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Items: 21


Single event visualization of unconventional secretion of FGF2.

Dimou E, Cosentino K, Platonova E, Ros U, Sadeghi M, Kashyap P, Katsinelos T, Wegehingel S, Noé F, García-Sáez AJ, Ewers H, Nickel W.

J Cell Biol. 2018 Nov 23. pii: jcb.201802008. doi: 10.1083/jcb.201802008. [Epub ahead of print]


Self-association and folding in membrane determine the mode of action of peptides from the lytic segment of sticholysins.

Ros U, Carretero GPB, Paulino J, Crusca E Jr, Pazos F, Cilli EM, Lanio ME, Schreier S, Alvarez C.

Biochimie. 2018 Oct 13;156:109-117. doi: 10.1016/j.biochi.2018.10.005. [Epub ahead of print]


Sticholysin II-mediated cytotoxicity involves the activation of regulated intracellular responses that anticipates cell death.

Soto C, Bergado G, Blanco R, Griñán T, Rodríguez H, Ros U, Pazos F, Lanio ME, Hernández AM, Álvarez C.

Biochimie. 2018 May;148:18-35. doi: 10.1016/j.biochi.2018.02.006. Epub 2018 Feb 13.


Insights on the structure-activity relationship of peptides derived from Sticholysin II.

Lima de Oliveira A, Maffud Cilli E, Ros U, Crusca E Jr, Lanio ME, Alvarez C, Schreier S, Aguiar Pertinhez T, Spisni A.

Biopolymers. 2018 Jan 23. doi: 10.1002/bip.23097. [Epub ahead of print]


Biophysical and biochemical strategies to understand membrane binding and pore formation by sticholysins, pore-forming proteins from a sea anemone.

Alvarez C, Ros U, Valle A, Pedrera L, Soto C, Hervis YP, Cabezas S, Valiente PA, Pazos F, Lanio ME.

Biophys Rev. 2017 Oct;9(5):529-544. doi: 10.1007/s12551-017-0316-0. Epub 2017 Aug 29. Review.


Differential binding and activity of the pore-forming toxin sticholysin II in model membranes containing diverse ceramide-derived lipids.

Soto C, Del Valle A, Valiente PA, Ros U, Lanio ME, Hernández AM, Alvarez C.

Biochimie. 2017 Jul;138:20-31. doi: 10.1016/j.biochi.2017.04.003. Epub 2017 Apr 7.


Necroptosis Execution Is Mediated by Plasma Membrane Nanopores Independent of Calcium.

Ros U, Peña-Blanco A, Hänggi K, Kunzendorf U, Krautwald S, Wong WW, García-Sáez AJ.

Cell Rep. 2017 Apr 4;19(1):175-187. doi: 10.1016/j.celrep.2017.03.024.


Damage of eukaryotic cells by the pore-forming toxin sticholysin II: Consequences of the potassium efflux.

Cabezas S, Ho S, Ros U, Lanio ME, Alvarez C, van der Goot FG.

Biochim Biophys Acta Biomembr. 2017 May;1859(5):982-992. doi: 10.1016/j.bbamem.2017.02.001. Epub 2017 Feb 4.


Disrupting a key hydrophobic pair in the oligomerization interface of the actinoporins impairs their pore-forming activity.

Mesa-Galloso H, Delgado-Magnero KH, Cabezas S, López-Castilla A, Hernández-González JE, Pedrera L, Alvarez C, Peter Tieleman D, García-Sáez AJ, Lanio ME, Ros U, Valiente PA.

Protein Sci. 2017 Mar;26(3):550-565. doi: 10.1002/pro.3104. Epub 2017 Feb 23.


Assembling the puzzle: Oligomerization of α-pore forming proteins in membranes.

Cosentino K, Ros U, García-Sáez AJ.

Biochim Biophys Acta. 2016 Mar;1858(3):457-466. doi: 10.1016/j.bbamem.2015.09.013. Epub 2015 Sep 12. Review.


The Presence of Sterols Favors Sticholysin I-Membrane Association and Pore Formation Regardless of Their Ability to Form Laterally Segregated Domains.

