De La Paz, M.L.1
Serrano, L.2
-
7
-
-
0031558811
-
Role of beta-turn residues in beta-hairpin formation and stability in designed peptides
-
Ramirez-Alvarado, M., Blanco, F.J., Niemann, H. & Serrano, L. Role of beta-turn residues in beta-hairpin formation and stability in designed peptides. J. Mol. Biol. 273, 898-912 (1997).
-
(1997)
J. Mol. Biol.
, vol.273
, pp. 898-912
-
-
Ramirez-Alvarado, M.1
Blanco, F.J.2
Niemann, H.3
Serrano, L.4
-
8
-
-
0035823232
-
Computer-aided design of beta-sheet peptides
-
Lopez de la Paz, M., Lacroix, E., Ramirez-Alvarado, M. & Serrano, L. Computer-aided design of beta-sheet peptides. J. Mol. Biol. 312, 229-246 (2001).
-
(2001)
J. Mol. Biol.
, vol.312
, pp. 229-246
-
-
Lopez De La Paz, M.1
Lacroix, E.2
Ramirez-Alvarado, M.3
Serrano, L.4
-
9
-
-
0033595706
-
Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
-
Vassar, R. et al. Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 286, 735-741 (1999).
-
(1999)
Science
, vol.286
, pp. 735-741
-
-
Vassar, R.1
-
10
-
-
0037551741
-
Protofibrils, pores, fibrils, and neurode generation: Separating the responsible protein aggregates from the innocent bystanders
-
Caughey, B. & Lansbury, P.T. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26, 267-298 (2003).
-
(2003)
Annu. Rev. Neurosci.
, vol.26
, pp. 267-298
-
-
Caughey, B.1
Lansbury, P.T.2
-
11
-
-
17944368176
-
The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Abeta protofibril formation
-
Nilsberth, C. et al. The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Abeta protofibril formation. Nat. Neurosci, 4, 887-893 (2001).
-
(2001)
Nat. Neurosci.
, vol.4
, pp. 887-893
-
-
Nilsberth, C.1
-
12
-
-
0028839438
-
Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease
-
McCutchen, S.L., Lai, Z., Miroy, G.J., Kelly, J.W. & Colon, W. Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease. Biochemistry 34, 13527-13536 (1995).
-
(1995)
Biochemistry
, vol.34
, pp. 13527-13536
-
-
McCutchen, S.L.1
Lai, Z.2
Miroy, G.J.3
Kelly, J.W.4
Colon, W.5
-
13
-
-
0027506498
-
Human lysozyme gene mutations cause hereditary systemic amyloidosis
-
Pepys, M.B. et al. Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature 362, 553-557 (1993).
-
(1993)
Nature
, vol.362
, pp. 553-557
-
-
Pepys, M.B.1
-
14
-
-
0034696835
-
Comparative studies of two transthyretin variants with protective effects on familial amyloidotic polyneuropathy: TTR R104H and TTR T119M
-
Almeida, M.R., Alves, I.L.Terazaki, H., Ando, Y. & Saraiva, M.J. Comparative studies of two transthyretin variants with protective effects on familial amyloidotic polyneuropathy: TTR R104H and TTR T119M. Biochem. Biophys. Res. Commun. 270, 1024-1028 (2000).
-
(2000)
Biochem. Biophys. Res. Commun.
, vol.270
, pp. 1024-1028
-
-
Almeida, M.R.1
Alves, I.L.2
Terazaki, H.3
Ando, Y.4
Saraiva, M.J.5
-
15
-
-
0035964955
-
Trans-suppression of misfolding in an amyloid disease
-
Hammarstrom, P., Schneider, F. & Kelly, J.W. Trans-suppression of misfolding in an amyloid disease. Science 293, 2459-2462 (2001).
-
(2001)
Science
, vol.293
, pp. 2459-2462
-
-
Hammarstrom, P.1
Schneider, F.2
Kelly, J.W.3
-
16
-
-
0030694782
-
The amyloidogenic potential of transthyretin variants correlates with their tendency to aggregate in solution
-
Quintas, A., Saraiva, M.J. & Brito, R.M. The amyloidogenic potential of transthyretin variants correlates with their tendency to aggregate in solution. FEBS Lett 418, 297-300 (1997).
-
(1997)
FEBS Lett.
