Search

Your search keyword '"Cutruzzolà, Francesca"' showing total 258 results
Start Over Author "Cutruzzolà, Francesca" Language english
258 results on '"Cutruzzolà, Francesca"'

2. Structure-based mechanism of riboregulation of the metabolic enzyme SHMT1

Author

Spizzichino, Sharon, Di Fonzo, Federica, Marabelli, Chiara, Tramonti, Angela, Chaves-Sanjuan, Antonio, Parroni, Alessia, Boumis, Giovanna, Liberati, Francesca Romana, Paone, Alessio, Montemiglio, Linda Celeste, Ardini, Matteo, Jakobi, Arjen J., Bharadwaj, Alok, Swuec, Paolo, Tartaglia, Gian Gaetano, Paiardini, Alessandro, Contestabile, Roberto, Mai, Antonello, Rotili, Dante, Fiorentino, Francesco, Macone, Alberto, Giorgi, Alessandra, Tria, Giancarlo, Rinaldo, Serena, Bolognesi, Martino, Giardina, Giorgio, and Cutruzzolà, Francesca

Published
2024
Full Text
View/download PDF

3. Biliverdin Reductase-A integrates insulin signaling with mitochondrial metabolism through phosphorylation of GSK3β

Author

Lanzillotta, Chiara, Tramutola, Antonella, Lanzillotta, Simona, Greco, Viviana, Pagnotta, Sara, Sanchini, Caterina, Di Angelantonio, Silvia, Forte, Elena, Rinaldo, Serena, Paone, Alessio, Cutruzzolà, Francesca, Cimini, Flavia Agata, Barchetta, Ilaria, Cavallo, Maria Gisella, Urbani, Andrea, Butterfield, D. Allan, Di Domenico, Fabio, Paul, Bindu D., Perluigi, Marzia, Duarte, Joao M.N., and Barone, Eugenio

Published
2024
Full Text
View/download PDF

4. Molecular insights into RmcA-mediated c-di-GMP consumption: Linking redox potential to biofilm morphogenesis in Pseudomonas aeruginosa

Author

Scribani Rossi, Chiara, Eckartt, Kelly, Scarchilli, Elisabetta, Angeli, Simone, Price-Whelan, Alexa, Di Matteo, Adele, Chevreuil, Maelenn, Raynal, Bertrand, Arcovito, Alessandro, Giacon, Noah, Fiorentino, Francesco, Rotili, Dante, Mai, Antonello, Espinosa-Urgel, Manuel, Cutruzzolà, Francesca, Dietrich, Lars E.P., Paone, Alessio, Paiardini, Alessandro, and Rinaldo, Serena

Published
2023
Full Text
View/download PDF

7. Retinoic acid-induced 1 gene haploinsufficiency alters lipid metabolism and causes autophagy defects in Smith-Magenis syndrome

Author

Turco, Elisa Maria, Giovenale, Angela Maria Giada, Sireno, Laura, Mazzoni, Martina, Cammareri, Alessandra, Marchioretti, Caterina, Goracci, Laura, Di Veroli, Alessandra, Marchesan, Elena, D’Andrea, Daniel, Falconieri, Antonella, Torres, Barbara, Bernardini, Laura, Magnifico, Maria Chiara, Paone, Alessio, Rinaldo, Serena, Della Monica, Matteo, D’Arrigo, Stefano, Postorivo, Diana, Nardone, Anna Maria, Zampino, Giuseppe, Onesimo, Roberta, Leoni, Chiara, Caicci, Federico, Raimondo, Domenico, Binda, Elena, Trobiani, Laura, De Jaco, Antonella, Tata, Ada Maria, Ferrari, Daniela, Cutruzzolà, Francesca, Mazzoccoli, Gianluigi, Ziviani, Elena, Pennuto, Maria, Vescovi, Angelo Luigi, and Rosati, Jessica

Published
2022
Full Text
View/download PDF

11. Cytosolic serine hydroxymethyltransferase controls lung adenocarcinoma cells migratory ability by modulating AMP kinase activity

