Johnson Agniswamy

1.6k total citations
55 papers, 1.3k citations indexed

About

Johnson Agniswamy is a scholar working on Infectious Diseases, Virology and Epidemiology. According to data from OpenAlex, Johnson Agniswamy has authored 55 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 40 papers in Infectious Diseases, 35 papers in Virology and 17 papers in Epidemiology. Recurrent topics in Johnson Agniswamy's work include HIV/AIDS drug development and treatment (38 papers), HIV Research and Treatment (35 papers) and Pneumocystis jirovecii pneumonia detection and treatment (17 papers). Johnson Agniswamy is often cited by papers focused on HIV/AIDS drug development and treatment (38 papers), HIV Research and Treatment (35 papers) and Pneumocystis jirovecii pneumonia detection and treatment (17 papers). Johnson Agniswamy collaborates with scholars based in United States, Japan and Armenia. Johnson Agniswamy's co-authors include Irene T. Weber, Arun K. Ghosh, Hiroaki Mitsuya, John M. Louis, Bin Fang, Robert W. Harrison, Masayuki Amano, Yuan‐Fang Wang, Jane M. Sayer and Yuan-Fang Wang and has published in prestigious journals such as Journal of Biological Chemistry, PLoS ONE and Biochemistry.

In The Last Decade

Johnson Agniswamy

54 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Johnson Agniswamy United States	24	745	601	446	304	180	55	1.3k
M.N.L. Nalam United States	21	689 0.9×	577 1.0×	658 1.5×	208 0.7×	127 0.7×	21	1.3k
K. E. B. PARKES United Kingdom	15	640 0.9×	513 0.9×	632 1.4×	400 1.3×	204 1.1×	32	1.4k
Simon Cocklin United States	28	891 1.2×	829 1.4×	942 2.1×	394 1.3×	141 0.8×	73	2.1k
Karen A. Kirby United States	26	1.2k 1.6×	1.1k 1.7×	585 1.3×	249 0.8×	424 2.4×	61	1.8k
Masayuki Amano Japan	24	946 1.3×	736 1.2×	313 0.7×	465 1.5×	274 1.5×	72	1.5k
Zhengqiang Wang United States	28	943 1.3×	731 1.2×	741 1.7×	684 2.3×	461 2.6×	84	2.0k
William E. Kohlbrenner United States	19	924 1.2×	695 1.2×	774 1.7×	521 1.7×	353 2.0×	34	1.9k
John H. Merrett United Kingdom	8	684 0.9×	499 0.8×	429 1.0×	293 1.0×	252 1.4×	10	1.2k
Boshi Huang China	23	724 1.0×	570 0.9×	624 1.4×	669 2.2×	396 2.2×	69	1.7k
Sally Redshaw United Kingdom	11	715 1.0×	594 1.0×	503 1.1×	376 1.2×	104 0.6×	26	1.3k

Countries citing papers authored by Johnson Agniswamy

Since Specialization

Citations

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

Fields of papers citing papers by Johnson Agniswamy

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Johnson Agniswamy

This figure shows the co-authorship network connecting the top 25 collaborators of Johnson Agniswamy. A scholar is included among the top collaborators of Johnson Agniswamy 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 Johnson Agniswamy. Johnson Agniswamy 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

Ghosh, Arun K., Arun K. Ghosh, Megan Johnson, et al.. (2023). Exploration of imatinib and nilotinib-derived templates as the P2-Ligand for HIV-1 protease inhibitors: Design, synthesis, protein X-ray structural studies, and biological evaluation. European Journal of Medicinal Chemistry. 255. 115385–115385. 4 indexed citations

Ghosh, Arun K., Dana Shahabi, Megan Johnson, et al.. (2023). Evaluation of darunavir-derived HIV-1 protease inhibitors incorporating P2′ amide-derivatives: Synthesis, biological evaluation and structural studies. Bioorganic & Medicinal Chemistry Letters. 83. 129168–129168. 3 indexed citations

Ghosh, Arun K., Arun K. Ghosh, Dana Shahabi, et al.. (2022). Design, Synthesis and X‐Ray Structural Studies of Potent HIV‐1 Protease Inhibitors Containing C‐4 Substituted Tricyclic Hexahydro‐Furofuran Derivatives as P2 Ligands. ChemMedChem. 17(9). e202200058–e202200058. 5 indexed citations

Iyer, Archana, et al.. (2021). Discovery of a new flavin N5-adduct in a tyrosine to phenylalanine variant of d-Arginine dehydrogenase. Archives of Biochemistry and Biophysics. 715. 109100–109100. 1 indexed citations

Agniswamy, Johnson, Daniel W. Kneller, Arun K. Ghosh, & Irene T. Weber. (2021). Novel HIV PR inhibitors with C4-substituted bis-THF and bis-fluoro-benzyl target the two active site mutations of highly drug resistant mutant PRS17. Biochemical and Biophysical Research Communications. 566. 30–35. 6 indexed citations

