S
Stefano Mangani
Researcher at University of Siena
Publications - 197
Citations - 6308
Stefano Mangani is an academic researcher from University of Siena. The author has contributed to research in topics: Crystal structure & Active site. The author has an hindex of 41, co-authored 190 publications receiving 5602 citations. Previous affiliations of Stefano Mangani include University of Florence & University of Modena and Reggio Emilia.
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A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis costs two nickels.
Stefano Benini,Wojciech Rypniewski,Keith S. Wilson,Silvia Miletti,Stefano Ciurli,Stefano Mangani +5 more
TL;DR: The mode of binding of the inhibitor, and a comparison between the native and inhibited urease structures, indicate a novel mechanism for enzymatic urea hydrolysis which reconciles the available structural and biochemical data.
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Carbonic anhydrase activators: X-ray crystallographic and spectroscopic investigations for the interaction of isozymes I and II with histamine.
Fabrizio Briganti,Stefano Mangani,Pierluigi Orioli,Andrea Scozzafava,Guido Vernaglione,Claudiu T. Supuran +5 more
TL;DR: X-ray crystallographic data for the adduct of HCA II with histamine showed that the activator molecule is bound at the entrance of the active site cavity in a position where it may actively participate in shuttling protons between the activeSite and the bulk solvent.
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Crystallization of soluble proteins in vapor diffusion for x-ray crystallography
TL;DR: A series of protocols for the crystallization of soluble proteins, especially the difficult ones, tailored for small-scale research groups is provided.
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Structural Insight into Potent Broad-Spectrum Inhibition with Reversible Recyclization Mechanism: Avibactam in Complex with CTX-M-15 and Pseudomonas aeruginosa AmpC β-Lactamases
Sushmita D. Lahiri,Stefano Mangani,Thomas F. Durand-Reville,Manuela Benvenuti,Filomena De Luca,Gautam Sanyal,Jean Denis Docquier +6 more
TL;DR: The structures of two clinically important β-lactamase enzymes bound to avibactam are described and the structures reveal similar binding modes in both enzymes and thus provide a rationale for the broad-spectrum inhibitory activity of avibactsam, which has recently been shown to be a reversible inhibitor.
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A redox switch in CopC: an intriguing copper trafficking protein that binds copper(I) and copper(II) at different sites.
TL;DR: The protein CopC from Pseudomonas syringae has been found capable of binding copper(I) and copper(II) at two different sites, occupied either one at a time or simultaneously, and indicates that CopC can exchange copper between two sites activated by a redox switch.