, vol.418
, pp. 297-300
-
-
Quintas, A.1
Saraiva, M.J.2
Brito, R.M.3
-
17
-
-
0034672768
-
Comparative calorimetric study of non-amyloidogenic and amyloidogenic variants of the homotetrameric protein transthyretin
-
Shnyrov, V.L. et al. Comparative calorimetric study of non-amyloidogenic and amyloidogenic variants of the homotetrameric protein transthyretin. Biophys. Chem. 88, 61-67 (2000).
-
(2000)
Biophys. Chem.
, vol.88
, pp. 61-67
-
-
Shnyrov, V.L.1
-
18
-
-
0036220131
-
Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme
-
Canet, D. et al. Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme. Nat. Struct. Biol. 9, 308-315 (2002).
-
(2002)
Nat. Struct. Biol.
, vol.9
, pp. 308-315
-
-
Canet, D.1
-
19
-
-
0033849915
-
Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants
-
Morozova-Roche, L.A. et al. Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants. J. Struct. Biol. 130, 339-351 (2000).
-
(2000)
J. Struct. Biol.
, vol.130
, pp. 339-351
-
-
Morozova-Roche, L.A.1
-
20
-
-
0035177019
-
Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy
-
Chamberlain, A.K., Receveur, V., Spencer, A., Redfield, C. & Dobson, C.M. Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy. Protein Sci. 10, 2525-2530 (2001).
-
(2001)
Protein Sci.
, vol.10
, pp. 2525-2530
-
-
Chamberlain, A.K.1
Receveur, V.2
Spencer, A.3
Redfield, C.4
Dobson, C.M.5
-
21
-
-
0031056829
-
Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
-
Booth, D.R. et al. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature 385, 787-793 (1997).
-
(1997)
Nature
, vol.385
, pp. 787-793
-
-
Booth, D.R.1
-
22
-
-
0036291145
-
Predicting changes in the stability of proteins and protein complexes: A study of more than 1000 mutations
-
Guerois, R., Nielsen, J.E. & Serrano, L. Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations. J. Mol. Biol. 320, 369-387 (2002).
-
(2002)
J. Mol. Biol.
, vol.320
, pp. 369-387
-
-
Guerois, R.1
Nielsen, J.E.2
Serrano, L.3
-
23
-
-
0032553332
-
Elucidating the folding problem of alpha-helices: Local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters
-
Lacroix, E., Viguera, A.R. & Serrano, L. Elucidating the folding problem of alpha-helices: Local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters. J. Mol. Biol. 284, 173-191 (1998).
-
(1998)
J. Mol. Biol.
, vol.284
, pp. 173-191
-
-
Lacroix, E.1
Viguera, A.R.2
Serrano, L.3
-
24
-
-
0029070488
-
Folding of protein G B1 domain studied by the conformational characterization of fragments comprising its secondary structure elements
-
Blanco, F.J. & Serrano, L. Folding of protein G B1 domain studied by the conformational characterization of fragments comprising its secondary structure elements. Eur. J. Biochem. 230, 634-649 (1995).
-
(1995)
Eur. J. Biochem.
, vol.230
, pp. 634-649
-
-
Blanco, F.J.1
Serrano, L.2
-
25
-
-
0030816685
-
Mechanism of helix induction by trifluoroethanol: A framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/ water mixtures back to water
-
Luo, P. & Baldwin, R.L. Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water. Biochemistry 36, 8413-8421 (1997).
-
(1997)
Biochemistry
, vol.36
, pp. 8413-8421
-
-
Luo, P.1
Baldwin, R.L.2
-
26
-
-
0030030956
-
First-order kinetic model of Alzheimer's beta-amyloid fibril extension in vitro
-
Naiki, H. & Nakakuki, K. First-order kinetic model of Alzheimer's beta-amyloid fibril extension in vitro. Lab. Invest 74, 374-383 (1996).
-
(1996)
Lab. Invest.
, vol.74
, pp. 374-383
-
-
Naiki, H.1
Nakakuki, K.2
-
27
-
-
0016772212
-
Comparison of predicted and observed secondary structure of t4 phage lysozyme
-
Mathews, B.W. Comparison of predicted and observed secondary structure of t4 phage lysozyme. Biochim. Biophys. Acta 405, 442-451 (1975).
-
(1975)
Biochim. Biophys. Acta
, vol.405
, pp. 442-451
-
-
Mathews, B.W.1
|