Author

Bouzidi, Amani, Magnifico, Maria Chiara, Paiardini, Alessandro, Macone, Alberto, Boumis, Giovanna, Giardina, Giorgio, Rinaldo, Serena, Liberati, Francesca Romana, Lauro, Clotilde, Limatola, Cristina, Lanzillotta, Chiara, Tramutola, Antonella, Perluigi, Marzia, Sgarbi, Gianluca, Solaini, Giancarlo, Baracca, Alessandra, Paone, Alessio, and Cutruzzolà, Francesca

Published
2020
Full Text
View/download PDF

13. Combined Delivery of miR-15/16 through Humanized Ferritin Nanocages for the Treatment of Chronic Lymphocytic Leukemia.

Author

Liberati, Francesca Romana, Di Russo, Sara, Barolo, Lorenzo, Peruzzi, Giovanna, Farina, Maria Vittoria, Spizzichino, Sharon, Di Fonzo, Federica, Quaglio, Deborah, Pisano, Luca, Botta, Bruno, Giorgi, Alessandra, Boffi, Alberto, Cutruzzolà, Francesca, Paone, Alessio, and Baiocco, Paola

Subjects
CHRONIC lymphocytic leukemia, FERRITIN, B cell lymphoma, B cells
Abstract

Chronic lymphocytic leukemia (CLL) is a widespread type of leukemia that predominantly targets B lymphocytes, undermining the balance between cell proliferation and apoptosis. In healthy B cells, miR-15/16, a tandem of microRNAs, functions as a tumor suppressor, curbing the expression of the antiapoptotic B cell lymphoma 2 protein (Bcl-2). Conversely, in CLL patients, a recurring deletion on chromosome 13q14, home to the miR15-a and miR16-1 genes, results in Bcl-2 overexpression, thereby fostering the onset of the pathology. In the present research, a novel approach utilizing humanized ferritin-based nanoparticles was employed to successfully deliver miR15-a and miR-16-1 into MEG01 cells, a model characterized by the classic CLL deletion and overexpression of the human ferritin receptor (TfR1). The loaded miR15-a and miR16-1, housed within modified HumAfFt, were efficiently internalized via the MEG01 cells and properly directed into the cytoplasm. Impressively, the concurrent application of miR15-a and miR16-1 demonstrated a robust capacity to induce apoptosis through the reduction in Bcl-2 expression levels. This technology, employing RNA-loaded ferritin nanoparticles, hints at promising directions in the battle against CLL, bridging the substantial gap left by traditional transfection agents and indicating a pathway that may offer hope for more effective treatments. [ABSTRACT FROM AUTHOR]

Published
2024
Full Text
View/download PDF

21. The phosphodiesterase RmcA contributes to the adaptation of Pseudomonas putida to l-arginine.

Author

Scribani-Rossi, Chiara, Molina-Henares, María Antonia, Angeli, Simone, Cutruzzolà, Francesca, Paiardini, Alessandro, Espinosa-Urgel, Manuel, and Rinaldo, Serena

Subjects
PSEUDOMONAS putida, ARGININE, LIFE cycles (Biology), MICROBIAL metabolism, NITROGEN cycle, BIOTECHNOLOGICAL microorganisms, HOMEOSTASIS
Abstract

Amino acids are crucial in nitrogen cycling and to shape the metabolism of microorganisms. Among them, arginine is a versatile molecule able to sustain nitrogen, carbon, and even ATP supply and to regulate multicellular behaviors such as biofilm formation. Arginine modulates the intracellular levels of 3′–5′cyclic diguanylic acid (c-di-GMP), a second messenger that controls biofilm formation, maintenance and dispersion. In Pseudomonas putida , KT2440, a versatile microorganism with wide biotechnological applications, modulation of c-di-GMP levels by arginine requires the transcriptional regulator ArgR, but the connections between arginine metabolism and c-di-GMP are not fully characterized. It has been recently demonstrated that arginine can be perceived by the opportunistic human pathogen Pseudomonas aeruginosa through the transducer RmcA protein (Redox regulator of c-di-GMP), which can directly decrease c-di-GMP levels and possibly affect biofilm architecture. A RmcA homolog is present in P. putida , but its function and involvement in arginine perceiving or biofilm life cycle had not been studied. Here, we present a preliminary characterization of the RmcA-dependent response to arginine in P. putida in modulating biofilm formation, c-di-GMP levels, and energy metabolism. This work contributes to further understanding the molecular mechanisms linking biofilm homeostasis and environmental adaptation. [ABSTRACT FROM AUTHOR]

