-
1
-
-
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
-
2
-
-
0030801746
-
The structure of amyloid fibrils by electron microscopy and X-ray diffraction
-
Sunde M., and Blake C.C. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv. Protein Chem. 50 (1997) 123-159
-
(1997)
Adv. Protein Chem.
, vol.50
, pp. 123-159
-
-
Sunde, M.1
Blake, C.C.2
-
4
-
-
11144222595
-
The binding of thioflavin-T to amyloid fibrils: localisation and implications
-
Krebs M.R., Bromley E.H., and Donald A.M. The binding of thioflavin-T to amyloid fibrils: localisation and implications. J. Struct. Biol. 149 (2005) 30-37
-
(2005)
J. Struct. Biol.
, vol.149
, pp. 30-37
-
-
Krebs, M.R.1
Bromley, E.H.2
Donald, A.M.3
-
5
-
-
3343003514
-
Techniques to study amyloid fibril formation in vitro
-
Nilsson M.R. Techniques to study amyloid fibril formation in vitro. Methods 34 (2004) 151-160
-
(2004)
Methods
, vol.34
, pp. 151-160
-
-
Nilsson, M.R.1
-
6
-
-
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. U. S. A. 96 (1999) 3590-3594
-
(1999)
Proc. Natl. Acad. Sci. U. S. A.
, 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
-
7
-
-
13144259646
-
Amyloid fibril formation by an SH3 domain
-
Guijarro J.I., Sunde M., Jones J.A., Campbell I.D., and Dobson C.M. Amyloid fibril formation by an SH3 domain. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 4224-4228
-
(1998)
Proc. Natl. Acad. Sci. U. S. A.
, vol.95
, pp. 4224-4228
-
-
Guijarro, J.I.1
Sunde, M.2
Jones, J.A.3
Campbell, I.D.4
Dobson, C.M.5
-
8
-
-
0033814617
-
Protein engineering as a strategy to avoid formation of amyloid fibrils
-
Villegas V., Zurdo J., Filimonov V.V., Avilés F.X., Dobson C.M., and Serrano L. Protein engineering as a strategy to avoid formation of amyloid fibrils. Protein Sci. 9 (2000) 1700-1708
-
(2000)
Protein Sci.
, vol.9
, pp. 1700-1708
-
-
Villegas, V.1
Zurdo, J.2
Filimonov, V.V.3
Avilés, F.X.4
Dobson, C.M.5
Serrano, L.6
-
9
-
-
9144264986
-
Polyglutamine expansion in ataxin-3 does not affect protein stability: implications for misfolding and disease
-
Chow M.K., Ellisdon A.M., Cabrita L.D., and Bottomley S.P. Polyglutamine expansion in ataxin-3 does not affect protein stability: implications for misfolding and disease. J. Biol. Chem. 279 (2004) 47643-47651
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 47643-47651
-
-
Chow, M.K.1
Ellisdon, A.M.2
Cabrita, L.D.3
Bottomley, S.P.4
-
10
-
-
3342902033
-
Modulation of S6 fibrillation by unfolding rates and gatekeeper residues
-
Pedersen J.S., Christensen G., and Otzen D.E. Modulation of S6 fibrillation by unfolding rates and gatekeeper residues. J. Mol. Biol. 341 (2004) 575-588
-
(2004)
J. Mol. Biol.
, vol.341
, pp. 575-588
-
-
Pedersen, J.S.1
Christensen, G.2
Otzen, D.E.3
-
11
-
-
1842790837
-
Aggregation of the Acylphosphatase from Sulfolobus solfataricus: the folded and partially unfolded states can both be precursors for amyloid formation
-
Plakoutsi G., Taddei N., Stefani M., and Chiti F. Aggregation of the Acylphosphatase from Sulfolobus solfataricus: the folded and partially unfolded states can both be precursors for amyloid formation. J. Biol. Chem. 279 (2004) 14111-14119
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 14111-14119
-
-
Plakoutsi, G.1
Taddei, N.2
Stefani, M.3
Chiti, F.4
-
12
-
-
23444447864
-
Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates
-
Plakoutsi G., Bemporad F., Calamai M., Taddei N., Dobson C.M., and Chiti F. Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates. J. Mol. Biol. 351 (2005) 910-922
-
(2005)
