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Items: 1 to 20 of 56

1.

Prions are a common mechanism for phenotypic inheritance in wild yeasts.

Halfmann R, Jarosz DF, Jones SK, Chang A, Lancaster AK, Lindquist S.

Nature. 2012 Feb 15;482(7385):363-8. doi: 10.1038/nature10875.

2.

Temperature dependence of the aggregation kinetics of Sup35 and Ure2p yeast prions.

Sabaté R, Villar-Piqué A, Espargaró A, Ventura S.

Biomacromolecules. 2012 Feb 13;13(2):474-83. doi: 10.1021/bm201527m.

PMID:
22176525
3.

The yeast prions [PSI+] and [URE3] are molecular degenerative diseases.

Wickner RB, Edskes HK, Bateman D, Kelly AC, Gorkovskiy A.

Prion. 2011 Oct-Dec;5(4):258-62. doi: 10.4161/pri.17748. Review.

4.

Suicidal [PSI+] is a lethal yeast prion.

McGlinchey RP, Kryndushkin D, Wickner RB.

Proc Natl Acad Sci U S A. 2011 Mar 29;108(13):5337-41. doi: 10.1073/pnas.1102762108.

5.

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.

Chembiochem. 2011 Feb 11;12(3):407-23. doi: 10.1002/cbic.201000602.

PMID:
21290543
6.

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.

Proteomics. 2010 Dec;10(23):4172-85. doi: 10.1002/pmic.201000260.

PMID:
21086517
7.

Conversion of a yeast prion protein to an infectious form in bacteria.

Garrity SJ, Sivanathan V, Dong J, Lindquist S, Hochschild A.

Proc Natl Acad Sci U S A. 2010 Jun 8;107(23):10596-601. doi: 10.1073/pnas.0913280107.

8.

Protein folding and aggregation in bacteria.

Sabate R, de Groot NS, Ventura S.

Cell Mol Life Sci. 2010 Aug;67(16):2695-715. doi: 10.1007/s00018-010-0344-4. Review.

PMID:
20358253
9.

Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion.

Sabaté R, Espargaró A, Saupe SJ, Ventura S.

Microb Cell Fact. 2009 Oct 28;8:56. doi: 10.1186/1475-2859-8-56.

10.

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

Sabaté R, Castillo V, Espargaró A, Saupe SJ, Ventura S.

FEBS J. 2009 Sep;276(18):5053-64. doi: 10.1111/j.1742-4658.2009.07202.x.

11.

Amyloids in bacterial inclusion bodies.

de Groot NS, Sabate R, Ventura S.

Trends Biochem Sci. 2009 Aug;34(8):408-16. doi: 10.1016/j.tibs.2009.03.009. Review.

PMID:
19647433
12.

Solid-state NMR spectroscopy reveals that E. coli inclusion bodies of HET-s(218-289) are amyloids.

Wasmer C, Benkemoun L, Sabaté R, Steinmetz MO, Coulary-Salin B, Wang L, Riek R, Saupe SJ, Meier BH.

Angew Chem Int Ed Engl. 2009;48(26):4858-60. doi: 10.1002/anie.200806100.

PMID:
19472238
13.

Kinetic and thermodynamic stability of bacterial intracellular aggregates.

Espargaró A, Sabaté R, Ventura S.

FEBS Lett. 2008 Oct 29;582(25-26):3669-73. doi: 10.1016/j.febslet.2008.09.049.

14.

Bacterial inclusion bodies contain amyloid-like structure.

Wang L, Maji SK, Sawaya MR, Eisenberg D, Riek R.

PLoS Biol. 2008 Aug 5;6(8):e195. doi: 10.1371/journal.pbio.0060195.

15.

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.

Biochim Biophys Acta. 2008 Oct;1783(10):1815-25. doi: 10.1016/j.bbamcr.2008.06.007.

16.

Recent structural and computational insights into conformational diseases.

Fernàndez-Busquets X, de Groot NS, Fernandez D, Ventura S.

Curr Med Chem. 2008;15(13):1336-49. Review.

PMID:
18537613
17.

Alternative assembly pathways of the amyloidogenic yeast prion determinant Sup35-NM.

Hess S, Lindquist SL, Scheibel T.

EMBO Rep. 2007 Dec;8(12):1196-201.

18.

Prions of fungi: inherited structures and biological roles.

Wickner RB, Edskes HK, Shewmaker F, Nakayashiki T.

Nat Rev Microbiol. 2007 Aug;5(8):611-8. Review.

19.

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

Morell M, Espargaró A, Avilés FX, Ventura S.

Proteomics. 2007 Apr;7(7):1023-36.

PMID:
17352427
20.

In vitro analysis of SpUre2p, a prion-related protein, exemplifies the relationship between amyloid and prion.

Immel F, Jiang Y, Wang YQ, Marchal C, Maillet L, Perrett S, Cullin C.

J Biol Chem. 2007 Mar 16;282(11):7912-20.

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