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Ana J. García-Sáez
Researcher at University of Cologne
Publications - 131
Citations - 10109
Ana J. García-Sáez is an academic researcher from University of Cologne. The author has contributed to research in topics: Membrane & Vesicle. The author has an hindex of 37, co-authored 115 publications receiving 6333 citations. Previous affiliations of Ana J. García-Sáez include Max Planck Society & University of Tübingen.
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Journal ArticleDOI
DRP1 interacts directly with BAX to induce its activation and apoptosis
Andreas Jenner,Aida Peña-Blanco,Raquel Salvador-Gallego,Begoña Ugarte-Uribe,Cris Zollo,Tariq Ganief,Jan Bierlmeier,Marcus Mund,Jason E. Lee,Jonas Ries,Dirk Schwarzer,Boris Macek,Ana J. García-Sáez +12 more
TL;DR: It is proposed that DRP1 can promote apoptosis by acting as noncanonical direct activator of BAX through physical contacts with its N‐terminal region.
Journal ArticleDOI
The membrane activity of BOK involves formation of large, stable toroidal pores and is promoted by cBID.
Yuniel Fernández-Marrero,Stephanie Bleicken,Kushal Kumar Das,Daniel Bachmann,Thomas Kaufmann,Ana J. García-Sáez +5 more
TL;DR: It is shown that BOK∆C can permeabilize liposomes, and cooperate with cBID, but its role in directly mediating mitochondrial permeabilization is unclear and may underlie a yet to be determined negative regulation.
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Single event visualization of unconventional secretion of FGF2
Eleni Dimou,Katia Cosentino,Evgenia Platonova,Uris Ros,Mohsen Sadeghi,Purba Kashyap,Taxiarchis Katsinelos,Sabine Wegehingel,Frank Noé,Ana J. García-Sáez,Helge Ewers,Helge Ewers,Walter Nickel +12 more
TL;DR: This work directly visualized individual FGF2 membrane translocation events at the plasma membrane using live cell TIRF microscopy and directly demonstrated FGF 2 oligomers at the inner leaflet of living cells with a FGF1 dimer being the most prominent species.
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Differences in activity of actinoporins are related with the hydrophobicity of their N-terminus
Uris Ros,Wendy Rodríguez-Vera,Lohans Pedrera,Pedro A. Valiente,Sheila Cabezas,María E. Lanio,Ana J. García-Sáez,Carlos Alvarez +7 more
TL;DR: A comparison of StI, StII, EqtII, and FraC activities with that of their respective N-terminal synthetic peptides shows that a higher hydrophobicity contributes to increase the activity, reinforcing the notion that this property must be taken into account to design new potent membranotropic agents.
Journal ArticleDOI
Detergent-activated BAX protein is a monomer.
Olena Ivashyna,Ana J. García-Sáez,Jonas Ries,Eric T. Christenson,Petra Schwille,Paul H. Schlesinger +5 more
TL;DR: It is concluded that detergent activation of BAX is not congruent with oligomerization and that in physiologic buffer conditions BAX can assume two stable monomeric conformations, one inactive and one active.