Diego M. Moreno

960 total citations
40 papers, 738 citations indexed

About

Diego M. Moreno is a scholar working on Molecular Biology, Molecular Medicine and Inorganic Chemistry. According to data from OpenAlex, Diego M. Moreno has authored 40 papers receiving a total of 738 indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 14 papers in Molecular Medicine and 12 papers in Inorganic Chemistry. Recurrent topics in Diego M. Moreno's work include Antibiotic Resistance in Bacteria (14 papers), Metal-Catalyzed Oxygenation Mechanisms (12 papers) and Metal complexes synthesis and properties (8 papers). Diego M. Moreno is often cited by papers focused on Antibiotic Resistance in Bacteria (14 papers), Metal-Catalyzed Oxygenation Mechanisms (12 papers) and Metal complexes synthesis and properties (8 papers). Diego M. Moreno collaborates with scholars based in Argentina, United States and France. Diego M. Moreno's co-authors include Alejandro J. Vila, Sandra Signorella, Verónica Daier, Robert A. Bonomo, Verónica Demicheli, Rafael Radí, Darío A. Estrı́n, Marcelo A. Martí, Claudia Palopoli and María‐Natalia Lisa and has published in prestigious journals such as Journal of Biological Chemistry, Nature Communications and Biochemistry.

In The Last Decade

Diego M. Moreno

39 papers receiving 729 citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name	h						Papers	Cites
Diego M. Moreno Argentina	18	254	237	152	146	102	40	738
Jos J. A. G. Kamps United Kingdom	12	313 1.2×	168 0.7×	39 0.3×	51 0.3×	84 0.8×	21	662
Hans‐Werner Adolph Germany	18	562 2.2×	506 2.1×	24 0.2×	154 1.1×	173 1.7×	21	1.2k
Andrew Fosberry United Kingdom	18	853 3.4×	261 1.1×	49 0.3×	140 1.0×	273 2.7×	26	1.4k
Maria Cristina Cardia Italy	21	297 1.2×	70 0.3×	39 0.3×	66 0.5×	138 1.4×	46	1.1k
David Jung United States	21	538 2.1×	122 0.5×	68 0.4×	205 1.4×	234 2.3×	35	1.5k
Michael Johnston United States	17	500 2.0×	56 0.2×	205 1.3×	120 0.8×	43 0.4×	26	789
Sebastián A. Testero Argentina	16	236 0.9×	196 0.8×	39 0.3×	61 0.4×	122 1.2×	37	812
O. Dideberg Belgium	13	219 0.9×	144 0.6×	55 0.4×	78 0.5×	63 0.6×	53	619
Marcy Hernick United States	14	372 1.5×	55 0.2×	23 0.2×	86 0.6×	32 0.3×	29	699
Vishnu Nayak Badavath India	18	232 0.9×	57 0.2×	25 0.2×	60 0.4×	126 1.2×	50	826

Countries citing papers authored by Diego M. Moreno

Since Specialization

Citations

This map shows the geographic impact of Diego M. Moreno'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 Diego M. Moreno with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Diego M. Moreno more than expected).

Fields of papers citing papers by Diego M. Moreno

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Diego M. Moreno. 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 Diego M. Moreno. The network helps show where Diego M. Moreno may publish in the future.

Co-authorship network of co-authors of Diego M. Moreno

This figure shows the co-authorship network connecting the top 25 collaborators of Diego M. Moreno. A scholar is included among the top collaborators of Diego M. Moreno 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 Diego M. Moreno. Diego M. Moreno is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Tomatis, Pablo E., María F. Mojica, Christopher R. Bethel, et al.. (2025). Cefiderocol “under siege”? Understanding the rise of NDM-mediated resistance to novel agents. Chemical Science. 16(27). 12519–12533. 4 indexed citations

Hinchliffe, Philip, et al.. (2025). Active site loops of membrane-anchored metallo-β-lactamases from environmental bacteria determine cephalosporinase activity. Antimicrobial Agents and Chemotherapy. 69(8). e0191824–e0191824.

