M. Prabu-Jeyabalan

2.1k total citations
19 papers, 1.7k citations indexed

About

M. Prabu-Jeyabalan is a scholar working on Infectious Diseases, Virology and Molecular Biology. According to data from OpenAlex, M. Prabu-Jeyabalan has authored 19 papers receiving a total of 1.7k indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Infectious Diseases, 18 papers in Virology and 9 papers in Molecular Biology. Recurrent topics in M. Prabu-Jeyabalan's work include HIV Research and Treatment (18 papers), HIV/AIDS drug development and treatment (18 papers) and Biochemical and Molecular Research (6 papers). M. Prabu-Jeyabalan is often cited by papers focused on HIV Research and Treatment (18 papers), HIV/AIDS drug development and treatment (18 papers) and Biochemical and Molecular Research (6 papers). M. Prabu-Jeyabalan collaborates with scholars based in United States, Japan and Türkiye. M. Prabu-Jeyabalan's co-authors include Celia A. Schiffer, E.A. Nalivaika, Nancy M. P. King, Piet Wigerinck, Marie‐Pierre de Béthune, M.N.L. Nalam, R.M. Bandaranayake, Geert Pille, Anik Peeters and Rudi Pauwels and has published in prestigious journals such as Journal of Molecular Biology, Journal of Virology and Journal of Medicinal Chemistry.

In The Last Decade

M. Prabu-Jeyabalan

19 papers receiving 1.6k citations

Peers

M. Prabu-Jeyabalan
E.A. Nalivaika United States
Debananda Das United States
Manos Perros United Kingdom
Sergei Gulnik United States
M.N.L. Nalam United States
William E. Kohlbrenner United States
Sudthida Vasavanonda United States
Jill C. Heimbach United States
Yasuhiro Koh United States
Linda Selk United States
E.A. Nalivaika United States
M. Prabu-Jeyabalan
Citations per year, relative to M. Prabu-Jeyabalan M. Prabu-Jeyabalan (= 1×) peers E.A. Nalivaika

Countries citing papers authored by M. Prabu-Jeyabalan

Since Specialization
Citations

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

Fields of papers citing papers by M. Prabu-Jeyabalan

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by M. Prabu-Jeyabalan. 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 M. Prabu-Jeyabalan. The network helps show where M. Prabu-Jeyabalan may publish in the future.

