Giuseppina De Simone
www.ibb.cnr.it
0000-0001-9783-5431
94 papers found
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Hydrophobic Substituents of the Phenylmethylsulfamide Moiety Can Be Used for the Development of New Selective Carbonic Anhydrase Inhibitors
Sulfolobus solfataricus thiol redox puzzle: characterization of an atypical protein disulfide oxidoreductase
Hypoxia-Targeting Carbonic Anhydrase IX Inhibitors by a New Series of Nitroimidazole-Sulfonamides/Sulfamides/Sulfamates
Thermal-Stable Carbonic Anhydrases: A Structural Overview
X-ray structure of the first `extremo-α-carbonic anhydrase', a dimeric enzyme from the thermophilic bacteriumSulfurihydrogenibium yellowstonenseYO3AOP1
Anticancer carbonic anhydrase inhibitors: a patent review (2008 – 2013)
Exploiting the hydrophobic and hydrophilic binding sites for designing carbonic anhydrase inhibitors
Faox enzymes inhibited Maillard reaction development during storage both in protein glucose model system and low lactose UHT milk
Kinetic and anion inhibition studies of a β-carbonic anhydrase (FbiCA 1) from the C4 plant Flaveria bidentis
Characterization of Carbonic Anhydrase IX Interactome Reveals Proteins Assisting Its Nuclear Localization in Hypoxic Cells
Development of Potent Carbonic Anhydrase Inhibitors Incorporating Both Sulfonamide and Sulfamide Groups
(In)organic anions as carbonic anhydrase inhibitors
Multiple Binding Modes of Inhibitors to Carbonic Anhydrases: How to Design Specific Drugs Targeting 15 Different Isoforms?
Structural and inhibition insights into carbonic anhydrase CDCA1 from the marine diatom Thalassiosira weissflogii
Carbonic Anhydrase IX as a Target for Designing Novel Anticancer Drugs
Carbonic anhydrase VII is S-glutathionylated without loss of catalytic activity and affinity for sulfonamide inhibitors
Editorial [ Hot Topic-II: Zinc Metallo-Enzymes as Target for Drug Design (Guest Editor: Giuseppina De Simone )]
Hydroxamate represents a versatile zinc binding group for the development of new carbonic anhydrase inhibitors
Carbonic anhydrase inhibitors: X-ray crystallographic studies for the binding of N-substituted benzenesulfonamides to human isoform II
Recent Advances in Structural Studies of the Carbonic Anhydrase Family: The Crystal Structure of Human CA IX and CA XIII
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