-
1
-
-
0142164890
-
Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysis
-
Polverino de Laureto P., et al. Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysis. J. Mol. Biol. 334 (2003) 129-141
-
(2003)
J. Mol. Biol.
, vol.334
, pp. 129-141
-
-
Polverino de Laureto, P.1
-
2
-
-
0021256895
-
Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein
-
Glenner G.G., and Wong C.W. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120 (1984) 885-890
-
(1984)
Biochem. Biophys. Res. Commun.
, vol.120
, pp. 885-890
-
-
Glenner, G.G.1
Wong, C.W.2
-
3
-
-
5344277556
-
Deciphering the molecular basis of memory failure in Alzheimer's disease
-
Walsh D.M., and Selkoe D.J. Deciphering the molecular basis of memory failure in Alzheimer's disease. Neuron 44 (2004) 181-193
-
(2004)
Neuron
, vol.44
, pp. 181-193
-
-
Walsh, D.M.1
Selkoe, D.J.2
-
4
-
-
26844546357
-
Prediction of "hot spots" of aggregation in disease-linked polypeptides
-
de Groot N., Pallares I., Aviles F., Vendrell J., and Ventura S. Prediction of "hot spots" of aggregation in disease-linked polypeptides. BMC Struct. Biol. 5 (2005) 18
-
(2005)
BMC Struct. Biol.
, vol.5
, pp. 18
-
-
de Groot, N.1
Pallares, I.2
Aviles, F.3
Vendrell, J.4
Ventura, S.5
-
5
-
-
33645240208
-
A systematic screen of beta(2)-microglobulin and insulin for amyloid-like segments
-
Ivanova M.I., Thompson M.J., and Eisenberg D. A systematic screen of beta(2)-microglobulin and insulin for amyloid-like segments. Proc. Natl. Acad. Sci. USA 103 (2006) 4079-4082
-
(2006)
Proc. Natl. Acad. Sci. USA
, vol.103
, pp. 4079-4082
-
-
Ivanova, M.I.1
Thompson, M.J.2
Eisenberg, D.3
-
6
-
-
2442553006
-
Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case
-
Ventura S., et al. Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case. Proc. Natl. Acad. Sci. USA 101 (2004) 7258-7263
-
(2004)
Proc. Natl. Acad. Sci. USA
, vol.101
, pp. 7258-7263
-
-
Ventura, S.1
-
7
-
-
33947517558
-
AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides
-
Conchillo-Sole O., de Groot N.S., Aviles F.X., Vendrell J., Daura X., and Ventura S. AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides. BMC Bioinformatics 8 (2007) 65
-
(2007)
BMC Bioinformatics
, vol.8
, pp. 65
-
-
Conchillo-Sole, O.1
de Groot, N.S.2
Aviles, F.X.3
Vendrell, J.4
Daura, X.5
Ventura, S.6
-
8
-
-
0036308719
-
Mutations that reduce aggregation of the Alzheimer's Abeta42 peptide: an unbiased search for the sequence determinants of Abeta amyloidogenesis
-
Wurth C., Guimard N.K., and Hecht M.H. Mutations that reduce aggregation of the Alzheimer's Abeta42 peptide: an unbiased search for the sequence determinants of Abeta amyloidogenesis. J. Mol. Biol. 319 (2002) 1279-1290
-
(2002)
J. Mol. Biol.
, vol.319
, pp. 1279-1290
-
-
Wurth, C.1
Guimard, N.K.2
Hecht, M.H.3
-
9
-
-
33644940173
-
Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities.
-
de Groot N.S., Aviles F.X., Vendrell J., and Ventura S. Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities. FEBS J. 273 (2006) 658-668
-
(2006)
FEBS J.