Published
2023
Full Text
View/download PDF

31. Nutrient Sensing and Biofilm Modulation: The Example of L-arginine in Pseudomonas.

Author

Scribani Rossi, Chiara, Barrientos-Moreno, Laura, Paone, Alessio, Cutruzzolà, Francesca, Paiardini, Alessandro, Espinosa-Urgel, Manuel, and Rinaldo, Serena

Subjects
ARGININE, BIOFILMS, PSEUDOMONAS, ANAEROBIC bacteria, BACTERIAL cells, BACTERIAL growth, ANTIBIOTICS
Abstract

Bacterial biofilm represents a multicellular community embedded within an extracellular matrix attached to a surface. This lifestyle confers to bacterial cells protection against hostile environments, such as antibiotic treatment and host immune response in case of infections. The Pseudomonas genus is characterised by species producing strong biofilms difficult to be eradicated and by an extraordinary metabolic versatility which may support energy and carbon/nitrogen assimilation under multiple environmental conditions. Nutrient availability can be perceived by a Pseudomonas biofilm which, in turn, readapts its metabolism to finally tune its own formation and dispersion. A growing number of papers is now focusing on the mechanism of nutrient perception as a possible strategy to weaken the biofilm barrier by environmental cues. One of the most important nutrients is amino acid L-arginine, a crucial metabolite sustaining bacterial growth both as a carbon and a nitrogen source. Under low-oxygen conditions, L-arginine may also serve for ATP production, thus allowing bacteria to survive in anaerobic environments. L-arginine has been associated with biofilms, virulence, and antibiotic resistance. L-arginine is also a key precursor of regulatory molecules such as polyamines, whose involvement in biofilm homeostasis is reported. Given the biomedical and biotechnological relevance of biofilm control, the state of the art on the effects mediated by the L-arginine nutrient on biofilm modulation is presented, with a special focus on the Pseudomonas biofilm. Possible biotechnological and biomedical applications are also discussed. [ABSTRACT FROM AUTHOR]

Published
2022
Full Text
View/download PDF

35. Cytosolic localization and in vitro assembly of human de novo thymidylate synthesis complex.

Author

Spizzichino, Sharon, Boi, Dalila, Boumis, Giovanna, Lucchi, Roberta, Liberati, Francesca Romana, Capelli, Davide, Montanari, Roberta, Pochetti, Giorgio, Piacentini, Roberta, Parisi, Giacomo, Paone, Alessio, Rinaldo, Serena, Contestabile, Roberto, Tramonti, Angela, Paiardini, Alessandro, Giardina, Giorgio, and Cutruzzolà, Francesca

Subjects
THYMIDYLATE synthase, TETRAHYDROFOLATE dehydrogenase, CARCINOMA in situ, PROTEIN-protein interactions, CANCER cells, DIHYDROPYRIMIDINE dehydrogenase
Abstract

De novo thymidylate synthesis is a crucial pathway for normal and cancer cells. Deoxythymidine monophosphate (dTMP) is synthesized by the combined action of three enzymes: serine hydroxymethyltransferase (SHMT1), dihydrofolate reductase (DHFR) and thymidylate synthase (TYMS), with the latter two being targets of widely used chemotherapeutics such as antifolates and 5‐fluorouracil. These proteins translocate to the nucleus after SUMOylation and are suggested to assemble in this compartment into the thymidylate synthesis complex. We report the intracellular dynamics of the complex in cancer cells by an in situ proximity ligation assay, showing that it is also detected in the cytoplasm. This result indicates that the role of the thymidylate synthesis complex assembly may go beyond dTMP synthesis. We have successfully assembled the dTMP synthesis complex in vitro, employing tetrameric SHMT1 and a bifunctional chimeric enzyme comprising human thymidylate synthase and dihydrofolate reductase. We show that the SHMT1 tetrameric state is required for efficient complex assembly, indicating that this aggregation state is evolutionarily selected in eukaryotes to optimize protein–protein interactions. Lastly, our results regarding the activity of the complete thymidylate cycle in vitro may provide a useful tool with respect to developing drugs targeting the entire complex instead of the individual components. [ABSTRACT FROM AUTHOR]

