S. Kumaran

1.3k total citations
41 papers, 1.0k citations indexed

About

S. Kumaran is a scholar working on Molecular Biology, Oncology and Rheumatology. According to data from OpenAlex, S. Kumaran has authored 41 papers receiving a total of 1.0k indexed citations (citations by other indexed papers that have themselves been cited), including 30 papers in Molecular Biology, 11 papers in Oncology and 5 papers in Rheumatology. Recurrent topics in S. Kumaran's work include Peptidase Inhibition and Analysis (9 papers), Nitrogen and Sulfur Effects on Brassica (7 papers) and Chemical Synthesis and Analysis (6 papers). S. Kumaran is often cited by papers focused on Peptidase Inhibition and Analysis (9 papers), Nitrogen and Sulfur Effects on Brassica (7 papers) and Chemical Synthesis and Analysis (6 papers). S. Kumaran collaborates with scholars based in India, United States and United Kingdom. S. Kumaran's co-authors include Joseph M. Jez, Gabriel Waksman, Julie A. Francois, Kumardeep Chaudhary, Abhishek Tuknait, Sandeep Singh, Gajendra P. S. Raghava, Balvinder Singh, Harinder Singh and Rajendra P. Roy and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

S. Kumaran

41 papers receiving 988 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
S. Kumaran India 16 740 175 108 105 75 41 1.0k
Yeon Gyu Yu South Korea 20 790 1.1× 109 0.6× 72 0.7× 203 1.9× 81 1.1× 73 1.2k
Suparerk Borwornpinyo Thailand 20 587 0.8× 90 0.5× 90 0.8× 79 0.8× 72 1.0× 87 1.3k
Mei Ge China 20 971 1.3× 81 0.5× 59 0.5× 107 1.0× 96 1.3× 58 1.4k
Joseph Dundas United States 4 1.1k 1.5× 131 0.7× 126 1.2× 242 2.3× 136 1.8× 6 1.6k
Shan Wu China 19 1.4k 1.8× 365 2.1× 201 1.9× 135 1.3× 104 1.4× 45 2.0k
Changsoo Chang United States 24 1.1k 1.5× 210 1.2× 93 0.9× 283 2.7× 86 1.1× 64 1.6k
Joseph H. Lorent Belgium 16 1.4k 1.8× 96 0.5× 44 0.4× 48 0.5× 103 1.4× 33 1.8k
Arjan Snijder Sweden 21 1.1k 1.5× 120 0.7× 90 0.8× 102 1.0× 84 1.1× 39 1.5k
Xiaojun Peng China 18 731 1.0× 158 0.9× 168 1.6× 47 0.4× 35 0.5× 26 960
Mariana Gallo Italy 16 524 0.7× 144 0.8× 61 0.6× 44 0.4× 35 0.5× 56 783

Countries citing papers authored by S. Kumaran

Since Specialization
Citations

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

Fields of papers citing papers by S. Kumaran

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

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

This figure shows the co-authorship network connecting the top 25 collaborators of S. Kumaran. A scholar is included among the top collaborators of S. 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 S. Kumaran. S. 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.
Boradia, Vishant Mahendra, et al.. (2023). Mycobacterium tuberculosis H37Rv enolase (Rv1023)- expression, characterization and effect of host dependent modifications on protein functionality. Biochimie. 214(Pt B). 102–113. 2 indexed citations
2.
Pandya, Vaibhav Kumar, et al.. (2022). Mechanistic insights on anserine hydrolyzing activities of human carnosinases. Biochimica et Biophysica Acta (BBA) - General Subjects. 1867(3). 130290–130290. 3 indexed citations
3.
Sharma, Gaurav, et al.. (2021). Moonlighting Biochemistry of Cysteine Synthase: A Species-specific Global Regulator. Journal of Molecular Biology. 433(22). 167255–167255. 2 indexed citations
4.
Rahisuddin, R., et al.. (2020). Molecular mechanism of selective substrate engagement and inhibitor disengagement of cysteine synthase. Journal of Biological Chemistry. 296. 100041–100041. 6 indexed citations
5.
Singh, Appu K., et al.. (2017). Structural and biochemical characterization of ligand recognition by CysB, the master regulator of sulfate metabolism. Biochimie. 142. 112–124. 18 indexed citations
6.
Singh, Appu K., et al.. (2015). Crystal Structure of Fad35R from Mycobacterium tuberculosis H37Rv in the Apo-State. PLoS ONE. 10(5). e0124333–e0124333. 4 indexed citations
7.
Singh, Appu K., et al.. (2014). Molecular Basis of Peptide Recognition in Metallopeptidase Dug1p from Saccharomyces cerevisiae. Biochemistry. 53(50). 7870–7883. 5 indexed citations
8.
Yi, Hankuil, Sanghamitra Dey, S. Kumaran, et al.. (2013). Structure of Soybean Serine Acetyltransferase and Formation of the Cysteine Regulatory Complex as a Molecular Chaperone. Journal of Biological Chemistry. 288(51). 36463–36472. 34 indexed citations
9.
Kumaran, S., Palani Perumal, C. Chellaram, T. Prem Anand, & V. Kaviyarasan. (2011). Screeining of fibrinolytic protease from south indian isolates of ganoderma lucidum. International Journal of Pharma and Bio Sciences. 7 indexed citations
10.
Pandya, Vaibhav Kumar, et al.. (2011). Mass spectrometry assay for studying kinetic properties of dipeptidases: Characterization of human and yeast dipeptidases. Analytical Biochemistry. 418(1). 134–142. 16 indexed citations
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Kumaran, S., L. Jagadish, Palani Perumal, et al.. (2010). Growth Optimization Conditions for the Production of Fibrinolytic Enzyme from Ganoderma lucidum. 2(4). 2 indexed citations
14.
Schroeder, Amy C., S. Kumaran, Leslie M. Hicks, et al.. (2008). Contributions of conserved serine and tyrosine residues to catalysis, ligand binding, and cofactor processing in the active site of tyrosine ammonia lyase. Phytochemistry. 69(7). 1496–1506. 32 indexed citations
15.
Cahoon, Rebecca E., et al.. (2007). Reaction Mechanism of Glutathione Synthetase from Arabidopsis thaliana. Journal of Biological Chemistry. 282(23). 17157–17165. 21 indexed citations
16.
Waksman, Gabriel, S. Kumaran, & Olga Lubman. (2004). SH2 domains: role, structure and implications for molecular medicine. Expert Reviews in Molecular Medicine. 6(3). 1–18. 68 indexed citations
17.
Kumaran, S., et al.. (2003). A quantitative structure–activity relationship study on Clostridium histolyticum collagenase inhibitors. Bioorganic & Medicinal Chemistry. 11(14). 3065–3071. 12 indexed citations
18.
Kumar, Dalip, et al.. (2003). A quantitative structure–activity relationship study of hydroxamate matrix metalloproteinase inhibitors derived from funtionalized 4-aminoprolines. Bioorganic & Medicinal Chemistry. 11(9). 1975–1981. 21 indexed citations
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Kumaran, S.. (1995). Application of a cholinesterase biosensor to screen for organophosphorus pesticides extracted from soil. Talanta. 42(4). 649–655. 67 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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