A Structural Investigation of the Interaction between a GC-376-Based Peptidomimetic PROTAC and Its Precursor with the Viral Main Protease of Coxsackievirus B3

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

Molecular Basis of Rare Diseases Associated to the Maturation of Mitochondrial [4Fe-4S]-Containing Proteins

Autor: Francesca Camponeschi, Simone Ciofi-Baffoni, Vito Calderone, Lucia Banci

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

Unraveling the mechanism of [4Fe‐4S] cluster assembly on the N‐terminal cluster binding site of NUBP1

Autor: Beatrice Bargagna, Sara Matteucci, Simone Ciofi‐Baffoni, Francesca Camponeschi, Lucia Banci

Publikováno v: Protein Science. 32

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e4cca21fe056223a2e8476f415ad2a69
https://doi.org/10.1002/pro.4625

Interconversion between [2Fe–2S] and [4Fe–4S] cluster glutathione complexes

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

In Cellulo Mössbauer and EPR Studies Bring New Evidence to the Long‐Standing Debate on Iron–Sulfur Cluster Binding in Human Anamorsin

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⟩

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5bcc73a995becac224d4941e2dcc8298
https://doi.org/10.1002/anie.202102910