J. Mol. Biol.
, vol.351
, pp. 910-922
-
-
Plakoutsi, G.1
Bemporad, F.2
Calamai, M.3
Taddei, N.4
Dobson, C.M.5
Chiti, F.6
-
13
-
-
33744905543
-
Exploring the mechanism of formation of native-like and precursor amyloid oligomers for the native acylphosphatase from Sulfolobus solfataricus
-
Plakoutsi G., Bemporad F., Monti M., Pagnozzi D., Pucci P., and Chiti F. Exploring the mechanism of formation of native-like and precursor amyloid oligomers for the native acylphosphatase from Sulfolobus solfataricus. Structure 14 (2006) 993-1001
-
(2006)
Structure
, vol.14
, pp. 993-1001
-
-
Plakoutsi, G.1
Bemporad, F.2
Monti, M.3
Pagnozzi, D.4
Pucci, P.5
Chiti, F.6
-
14
-
-
30344478570
-
Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus
-
Corazza A., Rosano C., Pagano K., Alverdi V., Esposito G., Capanni C., Bemporad F., Plakoutsi G., Stefani M., Chiti F., Zuccotti S., Bolognesi M., and Viglino P. Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus. Proteins 62 (2006) 64-79
-
(2006)
Proteins
, vol.62
, pp. 64-79
-
-
Corazza, A.1
Rosano, C.2
Pagano, K.3
Alverdi, V.4
Esposito, G.5
Capanni, C.6
Bemporad, F.7
Plakoutsi, G.8
Stefani, M.9
Chiti, F.10
Zuccotti, S.11
Bolognesi, M.12
Viglino, P.13
-
15
-
-
24344505390
-
Crystal structure and structural stability of acylphosphatase from hyperthermophilic archaeon Pyrococcus horikoshii OT3
-
Miyazono K., Sawano Y., and Tanokura M. Crystal structure and structural stability of acylphosphatase from hyperthermophilic archaeon Pyrococcus horikoshii OT3. Proteins 61 (2005) 196-205
-
(2005)
Proteins
, vol.61
, pp. 196-205
-
-
Miyazono, K.1
Sawano, Y.2
Tanokura, M.3
-
16
-
-
33751002965
-
NMR solution structure of the acylphosphatase from Escherichia coli
-
Pagano K., Ramazzotti M., Viglino P., Esposito G., Degl'Innocenti D., Taddei N., and Corazza A. NMR solution structure of the acylphosphatase from Escherichia coli. J. Biomol. NMR 36 (2006) 199-204
-
(2006)
J. Biomol. NMR
, vol.36
, pp. 199-204
-
-
Pagano, K.1
Ramazzotti, M.2
Viglino, P.3
Esposito, G.4
Degl'Innocenti, D.5
Taddei, N.6
Corazza, A.7
-
17
-
-
0026522991
-
Three-dimensional structure of acylphosphatase. Refinement and structure analysis
-
Pastore A., Saudek V., Ramponi G., and Williams R.J. Three-dimensional structure of acylphosphatase. Refinement and structure analysis. J. Mol. Biol. 224 (1992) 427-440
-
(1992)
J. Mol. Biol.
, vol.224
, pp. 427-440
-
-
Pastore, A.1
Saudek, V.2
Ramponi, G.3
Williams, R.J.4
-
18
-
-
0031568309
-
Crystal structure of common type acylphosphatase from bovine testis
-
Thunnissen M.M., Taddei N., Liguri G., Ramponi G., and Nordlund P. Crystal structure of common type acylphosphatase from bovine testis. Structure 5 (1997) 69-79
-
(1997)
Structure
, vol.5
, pp. 69-79
-
-
Thunnissen, M.M.1
Taddei, N.2
Liguri, G.3
Ramponi, G.4
Nordlund, P.5
-
19
-
-
14644399127
-
Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphatase
-
Zuccotti S., Rosano C., Ramazzotti M., Degl'Innocenti D., Stefani M., Manao G., and Bolognesi M. Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphatase. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 1177-1179
-
(2004)
Acta Crystallogr. D Biol. Crystallogr.