Ghosh, Arun K., Heather L. Osswald, Masayuki Amano, et al.. (2020). Structure-Based Design of Highly Potent HIV-1 Protease Inhibitors Containing New Tricyclic Ring P2-Ligands: Design, Synthesis, Biological, and X-ray Structural Studies. Journal of Medicinal Chemistry. 63(9). 4867–4879. 22 indexed citations

Pawar, Shrikant, Yuan‐Fang Wang, Johnson Agniswamy, et al.. (2019). Structural studies of antiviral inhibitor with HIV-1 protease bearing drug resistant substitutions of V32I, I47V and V82I. Biochemical and Biophysical Research Communications. 514(3). 974–978. 17 indexed citations

Kneller, Daniel W., Johnson Agniswamy, Arun K. Ghosh, & Irene T. Weber. (2019). Potent antiviral HIV-1 protease inhibitor combats highly drug resistant mutant PR20. Biochemical and Biophysical Research Communications. 519(1). 61–66. 13 indexed citations

Agniswamy, Johnson, et al.. (2018). Crystal structure of yeast nitronate monooxygenase from Cyberlindnera saturnus. Proteins Structure Function and Bioinformatics. 86(5). 599–605. 7 indexed citations

10.

Ghosh, Arun K., Prasanth R. Nyalapatla, Kalapala Venkateswara Rao, et al.. (2018). Design and Synthesis of Highly Potent HIV-1 Protease Inhibitors Containing Tricyclic Fused Ring Systems as Novel P2 Ligands: Structure–Activity Studies, Biological and X-ray Structural Analysis. Journal of Medicinal Chemistry. 61(10). 4561–4577. 32 indexed citations

11.

Agniswamy, Johnson, et al.. (2018). Steric hindrance controls pyridine nucleotide specificity of a flavin‐dependent NADH:quinone oxidoreductase. Protein Science. 28(1). 167–175. 7 indexed citations

12.

Ghosh, Arun K., Shin-ichiro Hattori, Hironori Hayashi, et al.. (2018). Design and Synthesis of Potent HIV-1 Protease Inhibitors Containing Bicyclic Oxazolidinone Scaffold as the P2 Ligands: Structure–Activity Studies and Biological and X-ray Structural Studies. Journal of Medicinal Chemistry. 61(21). 9722–9737. 26 indexed citations

13.

Ghosh, Arun K., Margherita Brindisi, Prasanth R. Nyalapatla, et al.. (2017). Design of novel HIV-1 protease inhibitors incorporating isophthalamide-derived P2-P3 ligands: Synthesis, biological evaluation and X-ray structural studies of inhibitor-HIV-1 protease complex. Bioorganic & Medicinal Chemistry. 25(19). 5114–5127. 14 indexed citations

14.

Agniswamy, Johnson, John M. Louis, Julien Roche, Robert W. Harrison, & Irene T. Weber. (2016). Structural Studies of a Rationally Selected Multi-Drug Resistant HIV-1 Protease Reveal Synergistic Effect of Distal Mutations on Flap Dynamics. PLoS ONE. 11(12). e0168616–e0168616. 37 indexed citations

15.

Agniswamy, Johnson, Hongling Yuan, Rudy Pelicaen, et al.. (2014). The Combined Structural and Kinetic Characterization of a Bacterial Nitronate Monooxygenase from Pseudomonas aeruginosa PAO1 Establishes NMO Class I and II. Journal of Biological Chemistry. 289(34). 23764–23775. 32 indexed citations

16.

Sayer, Jane M., Johnson Agniswamy, Irene T. Weber, & John M. Louis. (2010). Autocatalytic maturation, physical/chemical properties, and crystal structure of group N HIV‐1 protease: Relevance to drug resistance. Protein Science. 19(11). 2055–2072. 22 indexed citations

17.

Ghosh, Arun K., Chunxiao Xu, Kalapala Venkateswara Rao, et al.. (2010). Probing Multidrug‐Resistance and Protein–Ligand Interactions with Oxatricyclic Designed Ligands in HIV‐1 Protease Inhibitors. ChemMedChem. 5(11). 1850–1854. 44 indexed citations

18.

Radaev, Sergei, Johnson Agniswamy, & Peter D. Sun. (2009). A case of structure determination using pseudosymmetry. Acta Crystallographica Section D Biological Crystallography. 65(12). 1334–1340. 2 indexed citations

19.

Agniswamy, Johnson, Bin Fang, & Irene T. Weber. (2009). Conformational similarity in the activation of caspase-3 and -7 revealed by the unliganded and inhibited structures of caspase-7. APOPTOSIS. 14(10). 1135–1144. 24 indexed citations

20.

Chumanevich, Alexander A., et al.. (2008). Structural basis for executioner caspase recognition of P5 position in substrates. APOPTOSIS. 13(11). 1291–1302. 29 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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