Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Inés Romero-Carramiñana"'
Publikováno v:
iScience, Vol 27, Iss 6, Pp 109863- (2024)
Summary: T cells experience metabolic reprogramming to an enhanced glycolysis upon activation. Herein, we have investigated whether ATPase Inhibitory Factor 1 (IF1), the physiological inhibitor of mitochondrial ATP synthase, participates in rewiring
Externí odkaz:
https://doaj.org/article/c89d227347af4688973bd5d302b95332
Autor:
Inés Romero-Carramiñana, Pau B. Esparza-Moltó, Sonia Domínguez-Zorita, Cristina Nuevo-Tapioles, José M. Cuezva
Publikováno v:
Communications Biology, Vol 6, Iss 1, Pp 1-16 (2023)
Abstract The coexistence of two pools of ATP synthase in mitochondria has been largely neglected despite in vitro indications for the existence of reversible active/inactive state transitions in the F1-domain of the enzyme. Herein, using cells and mi
Externí odkaz:
https://doaj.org/article/ba2ddb490b514a279c22d6de56172efd
Autor:
Sonia Domínguez-Zorita, Inés Romero-Carramiñana, Fulvio Santacatterina, Pau B. Esparza-Moltó, Carolina Simó, Araceli del-Arco, Cristina Núñez de Arenas, Jorge Saiz, Coral Barbas, José M. Cuezva
Publikováno v:
Cell Death and Disease, Vol 14, Iss 7, Pp 1-19 (2023)
Abstract ATPase Inhibitory Factor 1 (IF1) regulates the activity of mitochondrial ATP synthase. The expression of IF1 in differentiated human and mouse cells is highly variable. In intestinal cells, the overexpression of IF1 protects against colon in
Externí odkaz:
https://doaj.org/article/7e4b079a3aba4439bee23493763afa95
Autor:
Laura Torresano, Fulvio Santacatterina, Sonia Domínguez-Zorita, Cristina Nuevo-Tapioles, Alfonso Núñez-Salgado, Pau B. Esparza-Moltó, Lucía González-Llorente, Inés Romero-Carramiñana, Cristina Núñez de Arenas, Brenda Sánchez-Garrido, Laura Nájera, Clara Salas, Mariano Provencio, José M. Cuezva
Publikováno v:
Oncogenesis, Vol 11, Iss 1, Pp 1-17 (2022)
Abstract Lung cancer is the leading cause of cancer-related death worldwide despite the success of therapies targeting oncogenic drivers and immune-checkpoint inhibitors. Although metabolic enzymes offer additional targets for therapy, the precise me
Externí odkaz:
https://doaj.org/article/490db6879736444798d619ec42ec108b
Publikováno v:
Frontiers in Physiology, Vol 13 (2022)
The ATP synthase is an essential multifunctional enzyme complex of mitochondria that produces most of cellular ATP, shapes the structure of the inner membrane into cristae and regulates the signals that control cell fate or demise. The ATPase Inhibit
Externí odkaz:
https://doaj.org/article/746af6bc36cc48b698cc9b35ace01e01
Autor:
Pau B Esparza-Moltó, Inés Romero-Carramiñana, Cristina Núñez de Arenas, Marta P Pereira, Noelia Blanco, Beatriz Pardo, Georgina R Bates, Carla Sánchez-Castillo, Rafael Artuch, Michael P Murphy, José A Esteban, José M Cuezva
Publikováno v:
PLoS Biology, Vol 19, Iss 5, p e3001252 (2021)
The mitochondrial ATP synthase emerges as key hub of cellular functions controlling the production of ATP, cellular signaling, and fate. It is regulated by the ATPase inhibitory factor 1 (IF1), which is highly abundant in neurons. Herein, we ablated
Externí odkaz:
https://doaj.org/article/3c469b3a87654a168245043c7e61234d
Autor:
Inés Romero-Carramiñana, Carla Sánchez-Castillo, Rafael Artuch, José M. Cuezva, Noelia Blanco, Georgina Bates, Pau B. Esparza-Moltó, José A. Esteban, Beatriz Pardo, Michael P. Murphy, Marta P. Pereira, Cristina Núñez de Arenas
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
PLoS Biology, Vol 19, Iss 5, p e3001252 (2021)
PLoS Biology
instname
PLoS Biology, Vol 19, Iss 5, p e3001252 (2021)
PLoS Biology
The mitochondrial ATP synthase emerges as key hub of cellular functions controlling the production of ATP, cellular signaling, and fate. It is regulated by the ATPase inhibitory factor 1 (IF1), which is highly abundant in neurons. Herein, we ablated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3faea67fdca298f15e3149c94b02d1fc
https://doi.org/10.1371/journal.pbio.3001252
https://doi.org/10.1371/journal.pbio.3001252
