Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Marta Loureiro-López"'
Autor:
Narcis A. Petriman, Marta Loureiro-López, Michael Taschner, Nevin K. Zacharia, Magdalena M. Georgieva, Niels Boegholm, André Mourão, Robert B. Russell, Jens S. Andersen, Esben Lorentzen
Publikováno v:
bioRxiv/The EMBO Journal
bioRxiv
bioRxiv
Cilia are ubiquitous eukaryotic organelles important to cellular motility, signalling and sensory reception. Cilium formation requires intraflagellar transport for trafficking of structural and signalling components. The large MDa IFT-B complex const
Autor:
Richard C. Hartley, Marta Loureiro-López, Shujing Ding, Sabine Arndt, Michael P. Murphy, John F. Mulvey, Nils Burger, Abigail A.I. Norman, Kurt Hoogewijs, Olga Sauchanka, Andrew M. James, Ian M. Fearnley, Thomas Krieg, Amin Mottahedin
Publikováno v:
Cell chemical biology. 29(4)
Mammalian complex I can adopt catalytically active (A-) or deactive (D-) states. A defining feature of the reversible transition between these two defined states is thought to be exposure of the ND3 subunit Cys39 residue in the D-state and its occlus
Functional role of respiratory supercomplexes in mice: SCAF1 relevance and segmentation of the Qpool
Autor:
José Antonio Enríquez, Jesús R. Huertas, Jesús Vázquez, Enrique Calvo, Sara Cogliati, Adela Guarás, Rafael A. Casuso, Rebeca Acín-Pérez, Pablo Hernansanz-Agustín, Yolanda Martí-Mateos, Marta Loureiro-López, Fernando García-Marqués, Juan Carlos Silla-Castro, Marta Carro-Alvarellos
Publikováno v:
Repisalud
Instituto de Salud Carlos III (ISCIII)
Digibug. Repositorio Institucional de la Universidad de Granada
instname
Digibug: Repositorio Institucional de la Universidad de Granada
Universidad de Granada (UGR)
Science Advances
Instituto de Salud Carlos III (ISCIII)
Digibug. Repositorio Institucional de la Universidad de Granada
instname
Digibug: Repositorio Institucional de la Universidad de Granada
Universidad de Granada (UGR)
Science Advances
Mitochondrial respiratory complexes assemble into supercomplexes (SC). Q-respirasome (III2 + IV) requires the supercomplex assembly factor (SCAF1) protein. The role of this factor in the N-respirasome (I + III2 + IV) and the physiological role of SCs
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca0da94fc352c074849f04a6953126d0
https://hdl.handle.net/20.500.12105/10714
https://hdl.handle.net/20.500.12105/10714
Autor:
Yolanda Martí-Mateos, Rafael A. Casuso, Enrique Calvo, Jesús R. Huertas, Marta Loureiro-López, Pablo Hernansanz-Agustín, Sara Cogliati, Fernando García-Marqués, José Antonio Enríquez, Jesús Vázquez, Marta Carro-Alvarellos, Jc. Silla-Castro, Rebeca Acín-Pérez, Adela Guarás
SummaryMitochondrial respiratory complexes assemble into different forms of supercomplexes (SC). In particular, SC III2+IV require the SCAF1 protein. However, the structural role of this factor in the formation of the respirasome (I+III2+IV) and the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d1a656072304e5fd1b5ff2370f801f3
Autor:
Adela Guarás, Ester Perales-Clemente, Enrique Calvo, Rebeca Acín-Pérez, Marta Loureiro-Lopez, Claire Pujol, Isabel Martínez-Carrascoso, Estefanía Nuñez, Fernando García-Marqués, María Angeles Rodríguez-Hernández, Ana Cortés, Francisca Diaz, Acisclo Pérez-Martos, Carlos T. Moraes, Patricio Fernández-Silva, Aleksandra Trifunovic, Plácido Navas, Jesús Vazquez, Jose A. Enríquez
Publikováno v:
Cell Reports, Vol 15, Iss 1, Pp 197-209 (2016)
Electrons feed into the mitochondrial electron transport chain (mETC) from NAD- or FAD-dependent enzymes. A shift from glucose to fatty acids increases electron flux through FAD, which can saturate the oxidation capacity of the dedicated coenzyme Q (
Externí odkaz:
https://doaj.org/article/398fede521514fbaa72a53db1ef4ebdc