-
1
-
-
0033855656
-
Review: Immunoglobulin light chain amyloidosis - The archetype of structural and pathogenic variability
-
Bellotti, V., Mangione, P., and Merlini, G. 2000. Review: Immunoglobulin light chain amyloidosis - The archetype of structural and pathogenic variability. J. Struct. Biol. 130: 280-289.
-
(2000)
J. Struct. Biol.
, vol.130
, pp. 280-289
-
-
Bellotti, V.1
Mangione, P.2
Merlini, G.3
-
2
-
-
28444454101
-
Amyloid fibril formation can proceed from different conformations of a partially unfolded protein
-
Calamai, M., Chiti, F., and Dobson, C.M. 2005. Amyloid fibril formation can proceed from different conformations of a partially unfolded protein. Biophys. J. 89: 4201-4210.
-
(2005)
Biophys. J.
, vol.89
, pp. 4201-4210
-
-
Calamai, M.1
Chiti, F.2
Dobson, C.M.3
-
3
-
-
1642452936
-
Formation of amyloid fibrils from fully reduced hen egg white lysozyme
-
Cao, A., Hu, D., and Lai, L. 2004. Formation of amyloid fibrils from fully reduced hen egg white lysozyme. Protein Sci. 13: 319-324.
-
(2004)
Protein Sci.
, vol.13
, pp. 319-324
-
-
Cao, A.1
Hu, D.2
Lai, L.3
-
4
-
-
18344363579
-
Prion disease: A deadly disease for protein misfolding
-
Chakraborty, C., Nandi, S., and Jana, S. 2005. Prion disease: A deadly disease for protein misfolding. Curr. Pharm. Biotechnol. 6: 167-177.
-
(2005)
Curr. Pharm. Biotechnol.
, vol.6
, pp. 167-177
-
-
Chakraborty, C.1
Nandi, S.2
Jana, S.3
-
5
-
-
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. 2000. Conversion of yeast phosphoglycerate kinase into amyloid-like structure. Proteins 39: 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
-
6
-
-
0033200063
-
Protein misfolding, evolution and disease
-
Dobson, C.M. 1999. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24: 329-332.
-
(1999)
Trends Biochem. Sci.
, vol.24
, pp. 329-332
-
-
Dobson, C.M.1
-
7
-
-
0347357617
-
Protein folding and misfolding
-
_. 2003. Protein folding and misfolding. Nature 426: 884-890.
-
(2003)
Nature
, vol.426
, pp. 884-890
-
-
-
8
-
-
3042673992
-
A highly amyloidogenic region of hen lysozyme
-
Frare, E., Polverino De Laureto, P., Zurdo, J., Dobson, C.M., and Fontana, A. 2004. A highly amyloidogenic region of hen lysozyme. J. Mol. Biol. 23: 1153-1165.
-
(2004)
J. Mol. Biol.
, vol.23
, pp. 1153-1165
-
-
Frare, E.1
Polverino De Laureto, P.2
Zurdo, J.3
Dobson, C.M.4
Fontana, A.5
-
9
-
-
13144259646
-
Amyloid fibril formation by an SH3 domain
-
Guijarro, J.I., Sunde, M., Jones, J.A., Campbell, I.D., and Dobson, C.M. 1998. Amyloid fibril formation by an SH3 domain. Proc. Natl. Acad. Sci. 95: 4224-4228.
-
(1998)
Proc. Natl. Acad. Sci.
, vol.95
, pp. 4224-4228
-
-
Guijarro, J.I.1
Sunde, M.2
Jones, J.A.3
Campbell, I.D.4
Dobson, C.M.5
-
10
-
-
77956935682
-
Vertebrate lysozyme
-
(ed. P.D. Boyer), Academic Press, New York
-
Imoto, T., Johnson, L.N., North, A.C.T., Philip, D.C., and Rupley, J. 1972. Vertebrate lysozyme. In The Enzymes, 3d ed., (ed. P.D. Boyer), Vol. 7, pp. 665-863. Academic Press, New York.
-
(1972)
The Enzymes, 3d Ed.
