D. Kumaran

1.9k total citations
50 papers, 1.2k citations indexed

About

D. Kumaran is a scholar working on Molecular Biology, Materials Chemistry and Neurology. According to data from OpenAlex, D. Kumaran has authored 50 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 35 papers in Molecular Biology, 15 papers in Materials Chemistry and 14 papers in Neurology. Recurrent topics in D. Kumaran's work include Enzyme Structure and Function (15 papers), Botulinum Toxin and Related Neurological Disorders (14 papers) and Biochemical and Structural Characterization (10 papers). D. Kumaran is often cited by papers focused on Enzyme Structure and Function (15 papers), Botulinum Toxin and Related Neurological Disorders (14 papers) and Biochemical and Structural Characterization (10 papers). D. Kumaran collaborates with scholars based in United States, India and Germany. D. Kumaran's co-authors include Subramanyam Swaminathan, Subramaniam Eswaramoorthy, William Furey, S. Ashraf Ahmed, S.K. Burley, Jorge Navaza, Martin Sax, F. William Studier, Richa Rawat and Thomas Binz and has published in prestigious journals such as Journal of Biological Chemistry, Nature Communications and The EMBO Journal.

In The Last Decade

D. Kumaran

50 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
D. Kumaran United States 21 555 462 235 144 142 50 1.2k
Seema Dalal United States 20 900 1.6× 96 0.2× 135 0.6× 58 0.4× 125 0.9× 41 1.5k
Connor F. McGrath United States 15 523 0.9× 190 0.4× 60 0.3× 117 0.8× 29 0.2× 21 1.0k
Junsang Ko South Korea 9 400 0.7× 120 0.3× 51 0.2× 36 0.3× 97 0.7× 14 620
Huijong Han Germany 17 728 1.3× 24 0.1× 78 0.3× 50 0.3× 103 0.7× 30 1.2k
Justyna Sawa‐Makarska Austria 17 861 1.6× 83 0.2× 15 0.1× 39 0.3× 239 1.7× 19 1.4k
Simon van Heyningen United Kingdom 17 590 1.1× 92 0.2× 74 0.3× 91 0.6× 26 0.2× 50 1.1k
Ana Paula Ulian de Araújo Brazil 23 1.0k 1.8× 29 0.1× 66 0.3× 34 0.2× 83 0.6× 87 1.5k
Craig R. Garen Canada 17 530 1.0× 71 0.2× 24 0.1× 137 1.0× 120 0.8× 42 785
Conceição A.S.A. Minetti United States 20 548 1.0× 53 0.1× 30 0.1× 55 0.4× 54 0.4× 40 928
Kyoung‐Seok Ryu South Korea 22 1.1k 1.9× 30 0.1× 29 0.1× 58 0.4× 131 0.9× 83 1.4k

