Joma Joy

920 total citations
26 papers, 540 citations indexed

About

Joma Joy is a scholar working on Molecular Biology, Public Health, Environmental and Occupational Health and Infectious Diseases. According to data from OpenAlex, Joma Joy has authored 26 papers receiving a total of 540 indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 11 papers in Public Health, Environmental and Occupational Health and 9 papers in Infectious Diseases. Recurrent topics in Joma Joy's work include Mosquito-borne diseases and control (11 papers), Viral Infections and Vectors (6 papers) and Click Chemistry and Applications (4 papers). Joma Joy is often cited by papers focused on Mosquito-borne diseases and control (11 papers), Viral Infections and Vectors (6 papers) and Click Chemistry and Applications (4 papers). Joma Joy collaborates with scholars based in Singapore, Germany and China. Joma Joy's co-authors include Jeffrey Hill, C. S. Brian Chia, Tad A. Holak, John Liang Kuan Wee, Sudipta Majumdar, Heiko Hermeking, Grzegorz M. Popowicz, Melgious Jin Yan Ang, Anders Poulsen and CongBao Kang and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

Joma Joy

26 papers receiving 537 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Joma Joy Singapore 12 289 197 126 98 51 26 540
Kah Fei Wan Singapore 15 312 1.1× 218 1.1× 135 1.1× 58 0.6× 45 0.9× 18 638
Yevgeniya Antonova‐Koch United States 11 188 0.7× 189 1.0× 75 0.6× 95 1.0× 52 1.0× 14 415
Hangjun Ke United States 12 294 1.0× 396 2.0× 67 0.5× 51 0.5× 69 1.4× 22 661
Jun Ping Quek Singapore 9 189 0.7× 139 0.7× 61 0.5× 65 0.7× 25 0.5× 10 321
Kathrin Buchholz United States 12 167 0.6× 491 2.5× 67 0.5× 56 0.6× 96 1.9× 12 674
María José Lafuente-Monasterio Spain 13 150 0.5× 274 1.4× 105 0.8× 69 0.7× 90 1.8× 14 459
Fabian Barthels Germany 11 188 0.7× 112 0.6× 48 0.4× 73 0.7× 33 0.6× 27 373
Christian Kersten Germany 12 229 0.8× 92 0.5× 75 0.6× 69 0.7× 65 1.3× 38 397
Marjorie Maynadier France 16 252 0.9× 253 1.3× 54 0.4× 249 2.5× 54 1.1× 26 701
Julien Lancelot France 16 497 1.7× 149 0.8× 75 0.6× 111 1.1× 22 0.4× 22 828

