Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Aida Peña-Blanco"'
Autor:
Uris Ros, Aida Peña-Blanco, Kay Hänggi, Ulrich Kunzendorf, Stefan Krautwald, W. Wei-Lynn Wong, Ana J. García-Sáez
Publikováno v:
Cell Reports, Vol 19, Iss 1, Pp 175-187 (2017)
Necroptosis is a form of regulated necrosis that results in cell death and content release after plasma membrane permeabilization. However, little is known about the molecular events responsible for the disruption of the plasma membrane. Here, we fin
Externí odkaz:
https://doaj.org/article/f772884ba0c946f4a0b83a88032db294
Autor:
Ana J. García-Sáez, Gregg G. Gundersen, Aida Peña-Blanco, Dan Grozki, Reuven Stein, Ayelet R. Amsalem-Zafran, Howard J. Worman, Liora Lindenboim, Didier Hodzic, Christoph Borner
Publikováno v:
Cell Death Discovery, Vol 6, Iss 1, Pp 1-15 (2020)
Cell Death Discovery
Cell Death Discovery
The canonical function of Bcl-2 family proteins is to regulate mitochondrial membrane integrity. In response to apoptotic signals the multi-domain pro-apoptotic proteins Bax and Bak are activated and perforate the mitochondrial outer membrane by a me
Autor:
Katia Cosentino, Vanessa Hertlein, Andreas Jenner, Timo Dellmann, Milos Gojkovic, Aida Peña-Blanco, Shashank Dadsena, Noel Wajngarten, John S.H. Danial, Jervis Vermal Thevathasan, Markus Mund, Jonas Ries, Ana J. Garcia-Saez
Publikováno v:
Molecular Cell. 82:933-949.e9
BAX and BAK are key apoptosis regulators that mediate the decisive step of mitochondrial outer membrane permeabilization. However, the mechanism by which they assemble the apoptotic pore remains obscure. Here, we report that BAX and BAK present disti
Autor:
Jan B. Parys, David Schlütermann, Hendrik Niemann, Stefanie Weidtkamp-Peters, Samuel Itskanov, Ana J. García-Sáez, Elisabeth Wesbuer, Niklas Berleth, Marian Frank, Andrea Borchardt, Björn Stork, Peter Proksch, Andreas Barbian, Tomas Luyten, Jana Deitersen, Arun Kumar Kondadi, Philip Böhler, Nora Wallot-Hieke, Alexander M. van der Bliek, Sebastian Wesselborg, Fabian Stuhldreier, Wenxian Wu, Ruchika Anand, Andreas S. Reichert, Aida Peña-Blanco
Publikováno v:
Cell Death and Disease, Vol 9, Iss 3, Pp 1-17 (2018)
Cell Death & Disease
Cell death & disease, vol 9, iss 3
Cell Death & Disease
Cell death & disease, vol 9, iss 3
Mitochondria are cellular organelles with crucial functions in the generation and distribution of ATP, the buffering of cytosolic Ca2+ and the initiation of apoptosis. Compounds that interfere with these functions are termed mitochondrial toxins, man
Autor:
Andreas Jenner, Andreas Villunger, Manuel D. Haschka, Theresia Zuleger, Tassula Proikas-Cezanne, Aida Peña-Blanco, Ana J. García-Sáez
Publikováno v:
Cell Death & Differentiation. 29:2105-2105
Autor:
Ulrich Kunzendorf, Kay Hänggi, Uris Ros, Ana J. García-Sáez, W. Wei-Lynn Wong, Aida Peña-Blanco, Stefan Krautwald
Publikováno v:
Cell Reports
Cell Reports, Vol 19, Iss 1, Pp 175-187 (2017)
Cell Reports, Vol 19, Iss 1, Pp 175-187 (2017)
Summary Necroptosis is a form of regulated necrosis that results in cell death and content release after plasma membrane permeabilization. However, little is known about the molecular events responsible for the disruption of the plasma membrane. Here
Autor:
Aida Peña-Blanco, Ana J. García-Sáez, Theresia Zuleger, Andreas Villunger, Tassula Proikas-Cezanne, Andreas Jenner, Manuel D. Haschka
Publikováno v:
Cell Death and Differentiation
Antimitotic drugs are extensively used in the clinics to treat different types of cancer. They can retain cells in a prolonged mitotic arrest imposing two major fates, mitotic slippage, or mitotic cell death. While the former is molecularly well char
Autor:
Ana J. García-Sáez, Aida Peña-Blanco
Publikováno v:
The FEBS journal. 285(3)
Bax and Bak are members of the Bcl-2 family and core regulators of the intrinsic pathway of apoptosis. Upon apoptotic stimuli, they are activated and oligomerize at the mitochondrial outer membrane (MOM) to mediate its permeabilization, which is cons
Autor:
Aida Peña-Blanco, Travis H. Stracker, Lluís Palenzuela, Anja Groth, Brian Raught, Philip A. Knobel, Katrin Rein, Alain de Bruin, Julien Colombelli, Teresa López-Rovira, Sandra Segura-Bayona, Etienne Coyaud, Stephen Forrow, Sameh A. Youssef, Helena González-Burón
Publikováno v:
Dipòsit Digital de la UB
Universidad de Barcelona
Segura-Bayona, S, Knobel, P A, Gonzalez-Buron, H, Youssef, S A, Peña-Blanco, A, Coyaud, E, Lopez-Rovira, T, Rein, K, Palenzuela, L, Colombelli, J, Forrow, S, Raught, B, Groth, A, De Bruin, A & Stracker, T H 2017, ' Differential requirements for Tousled-like kinases 1 and 2 in mammalian development ', Cell Death and Differentiation, vol. 24, no. 11, pp. 1872-1885 . https://doi.org/10.1038/cdd.2017.108
Cell death and differentiation, 24(11), 1872-1885. Nature Publishing Group
Cell Death and Differentiation, 24(11), 1872. Nature Publishing Group
Recercat. Dipósit de la Recerca de Catalunya
instname
Universidad de Barcelona
Segura-Bayona, S, Knobel, P A, Gonzalez-Buron, H, Youssef, S A, Peña-Blanco, A, Coyaud, E, Lopez-Rovira, T, Rein, K, Palenzuela, L, Colombelli, J, Forrow, S, Raught, B, Groth, A, De Bruin, A & Stracker, T H 2017, ' Differential requirements for Tousled-like kinases 1 and 2 in mammalian development ', Cell Death and Differentiation, vol. 24, no. 11, pp. 1872-1885 . https://doi.org/10.1038/cdd.2017.108
Cell death and differentiation, 24(11), 1872-1885. Nature Publishing Group
Cell Death and Differentiation, 24(11), 1872. Nature Publishing Group
Recercat. Dipósit de la Recerca de Catalunya
instname
The regulation of chromatin structure is critical for a wide range of essential cellular processes. The Tousled-like kinases, TLK1 and TLK2, regulate ASF1, a histone H3/H4 chaperone, and likely other substrates, and their activity has been implicated
Autor:
Andreas Jenner, Aida Peña‐Blanco, Raquel Salvador‐Gallego, Begoña Ugarte‐Uribe, Cristiana Zollo, Tariq Ganief, Jan Bierlmeier, Markus Mund, Jason E Lee, Jonas Ries, Dirk Schwarzer, Boris Macek, Ana J Garcia‐Saez
Publikováno v:
The EMBO Journal. 41(8)
The apoptotic executioner protein BAX and the dynamin-like protein DRP1 co-localize at mitochondria during apoptosis to mediate mitochondrial permeabilization and fragmentation. However, the molecular basis and functional consequences of this interpl