Zobrazeno 1 - 10
of 109
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
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 9, p 4848 (2021)
Multiple mitochondrial dysfunctions syndrome (MMDS) is a rare neurodegenerative disorder associated with mutations in genes with a vital role in the biogenesis of mitochondrial [4Fe–4S] proteins. Mutations in one of these genes encoding for BOLA3 p
Externí odkaz:
https://doaj.org/article/34107e13457649d99a126b6538c373d1
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e4cca21fe056223a2e8476f415ad2a69
https://doi.org/10.1002/pro.4625
https://doi.org/10.1002/pro.4625
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b078cd393e09477db41bc7faf641cd74
https://doi.org/10.1021/jacs.1c13626
https://doi.org/10.1021/jacs.1c13626
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.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa58827c5bd45ab5248294622936f559
https://doi.org/10.1039/d1cc03566e
https://doi.org/10.1039/d1cc03566e
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