Countries citing papers authored by Joma Joy

Since Specialization
Citations

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

Fields of papers citing papers by Joma Joy

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Joma Joy

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

All Works

20 of 20 papers shown
1.
Gan, Wang, Zhenyang Yu, Hwee Ting Ang, et al.. (2024). Button-Push On-Demand Synthesis for Rapid Optimization of Antiviral Peptidomimetics. Journal of the American Chemical Society. 146(45). 31321–31329. 1 indexed citations
2.
Tang, Guanghui, Nithya Baburajendran, Anders Poulsen, et al.. (2021). Strategic Design of Catalytic Lysine‐Targeting Reversible Covalent BCR‐ABL Inhibitors**. Angewandte Chemie. 133(31). 17268–17274. 5 indexed citations
3.
Tang, Guanghui, Nithya Baburajendran, Anders Poulsen, et al.. (2021). Strategic Design of Catalytic Lysine‐Targeting Reversible Covalent BCR‐ABL Inhibitors**. Angewandte Chemie International Edition. 60(31). 17131–17137. 66 indexed citations
4.
Liu, Bo, Yi Yang See, Gang Wang, et al.. (2021). A head-to-head comparison of the inhibitory activities of 15 peptidomimetic SARS-CoV-2 3CLpro inhibitors. Bioorganic & Medicinal Chemistry Letters. 48. 128263–128263. 18 indexed citations
5.
Baburajendran, Nithya, Grace Lin, Weijun Xu, et al.. (2021). Structure–activity relationship studies of allosteric inhibitors of EYA2 tyrosine phosphatase. Protein Science. 31(2). 422–431. 6 indexed citations
6.
Li, Yan, Anna Ngo, Shuang Liu, et al.. (2017). Backbone resonance assignments for the SET domain of human methyltransferase NSD3 in complex with its cofactor. Biomolecular NMR Assignments. 11(2). 225–229. 1 indexed citations
7.
Chu, Justin Jang Hann, Regina Ching Hua Lee, Melgious Jin Yan Ang, et al.. (2015). Antiviral activities of 15 dengue NS2B-NS3 protease inhibitors using a human cell-based viral quantification assay. Antiviral Research. 118. 68–74. 40 indexed citations
8.
Koh, Xiaoying, Joma Joy, Kah Fei Wan, et al.. (2015). Identification of covalent active site inhibitors of dengue virus protease. Drug Design Development and Therapy. 9. 6389–6389. 25 indexed citations
9.
Xu, Jin, Anqi Chen, Joma Joy, et al.. (2013). Rational Design of Resorcylic Acid Lactone Analogues as Covalent MNK1/2 Kinase Inhibitors by Tuning the Reactivity of an Enamide Michael Acceptor. ChemMedChem. 8(9). 1483–1494. 27 indexed citations
10.
Huang, Qiwei, Qingxin Li, Joma Joy, et al.. (2013). Lyso-myristoyl phosphatidylcholine micelles sustain the activity of Dengue non-structural (NS) protein 3 protease domain fused with the full-length NS2B. Protein Expression and Purification. 92(2). 156–162. 17 indexed citations
11.
Ang, Melgious Jin Yan, Anders Poulsen, Zhitao Li, et al.. (2013). Substrate-based peptidomimetic inhibitors of the Murray Valley encephalitis virus NS2B/NS3 serine protease: A P1–P4 SAR study. European Journal of Medicinal Chemistry. 68. 72–80. 2 indexed citations
12.
Ang, Melgious Jin Yan, Zhitao Li, Fui Mee Ng, et al.. (2013). A P2 and P3 substrate specificity comparison between the Murray Valley encephalitis and West Nile virus NS2B/NS3 protease using C-terminal agmatine dipeptides. Peptides. 52. 49–52. 6 indexed citations
13.
Kim, Youngmee, Shovanlal Gayen, CongBao Kang, et al.. (2013). NMR Analysis of a Novel Enzymatically Active Unlinked Dengue NS2B-NS3 Protease Complex. Journal of Biological Chemistry. 288(18). 12891–12900. 90 indexed citations
14.
Ang, Melgious Jin Yan, et al.. (2013). Novel agmatine dipeptide inhibitors against the West Nile virus NS2B/NS3 protease: A P3 and N-cap optimization study. European Journal of Medicinal Chemistry. 62. 199–205. 16 indexed citations
15.
Joy, Joma, et al.. (2011). Novel agmatine and agmatine-like peptidomimetic inhibitors of the West Nile virus NS2B/NS3 serine protease. European Journal of Medicinal Chemistry. 46(7). 3130–3134. 26 indexed citations
16.
Joy, Joma, et al.. (2010). Biochemical characterisation of Murray Valley encephalitis virus proteinase. FEBS Letters. 584(14). 3149–3152. 6 indexed citations
17.
Joy, Joma, Madhumita Ghosh, Oliver Popp, et al.. (2006). Identification of calpain cleavage sites in the G1 cyclin-dependent kinase inhibitor p19INK4d. Biological Chemistry. 387(3). 329–35. 11 indexed citations
18.
Smialowski, Pawel, Mahavir Singh, Aleksandra Mikolajka, et al.. (2005). NMR and mass spectrometry studies of putative interactions of cell cycle proteins pRb and CDK6 with cell differentiation proteins MyoD and ID-2. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1750(1). 48–60. 7 indexed citations
19.
Popowicz, Grzegorz M., et al.. (2005). The crystal structure of the non-liganded 14-3-3σ protein: insights into determinants of isoform specific ligand binding and dimerization. Cell Research. 15(4). 219–227. 91 indexed citations
20.
Merril, C R, G. Joseph Creed, Joma Joy, & Arthur D. Olson. (1993). Identification and use of constitutive proteins for the normalization of high resolution electrophoretograms.. PubMed. 3(6). 329–33. 4 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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