High speed atomic force microscopy to investigate the interactions between toxic Aβ 1-42 peptides and model membranes in real time: impact of the membrane composition von Ewald, M, Henry, S, Lambert, E, Feuillie, C, Bobo, C, Cullin, C, Lecomte, S, Molinari, M

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A tensegrity driven DNA nanopore von Mendoza, O, Calmet, P, Alves, I, Lecomte, S, Raoux, M, Cullin, C, Elezgaray, J

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Guidelines and recommendations on yeast cell death nomenclature von Carmona-Gutierrez, Didac, Bauer, Maria Anna, Zimmermann, Andreas, Aguilera, Andrés, Austriaco, Nicanor, Ayscough, Kathryn, Balzan, Rena, Bar-Nun, Shoshana, Barrientos, Antonio, Belenky, Peter, Blondel, Marc, Braun, Ralf J, Breitenbach, Michael, Burhans, William C, Büttner, Sabrina, Cavalieri, Duccio, Chang, Michael, Cooper, Katrina F, Côrte-Real, Manuela, Costa, Vítor, Cullin, Christophe, Dawes, Ian, Dengjel, Jörn, Dickman, Martin B, Eisenberg, Tobias, Fahrenkrog, Birthe, Fasel, Nicolas, Fröhlich, Kai-Uwe, Gargouri, Ali, Giannattasio, Sergio, Goffrini, Paola, Gourlay, Campbell W, Grant, Chris M, Greenwood, Michael T, Guaragnella, Nicoletta, Heger, Thomas, Heinisch, Jürgen, Herker, Eva, Herrmann, Johannes M, Hofer, Sebastian, Jiménez-Ruiz, Antonio, Jungwirth, Helmut, Kainz, Katharina, Kontoyiannis, Dimitrios P, Ludovico, Paula, Manon, Stéphen, Martegani, Enzo, Mazzoni, Cristina, Megeney, Lynn A, Meisinger, Chris, Nielsen, Jens, Nyström, Thomas, Osiewacz, Heinz D, Outeiro, Tiago F, Park, Hay-Oak, Pendl, Tobias, Petranovic, Dina, Picot, Stephane, Polčic, Peter, Powers, Ted, Ramsdale, Mark, Rinnerthaler, Mark, Rockenfeller, Patrick, Ruckenstuhl, Christoph, Schaffrath, Raffael, Segovia, Maria, Severin, Fedor F, Sharon, Amir, Sigrist, Stephan J, Sommer-Ruck, Cornelia, Sousa, Maria João, Thevelein, Johan M, Thevissen, Karin, Titorenko, Vladimir, Toledano, Michel B, Tuite, Mick, Vögtle, F-Nora, Westermann, Benedikt, Winderickx, Joris, Wissing, Silke, Wölfl, Stefan, Zhang, Zhaojie J, Zhao, Richard Y, Zhou, Bing, Galluzzi, Lorenzo, Kroemer, Guido, Madeo, Frank

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Interaction of Aβ 1-42 peptide or their variant with model membrane of different composition probed by infrared nanospectroscopy von Henry, S, Bercu, N B, Bobo, C, Cullin, C, Molinari, M, Lecomte, S

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High speed atomic force microscopy to investigate the interactions between toxic Aβ1-42 peptides and model membranes in real time: impact of the membrane composition von Ewald, M, Henry, S, Lambert, E, Feuillie, C, Bobo, C, Cullin, C, Lecomte, S, Molinari, M

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Interaction of Aβ1-42 peptide or their variant with model membrane of different composition probed by infrared nanospectroscopy von Henry, S, Bercu, N. B, Bobo, C, Cullin, C, Molinari, M, Lecomte, S

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Isolation of drugs active against mammalian prions using a yeast-based screening assay von Meijer, Laurent, Blondel, Marc, Talarek, Nicolas, Cullin, Christophe, Mettey, Yvette, Bach, Stéphane, Vierfond, Jean-Michel, Dormont, Dominique, Andrieu, Thibault, Galons, Hervé

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Les prions : une histoire de souris, d'homme... et de levure von CULLIN, C

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simple and efficient method for direct gene deletion in Saccharomyces cerevisiae von Baudin, A, Ozier-Kalogeropoulos, O, Denouel, A, Cullin, C

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Interaction of A beta(1-42) peptide or their variant with model membrane of different composition probed by infrared nanospectroscopy von Henry, S., Bercu, N. B., Bobo, C., Cullin, C., Molinari, M., Lecomte, S.

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Stability, Folding, Dimerization, and Assembly Properties of the Yeast Prion Ure2p von Thual, Carine, Bousset, Luc, Komar, Anton A, Walter, Stefan, Buchner, Johannes, Cullin, Christophe, Melki, Ronald

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High speed atomic force microscopy to investigate the interactions between toxic Aβ 1-42 peptides and model membranes in real time: impact of the membrane composition: Nanoscale von Ewald, M., Henry, S., Lambert, E., Feuillie, C., Bobo, C., Cullin, C., Lecomte, S., Molinari, M.

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The protein-only theory and the yeast Saccharomyces cerevisiae: the prions and the propagons von Fernandez-Bellot, E, Cullin, C

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In Vivo and In Vitro Analyses of Toxic Mutants of HET-s: FTIR Antiparallel Signature Correlates with Amyloid Toxicity von Berthelot, Karine, Ta, Ha Phuong, Géan, Julie, Lecomte, Sophie, Cullin, Christophe

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Functional analysis of Rrp7p, an essential yeast protein involved in pre-rRNA processing and ribosome assembly von Baudin-Baillieu, Agnès, Tollervey, David, Cullin, Christophe, Lacroute, François

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A tensegrity driven DNA nanoporeElectronic supplementary information (ESI) available. See DOI: 10.1039/c7nr01901g von Mendoza, O, Calmet, P, Alves, I, Lecomte, S, Raoux, M, Cullin, C, Elezgaray, J

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Maximizing the expression of mammalian cytochrome P-450 monooxygenase activities in yeast cells von Urban, P., Cullin, C., Pompon, D.

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The [URE3] prion is not conserved among Saccharomyces species von Talarek, Nicolas, Maillet, Laurent, Cullin, Christophe, Aigle, Michel

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Comparative Studies of Nontoxic and Toxic Amyloids Interacting with Membrane Models at the Air−Water Interface von Ta, Ha Phuong, Berthelot, Karine, Coulary-Salin, Bénédicte, Desbat, Bernard, Géan, Julie, Servant, Laurent, Cullin, Christophe, Lecomte, Sophie

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The mechanisms of [URE3] prion elimination demonstrate that large aggregates of Ure2p are dead-end products von Cullin, Christophe, Ripaud, Leslie, Maillet, Laurent

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