-
1
-
-
0031932169
-
Protein aggregation: Folding aggregates, inclusion bodies and amyloid
-
Fink A. Protein aggregation: folding aggregates, inclusion bodies and amyloid. Fold Des. 3:1998;R9-R23.
-
(1998)
Fold Des.
, vol.3
-
-
Fink, A.1
-
2
-
-
0037317334
-
Protein folding and disease: A view from the first Horizon Symposium
-
Dobson C.M. Protein folding and disease: a view from the first Horizon Symposium. Nature Rev. Drug Discov. 2:2003;154-160.
-
(2003)
Nature Rev. Drug Discov.
, vol.2
, pp. 154-160
-
-
Dobson, C.M.1
-
3
-
-
0029981197
-
Alternative conformations of amyloidogenic proteins govern their behavior
-
Kelly J.W. Alternative conformations of amyloidogenic proteins govern their behavior. Curr. Opin. Struct. Biol. 6:1996;11-17.
-
(1996)
Curr. Opin. Struct. Biol.
, vol.6
, pp. 11-17
-
-
Kelly, J.W.1
-
4
-
-
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
-
5
-
-
0030841343
-
Conformational diseases
-
Carrell R.W., Lomas D.A. Conformational diseases. Lancet. 350:1997;134-138.
-
(1997)
Lancet
, vol.350
, pp. 134-138
-
-
Carrell, R.W.1
Lomas, D.A.2
-
6
-
-
0035237310
-
Protein folding and its links with human disease
-
Dobson C.M. Protein folding and its links with human disease. Biochem. Soc. Symp. 68:2001;1-26.
-
(2001)
Biochem. Soc. Symp.
, vol.68
, pp. 1-26
-
-
Dobson, C.M.1
-
7
-
-
0035827318
-
Protein misfolding and disease: Protein refolding and therapy
-
Soto C. Protein misfolding and disease: protein refolding and therapy. FEBS Letters. 498:2001;204-207.
-
(2001)
FEBS Letters
, vol.498
, pp. 204-207
-
-
Soto, C.1
-
8
-
-
0030801746
-
The structure of amyloid fibrils by electron microscopy and X-ray diffraction
-
Sunde M., Blake C.C. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Advan. Protein Chem. 50:1997;123-159.
-
(1997)
Advan. Protein Chem.
, vol.50
, pp. 123-159
-
-
Sunde, M.1
Blake, C.C.2
-
9
-
-
13144259646
-
Amyloid fibril formation by an SH3 domain
-
Guijarro J.I., Sunde M., Jones J.A., Campbell I.D., Dobson C.M. Amyloid fibril formation by an SH3 domain. Proc. Natl Acad. Sci. USA. 95:1998;4224-4228.
-
(1998)
Proc. Natl Acad. Sci. USA
, 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
-
-
0033616575
-
Designing conditions for in vitro formation of amyloid protofilaments and fibrils
-
Chiti F., Webster P., Taddei N., Clark A., Stefani M., Ramponi G., 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
-
11
-
-
0033200063
-
Protein misfolding, evolution and disease
-
Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24:1999;329-332.
-
(1999)
Trends Biochem. Sci.
, vol.24
, pp. 329-332
-
-
Dobson, C.M.1
-
12
-
-
0026484261
-
SH2 and SH3 domains: From structure to function
-
Pawson T., Gish G.D. SH2 and SH3 domains: from structure to function. Cell. 71:1992;359-362.
-
(1992)
Cell
, vol.71
, pp. 359-362
-
-
Pawson, T.1
Gish, G.D.2
-
13
-
-
0027191192
-
Solution structure and ligand-binding site of the SH3 domain of the p85α subunit of phosphatidylinositol 3-kinase
-
Booker G.W., Gout I., Downing A.K., Driscoll P.C., Boyd J., Waterfield M.D., Campbell I.D. Solution structure and ligand-binding site of the SH3 domain of the p85α subunit of phosphatidylinositol 3-kinase. Cell. 73:1993;813-822.
-
(1993)
Cell
, vol.73
, pp. 813-822
-
-
Booker, G.W.1
Gout, I.2
Downing, A.K.3
Driscoll, P.C.4
Boyd, J.5
Waterfield, M.D.6
Campbell, I.D.7
-
14
-
-
0026437577
-
Crystal structure of a Src-homology 3 (SH3) domain
-
Musacchio A., Noble M., Paupit R., Wierenga R., Saraste M. Crystal structure of a Src-homology 3 (SH3) domain. Nature. 359:1992;851-855.