, vol.60
, pp. 1177-1179
-
-
Zuccotti, S.1
Rosano, C.2
Ramazzotti, M.3
Degl'Innocenti, D.4
Stefani, M.5
Manao, G.6
Bolognesi, M.7
-
20
-
-
41549161190
-
The degree of structural protection at the edge b-strands determines the pathway of amyloid formation in globular proteins
-
Soldi G., Bemporad F., and Chiti F. The degree of structural protection at the edge b-strands determines the pathway of amyloid formation in globular proteins. J. Am. Chem. Soc. 130 (2008) 4295-4302
-
(2008)
J. Am. Chem. Soc.
, vol.130
, pp. 4295-4302
-
-
Soldi, G.1
Bemporad, F.2
Chiti, F.3
-
21
-
-
0017123760
-
A new synthesis of benzoyl phosphate: a substrate for acyl phosphatase assay
-
Camici G., Manao G., Cappugi G., and Ramponi G. A new synthesis of benzoyl phosphate: a substrate for acyl phosphatase assay. Experientia 32 (1976) 535-536
-
(1976)
Experientia
, vol.32
, pp. 535-536
-
-
Camici, G.1
Manao, G.2
Cappugi, G.3
Ramponi, G.4
-
22
-
-
3142745308
-
Studying the folding process of the acylphosphatase from Sulfolobus solfataricus. A comparative analysis with other proteins from the same superfamily
-
Bemporad F., Capanni C., Calamai M., Tutino M.L., Stefani M., and Chiti F. Studying the folding process of the acylphosphatase from Sulfolobus solfataricus. A comparative analysis with other proteins from the same superfamily. Biochemistry 43 (2004) 9116-9126
-
(2004)
Biochemistry
, vol.43
, pp. 9116-9126
-
-
Bemporad, F.1
Capanni, C.2
Calamai, M.3
Tutino, M.L.4
Stefani, M.5
Chiti, F.6
-
23
-
-
0023697408
-
Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
-
Santoro M.M., and Bolen D.W. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27 (1988) 8063-8068
-
(1988)
Biochemistry
, vol.27
, pp. 8063-8068
-
-
Santoro, M.M.1
Bolen, D.W.2
-
25
-
-
0030814166
-
Insights into acylphosphatase structure and catalytic mechanism
-
Stefani M., Taddei N., and Ramponi G. Insights into acylphosphatase structure and catalytic mechanism. Cell. Mol. Life Sci. 53 (1997) 141-151
-
(1997)
Cell. Mol. Life Sci.
, vol.53
, pp. 141-151
-
-
Stefani, M.1
Taddei, N.2
Ramponi, G.3
-
26
-
-
0028820703
-
Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding
-
Myers J.K., Pace C.N., and Scholtz J.M. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4 (1995) 2138-2148
-
(1995)
Protein Sci.
, vol.4
, pp. 2138-2148
-
-
Myers, J.K.1
Pace, C.N.2
Scholtz, J.M.3
-
27
-
-
0038219626
-
Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina
-
Balguerie A., Dos Reis S., Ritter C., Chaignepain S., Coulary-Salin B., Forge V., Bathany K., Lascu I., Schmitter J.M., Riek R., and Saupe S.J. Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina. EMBO J. 22 (2003) 2071-2081
-
(2003)
EMBO J.
