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[null,"1.","Record Nr.",null,"UNINA9910765744603321"]
[null,null,"Autore",null,"Supuran Claudiu T."]
[null,null,"Titolo",null,"Carbonic anhydrases and metabolism / / Claudiu T. Supuran"]
[null,null,"Pubbl/distr/stampa",null,"Basel, Switzerland : , : MDPI, , [2019]"]
[{"$nulls":4},"©2019"]
[null,null,"ISBN",null,"3-03897-801-9"]
[null,null,"Descrizione fisica",null,"1 online resource (184 pages)"]
[null,null,"Disciplina",null,"572.51"]
[null,null,"Soggetti",null,"Metalloenzymes"]
[null,null,"Lingua di pubblicazione",null,"Inglese"]
[null,null,"Formato",null,"Materiale a stampa"]
[null,null,null,"Livello bibliografico","Monografia"]
[null,null,"Nota di contenuto",null,"About the Special Issue Editor  vii -- Claudiu T. Supuran Carbonic Anhydrases and Metabolism Reprinted from: Metabolites 2018, 8, 25, doi:10.3390/metabo8020025 . 1 -- Claudiu T. Supuran Carbonic Anhydrase Inhibition and the Management of Hypoxic Tumors Reprinted from: Metabolites 2017, 7, 48, doi:10.3390/metabo7030048 . 6 -- Paul C. McDonald, Mridula Swayampakula and Shoukat Dedhar Coordinated Regulation of Metabolic Transporters and Migration/Invasion by Carbonic Anhydrase IX Reprinted from: Metabolites 2018, 8, 20, doi:10.3390/metabo8010020 . 19 -- Mam Y. Mboge, Brian P. Mahon, Robert McKenna and Susan C. Frost Carbonic Anhydrases: Role in pH Control and Cancer Reprinted from: Metabolites 2018, 8, 19, doi:10.3390/metabo8010019 . 30 -- Carol Ward, James Meehan, Mark Gray, Ian H. Kunkler, Simon P. Langdon and David J. Argyle Carbonic Anhydrase IX (CAIX), Cancer, and Radiation Responsiveness Reprinted from: Metabolites 2018, 8, 13, doi:10.3390/metabo8010013 . 61 -- Elisabetta Iessi, Mariantonia Logozzi, Davide Mizzoni, Rossella Di Raimo, Claudiu T. Supuran and Stefano Fais Rethinking the Combination of Proton Exchanger Inhibitors in Cancer Therapy Reprinted from: Metabolites 2018, 8, 2, doi:10.3390/metabo8010002  79 -- Niccol `o Chiaramonte, Maria Novella Romanelli, Elisabetta Teodori and Claudiu T. Supuran Amino Acids as Building Blocks for Carbonic Anhydrase Inhibitors Reprinted from: Metabolites 2018, 8, 36, doi:10.3390/metabo8020036 . 99 -- Morteza Abdoli, Murat Bozdag, Andrea Angeli and Claudiu T. Supuran Benzamide-4-Sulfonamides Are Effective Human Carbonic Anhydrase I, II, VII, and IX Inhibitors Reprinted from: Metabolites 2018, 8, 37, doi:"]
[{"$nulls":4},"10.3390/metabo8020037 . 121 -- Ashok Aspatwar, Susanna Haapanen and Seppo Parkkila An Update on the Metabolic Roles of Carbonic Anhydrases in the Model Alga Chlamydomonas reinhardtii Reprinted from: Metabolites 2018, 8, 22, doi:10.3390/metabo8010022 . 132 -- Silvia Bua, Susanna Haapanen, Marianne Kuuslahti, Seppo Parkkila and Claudiu T. Supuran Activation Studies of the β-Carbonic Anhydrase from the Pathogenic Protozoan Entamoeba histolytica with Amino Acids and Amines Reprinted from: Metabolites 2019, 9, 26, doi:10.3390/metabo9020026 . 148 -- Claudiu T. Supuran and Clemente Capasso An Overview of the Bacterial Carbonic Anhydrases Reprinted from: Metabolites 2017, 7, 56, doi:10.3390/metabo7040056 . 156."]
[null,null,null,"Sommario/riassunto","Carbonic anhydrases (CAs; EC 4.2.1.1) are metalloenzymes present in all kingdoms of life, as they equilibrate the reaction between three simple but essential chemical species: CO2, bicarbonate, and protons. Discovered more than 80 years ago, in 1933, these enzymes have been extensively investigated due to the biomedical application of their inhibitors, but also because they are an extraordinary example of convergent evolution, with seven genetically distinct CA families that evolved independently in Bacteria, Archaea, and Eukarya. CAs are also among the most efficient enzymes known in nature, due to the fact that the uncatalyzed hydration of CO2 is a very slow process and the physiological demands for its conversion to ionic, soluble species is very high. Inhibition of the CAs has pharmacological applications in many fields, such as antiglaucoma, anticonvulsant, antiobesity, and anticancer agents/diagnostic tools, but is also emerging for designing anti-infectives, i.e., antifungal, antibacterial, and antiprotozoan agents with a novel mechanism of action. Mitochondrial CAs are implicated in de novo lipogenesis, and thus selective inhibitors of such enzymes may be useful for the development of new antiobesity drugs. As tumor metabolism is diverse compared to that of normal cells, ultimately, relevant contributions on the role of the tumor-associated isoforms CA IX and XII in these phenomena have been published and the two isoforms have been validated as novel antitumor/antimetastatic drug targets, with antibodies and small-molecule inhibitors in various stages of clinical development. CAs also play a crucial role in other metabolic processes connected with urea biosynthesis, gluconeogenesis, and so on, since many carboxylation reactions catalyzed by acetyl-coenzyme A carboxylase or pyruvate carboxylase use bicarbonate, not CO2, as a substrate. In organisms other than mammals, e.g., plants, algae, and cyanobacteria, CAs are involved in photosynthesis, whereas in many parasites (fungi, protozoa), they are involved in the de novo synthesis of important metabolites (lipids, nucleic acids, etc.). The metabolic effects related to interference with CA activity, however, have been scarcely investigated. The present Special Issue of Metabolites aims to fill this gap by presenting the latest developments in the field of CAs and their role in metabolism."]