-
(1992)
Nature
, vol.359
, pp. 851-855
-
-
Musacchio, A.1
Noble, M.2
Paupit, R.3
Wierenga, R.4
Saraste, M.5
-
15
-
-
0027102571
-
Solution structure of the SH3 domain of Src and identification of its ligand binding site
-
Yu H., Rosin M.K., Shin T.B., Seidel-Duggan C., Brugge J.S., Schreiver S.L. Solution structure of the SH3 domain of Src and identification of its ligand binding site. Science. 258:1992;1655-1668.
-
(1992)
Science
, vol.258
, pp. 1655-1668
-
-
Yu, H.1
Rosin, M.K.2
Shin, T.B.3
Seidel-Duggan, C.4
Brugge, J.S.5
Schreiver, S.L.6
-
16
-
-
0035839035
-
Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain
-
Zurdo J., Guijarro J.I., Jimenez J.L., Saibil H.R., Dobson C.M. Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain. J. Mol. Biol. 311:2001;325-340.
-
(2001)
J. Mol. Biol.
, vol.311
, pp. 325-340
-
-
Zurdo, J.1
Guijarro, J.I.2
Jimenez, J.L.3
Saibil, H.R.4
Dobson, C.M.5
-
17
-
-
0034834580
-
Preparation and characterization of purified amyloid fibrils
-
Zurdo J., Guijarro J.I., Dobson C.M. Preparation and characterization of purified amyloid fibrils. J. Am. Chem. Soc. 123:2001;8141-8142.
-
(2001)
J. Am. Chem. Soc.
, vol.123
, pp. 8141-8142
-
-
Zurdo, J.1
Guijarro, J.I.2
Dobson, C.M.3
-
18
-
-
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., Lansbury P.T. Jr. 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 P.T., Jr.2
-
19
-
-
0042847751
-
Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
-
Jiménez J.L., Guijarro J.I., Orlova E., Zurdo J., Dobson C.M., Sunde M., Saibil H.R. Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J. 18:1999;815-821.
-
(1999)
EMBO J.
, vol.18
, pp. 815-821
-
-
Jiménez, J.L.1
Guijarro, J.I.2
Orlova, E.3
Zurdo, J.4
Dobson, C.M.5
Sunde, M.6
Saibil, H.R.7
-
20
-
-
0016287131
-
Selective staining as a function of amyloid composition and structure: Histochemical analysis of the alkaline Congo Red, standardized toluidine blue and iodine methods
-
Cooper J.H. Selective staining as a function of amyloid composition and structure: histochemical analysis of the alkaline Congo Red, standardized toluidine blue and iodine methods. Lab. Invest. 31:1974;232-238.
-
(1974)
Lab. Invest.
, vol.31
, pp. 232-238
-
-
Cooper, J.H.1
-
21
-
-
0030623527
-
Probing the partly folded states of proteins by limited proteolysis
-
Fontana A., Polverino de Laureto P., De Filippis V., Scaramella E., Zambonin M. Probing the partly folded states of proteins by limited proteolysis. Fold Des. 2:1997;R17-R28.
-
(1997)
Fold Des.
, vol.2
-
-
Fontana, A.1
Polverino De Laureto, P.2
De Filippis, V.3
Scaramella, E.4
Zambonin, M.5
-
22
-
-
0000076530
-
Limited proteolysis in the study of protein conformation
-
E.E. Sterchi, & W. Stöcker. Heidelberg: Springer
-
Fontana A., Polverino de Laureto P., De Filippis V., Scaramella E., Zambonin M. Limited proteolysis in the study of protein conformation. Sterchi E.E., Stöcker W. Proteolytic Enzymes: Tools and Targets. 1999;257-284 Springer, Heidelberg.
-
(1999)
Proteolytic Enzymes: Tools and Targets
, pp. 257-284
-
-
Fontana, A.1
Polverino De Laureto, P.2
De Filippis, V.3
Scaramella, E.4
Zambonin, M.5
-
23
-
-
0034826545
-
Stepwise proteolytic removal of the β-subdomain in α-lactalbumin. The protein remains folded and can form the molten globule in acid solution
-
Polverino de Laureto P., Vinante D., Scaramella E., Frare E., Fontana A. Stepwise proteolytic removal of the β-subdomain in α-lactalbumin. The protein remains folded and can form the molten globule in acid solution. Eur. J. Biochem. 268:2001;4324-4633.
-
(2001)
Eur. J. Biochem.
