Mahesh Aitha

615 total citations
19 papers, 515 citations indexed

About

Mahesh Aitha is a scholar working on Molecular Medicine, Molecular Biology and Pharmacology. According to data from OpenAlex, Mahesh Aitha has authored 19 papers receiving a total of 515 indexed citations (citations by other indexed papers that have themselves been cited), including 11 papers in Molecular Medicine, 8 papers in Molecular Biology and 4 papers in Pharmacology. Recurrent topics in Mahesh Aitha's work include Antibiotic Resistance in Bacteria (11 papers), Antibiotics Pharmacokinetics and Efficacy (4 papers) and Electron Spin Resonance Studies (3 papers). Mahesh Aitha is often cited by papers focused on Antibiotic Resistance in Bacteria (11 papers), Antibiotics Pharmacokinetics and Efficacy (4 papers) and Electron Spin Resonance Studies (3 papers). Mahesh Aitha collaborates with scholars based in United States, United Kingdom and Japan. Mahesh Aitha's co-authors include Michael W. Crowder, David L. Tierney, Hao Yang, Robert A. Bonomo, Amy R. Marts, Brian Bennett, Stephen J. Benkovic, Mark Hedglin, Mariano M. González and Leticia I. Llarrull and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

Mahesh Aitha

18 papers receiving 513 citations

Peers

Mahesh Aitha

PHARM

EPIDE

Samuel T. Cahill United Kingdom

María‐Natalia Lisa France

Pauline A. Lang United Kingdom

Sara López Spain

J. Spencer United Kingdom

Marianne P. Carey United States

Kathy Johns Canada

Gopal R. Periyannan United States

O.A. Pemberton United States

Jean-Marie Frère Belgium

Samuel T. Cahill United Kingdom

Mahesh Aitha

330 ×0.9

137 ×0.8

143 ×0.9

PHARM

118 ×0.8

147 ×1.4

EPIDE

Citations per year, relative to Mahesh Aitha Mahesh Aitha (= 1×) peers Samuel T. Cahill

Countries citing papers authored by Mahesh Aitha

Since Specialization

Citations

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

Fields of papers citing papers by Mahesh Aitha

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Mahesh Aitha. 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 Mahesh Aitha. The network helps show where Mahesh Aitha may publish in the future.

Co-authorship network of co-authors of Mahesh Aitha

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

All Works

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19 of 19 papers shown

Dranchak, Patricia, Mahesh Aitha, Ravi Tharakan, et al.. (2025). A general assay platform to study protein pharmacology using ligand-dependent structural dynamics. Nature Communications. 16(1). 4342–4342.

Dranchak, Patricia, Mahesh Aitha, Takayuki Katoh, et al.. (2022). Serum-Stable and Selective Backbone-N-Methylated Cyclic Peptides That Inhibit Prokaryotic Glycolytic Mutases. ACS Chemical Biology. 17(8). 2284–2295. 20 indexed citations

Wiedmann, Mareike M., Patricia Dranchak, Mahesh Aitha, et al.. (2021). Structure–activity relationship of ipglycermide binding to phosphoglycerate mutases. Journal of Biological Chemistry. 296. 100628–100628. 6 indexed citations

Hedglin, Mark, Mahesh Aitha, Anthony M. Pedley, & Stephen J. Benkovic. (2019). Replication protein A dynamically regulates monoubiquitination of proliferating cell nuclear antigen. Journal of Biological Chemistry. 294(13). 5157–5168. 22 indexed citations

Cheng, Zishuo, Hao Yang, Mahesh Aitha, et al.. (2017). Probing the Interaction of Aspergillomarasmine A with Metallo-β-lactamases NDM-1, VIM-2, and IMP-7. ACS Infectious Diseases. 4(2). 135–145. 47 indexed citations

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

Hedglin, Mark, Mahesh Aitha, & Stephen J. Benkovic. (2017). Monitoring the Retention of Human Proliferating Cell Nuclear Antigen at Primer/Template Junctions by Proteins That Bind Single-Stranded DNA. Biochemistry. 56(27). 3415–3421. 15 indexed citations

Meng, Fan, et al.. (2016). Biochemical and spectroscopic characterization of the catalytic domain of MMP16 (cdMMP16). JBIC Journal of Biological Inorganic Chemistry. 21(4). 523–535. 1 indexed citations

Aitha, Mahesh, et al.. (2016). Probing substrate binding to the metal binding sites in metallo-β-lactamase L1 during catalysis. MedChemComm. 7(1). 194–201. 6 indexed citations

10.

Aitha, Mahesh, Abraham Moller, Indra D. Sahu, et al.. (2015). Investigating the position of the hairpin loop in New Delhi metallo-β-lactamase, NDM-1, during catalysis and inhibitor binding. Journal of Inorganic Biochemistry. 156. 35–39. 23 indexed citations

11.

Aitha, Mahesh, Lindsay Moritz, Indra D. Sahu, et al.. (2015). Conformational dynamics of metallo-β-lactamase CcrA during catalysis investigated by using DEER spectroscopy. JBIC Journal of Biological Inorganic Chemistry. 20(3). 585–594. 17 indexed citations

12.

Oelschlaeger, Peter, et al.. (2015). Meropenem and Chromacef Intermediates Observed in IMP-25 Metallo-β-Lactamase-Catalyzed Hydrolysis. Antimicrobial Agents and Chemotherapy. 59(7). 4326–4330. 9 indexed citations

13.

Yang, Hao, et al.. (2015). Metal Ion Dependence of the Matrix Metalloproteinase-1 Mechanism. Biochemistry. 54(23). 3631–3639. 12 indexed citations

14.

Aitha, Mahesh, et al.. (2014). Dilution of dipolar interactions in a spin-labeled, multimeric metalloenzyme for DEER studies. Journal of Inorganic Biochemistry. 136. 40–46. 8 indexed citations

15.

Aitha, Mahesh, Amy R. Marts, Abraham Moller, et al.. (2014). Biochemical, Mechanistic, and Spectroscopic Characterization of Metallo-β-lactamase VIM-2. Biochemistry. 53(46). 7321–7331. 53 indexed citations

16.

Yang, Hao, Mahesh Aitha, Amy R. Marts, et al.. (2014). Spectroscopic and Mechanistic Studies of Heterodimetallic Forms of Metallo-β-lactamase NDM-1. Journal of the American Chemical Society. 136(20). 7273–7285. 59 indexed citations

17.

Yang, Ke‐Wu, et al.. (2013). New β-phospholactam as a carbapenem transition state analog: Synthesis of a broad-spectrum inhibitor of metallo-β-lactamases. Bioorganic & Medicinal Chemistry Letters. 23(21). 5855–5859. 25 indexed citations

18.

Hamada, Yahia Z., et al.. (2013). Reactions of Zn2+, Cd2+ and Hg2+ with Free Adenine. 2(2). 77–84. 1 indexed citations

19.

Yang, Hao, et al.. (2012). Mechanistic and Spectroscopic Studies of Metallo-β-lactamase NDM-1. Biochemistry. 51(18). 3839–3847. 86 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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