, vol.7
, pp. 665-863
-
-
Imoto, T.1
Johnson, L.N.2
North, A.C.T.3
Philip, D.C.4
Rupley, J.5
-
11
-
-
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. 2006. Amyloid formation under physiological conditions proceeds via a native-like folding intermediate. Nat. Struct. Mol. Biol. 13: 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
-
12
-
-
18244364614
-
Long-range interactions within a nonnative protein
-
Klein-Seetharaman, J., Oikawa, M., Grimshaw, S.B., Wirmer, J., Duchardt, E., Ueda, T., Imoto, T., Smith, L.J., Dobson, C.M., and Schwalbe, H. 2002. Long-range interactions within a nonnative protein. Science 295: 1719-1722.
-
(2002)
Science
, vol.295
, pp. 1719-1722
-
-
Klein-Seetharaman, J.1
Oikawa, M.2
Grimshaw, S.B.3
Wirmer, J.4
Duchardt, E.5
Ueda, T.6
Imoto, T.7
Smith, L.J.8
Dobson, C.M.9
Schwalbe, H.10
-
13
-
-
0033059275
-
Amyloid-like aggregates of a plant protein: A case of a sweet-tasting protein, monellin
-
Konno, T., Murata, K., and Nagayama, K. 1999. Amyloid-like aggregates of a plant protein: A case of a sweet-tasting protein, monellin. FEBS Lett. 454: 122-126.
-
(1999)
FEBS Lett.
, vol.454
, pp. 122-126
-
-
Konno, T.1
Murata, K.2
Nagayama, K.3
-
14
-
-
0027502784
-
Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution
-
LeVine, H. 1993. Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution. Protein Sci. 2: 404-410.
-
(1993)
Protein Sci.
, vol.2
, pp. 404-410
-
-
LeVine, H.1
-
15
-
-
0036389787
-
Mapping long-range contacts in a highly unfolded protein
-
Lietzow, M.A., Jamin, M., Jane Dyson, H.J., and Wright, P.E. 2002. Mapping long-range contacts in a highly unfolded protein. J. Mol. Biol. 322: 655-662.
-
(2002)
J. Mol. Biol.
, vol.322
, pp. 655-662
-
-
Lietzow, M.A.1
Jamin, M.2
Jane Dyson, H.J.3
Wright, P.E.4
-
16
-
-
0037059063
-
De novo designed peptide-based amyloid fibrils
-
Lopez de La Paz, M., Goldie, K., Zurdo, J., Lacroix, E., Dobson, C.M., Hoenger, A., and Serrano, L. 2002. De novo designed peptide-based amyloid fibrils. Proc. Natl. Acad. Sci. 99: 16052-16057.
-
(2002)
Proc. Natl. Acad. Sci.
, vol.99
, pp. 16052-16057
-
-
Lopez De La Paz, M.1
Goldie, K.2
Zurdo, J.3
Lacroix, E.4
Dobson, C.M.5
Hoenger, A.6
Serrano, L.7
-
17
-
-
0032991055
-
15N-labeled hen lysozyme in Pichia pastoris and identification of the site in hen lysozyme where phosphate ion binds using NMR measurements
-
15N-labeled hen lysozyme in Pichia pastoris and identification of the site in hen lysozyme where phosphate ion binds using NMR measurements. FEBS Lett. 448: 33-37.
-
(1999)
FEBS Lett.
, vol.448
, pp. 33-37
-
-
Mine, S.1
Ueda, T.2
Hashimoto, Y.3
Tanaka, Y.4
Imoto, T.5
-
18
-
-
1642488929
-
Pressure-dissociable reversible assembly of intrinsically denatured lysozyme is a precursor for amyloid fibrils
-
Niraula, T.N., Konno, T., Li, H., Yamada, H., Akasaka, K., and Tachibana, H. 2004. Pressure-dissociable reversible assembly of intrinsically denatured lysozyme is a precursor for amyloid fibrils. Proc. Natl. Acad. Sci. 101: 4089-4093.
-
(2004)
Proc. Natl. Acad. Sci.