Published
2022
Full Text
View/download PDF

36. Crystal structure of Aspergillus fumigatusAroH, an aromatic amino acid aminotransferase.

Author

Spizzichino, Sharon, Pampalone, Gioena, Dindo, Mirco, Bruno, Agostino, Romani, Luigina, Cutruzzolà, Francesca, Zelante, Teresa, Pieroni, Marco, Cellini, Barbara, and Giardina, Giorgio

Abstract

Aspergillus fumigatus is a saprophytic ubiquitous fungus whose spores can trigger reactions such as allergic bronchopulmonary aspergillosis or the fatal invasive pulmonary aspergillosis. To survive in the lungs, the fungus must adapt to a hypoxic and nutritionally restrictive environment, exploiting the limited availability of aromatic amino acids (AAAs) in the best possible way, as mammals do not synthesize them. A key enzyme for AAAs catabolism in A. fumigatus is AroH, a pyridoxal 5′‐phosphate‐dependent aromatic aminotransferase. AroH was recently shown to display a broad substrate specificity, accepting L‐kynurenine and α‐aminoadipate as amino donors besides AAAs. Given its pivotal role in the adaptability of the fungus to nutrient conditions, AroH represents a potential target for the development of innovative therapies against A. fumigatus‐related diseases. We have solved the crystal structure of Af‐AroH at 2.4 Å resolution and gained new insight into the dynamics of the enzyme's active site, which appears to be crucial for the design of inhibitors. The conformational plasticity of the active site pocket is probably linked to the wide substrate specificity of AroH. [ABSTRACT FROM AUTHOR]

Published
2022
Full Text
View/download PDF

38. Structure and metal‐binding properties of PA4063, a novel player in periplasmic zinc trafficking by Pseudomonas aeruginosa.

Author

Fiorillo, Annarita, Battistoni, Andrea, Ammendola, Serena, Secli, Valerio, Rinaldo, Serena, Cutruzzolà, Francesca, Demitri, Nicola, and Ilari, Andrea

Subjects
PSEUDOMONAS aeruginosa, ZINC transporters, ZINC ions, ESSENTIAL nutrients, GRAM-negative bacteria, ZINC, PSEUDOMONAS
Abstract

The capability to obtain essential nutrients in hostile environments is a critical skill for pathogens. Under zinc‐deficient conditions, Pseudomonas aeruginosa expresses a pool of metal homeostasis control systems that is complex compared with other Gram‐negative bacteria and has only been partially characterized. Here, the structure and zinc‐binding properties of the protein PA4063, the first component of the PA4063–PA4066 operon, are described. PA4063 has no homologs in other organisms and is characterized by the presence of two histidine‐rich sequences. ITC titration detected two zinc‐binding sites with micromolar affinity. Crystallographic characterization, performed both with and without zinc, revealed an α/β‐sandwich structure that can be classified as a noncanonical ferredoxin‐like fold since it differs in size and topology. The histidine‐rich stretches located at the N‐terminus and between β3 and β4 are disordered in the apo structure, but a few residues become structured in the presence of zinc, contributing to coordination in one of the two sites. The ability to bind two zinc ions at relatively low affinity, the absence of catalytic cavities and the presence of two histidine‐rich loops are properties and structural features which suggest that PA4063 might play a role as a periplasmic zinc chaperone or as a concentration sensor useful for optimizing the response of the pathogen to zinc deficiency. [ABSTRACT FROM AUTHOR]

Published
2021
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results