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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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Molecular mechanisms of cell death: recommendations of the Nomenclature Committee on Cell Death 2018.

Lorenzo Galluzzi, +186 more
TL;DR: The Nomenclature Committee on Cell Death (NCCD) has formulated guidelines for the definition and interpretation of cell death from morphological, biochemical, and functional perspectives.
Journal Article

Molecular mechanisms of cell death: recommendations of the Nomenclature Committee on Cell Death 2018

Lorenzo Galluzzi, +168 more
- 01 Jan 2018 - 
TL;DR: An updated classification of cell death subroutines focusing on mechanistic and essential aspects of the process is proposed, and the utility of neologisms that refer to highly specialized instances of these processes are discussed.
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Bax, Bak and beyond - mitochondrial performance in apoptosis.

TL;DR: A new perspective is emerging, in which the control of apoptosis by Bax and Bak goes beyond them and is highly influenced by additional mitochondrial components, and the contribution of mitochondrial composition, dynamics and interaction with other organelles to apoptosis commitment is considered.
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Effect of line tension on the lateral organization of lipid membranes

TL;DR: The results revealed a linear increase of the temperature of domain formation and domain growth rate with line tension, and domain budding was shown to depend on height mismatch, which contribute significantly to knowledge of the physical-chemical parameters that control membrane organization.
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Bax assembly into rings and arcs in apoptotic mitochondria is linked to membrane pores.

TL;DR: The data identify the supramolecular organization of Bax during apoptosis and support a molecular mechanism in which Bax fully or partially delineates pores of different sizes to permeabilize the mitochondrial outer membrane.