Castillo V - Search Results

1

Prediction of the aggregation propensity of proteins from the primary sequence: aggregation properties of proteomes.

Castillo V, Graña-Montes R, Sabate R, Ventura S. Castillo V, et al. Biotechnol J. 2011 Jun;6(6):674-85. doi: 10.1002/biot.201000331. Epub 2011 Apr 29. Biotechnol J. 2011. PMID: 21538897 Review.

2

The in vivo and in vitro aggregation properties of globular proteins correlate with their conformational stability: the SH3 case.

Espargaró A, Castillo V, de Groot NS, Ventura S. Espargaró A, et al. Among authors: castillo v. J Mol Biol. 2008 May 16;378(5):1116-31. doi: 10.1016/j.jmb.2008.03.020. Epub 2008 Mar 19. J Mol Biol. 2008. PMID: 18423663

3

Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases.

Castillo V, Ventura S. Castillo V, et al. PLoS Comput Biol. 2009 Aug;5(8):e1000476. doi: 10.1371/journal.pcbi.1000476. Epub 2009 Aug 21. PLoS Comput Biol. 2009. PMID: 19696882 Free PMC article.

4

The aggregation properties of Escherichia coli proteins associated with their cellular abundance.

Castillo V, Graña-Montes R, Ventura S. Castillo V, et al. Biotechnol J. 2011 Jun;6(6):752-60. doi: 10.1002/biot.201100014. Epub 2011 Apr 29. Biotechnol J. 2011. PMID: 21538899

5

AGGRESCAN: method, application, and perspectives for drug design.

de Groot NS, Castillo V, Graña-Montes R, Ventura S. de Groot NS, et al. Among authors: castillo v. Methods Mol Biol. 2012;819:199-220. doi: 10.1007/978-1-61779-465-0_14. Methods Mol Biol. 2012. PMID: 22183539

6

The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain.

Castillo V, Chiti F, Ventura S. Castillo V, et al. PLoS One. 2013;8(3):e58297. doi: 10.1371/journal.pone.0058297. Epub 2013 Mar 7. PLoS One. 2013. PMID: 23505482 Free PMC article.

7

Energy barriers for HET-s prion forming domain amyloid formation.

Sabaté R, Castillo V, Espargaró A, Saupe SJ, Ventura S. Sabaté R, et al. Among authors: castillo v. FEBS J. 2009 Sep;276(18):5053-64. doi: 10.1111/j.1742-4658.2009.07202.x. Epub 2009 Aug 4. FEBS J. 2009. PMID: 19682303 Free article.

8

Designing out disulfide bonds of leech carboxypeptidase inhibitor: implications for its folding, stability and function.

Arolas JL, Castillo V, Bronsoms S, Aviles FX, Ventura S. Arolas JL, et al. Among authors: castillo v. J Mol Biol. 2009 Sep 18;392(2):529-46. doi: 10.1016/j.jmb.2009.06.049. Epub 2009 Jun 25. J Mol Biol. 2009. PMID: 19559710

9

Deciphering the role of the thermodynamic and kinetic stabilities of SH3 domains on their aggregation inside bacteria.

Castillo V, Espargaró A, Gordo V, Vendrell J, Ventura S. Castillo V, et al. Proteomics. 2010 Dec;10(23):4172-85. doi: 10.1002/pmic.201000260. Proteomics. 2010. PMID: 21086517

10

Contribution of disulfide bonds to stability, folding, and amyloid fibril formation: the PI3-SH3 domain case.

Graña-Montes R, de Groot NS, Castillo V, Sancho J, Velazquez-Campoy A, Ventura S. Graña-Montes R, et al. Among authors: castillo v. Antioxid Redox Signal. 2012 Jan 1;16(1):1-15. doi: 10.1089/ars.2011.3936. Epub 2011 Sep 15. Antioxid Redox Signal. 2012. PMID: 21797671

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