Manuela Benvenuti
About
Manuela Benvenuti is a scholar working on Molecular Medicine, Molecular Biology and Materials Chemistry.
According to data from OpenAlex, Manuela Benvenuti has authored 37 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 13 papers in Molecular Medicine, 11 papers in Molecular Biology and 9 papers in Materials Chemistry. Recurrent topics in Manuela Benvenuti's work include Antibiotic Resistance in Bacteria (13 papers), Enzyme Structure and Function (9 papers) and Electrospun Nanofibers in Biomedical Applications (6 papers). Manuela Benvenuti is often cited by papers focused on Antibiotic Resistance in Bacteria (13 papers), Enzyme Structure and Function (9 papers) and Electrospun Nanofibers in Biomedical Applications (6 papers). Manuela Benvenuti collaborates with scholars based in Italy, United States and France. Manuela Benvenuti's co-authors include Stefano Mangani, Jean‐Denis Docquier, Filomena De Luca, Gian María Rossolini, V. Calderone, Thomas F. Durand-Réville, Sushmita D. Lahiri, Cecilia Pozzi, Rolando Barbucci and Gautam Sanyal and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.
In The Last Decade
Manuela Benvenuti
37 papers receiving 1.3k citations
Peers
Manuela Benvenuti
Peter Oelschlaeger United States
Christian Damblon Belgium
M. Galleni Belgium
Donatella Tondi Italy
A.P. Kuzin United States
Christian Hubschwerlen Switzerland
Cecilia Pozzi Italy
Hidenori Yoshizawa Japan
Mekhala Pati United States
Adriana Badarau United Kingdom
Citations per year, relative to Manuela Benvenuti Manuela Benvenuti (= 1×)
peers
Peter Oelschlaeger
Countries citing papers authored by Manuela Benvenuti
Since
Specialization
Citations
This map shows the geographic impact of Manuela Benvenuti's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Manuela Benvenuti with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Manuela Benvenuti more than expected).
Fields of papers citing papers by Manuela Benvenuti
Since
Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences
This network shows the impact of papers produced by Manuela Benvenuti. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Manuela Benvenuti. The network helps show where Manuela Benvenuti may publish in the future.
Co-authorship network of co-authors of Manuela Benvenuti
This figure shows the co-authorship network connecting the top 25 collaborators of Manuela Benvenuti. A scholar is included among the top collaborators of Manuela Benvenuti based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Manuela Benvenuti. Manuela Benvenuti is excluded from the visualization to improve readability, since they are connected to all nodes in the network.
All Works
1.
Hernandez, Jean‐François, Filomena Sannio, Manuela Benvenuti, et al.. (2021). 1,2,4-Triazole-3-thione compounds with a 4-ethyl alkyl/aryl sulfide substituent are broad-spectrum metallo-β-lactamase inhibitors with re-sensitization activity. European Journal of Medicinal Chemistry. 226. 113873–113873.
2.
Liu, Bin, Robert E. Lee Trout, Guo‐Hua Chu, et al.. (2019). Discovery of Taniborbactam (VNRX-5133): A Broad-Spectrum Serine- and Metallo-β-lactamase Inhibitor for Carbapenem-Resistant Bacterial Infections. Journal of Medicinal Chemistry. 63(6). 2789–2801.
3.
Pozzi, Cecilia, F. Di Pisa, Manuela Benvenuti, & Stefano Mangani. (2018). The structure of the human glutaminyl cyclase–SEN177 complex indicates routes for developing new potent inhibitors as possible agents for the treatment of neurological disorders. JBIC Journal of Biological Inorganic Chemistry. 23(8). 1219–1226.
4.
Pisa, F. Di, Cecilia Pozzi, Manuela Benvenuti, et al.. (2017). Boric acid and acetate anion binding to subclass B3 metallo-β-lactamase BJP-1 provides clues for mechanism of action and inhibitor design. Inorganica Chimica Acta. 470. 331–341.
5.
Pisa, F. Di, et al.. (2015). The soluble Y115E–Y117E variant of human glutaminyl cyclase is a valid target for X-ray and NMR screening of inhibitors against Alzheimer disease. Acta Crystallographica Section F Structural Biology Communications. 71(8). 986–992.