, vol.22
, pp. 2071-2081
-
-
Balguerie, A.1
Dos Reis, S.2
Ritter, C.3
Chaignepain, S.4
Coulary-Salin, B.5
Forge, V.6
Bathany, K.7
Lascu, I.8
Schmitter, J.M.9
Riek, R.10
Saupe, S.J.11
-
28
-
-
0242353209
-
Architecture of Ure2p prion filaments: the N-terminal domains form a central core fiber
-
Baxa U., Taylor K.L., Wall J.S., Simon M.N., Cheng N., Wickner R.B., and Steven A.C. Architecture of Ure2p prion filaments: the N-terminal domains form a central core fiber. J. Biol. Chem. 278 (2003) 43717-43727
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 43717-43727
-
-
Baxa, U.1
Taylor, K.L.2
Wall, J.S.3
Simon, M.N.4
Cheng, N.5
Wickner, R.B.6
Steven, A.C.7
-
29
-
-
0030712145
-
Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae
-
Glover J.R., Kowal A.S., Schirmer E.C., Patino M.M., Liu J.J., and Lindquist S. Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell 89 (1997) 811-819
-
(1997)
Cell
, vol.89
, pp. 811-819
-
-
Glover, J.R.1
Kowal, A.S.2
Schirmer, E.C.3
Patino, M.M.4
Liu, J.J.5
Lindquist, S.6
-
30
-
-
0037124337
-
The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro
-
Bousset L., Thomson N.H., Radford S.E., and Melki R. The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro. EMBO J. 17 (2002) 2903-2911
-
(2002)
EMBO J.
, vol.17
, pp. 2903-2911
-
-
Bousset, L.1
Thomson, N.H.2
Radford, S.E.3
Melki, R.4
-
31
-
-
27744566676
-
Structure of the prion Ure2p in protein fibrils assembled in vitro
-
Fay N., Redeker V., Savistchenko J., Dubois S., Bousset L., and Melki R. Structure of the prion Ure2p in protein fibrils assembled in vitro. J. Biol. Chem. 280 (2004) 37149-37158
-
(2004)
J. Biol. Chem.
, vol.280
, pp. 37149-37158
-
-
Fay, N.1
Redeker, V.2
Savistchenko, J.3
Dubois, S.4
Bousset, L.5
Melki, R.6
-
32
-
-
34249689651
-
Hsp40 interacts directly with the native state of the yeast prion protein Ure2 and inhibits formation of amyloid-like fibrils
-
Lian H., Zhang H., Zhang Z., Loovers H.M., Jones G.W., Rowling P.J.E., Itzhaki L.S., Zhou J., and Perrett S. Hsp40 interacts directly with the native state of the yeast prion protein Ure2 and inhibits formation of amyloid-like fibrils. J. Biol. Chem. 282 (2007) 11931-11940
-
(2007)
J. Biol. Chem.
, vol.282
, pp. 11931-11940
-
-
Lian, H.1
Zhang, H.2
Zhang, Z.3
Loovers, H.M.4
Jones, G.W.5
Rowling, P.J.E.6
Itzhaki, L.S.7
Zhou, J.8
Perrett, S.9
-
33
-
-
0037022563
-
Natural b-sheet proteins use negative design to avoid edge-to-edge aggregation
-
Richardson J.S., and Richardson D.C. Natural b-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 2754-2759
-
(2002)
Proc. Natl. Acad. Sci. U. S. A.
, vol.99
, pp. 2754-2759
-
-
Richardson, J.S.1
Richardson, D.C.2
-
34
-
-
33745889333
-
Folding of Cu/Zn superoxide dismutase suggests structural hotspots for gain of neurotoxic function in ALS: parallels to precursors in amyloid disease
-
Nordlund A., and Oliveberg M. Folding of Cu/Zn superoxide dismutase suggests structural hotspots for gain of neurotoxic function in ALS: parallels to precursors in amyloid disease. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 10218-10223
-
(2006)
Proc. Natl. Acad. Sci. U. S. A.
, vol.103
, pp. 10218-10223
-
-
Nordlund, A.1
Oliveberg, M.2
-
35
-
-
28444464509
-
Amyloid formation of a protein in the absence of initial unfolding and destabilization of the native state
-
Soldi G., Bemporad F., Torrassa S., Relini A., Ramazzotti M., Taddei N., and Chiti F. Amyloid formation of a protein in the absence of initial unfolding and destabilization of the native state. Biophys. J. 89 (2005) 4234-4244
-
(2005)
Biophys. J.
, vol.89
, pp. 4234-4244
-
-
Soldi, G.1
Bemporad, F.2
Torrassa, S.3
Relini, A.4
Ramazzotti, M.5
Taddei, N.6
Chiti, F.7
|