Co-authorship network of co-authors of M. Prabu-Jeyabalan

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

All Works

19 of 19 papers shown
1.
Mittal, Seema, Nancy M. P. King, M. Prabu-Jeyabalan, et al.. (2013). Structural and Thermodynamic Basis of Amprenavir/Darunavir and Atazanavir Resistance in HIV-1 Protease with Mutations at Residue 50. Journal of Virology. 87(8). 4176–4184. 23 indexed citations
2.
Tan‐Wilson, Anna L., et al.. (2012). The PA domain is crucial for determining optimum substrate length for soybean protease C1: Structure and kinetics correlate with molecular function. Plant Physiology and Biochemistry. 53. 27–32. 21 indexed citations
3.
King, Nancy M. P., M. Prabu-Jeyabalan, R.M. Bandaranayake, et al.. (2012). Extreme Entropy–Enthalpy Compensation in a Drug-Resistant Variant of HIV-1 Protease. ACS Chemical Biology. 7(9). 1536–1546. 72 indexed citations
4.
Ali, Akbar, R.M. Bandaranayake, Yufeng Cai, et al.. (2010). Molecular Basis for Drug Resistance in HIV-1 Protease. Viruses. 2(11). 2509–2535. 113 indexed citations
5.
Bandaranayake, R.M., M. Prabu-Jeyabalan, Junko Kakizawa, Wataru Sugiura, & Celia A. Schiffer. (2008). Structural Analysis of Human Immunodeficiency Virus Type 1 CRF01_AE Protease in Complex with the Substrate p1-p6. Journal of Virology. 82(13). 6762–6766. 14 indexed citations
6.
Altman, Michael D., E.A. Nalivaika, M. Prabu-Jeyabalan, Celia A. Schiffer, & Bruce Tidor. (2007). Computational design and experimental study of tighter binding peptides to an inactivated mutant of HIV‐1 protease. Proteins Structure Function and Bioinformatics. 70(3). 678–694. 38 indexed citations
7.
Prabu-Jeyabalan, M., E.A. Nalivaika, Keith P. Romano, & Celia A. Schiffer. (2006). Mechanism of Substrate Recognition by Drug-Resistant Human Immunodeficiency Virus Type 1 Protease Variants Revealed by a Novel Structural Intermediate. Journal of Virology. 80(7). 3607–3616. 43 indexed citations
8.
Prabu-Jeyabalan, M., et al.. (2006). Role of Invariant Thr80 in Human Immunodeficiency Virus Type 1 Protease Structure, Function, and Viral Infectivity. Journal of Virology. 80(14). 6906–6916. 30 indexed citations
9.
Prabu-Jeyabalan, M., Nancy M. P. King, E.A. Nalivaika, et al.. (2006). Substrate Envelope and Drug Resistance: Crystal Structure of RO1 in Complex with Wild-Type Human Immunodeficiency Virus Type 1 Protease. Antimicrobial Agents and Chemotherapy. 50(4). 1518–1521. 28 indexed citations
10.
Surleraux, Dominique, Geert Pille, Louis Maes, et al.. (2005). Design of HIV-1 Protease Inhibitors Active on Multidrug-Resistant Virus. Journal of Medicinal Chemistry. 48(6). 1965–1973. 59 indexed citations
11.
King, Nancy M. P., M. Prabu-Jeyabalan, E.A. Nalivaika, & Celia A. Schiffer. (2004). Combating Susceptibility to Drug ResistanceLessons from HIV-1 Protease. Chemistry & Biology. 11(10). 1333–1338. 54 indexed citations
12.
King, Nancy M. P., M. Prabu-Jeyabalan, E.A. Nalivaika, & Celia A. Schiffer. (2004). Combating Susceptibility to Drug Resistance. Chemistry & Biology. 11(10). 1333–1338. 116 indexed citations
13.
Surleraux, Dominique, Abdellah Tahri, Geert Pille, et al.. (2004). Discovery and Selection of TMC114, a Next Generation HIV-1 Protease Inhibitor. Journal of Medicinal Chemistry. 48(6). 1813–1822. 199 indexed citations
14.
Prabu-Jeyabalan, M., E.A. Nalivaika, Nancy M. P. King, & Celia A. Schiffer. (2004). Structural Basis for Coevolution of a Human Immunodeficiency Virus Type 1 Nucleocapsid-p1 Cleavage Site with a V82A Drug-Resistant Mutation in Viral Protease. Journal of Virology. 78(22). 12446–12454. 84 indexed citations
15.
King, Nancy M. P., M. Prabu-Jeyabalan, E.A. Nalivaika, et al.. (2004). Structural and Thermodynamic Basis for the Binding of TMC114, a Next-Generation Human Immunodeficiency Virus Type 1 Protease Inhibitor. Journal of Virology. 78(21). 12012–12021. 191 indexed citations
16.
Prabu-Jeyabalan, M., E.A. Nalivaika, & Celia A. Schiffer. (2002). Substrate Shape Determines Specificity of Recognition for HIV-1 Protease. Structure. 10(3). 369–381. 262 indexed citations
17.
King, Nancy M. P., M. Prabu-Jeyabalan, E.A. Nalivaika, et al.. (2002). Lack of synergy for inhibitors targeting a multi‐drug‐resistant HIV‐1 protease. Protein Science. 11(2). 418–429. 88 indexed citations
18.
Prabu-Jeyabalan, M., E.A. Nalivaika, Nancy M. P. King, & Celia A. Schiffer. (2002). Viability of a Drug-Resistant Human Immunodeficiency Virus Type 1 Protease Variant: Structural Insights for Better Antiviral Therapy. Journal of Virology. 77(2). 1306–1315. 94 indexed citations
19.
Prabu-Jeyabalan, M., E.A. Nalivaika, & Celia A. Schiffer. (2000). How does a symmetric dimer recognize an asymmetric substrate? a substrate complex of HIV-1 protease. Journal of Molecular Biology. 301(5). 1207–1220. 144 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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