Palopoli, Claudia, et al.. (2025). The relative impact of ligand flexibility and redox potential on the activity of Cu superoxide dismutase mimics. Dalton Transactions. 54(10). 4187–4200. 1 indexed citations

Sebastiani, Federico, Diego M. Moreno, Darío A. Estrı́n, et al.. (2024). Proximal ligand tunes active site structure and reactivity in bacterial L. monocytogenes coproheme ferrochelatase. Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy. 313. 124120–124120. 1 indexed citations

Bethel, Christopher R., Yoshikazu Ishii, Diego M. Moreno, et al.. (2024). The interaction of the azetidine thiazole side chain with the active site loop (ASL) 3 drives the evolution of IMP metallo-β-lactamase against tebipenem. Antimicrobial Agents and Chemotherapy. 68(8). e0068724–e0068724. 2 indexed citations

Mojica, María F., Philip Hinchliffe, V. Rodríguez Martínez, et al.. (2024). Rational Design of Benzobisheterocycle Metallo-β-Lactamase Inhibitors: A Tricyclic Scaffold Enhances Potency against Target Enzymes. Journal of Medicinal Chemistry. 67(5). 3795–3812. 1 indexed citations

Mojica, María F., Christopher R. Bethel, Yoshikazu Ishii, et al.. (2024). Structural role of K224 in taniborbactam inhibition of NDM-1. Antimicrobial Agents and Chemotherapy. 68(2). e0133223–e0133223. 9 indexed citations

Zanor, María Inés, et al.. (2023). Selective inhibition of the amyloid matrix of Escherichia coli biofilms by a bifunctional microbial metabolite. npj Biofilms and Microbiomes. 9(1). 81–81. 10 indexed citations

Terrier, Christophe Le, et al.. (2023). Structural basis of metallo-β-lactamase resistance to taniborbactam. Antimicrobial Agents and Chemotherapy. 68(2). e0116823–e0116823. 20 indexed citations

10.

Moreno, Diego M., et al.. (2023). Updates on moleculARweb, the Swiss Portal for Chemistry and Structural Biology Education Using Augmented and now also Virtual Reality. CHIMIA International Journal for Chemistry. 77(4). 264–264. 3 indexed citations

11.

Mojica, María F., Christopher R. Bethel, Yoshikazu Ishii, et al.. (2023). 2178. Resistance to Cefepime/Taniborbactam in NDM-1 -Are We Losing the Battle against MDROs?. Open Forum Infectious Diseases. 10(Supplement_2). 1 indexed citations

12.

Orio, Andrea G. Albarracín, Pablo E. Tomatis, Diego M. Moreno, et al.. (2022). Longitudinal Evolution of the Pseudomonas-Derived Cephalosporinase (PDC) Structure and Activity in a Cystic Fibrosis Patient Treated with β-Lactams. mBio. 13(5). e0166322–e0166322. 17 indexed citations

13.

Hinchliffe, Philip, Diego M. Moreno, María F. Mojica, et al.. (2021). 2-Mercaptomethyl Thiazolidines (MMTZs) Inhibit All Metallo-β-Lactamase Classes by Maintaining a Conserved Binding Mode. ACS Infectious Diseases. 7(9). 2697–2706. 15 indexed citations

14.

Chorostecki, Uciel, Julieta L. Mateos, Nicolás G. Bologna, et al.. (2020). Identification of key sequence features required for microRNA biogenesis in plants. Nature Communications. 11(1). 5320–5320. 29 indexed citations

15.

Inda, María Eugenia, et al.. (2020). A Transmembrane Histidine Kinase Functions as a pH Sensor. Biomolecules. 10(8). 1183–1183. 9 indexed citations

16.

Daier, Verónica, et al.. (2018). Using theoretical calculations to predict the redox potential of mononuclear manganese complexes. New Journal of Chemistry. 42(18). 14827–14831. 1 indexed citations

17.

Palopoli, Claudia, Verónica Daier, Éric Rivière, et al.. (2018). Tuning the MnII2/MnIII2 redox cycle of a phenoxo-bridged diMn catalase mimic with terminal carboxylate donors. Journal of Inorganic Biochemistry. 182. 29–36. 8 indexed citations

18.

Lisa, María‐Natalia, Mahesh Aitha, Mariano M. González, et al.. (2017). A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases. Nature Communications. 8(1). 538–538. 105 indexed citations

19.

Moreno, Diego M., et al.. (2014). Host-Specific Enzyme-Substrate Interactions in SPM-1 Metallo-β-Lactamase Are Modulated by Second Sphere Residues. PLoS Pathogens. 10(1). e1003817–e1003817. 30 indexed citations

20.

Rudzka, K., Diego M. Moreno, Betty Eipper, et al.. (2012). Coordination of peroxide to the CuM center of peptidylglycine α-hydroxylating monooxygenase (PHM): structural and computational study. JBIC Journal of Biological Inorganic Chemistry. 18(2). 223–232. 23 indexed citations

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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