Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Chiara Cefaro"'
Autor:
Emmanouela Kallergi, Lucia Banci, Chiara Cefaro, Isabella C. Felli, Nitsa Katrakili, Anna Pavelkova, Kostas Tokatlidis, Maria Andreadaki, Ivano Bertini, Karolina Gajda, Charalambos Pozidis, Angelo Gallo, Simone Ciofi-Baffoni
Publikováno v:
Journal of Molecular Biology. 425:594-608
The functional role of unstructured protein domains is an emerging field in the frame of intrinsically disordered proteins. The involvement of intrinsically disordered domains (IDDs) in protein targeting and biogenesis processes in mitochondria is so
Autor:
Lucia Banci, Charalambos Pozidis, Riccardo Peruzzini, Kostas Tokatlidis, Maria Andreadaki, Simone Ciofi-Baffoni, Karolina Gajda, Emmanouela Kallergi, Chiara Cefaro, Nitsa Katrakili, Paraskevi Kritsiligkou, Ivano Bertini
Publikováno v:
ACS Chemical Biology. 7:707-714
The interaction of Mia40 with Erv1/ALR is central to the oxidative protein folding in the intermembrane space of mitochondria (IMS) as Erv1/ALR oxidizes reduced Mia40 to restore its functional state. Here we address the role of Mia40 in the import an
Publikováno v:
Journal of Biological Chemistry
Human Cox17 is the mitochondrial copper chaperone responsible for supplying copper ions, through the assistance of Sco1, Sco2, and Cox11, to cytochrome c oxidase, the terminal enzyme of the mitochondrial energy-transducing respiratory chain. It consi
Autor:
Lucia Banci, Kostas Tokatlidis, Chiara Cefaro, Dionisia P. Sideris, Ivano Bertini, Nitsa Katrakili, Manuele Martinelli, Simone Ciofi-Baffoni, Angelo Gallo
Publikováno v:
Nature Structural & Molecular Biology. 16:198-206
MIA40 has a key role in oxidative protein folding in the mitochondrial intermembrane space. We present the solution structure of human MIA40 and its mechanism as a catalyst of oxidative folding. MIA40 has a 66-residue folded domain made of an alpha-h
Autor:
Luciano A. Abriata, Lucia Banci, Chiara Cefaro, Karolina Gajda, Marcos N. Morgada, Alejandro J. Vila
Publikováno v:
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Maturation of cytochrome oxidases is a complex process requiring assembly of several subunits and adequate uptake of the metal cofactors. Two orthologous Sco proteins (Sco1 and Sco2) are essential for the correct assembly of the dicopper CuA site in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::090798de4f291ea0ba62fd3c14445892
http://www.pnas.org/content/112/38/11771
http://www.pnas.org/content/112/38/11771
Autor:
Ivano Bertini, Lucia Banci, Kostas Tokatlidis, Simone Ciofi-Baffoni, Vito Calderone, Angelo Gallo, Chiara Cefaro
The oxidative folding mechanism in the intermembrane space of human mitochondria underpins a disulfide relay system consisting of the import receptor Mia40 and the homodimeric FAD-dependent thiol oxidase ALR. The flavoprotein ALR receives two electro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8f896b4c6de5f1a0129b15eec115c66
http://hdl.handle.net/2318/1825777
http://hdl.handle.net/2318/1825777
Autor:
Eirini Lionaki, Chiara Cefaro, Lucia Banci, Vito Calderone, Emmanouela Kallergi, Simone Ciofi-Baffoni, Charalambos Pozidis, Angelo Gallo, Ivano Bertini, Kostas Tokatlidis
Publikováno v:
Proceedings of the National Academy of Sciences
ICT FP7 Publications Database
Europe PubMed Central
ICT FP7 Publications Database
Europe PubMed Central
Oxidative protein folding in the mitochondrial intermembrane space requires the transfer of a disulfide bond from MIA40 to the substrate. During this process MIA40 is reduced and regenerated to a functional state through the interaction with the flav
Autor:
Ivano Bertini, Enrico Luchinat, Dionisia P. Sideris, Chiara Cefaro, Isabella C. Felli, Kostas Tokatlidis, Angelo Gallo, Leonardo Gonnelli, Lucia Banci, Simone Ciofi-Baffoni, Lucia Cenacchi
Several proteins of the mitochondrial intermembrane space are targeted by internal targeting signals. A class of such proteins with α-helical hairpin structure bridged by two intramolecular disulfides is trapped by a Mia40-dependent oxidative proces
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71b90ecc673796ee379a51cd5b1c6cf0
http://hdl.handle.net/2318/1825776
http://hdl.handle.net/2318/1825776
Autor:
Chiara Cefaro, Silvia Borioni, Armandodoriano Bianco, Antonello Alvino, Giancarlo Ortaggi, Marco Franceschin
Most known perylene diimides are lipophilic, with few exceptions of hydrophilic derivatives. Even in the latter case, the compounds have limited water solubility and show a strong tendency to self-aggregation. In this paper we present the synthesis o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9025317b3be27315858ba56d90a9dd4a
http://hdl.handle.net/11573/360497
http://hdl.handle.net/11573/360497