, vol.101
, pp. 4089-4093
-
-
Niraula, T.N.1
Konno, T.2
Li, H.3
Yamada, H.4
Akasaka, K.5
Tachibana, H.6
-
19
-
-
14144254725
-
Effect of the structure of the denatured state of lysozyme on the aggregation reaction at the early stages of folding from the reduced form
-
Ohkuri, T., Shioi, S., Imoto, T., and Ueda, T. 2005. Effect of the structure of the denatured state of lysozyme on the aggregation reaction at the early stages of folding from the reduced form. J. Mol. Biol. 347: 159-168.
-
(2005)
J. Mol. Biol.
, vol.347
, pp. 159-168
-
-
Ohkuri, T.1
Shioi, S.2
Imoto, T.3
Ueda, T.4
-
20
-
-
0037165609
-
Amyloid fibrils from the mammalian protein prothymosin α
-
Pavlov, N.A., Cherny, D.I., Heim, G., Jovin, T.M., and Subramaniam, V. 2002. Amyloid fibrils from the mammalian protein prothymosin α. FEBS Lett. 517: 37-40.
-
(2002)
FEBS Lett.
, vol.517
, pp. 37-40
-
-
Pavlov, N.A.1
Cherny, D.I.2
Heim, G.3
Jovin, T.M.4
Subramaniam, V.5
-
21
-
-
0035957696
-
Amyloid fibril formation by a helical cytochrome
-
Pertinhez, T.A., Bouchard, M., Tomlinson, E.J., Wain, R., Ferguson, S.J., Dobson, C.M., and Smith, L.J. 2001. Amyloid fibril formation by a helical cytochrome. FEBS Lett. 495: 184-186.
-
(2001)
FEBS Lett.
, vol.495
, pp. 184-186
-
-
Pertinhez, T.A.1
Bouchard, M.2
Tomlinson, E.J.3
Wain, R.4
Ferguson, S.J.5
Dobson, C.M.6
Smith, L.J.7
-
22
-
-
0030759665
-
Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea
-
Schwalbe, H., Fiebig, K.M., Buck, M., Jones, J.A., Grimshaw, S.B., Spencer, A., Glaser, S.J., Smith, L.J., and Dobson, C.M. 1997. Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea. Biochemistry 36: 8977-8991.
-
(1997)
Biochemistry
, vol.36
, pp. 8977-8991
-
-
Schwalbe, H.1
Fiebig, K.M.2
Buck, M.3
Jones, J.A.4
Grimshaw, S.B.5
Spencer, A.6
Glaser, S.J.7
Smith, L.J.8
Dobson, C.M.9
-
23
-
-
0035919635
-
Persistence of native-like topology in a denatured protein in 8 M urea
-
Shortle, D. and Ackerman, M.S. 2001. Persistence of native-like topology in a denatured protein in 8 M urea. Science 293: 487-489.
-
(2001)
Science
, vol.293
, pp. 487-489
-
-
Shortle, D.1
Ackerman, M.S.2
-
24
-
-
0031592945
-
Common core structure of amyloid fibrils by synchrotron X-ray diffraction
-
Sunde, M., Serpell, L.C., Bartlam, M., Fraser, P.E., Pepys, M.B., and Blake, C.C. 1997. Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J. Mol. Biol. 273: 729-739.
-
(1997)
J. Mol. Biol.
, vol.273
, pp. 729-739
-
-
Sunde, M.1
Serpell, L.C.2
Bartlam, M.3
Fraser, P.E.4
Pepys, M.B.5
Blake, C.C.6
-
25
-
-
0025221747
-
Effect of chemical modifications of tryptophan residues on the folding of reduced hen egg-white lysozyme
-
Ueda, T., Yamada, H., Aoki, H., and Imoto, T. 1990. Effect of chemical modifications of tryptophan residues on the folding of reduced hen egg-white lysozyme. J. Biochem. 108: 886-892.
-
(1990)
J. Biochem.
, vol.108
, pp. 886-892
-
-
Ueda, T.1
Yamada, H.2
Aoki, H.3
Imoto, T.4
-
26
-
-
0028882318
-
Kinetically trapped structure in the renaturation of reduced oxindolealanine 62 lysozyme
-
Ueda, T., Abe, Y., Ohkuri, T., Kawano, K., Terada, Y., and Imoto, T. 1995. Kinetically trapped structure in the renaturation of reduced oxindolealanine 62 lysozyme. Biochemistry 34: 16178-16185.