Countries citing papers authored by D. Kumaran

Since Specialization
Citations

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

Fields of papers citing papers by D. Kumaran

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of D. Kumaran

This figure shows the co-authorship network connecting the top 25 collaborators of D. Kumaran. A scholar is included among the top collaborators of D. Kumaran 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 D. Kumaran. D. Kumaran 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.
Kumaran, D., James Byrnes, Dale F. Kreitler, et al.. (2024). A hemoprotein with a zinc-mirror heme site ties heme availability to carbon metabolism in cyanobacteria. Nature Communications. 15(1). 3167–3167. 6 indexed citations
2.
Wolabu, Tezera W., Hui Wang, Jianfei Yun, et al.. (2024). Sorghum SbGhd7 is a major regulator of floral transition and directly represses genes crucial for flowering activation. New Phytologist. 242(2). 786–796. 4 indexed citations
3.
Ebrahim, Ali, Blake T. Riley, D. Kumaran, et al.. (2022). The temperature-dependent conformational ensemble of SARS-CoV-2 main protease (Mpro). IUCrJ. 9(5). 682–694. 35 indexed citations
4.
Azhahianambi, P., M. Madhanmohan, N. Madan, et al.. (2021). Successful treatment of severe form of bovine tropical theileriosis in dairy cattle and genotyping of Theileria annulata isolates of Tamil Nadu, India. Veterinary Parasitology Regional Studies and Reports. 26. 100628–100628. 7 indexed citations
5.
Kumaran, D., et al.. (2015). Interactions of a potent cyclic peptide inhibitor with the light chain of botulinum neurotoxin A: Insights from X-ray crystallography. Bioorganic & Medicinal Chemistry. 23(22). 7264–7273. 11 indexed citations
6.
Kumar, Gyanendra, D. Kumaran, S. Ashraf Ahmed, & Subramanyam Swaminathan. (2012). Peptide inhibitors of botulinum neurotoxin serotype A: design, inhibition, cocrystal structures, structure–activity relationship and pharmacophore modeling. Acta Crystallographica Section D Biological Crystallography. 68(5). 511–520. 17 indexed citations
8.
Kumaran, D., et al.. (2012). Structure of a periplasmic glucose-binding protein fromThermotoga maritima. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 68(12). 1460–1464. 5 indexed citations
9.
Kamat, Siddhesh S., Gregory P. Holmes‐Hampton, Ashima Bagaria, et al.. (2011). The catalase activity of diiron adenine deaminase. Protein Science. 20(12). 2080–2094. 10 indexed citations
10.
Xiang, Dao Feng, Chengfu Xu, D. Kumaran, et al.. (2009). Functional Annotation of Two New Carboxypeptidases from the Amidohydrolase Superfamily of Enzymes. Biochemistry. 48(21). 4567–4576. 13 indexed citations
11.
Kumaran, D., Richa Rawat, S. Ashraf Ahmed, & Subramanyam Swaminathan. (2008). Substrate Binding Mode and Its Implication on Drug Design for Botulinum Neurotoxin A. PLoS Pathogens. 4(9). e1000165–e1000165. 45 indexed citations
12.
Kumaran, D., et al.. (2008). Structure- and Substrate-based Inhibitor Design for Clostridium botulinum Neurotoxin Serotype A. Journal of Biological Chemistry. 283(27). 18883–18891. 50 indexed citations
13.
Guy, Jodie E., Edward Whittle, D. Kumaran, Ylva Lindqvist, & John Shanklin. (2007). The Crystal Structure of the Ivy Δ4-16:0-ACP Desaturase Reveals Structural Details of the Oxidized Active Site and Potential Determinants of Regioselectivity. Journal of Biological Chemistry. 282(27). 19863–19871. 44 indexed citations
14.
Kumaran, D., Subramaniam Eswaramoorthy, F. William Studier, & Subramanyam Swaminathan. (2005). Structure and mechanism of ADP‐ribose‐1″‐monophosphatase (Appr‐1″‐pase), a ubiquitous cellular processing enzyme. Protein Science. 14(3). 719–726. 35 indexed citations
15.
Yuan, Ping, Gregory Jedd, D. Kumaran, et al.. (2003). A HEX-1 crystal lattice required for Woronin body function in Neurospora crassa. Nature Structural & Molecular Biology. 10(4). 264–270. 67 indexed citations
16.
Kumaran, D., et al.. (2003). Crystal structure of a putative CN hydrolase from yeast. Proteins Structure Function and Bioinformatics. 52(2). 283–291. 44 indexed citations
17.
Kumaran, D., et al.. (2002). Fast N-CO rotational equilibria in twist-boat conformations of N -ethoxycarbonyl- r- 2 , c -6-diphenylpiperidin-4-ones and N -ethoxycarbonyl- r -2, c -6-diphenylpiperidines. Indian Journal of Chemistry Section B-organic Chemistry Including Medicinal Chemistry. 41(3). 614–627. 10 indexed citations
18.
Kumaran, D., et al.. (2001). Crystallization and preliminary X-ray analysis ofBorrelia burgdorferiouter surface protein C (OspC). Acta Crystallographica Section D Biological Crystallography. 57(2). 298–300. 7 indexed citations
19.
Kumaran, D.. (2001). Crystal structure of outer surface protein C (OspC) from the Lyme disease spirochete, Borrelia burgdorferi. The EMBO Journal. 20(5). 971–978. 99 indexed citations
20.
Kumaran, D., et al.. (2001). Structure of staphylococcal enterotoxin C2 at various pH levels. Acta Crystallographica Section D Biological Crystallography. 57(9). 1270–1275. 20 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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