, vol.268
, pp. 4324-4633
-
-
Polverino De Laureto, P.1
Vinante, D.2
Scaramella, E.3
Frare, E.4
Fontana, A.5
-
24
-
-
0037110569
-
The molten globule of bovine α-lactalbumin at neutral pH induced by heat, trifluoroethanol and oleic acid: A comparative analysis by circular dichroism spectroscopy and limited proteolysis
-
Polverino de Laureto P., Frare E., Gottardo R., Fontana A. The molten globule of bovine α-lactalbumin at neutral pH induced by heat, trifluoroethanol and oleic acid: a comparative analysis by circular dichroism spectroscopy and limited proteolysis. Proteins: Struct. Funct. Genet. 49:2002;385-397.
-
(2002)
Proteins: Struct. Funct. Genet.
, vol.49
, pp. 385-397
-
-
Polverino De Laureto, P.1
Frare, E.2
Gottardo, R.3
Fontana, A.4
-
25
-
-
0036891687
-
Partly folded states of members of the lysozyme/lactalbumin superfamily: A comparative study by circular dichroism spectroscopy and limited proteolysis
-
Polverino de Laureto P., Frare E., Gottardo R., Van Dael H., Fontana A. Partly folded states of members of the lysozyme/lactalbumin superfamily: a comparative study by circular dichroism spectroscopy and limited proteolysis. Protein Sci. 11:2002;2932-2946.
-
(2002)
Protein Sci.
, vol.11
, pp. 2932-2946
-
-
Polverino De Laureto, P.1
Frare, E.2
Gottardo, R.3
Van Dael, H.4
Fontana, A.5
-
26
-
-
0023055086
-
Correlation between sites of limited proteolysis and segmental mobility in thermolysin
-
Fontana A., Fassina G., Vita C., Dalzoppo D., Zamai M., Zambonin M. Correlation between sites of limited proteolysis and segmental mobility in thermolysin. Biochemistry. 25:1986;1847-1851.
-
(1986)
Biochemistry
, vol.25
, pp. 1847-1851
-
-
Fontana, A.1
Fassina, G.2
Vita, C.3
Dalzoppo, D.4
Zamai, M.5
Zambonin, M.6
-
27
-
-
0032698757
-
Limited proteolysis of bovine α-lactalbumin: Isolation and characterization of protein domains
-
Polverino de Laureto P., Scaramella E., Frigo M., Gefter-Wondrich F., De Filippis V., Zambonin M., Fontana A. Limited proteolysis of bovine α-lactalbumin: isolation and characterization of protein domains. Protein Sci. 8:1999;2290-2303.
-
(1999)
Protein Sci.
, vol.8
, pp. 2290-2303
-
-
Polverino De Laureto, P.1
Scaramella, E.2
Frigo, M.3
Gefter-Wondrich, F.4
De Filippis, V.5
Zambonin, M.6
Fontana, A.7
-
28
-
-
0014723020
-
The specificity and mechanism of pepsin action
-
Fruton J.S. The specificity and mechanism of pepsin action. Advan. Enzymol. 33:1970;401-443.
-
(1970)
Advan. Enzymol.
, vol.33
, pp. 401-443
-
-
Fruton, J.S.1
-
29
-
-
0021415850
-
The synthesis, purification, and evaluation of a chromophoric substrate for pepsin and other aspartyl proteases: Design of a substrate based on subsite preferences
-
Dunn B.M., Kammermann B., McCurry K.R. The synthesis, purification, and evaluation of a chromophoric substrate for pepsin and other aspartyl proteases: design of a substrate based on subsite preferences. Anal. Biochem. 138:1984;68-73.
-
(1984)
Anal. Biochem.
, vol.138
, pp. 68-73
-
-
Dunn, B.M.1
Kammermann, B.2
McCurry, K.R.3
-
30
-
-
0027502784
-
Thioflavine-T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution
-
LeVine H. Thioflavine-T interaction with synthetic Alzheimer's disease β-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2:1993;404-410.
-
(1993)
Protein Sci.
, vol.2
, pp. 404-410
-
-
LeVine, H.1
-
31
-
-
0032849874
-
Quantification of β-sheet amyloid fibril structures with thioflavin-T
-
LeVine H. Quantification of β-sheet amyloid fibril structures with thioflavin-T. Methods Enzymol. 309:1999;275-285.
-
(1999)
Methods Enzymol.
, vol.309
, pp. 275-285
-
-
LeVine, H.1
-
32
-
-
0031444010
-
Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein
-
Harper J.D., Lieber C.M., Lansbury P.T. Jr. Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein. Chem. Biol. 4:1997;951-959.
-
(1997)
Chem. Biol.
, vol.4
, pp. 951-959
-
-
Harper, J.D.1
Lieber, C.M.2
Lansbury P.T., Jr.3
-
33
-
-
0033520461
-
Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates
-
Walsh D.M., Hartley D.M., Kusumoto Y., Fezoui Y., Condron M.M., Lomakin A., et al. Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. J. Biol. Chem. 274:1999;25945-25952.
