Zobrazeno 1 - 10
of 108
pro vyhledávání: '"Simone Ciofi-Baffoni"'
Autor:
Alessia De Santis, Deborah Grifagni, Andrea Orsetti, Elena Lenci, Antonio Rosato, Mariapina D’Onofrio, Andrea Trabocchi, Simone Ciofi-Baffoni, Francesca Cantini, Vito Calderone
Publikováno v:
Biomolecules, Vol 14, Iss 10, p 1260 (2024)
The conservation of the main protease in viral genomes, combined with the absence of a homologous protease in humans, makes this enzyme family an ideal target for developing broad-spectrum antiviral drugs with minimized host toxicity. GC-376, a pepti
Externí odkaz:
https://doaj.org/article/e9ef22ae83444f268486edbe5fa60502
Autor:
Yuxuan Ji, Li Wei, Anqi Da, Holger Stark, Peter-Leon Hagedoorn, Simone Ciofi-Baffoni, Sally A. Cowley, Ricardo O. Louro, Smilja Todorovic, Maria Andrea Mroginski, Yvain Nicolet, Maxie M. Roessler, Nick E. Le Brun, Mario Piccioli, William S. James, Wilfred R. Hagen, Kourosh H. Ebrahimi
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Externí odkaz:
https://doaj.org/article/14e01c9c674845c487345b274dc920b1
Publikováno v:
Biomolecules, Vol 12, Iss 7, p 1009 (2022)
The importance of mitochondria in mammalian cells is widely known. Several biochemical reactions and pathways take place within mitochondria: among them, there are those involving the biogenesis of the iron–sulfur (Fe-S) clusters. The latter are ev
Externí odkaz:
https://doaj.org/article/66275a09e5ad41f9a486720d00a80761
Autor:
Simone Ciofi-Baffoni, Claudia Andreini
Publikováno v:
Inorganics, Vol 10, Iss 4, p 52 (2022)
Iron-sulfur (Fe/S) clusters are protein cofactors that play a crucial role in essential cellular functions. Their ability to rapidly exchange electrons with several redox active acceptors makes them an efficient system for fulfilling diverse cellular
Externí odkaz:
https://doaj.org/article/02bf43254ca14a5d96edd2e7c7ccf4b7
Autor:
Marta A Uzarska, Veronica Nasta, Benjamin D Weiler, Farah Spantgar, Simone Ciofi-Baffoni, Maria Rosaria Saviello, Leonardo Gonnelli, Ulrich Mühlenhoff, Lucia Banci, Roland Lill
Publikováno v:
eLife, Vol 5 (2016)
Assembly of mitochondrial iron-sulfur (Fe/S) proteins is a key process of cells, and defects cause many rare diseases. In the first phase of this pathway, ten Fe/S cluster (ISC) assembly components synthesize and insert [2Fe-2S] clusters. The second
Externí odkaz:
https://doaj.org/article/542cec6e518847f58ec908a4fd547ae8
Publikováno v:
Protein Science. 32
Publikováno v:
Journal of the American Chemical Society. 144:5713-5717
Human lipoyl synthase (LIAS) is an enzyme containing two [4Fe-4S] clusters (named FeS
Autor:
Michele Invernici, Giulia Selvolini, José Malanho Silva, Giovanna Marrazza, Simone Ciofi-Baffoni, Mario Piccioli
Publikováno v:
Chemical Communications. 58:3533-3536
A dynamic interconversion between a dinuclear [FeIIFeIIIS2(GS)4]3− complex and a tetranuclear [FeII2FeIII2S4(GS)4]2− complex can be operative in the mitochondrial labile iron pool.
Publikováno v:
Frontiers Research Topics ISBN: 9782832524206
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5059ec6e45344dc49a45502c910adaf4
https://doi.org/10.3389/978-2-8325-2420-6
https://doi.org/10.3389/978-2-8325-2420-6
Autor:
Geneviève Blondin, Martin Clémancey, Lucia Banci, Francesca Camponeschi, Simone Ciofi-Baffoni, Sara Matteucci
Publikováno v:
Angewandte Chemie International Edition
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2021, 60 (27), pp.14841-14845. ⟨10.1002/anie.202102910⟩
Angewandte Chemie (International Ed. in English)
Angewandte Chemie International Edition, 2021, 60 (27), pp.14841-14845. ⟨10.1002/anie.202102910⟩
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2021, 60 (27), pp.14841-14845. ⟨10.1002/anie.202102910⟩
Angewandte Chemie (International Ed. in English)
Angewandte Chemie International Edition, 2021, 60 (27), pp.14841-14845. ⟨10.1002/anie.202102910⟩
Human anamorsin is an iron–sulfur (Fe–S)‐cluster‐binding protein acting as an electron donor in the early steps of cytosolic iron–sulfur protein biogenesis. Human anamorsin belongs to the eukaryotic CIAPIN1 protein family and contains two h