What is he best known for?
The fields of study he is best known for:
Stefano Mangani mainly investigates Crystallography, Active site, Crystal structure, Biochemistry and Stereochemistry.
His Crystallography research includes elements of Adduct, Molecule, Metal, Copper and Protein structure.
His Active site study combines topics in areas such as Hydrolase, Metal ions in aqueous solution and Urease.
His work in Crystal structure tackles topics such as Inorganic chemistry which are related to areas like Nickel, Ferrous, Ferritin and Ceruloplasmin.
His work on Binding site, Cytochrome c oxidase and Transport protein as part of general Biochemistry research is often related to Bacterial genome size, thus linking different fields of science.
His study looks at the relationship between Stereochemistry and fields such as Enzyme, as well as how they intersect with chemical problems.
His most cited work include:
- 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. (318 citations)
- Carbonic anhydrase activators: X-ray crystallographic and spectroscopic investigations for the interaction of isozymes I and II with histamine. (212 citations)
- Crystallization of soluble proteins in vapor diffusion for x-ray crystallography (139 citations)
What are the main themes of his work throughout his whole career to date?
His scientific interests lie mostly in Crystallography, Stereochemistry, Crystal structure, Biochemistry and Enzyme.
His Crystallography study incorporates themes from Inorganic chemistry, Zinc, Ligand, Molecule and Copper.
His work in Stereochemistry addresses subjects such as Active site, which are connected to disciplines such as Urease.
His work in Crystal structure addresses issues such as Nickel, which are connected to fields such as Diastereomer.
He studies Hydrolase which is a part of Enzyme.
His Hydrolase research is multidisciplinary, incorporating perspectives in Matrix metalloproteinase, Beta-lactamase and Protein quaternary structure.
He most often published in these fields:
- Crystallography (44.44%)
- Stereochemistry (36.00%)
- Crystal structure (31.11%)
What were the highlights of his more recent work (between 2016-2021)?
- Enzyme (25.33%)
- Biochemistry (28.00%)
- Drug discovery (4.44%)
In recent papers he was focusing on the following fields of study:
His primary scientific interests are in Enzyme, Biochemistry, Drug discovery, Crystallography and Trypanosoma brucei.
Stefano Mangani combines subjects such as Drug, Pseudomonas aeruginosa, Bacteria, Stereochemistry and In vivo with his study of Enzyme.
His Pseudomonas aeruginosa research incorporates themes from Protein structure, Peptide sequence, Hydrolase and Serine.
Many of his studies involve connections with topics such as Bacterial outer membrane and Stereochemistry.
His work in the fields of Biochemistry, such as Transferase, Cofactor, Protein engineering and Protein family, intersects with other areas such as Antifolate.
Stefano Mangani performs multidisciplinary study on Crystallography and Biomineralization in his works.
Between 2016 and 2021, his most popular works were:
- An update on β-lactamase inhibitor discovery and development (87 citations)
- Discovery of Taniborbactam (VNRX-5133): A Broad-Spectrum Serine- And Metallo-β-lactamase Inhibitor for Carbapenem-Resistant Bacterial Infections (49 citations)
- VNRX-5133 (Taniborbactam), a broad-spectrum inhibitor of serine- And metallo-β-lactamases, restores activity of cefepime in enterobacterales and Pseudomonas aeruginosa (37 citations)
In his most recent research, the most cited papers focused on:
Enzyme, Biochemistry, Antibiotics, Microbiology and Pseudomonas aeruginosa are his primary areas of study.
The concepts of his Enzyme study are interwoven with issues in Stereochemistry and In vivo.
His Stereochemistry study frequently draws parallels with other fields, such as Drug.
His work on Trypanosoma brucei and Drug discovery as part of general Biochemistry research is frequently linked to Pteridine reductase, thereby connecting diverse disciplines of science.
His research integrates issues of Carbapenem-resistant enterobacteriaceae and Serine in his study of Microbiology.
His study in Bacteria is interdisciplinary in nature, drawing from both Hydrolase, Peptide sequence, Avibactam and Protein structure.
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