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 25945-25952
-
-
Walsh, D.M.1
Hartley, D.M.2
Kusumoto, Y.3
Fezoui, Y.4
Condron, M.M.5
Lomakin, A.6
-
34
-
-
0034646391
-
Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid
-
Conway K.A., Harper J.D., Lansbury P.T. Jr. Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid. Biochemistry. 39:2000;2552-2563.
-
(2000)
Biochemistry
, vol.39
, pp. 2552-2563
-
-
Conway, K.A.1
Harper, J.D.2
Lansbury P.T., Jr.3
-
35
-
-
0028464669
-
SH3 domains: Molecular "velcro"
-
Morton C.J., Campbell I.D. SH3 domains: molecular "velcro" Curr. Biol. 4:1994;615-617.
-
(1994)
Curr. Biol.
, vol.4
, pp. 615-617
-
-
Morton, C.J.1
Campbell, I.D.2
-
36
-
-
0036411969
-
Insights into the origin of the tendency of the PI3-SH3 domain to form amyloid fibrils
-
Ventura S., Lacroix E., Serrano L. Insights into the origin of the tendency of the PI3-SH3 domain to form amyloid fibrils. J. Mol. Biol. 322:2002;1147-1158.
-
(2002)
J. Mol. Biol.
, vol.322
, pp. 1147-1158
-
-
Ventura, S.1
Lacroix, E.2
Serrano, L.3
-
37
-
-
0035800097
-
Vesicle permeabilization by protofibrillar alpha-synuclein: Implications for the pathogenesis and treatment of Parkinson's disease
-
Volles M.J., Lee S.J., Rochet J.C., Shtilerman M.D., Ding T.T., Kessler J.C., Lansbury P.T. Jr. Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease. Biochemistry. 40:2001;7812-7819.
-
(2001)
Biochemistry
, vol.40
, pp. 7812-7819
-
-
Volles, M.J.1
Lee, S.J.2
Rochet, J.C.3
Shtilerman, M.D.4
Ding, T.T.5
Kessler, J.C.6
Lansbury P.T., Jr.7
-
38
-
-
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
-
39
-
-
0037130174
-
Neurodegenerative disease: Amyloid pores from pathogenic mutations
-
Lashuel H.A., Hartley D., Petre B.M., Walz T., Lansbury P.T. Jr. Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature. 418:2002;291.
-
(2002)
Nature
, vol.418
, pp. 291
-
-
Lashuel, H.A.1
Hartley, D.2
Petre, B.M.3
Walz, T.4
Lansbury P.T., Jr.5
-
40
-
-
0036855661
-
Deciphering the genesis and fate of amyloid beta-protein yields novel therapies for Alzheimer disease
-
Selkoe D.J. Deciphering the genesis and fate of amyloid beta-protein yields novel therapies for Alzheimer disease. J. Clin. Invest. 110:2002;1375-1381.
-
(2002)
J. Clin. Invest.
, vol.110
, pp. 1375-1381
-
-
Selkoe, D.J.1
-
41
-
-
0029923751
-
Structure of the C-terminal end on the nascent peptide influences translation-termination
-
Björnsson A., Mottagui-Tabar S., Isaksson L.A. Structure of the C-terminal end on the nascent peptide influences translation-termination. EMBO J. 15:1996;1696-1704.
-
(1996)
EMBO J.
, vol.15
, pp. 1696-1704
-
-
Björnsson, A.1
Mottagui-Tabar, S.2
Isaksson, L.A.3
-
42
-
-
0028175762
-
The second to last amino acid in the nascent peptide as a codon context determinant
-
Mottagui-Tabar S., Björnsson A., Isaksson L.A. The second to last amino acid in the nascent peptide as a codon context determinant. EMBO J. 13:1994;249-257.
-
(1994)
EMBO J.
, vol.13
, pp. 249-257
-
-
Mottagui-Tabar, S.1
Björnsson, A.2
Isaksson, L.A.3
-
43
-
-
0016151380
-
Proteinase K from Tritirachium album Limber
-
Ebeling W., Hennrich N., Klockow M., Metz H., Orth H.D., Lang H. Proteinase K from Tritirachium album Limber. Eur. J. Biochem. 47:1974;91-97.
-
(1974)
Eur. J. Biochem.
, vol.47
, pp. 91-97
-
-
Ebeling, W.1
Hennrich, N.2
Klockow, M.3
Metz, H.4
Orth, H.D.5
Lang, H.6
|