, vol.273
, pp. 658-668
-
-
de Groot, N.S.1
Aviles, F.X.2
Vendrell, J.3
Ventura, S.4
-
10
-
-
41049088527
-
Fourier transform infrared spectroscopy analysis of the conformational quality of recombinant proteins within inclusion bodies
-
Doglia S.M., Ami D., Natalello A., Gatti-Lafranconi P., and Lotti M. Fourier transform infrared spectroscopy analysis of the conformational quality of recombinant proteins within inclusion bodies. Biotechnol. J. 3 (2008) 193-201
-
(2008)
Biotechnol. J.
, vol.3
, pp. 193-201
-
-
Doglia, S.M.1
Ami, D.2
Natalello, A.3
Gatti-Lafranconi, P.4
Lotti, M.5
-
11
-
-
15244362270
-
Amyloid-like properties of bacterial inclusion bodies
-
Carrio M., Gonzalez-Montalban N., Vera A., Villaverde A., and Ventura S. Amyloid-like properties of bacterial inclusion bodies. J. Mol. Biol. 347 (2005) 1025-1037
-
(2005)
J. Mol. Biol.
, vol.347
, pp. 1025-1037
-
-
Carrio, M.1
Gonzalez-Montalban, N.2
Vera, A.3
Villaverde, A.4
Ventura, S.5
-
12
-
-
51049095117
-
Inclusion Bodies: specificity in their aggregation process and amyloid-like structure
-
Morell M., Bravo R., Espargaro A., Sisquella X., Avilés F.X., X. F.-B., and Ventura X. Inclusion Bodies: specificity in their aggregation process and amyloid-like structure. Biochim. Biophys. Acta. 1783 (2008) 1815-1825
-
(2008)
Biochim. Biophys. Acta.
, vol.1783
, pp. 1815-1825
-
-
Morell, M.1
Bravo, R.2
Espargaro, A.3
Sisquella, X.4
Avilés, F.X.5
X., F.-B.6
Ventura, X.7
-
13
-
-
0036308719
-
Mutations that reduce aggregation of the Alzheimer's Abeta42 peptide: an unbiased search for the sequence determinants of Abeta amyloidogenesis
-
Wurth C., Guimard N.K., and Hecht M.H. Mutations that reduce aggregation of the Alzheimer's Abeta42 peptide: an unbiased search for the sequence determinants of Abeta amyloidogenesis. J. Mol. Biol. 319 (2002) 1279-1290
-
(2002)
J. Mol. Biol.
, vol.319
, pp. 1279-1290
-
-
Wurth, C.1
Guimard, N.K.2
Hecht, M.H.3
-
14
-
-
26844569776
-
Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins
-
Garcia-Fruitos E., Gonzalez-Montalban N., Morell M., Vera A., Ferraz R.M., Aris A., Ventura S., and Villaverde A. Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins. Microb. Cell Fact. 4 (2005) 27
-
(2005)
Microb. Cell Fact.
, vol.4
, pp. 27
-
-
Garcia-Fruitos, E.1
Gonzalez-Montalban, N.2
Morell, M.3
Vera, A.4
Ferraz, R.M.5
Aris, A.6
Ventura, S.7
Villaverde, A.8
-
15
-
-
0034616258
-
Fine architecture of bacterial inclusion bodies
-
Carrio M.M., Cubarsi R., and Villaverde A. Fine architecture of bacterial inclusion bodies. FEBS Lett. 471 (2000) 7-11
-
(2000)
FEBS Lett.
, vol.471
, pp. 7-11
-
-
Carrio, M.M.1
Cubarsi, R.2
Villaverde, A.3
-
16
-
-
13144249171
-
Conformational stability and thermodynamics of folding of ribonucleases Sa, Sa2 and Sa3
-
Pace C.N., et al. Conformational stability and thermodynamics of folding of ribonucleases Sa, Sa2 and Sa3. J. Mol. Biol. 279 (1998) 271-286
-
(1998)
J. Mol. Biol.
, vol.279
, pp. 271-286
-
-
Pace, C.N.1
-
17
-
-
7044223181
-
Probing the unfolding region of ribonuclease A by site-directed mutagenesis
-
Koditz J., Ulbrich-Hofmann R., and Arnold U. Probing the unfolding region of ribonuclease A by site-directed mutagenesis. Eur. J. Biochem. 271 (2004) 4147-4156
-
(2004)
Eur. J. Biochem.