-
(1995)
Biochemistry
, vol.34
, pp. 16178-16185
-
-
Ueda, T.1
Abe, Y.2
Ohkuri, T.3
Kawano, K.4
Terada, Y.5
Imoto, T.6
-
27
-
-
0030296338
-
Identification of the peptide region that folds native conformation in the early stage of the renaturation of reduced lysozyme
-
Ueda, T., Ohkuri, T., and Imoto, T. 1996. Identification of the peptide region that folds native conformation in the early stage of the renaturation of reduced lysozyme. Biochem. Biophys. Res. Commun. 228: 203-208.
-
(1996)
Biochem. Biophys. Res. Commun.
, vol.228
, pp. 203-208
-
-
Ueda, T.1
Ohkuri, T.2
Imoto, T.3
-
28
-
-
0141677840
-
A protein-chameleon: Conformational plasticity of α-synuclein, a disordered protein involved in neurodegenerative disorders
-
Uversky, V.N. 2003. A protein-chameleon: Conformational plasticity of α-synuclein, a disordered protein involved in neurodegenerative disorders. J. Biomol. Struct. Dyn. 21: 211-234.
-
(2003)
J. Biomol. Struct. Dyn.
, vol.21
, pp. 211-234
-
-
Uversky, V.N.1
-
29
-
-
2342569618
-
Conformational constraints for amyloid fibrillation: The importance of being unfolded
-
Uversky, V.N. and Fink, A.L. 2004. Conformational constraints for amyloid fibrillation: The importance of being unfolded. Biochim. Biophys. Acta 1698: 131-153.
-
(2004)
Biochim. Biophys. Acta
, vol.1698
, pp. 131-153
-
-
Uversky, V.N.1
Fink, A.L.2
-
30
-
-
19944414648
-
Amyloid associated proteins in Alzheimer's and prion disease
-
Veerhuis, R., Boshuizen, R.S., and Familian, A. 2005. Amyloid associated proteins in Alzheimer's and prion disease. Curr. Drug Targets CNS Neurol. Disord. 4: 235-248.
-
(2005)
Curr. Drug Targets CNS Neurol. Disord.
, vol.4
, pp. 235-248
-
-
Veerhuis, R.1
Boshuizen, R.S.2
Familian, A.3
-
31
-
-
0027482556
-
NMR relaxation and protein mobility
-
Wagner, G. 1993. NMR relaxation and protein mobility. Curr. Opin. Struct. Biol. 3: 748-754.
-
(1993)
Curr. Opin. Struct. Biol.
, vol.3
, pp. 748-754
-
-
Wagner, G.1
-
32
-
-
8844259690
-
Modulation of compactness and long-range interactions of unfolded lysozyme by single point mutations
-
Wirmer, J., Schlorb, C., Klein-Seetharaman, J., Hirano, R., Ueda, T., Imoto, T., and Schwalbe, H. 2004. Modulation of compactness and long-range interactions of unfolded lysozyme by single point mutations. Angew. Chem. Int. Ed. Engl. 43: 5780-5785.
-
(2004)
Angew. Chem. Int. Ed. Engl.
, vol.43
, pp. 5780-5785
-
-
Wirmer, J.1
Schlorb, C.2
Klein-Seetharaman, J.3
Hirano, R.4
Ueda, T.5
Imoto, T.6
Schwalbe, H.7
-
33
-
-
0034646397
-
The process of amyloid-like fibril formation by methionine aminopeptidase from a hyperthermophile Pyrococcus furiosus
-
Yutani, K., Takayama, G., Goda, S., Yamagata, Y., Maki, S., Namba, K., Tsunasawa, S., and Ogasahara, K. 2000. The process of amyloid-like fibril formation by methionine aminopeptidase from a hyperthermophile Pyrococcus furiosus. Biochemistry 39: 2769-2777.
-
(2000)
Biochemistry
, vol.39
, pp. 2769-2777
-
-
Yutani, K.1
Takayama, G.2
Goda, S.3
Yamagata, Y.4
Maki, S.5
Namba, K.6
Tsunasawa, S.7
Ogasahara, K.8
|