Ventura S - Search Results

1

Bacterial inclusion bodies of Alzheimer's disease β-amyloid peptides can be employed to study native-like aggregation intermediate states.

Dasari M, Espargaro A, Sabate R, Lopez del Amo JM, Fink U, Grelle G, Bieschke J, Ventura S, Reif B. Dasari M, et al. Among authors: ventura s. Chembiochem. 2011 Feb 11;12(3):407-23. doi: 10.1002/cbic.201000602. Epub 2011 Jan 10. Chembiochem. 2011. PMID: 21290543

2

Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case.

Ventura S, Zurdo J, Narayanan S, Parreño M, Mangues R, Reif B, Chiti F, Giannoni E, Dobson CM, Aviles FX, Serrano L. Ventura S, et al. Proc Natl Acad Sci U S A. 2004 May 11;101(19):7258-63. doi: 10.1073/pnas.0308249101. Epub 2004 May 3. Proc Natl Acad Sci U S A. 2004. PMID: 15123800 Free PMC article.

3

Amyloid-like properties of bacterial inclusion bodies.

Carrió M, González-Montalbán N, Vera A, Villaverde A, Ventura S. Carrió M, et al. Among authors: ventura s. J Mol Biol. 2005 Apr 15;347(5):1025-37. doi: 10.1016/j.jmb.2005.02.030. J Mol Biol. 2005. PMID: 15784261

4

Detection of transient protein-protein interactions by bimolecular fluorescence complementation: the Abl-SH3 case.

Morell M, Espargaró A, Avilés FX, Ventura S. Morell M, et al. Among authors: ventura s. Proteomics. 2007 Apr;7(7):1023-36. doi: 10.1002/pmic.200600966. Proteomics. 2007. PMID: 17352427

5

Prion and non-prion amyloids of the HET-s prion forming domain.

Sabaté R, Baxa U, Benkemoun L, Sánchez de Groot N, Coulary-Salin B, Maddelein ML, Malato L, Ventura S, Steven AC, Saupe SJ. Sabaté R, et al. Among authors: ventura s. J Mol Biol. 2007 Jul 20;370(4):768-83. doi: 10.1016/j.jmb.2007.05.014. Epub 2007 May 22. J Mol Biol. 2007. PMID: 17532341

6

Study and selection of in vivo protein interactions by coupling bimolecular fluorescence complementation and flow cytometry.

Morell M, Espargaro A, Aviles FX, Ventura S. Morell M, et al. Among authors: ventura s. Nat Protoc. 2008;3(1):22-33. doi: 10.1038/nprot.2007.496. Nat Protoc. 2008. PMID: 18193018

7

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: ventura s. 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

8

Inclusion bodies: specificity in their aggregation process and amyloid-like structure.

Morell M, Bravo R, Espargaró A, Sisquella X, Avilés FX, Fernàndez-Busquets X, Ventura S. Morell M, et al. Among authors: ventura s. Biochim Biophys Acta. 2008 Oct;1783(10):1815-25. doi: 10.1016/j.bbamcr.2008.06.007. Epub 2008 Jun 19. Biochim Biophys Acta. 2008. PMID: 18619498 Free article.

9

Studies on bacterial inclusion bodies.

de Groot NS, Espargaró A, Morell M, Ventura S. de Groot NS, et al. Among authors: ventura s. Future Microbiol. 2008 Aug;3(4):423-35. doi: 10.2217/17460913.3.4.423. Future Microbiol. 2008. PMID: 18651814 Review.

10

Kinetic and thermodynamic stability of bacterial intracellular aggregates.

Espargaró A, Sabaté R, Ventura S. Espargaró A, et al. Among authors: ventura s. FEBS Lett. 2008 Oct 29;582(25-26):3669-73. doi: 10.1016/j.febslet.2008.09.049. Epub 2008 Oct 7. FEBS Lett. 2008. PMID: 18840434 Free article.

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