, vol.271
, pp. 4147-4156
-
-
Koditz, J.1
Ulbrich-Hofmann, R.2
Arnold, U.3
-
18
-
-
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
-
19
-
-
34247525991
-
Detection of transient protein-protein interactions by bimolecular fluorescence complementation: the Abl-SH3 case
-
Morell M., Espargaro A., Aviles F.X., and Ventura S. Detection of transient protein-protein interactions by bimolecular fluorescence complementation: the Abl-SH3 case. Proteomics 7 (2007) 1023-1036
-
(2007)
Proteomics
, vol.7
, pp. 1023-1036
-
-
Morell, M.1
Espargaro, A.2
Aviles, F.X.3
Ventura, S.4
-
20
-
-
33846222898
-
Inclusion body anatomy and functioning of chaperone-mediated in vivo inclusion body disassembly during high-level recombinant protein production in Escherichia coli
-
Rinas U., Hoffmann F., Betiku E., Estape D., and Marten S. Inclusion body anatomy and functioning of chaperone-mediated in vivo inclusion body disassembly during high-level recombinant protein production in Escherichia coli. J. Biotechnol. 127 (2007) 244-257
-
(2007)
J. Biotechnol.
, vol.127
, pp. 244-257
-
-
Rinas, U.1
Hoffmann, F.2
Betiku, E.3
Estape, D.4
Marten, S.5
-
21
-
-
33750991319
-
Effect of temperature on protein quality in bacterial inclusion bodies
-
de Groot N.S., and Ventura S. Effect of temperature on protein quality in bacterial inclusion bodies. FEBS Lett. 580 (2006) 6471-6476
-
(2006)
FEBS Lett.
, vol.580
, pp. 6471-6476
-
-
de Groot, N.S.1
Ventura, S.2
-
22
-
-
0036266942
-
Conformational strain in the hydrophobic core and its implications for protein folding and design
-
Ventura S., Vega M.C., Lacroix E., Angrand I., Spagnolo L., and Serrano L. Conformational strain in the hydrophobic core and its implications for protein folding and design. Nat. Struct. Biol. 9 (2002) 485-493
-
(2002)
Nat. Struct. Biol.
, vol.9
, pp. 485-493
-
-
Ventura, S.1
Vega, M.C.2
Lacroix, E.3
Angrand, I.4
Spagnolo, L.5
Serrano, L.6
-
23
-
-
33745991934
-
Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates
-
de Groot N.S., and Ventura S. Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates. J. Biotechnol. 125 (2006) 110-113
-
(2006)
J. Biotechnol.
, vol.125
, pp. 110-113
-
-
de Groot, N.S.1
Ventura, S.2
-
24
-
-
1042277916
-
Thermal stability of chemically denatured green fluorescent protein (GFP). A preliminary study
-
Nagy A., Malnasi-Csizmadia A., Somogyi B., and Lorinczy D. Thermal stability of chemically denatured green fluorescent protein (GFP). A preliminary study. Thermochim. Acta 410 (2004) 161-163
-
(2004)
Thermochim. Acta
, vol.410
, pp. 161-163
-
-
Nagy, A.1
Malnasi-Csizmadia, A.2
Somogyi, B.3
Lorinczy, D.4
-
25
-
-
34447649757
-
Conformational properties of aggregated polypeptides determine ClpB-dependence in the disaggregation process
-
Lewandowska A., Matuszewska M., and Liberek K. Conformational properties of aggregated polypeptides determine ClpB-dependence in the disaggregation process. J. Mol. Biol. 371 (2007) 800-811
-
(2007)
J. Mol. Biol.
, vol.371
, pp. 800-811
-
-
Lewandowska, A.1
Matuszewska, M.2
Liberek, K.3
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