Pedrera L, Gomide AB, Sánchez RE, Ros U, Wilke N, Pazos F, Lanio ME, Itri R, Fanani ML, Alvarez C.

Langmuir. 2015 Sep 15;31(36):9911-23. doi: 10.1021/acs.langmuir.5b01687. Epub 2015 Sep 2.


Differences in activity of actinoporins are related with the hydrophobicity of their N-terminus.

Ros U, Rodríguez-Vera W, Pedrera L, Valiente PA, Cabezas S, Lanio ME, García-Sáez AJ, Alvarez C.

Biochimie. 2015 Sep;116:70-8. doi: 10.1016/j.biochi.2015.06.024. Epub 2015 Jun 29.


More Than a Pore: The Interplay of Pore-Forming Proteins and Lipid Membranes.

Ros U, García-Sáez AJ.

J Membr Biol. 2015 Jun;248(3):545-61. doi: 10.1007/s00232-015-9820-y. Epub 2015 Jun 19. Review.


Toxicity of an α-pore-forming toxin depends on the assembly mechanism on the target membrane as revealed by single molecule imaging.

Subburaj Y, Ros U, Hermann E, Tong R, García-Sáez AJ.

J Biol Chem. 2015 Feb 20;290(8):4856-65. doi: 10.1074/jbc.M114.600676. Epub 2014 Dec 18.


Sticholysin I-membrane interaction: an interplay between the presence of sphingomyelin and membrane fluidity.

Pedrera L, Fanani ML, Ros U, Lanio ME, Maggio B, Alvarez C.

Biochim Biophys Acta. 2014 Jul;1838(7):1752-9. doi: 10.1016/j.bbamem.2014.03.011. Epub 2014 Mar 26.


The sticholysin family of pore-forming toxins induces the mixing of lipids in membrane domains.

Ros U, Edwards MA, Epand RF, Lanio ME, Schreier S, Yip CM, Alvarez C, Epand RM.

Biochim Biophys Acta. 2013 Nov;1828(11):2757-62. doi: 10.1016/j.bbamem.2013.08.001. Epub 2013 Aug 14.


Functional and topological studies with Trp-containing analogs of the peptide StII(1-30) derived from the N-terminus of the pore forming toxin sticholysin II: contribution to understand its orientation in membrane.

Ros U, Souto AL, de Oliveira FJ, Crusca E Jr, Pazos F, Cilli EM, Lanio ME, Schreier S, Alvarez C.

Biopolymers. 2013 Jul;100(4):337-46. doi: 10.1002/bip.22211.


The membranotropic activity of N-terminal peptides from the pore-forming proteins sticholysin I and II is modulated by hydrophobic and electrostatic interactions as well as lipid composition.

Ros U, Pedrera L, Diaz D, Karam JC, Sudbrack TP, Valiente PA, MartÍnez D, Cilli EM, Pazos F, Itri R, Lanio ME, Schreier S, Ávarez C.

J Biosci. 2011 Dec;36(5):781-91.


Correlations between differences in amino-terminal sequences and different hemolytic activity of sticholysins.

Cilli EM, Pigossi FT, Crusca E Jr, Ros U, Martinez D, Lanio ME, Alvarez C, Schreier S.

Toxicon. 2007 Dec 15;50(8):1201-4. Epub 2007 Aug 3.


Sticholysins I and II interaction with cationic micelles promotes toxins' conformational changes and enhanced hemolytic activity.

Lanio ME, Alvarez C, Ochoa C, Ros U, Pazos F, Martínez D, Tejuca M, Eugenio LM, Casallanovo F, Dyszy FH, Schreier S, Lissi E.

Toxicon. 2007 Nov;50(6):731-9. Epub 2007 Jun 26.


Model peptides mimic the structure and function of the N-terminus of the pore-forming toxin sticholysin II.

Casallanovo F, de Oliveira FJ, de Souza FC, Ros U, Martínez Y, Pentón D, Tejuca M, Martínez D, Pazos F, Pertinhez TA, Spisni A, Cilli EM, Lanio ME, Alvarez C, Schreier S.

Biopolymers. 2006;84(2):169-80.


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