6.
Lahiri, Sushmita D., Stefano Mangani, Haris Jahić, et al.. (2014). Molecular Basis of Selective Inhibition and Slow Reversibility of Avibactam against Class D Carbapenemases: A Structure-Guided Study of OXA-24 and OXA-48. ACS Chemical Biology. 10(2). 591–600.
7.
Docquier, Jean‐Denis, Manuela Benvenuti, V. Calderone, Gian María Rossolini, & Stefano Mangani. (2011). Structure of the extended-spectrum β-lactamase TEM-72 inhibited by citrate. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67(3). 303–306.
8.
Luca, Filomena De, Manuela Benvenuti, Filippo Carboni, et al.. (2011). Evolution to carbapenem-hydrolyzing activity in noncarbapenemase class D β-lactamase OXA-10 by rational protein design. Proceedings of the National Academy of Sciences. 108(45). 18424–18429.
9.
Docquier, Jean‐Denis, V. Calderone, Filomena De Luca, et al.. (2009). Crystal Structure of the OXA-48 β-Lactamase Reveals Mechanistic Diversity among Class D Carbapenemases. Chemistry & Biology. 16(5). 540–547.
10.
Leone, R., et al.. (2008). Structural Insights into the Catalytic Mechanism of the Bacterial Class B Phosphatase AphA Belonging to the DDDD Superfamily of Phosphohydrolases. Journal of Molecular Biology. 384(2). 478–488.
11.
Mangani, Stefano, Manuela Benvenuti, Arthur J.G. Moir, et al.. (2006). Characterization of the metallocenter of rabbit skeletal muscle AMP deaminase. Evidence for a dinuclear zinc site. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1774(2). 312–322.
12.
Calderone, V., et al.. (2005). A Structure-based Proposal for the Catalytic Mechanism of the Bacterial Acid Phosphatase AphA belonging to the DDDD Superfamily of Phosphohydrolases. Journal of Molecular Biology. 355(4). 708–721.
13.
Benvenuti, Manuela, V. Calderone, Serena Schippa, et al.. (2003). Expression, purification, crystallization and preliminary X-ray characterization of the class B acid phosphatase (AphA) fromEscherichia coli. Acta Crystallographica Section D Biological Crystallography. 59(6). 1058–1060.
14.
Arnesano, Fabio, Lucia Banci, Manuela Benvenuti, et al.. (2003). The Evolutionarily Conserved Trimeric Structure of CutA1 Proteins Suggests a Role in Signal Transduction. Journal of Biological Chemistry. 278(46). 45999–46006.
15.
Calderone, V., et al.. (2003). The First Structure of a Bacterial Class B Acid Phosphatase Reveals Further Structural Heterogeneity Among Phosphatases of the Haloacid Dehalogenase Fold. Journal of Molecular Biology. 335(3). 761–773.
16.
Ranieri-Raggi, Maria, Antonio Raggi, Daniela Martini, Manuela Benvenuti, & Stefano Mangani. (2002). XAS of dilute biological samples. Journal of Synchrotron Radiation. 10(1). 69–70.
17.
Benvenuti, Manuela, et al.. (1999). Crystallization and preliminary crystallographic analysis of the hydroxyquinol 1,2-dioxygenase from Nocardioides simplex 3E: a novel dioxygenase involved in the biodegradation of polychlorinated aromatic compounds. Acta Crystallographica Section D Biological Crystallography. 55(4). 901–903.
18.
Barbucci, Rolando, et al.. (1989). Synthesis and physicochemical characterization of a new material (PUPA) based on polyurethane and poly(amido-amine) components capable of strongly adsorbing quantities of heparin. Biomaterials. 10(5). 299–308.
19.
Barbucci, Rolando, et al.. (1987). A material (PUPA) presenting both the properties of polyurethanes and the capacity of adsorbing a high quantity of heparin. Biomaterials. 8(4). 306–310.
20.
Barbucci, Rolando, et al.. (1985). Heparinizable materials (IV). Surface-grafting on poly(ethylene terephthalate) of heparin-complexing poly(amido-amine) chains. Biomaterials. 6(2). 102–104.
Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.
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