Kunchithapadam Swaminathan

2.7k total citations
71 papers, 2.2k citations indexed

About

Kunchithapadam Swaminathan is a scholar working on Molecular Biology, Materials Chemistry and Biotechnology. According to data from OpenAlex, Kunchithapadam Swaminathan has authored 71 papers receiving a total of 2.2k indexed citations (citations by other indexed papers that have themselves been cited), including 48 papers in Molecular Biology, 16 papers in Materials Chemistry and 14 papers in Biotechnology. Recurrent topics in Kunchithapadam Swaminathan's work include Enzyme Structure and Function (16 papers), Enzyme Production and Characterization (12 papers) and Biochemical and Molecular Research (5 papers). Kunchithapadam Swaminathan is often cited by papers focused on Enzyme Structure and Function (16 papers), Enzyme Production and Characterization (12 papers) and Biochemical and Molecular Research (5 papers). Kunchithapadam Swaminathan collaborates with scholars based in Singapore, United States and Australia. Kunchithapadam Swaminathan's co-authors include Ronen Marmorstein, H. Eric Xu, Bharat Patel, Julien Lescar, Subhash G. Vasudevan, Nan Li, Yongqian Zhao, Sheng Luan, Kuntal Pal and Augen A. Pioszak and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Kunchithapadam Swaminathan

71 papers receiving 2.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Kunchithapadam Swaminathan Singapore 25 1.2k 317 297 220 212 71 2.2k
Michael J. Holland United States 31 2.6k 2.2× 216 0.7× 160 0.5× 141 0.6× 351 1.7× 80 3.4k
Andrew C. Storer Canada 25 1.4k 1.2× 310 1.0× 234 0.8× 60 0.3× 135 0.6× 43 2.4k
Daniel Gillet France 27 971 0.8× 278 0.9× 114 0.4× 343 1.6× 82 0.4× 77 2.2k
Pedro José Barbosa Pereira Portugal 29 1.4k 1.2× 125 0.4× 90 0.3× 109 0.5× 131 0.6× 89 2.4k
Achim Dickmanns Germany 33 2.4k 2.0× 139 0.4× 60 0.2× 154 0.7× 205 1.0× 70 3.1k
J.A.R.G. Barbosa Brazil 25 1.2k 1.0× 158 0.5× 90 0.3× 72 0.3× 134 0.6× 103 2.0k
M A Brown United States 13 1.3k 1.1× 205 0.6× 123 0.4× 134 0.6× 160 0.8× 16 2.5k
Takae Towatari Japan 25 1.4k 1.2× 211 0.7× 107 0.4× 180 0.8× 139 0.7× 43 2.6k
M. Renko Slovenia 21 1.4k 1.2× 189 0.6× 61 0.2× 116 0.5× 138 0.7× 37 2.5k
Gladys Mirey France 24 1.8k 1.5× 141 0.4× 77 0.3× 155 0.7× 199 0.9× 41 2.6k

Countries citing papers authored by Kunchithapadam Swaminathan

Since Specialization
Citations

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

Fields of papers citing papers by Kunchithapadam Swaminathan

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Kunchithapadam Swaminathan

This figure shows the co-authorship network connecting the top 25 collaborators of Kunchithapadam Swaminathan. A scholar is included among the top collaborators of Kunchithapadam Swaminathan 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 Kunchithapadam Swaminathan. Kunchithapadam Swaminathan 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.
Zhang, Qian, Hong Y. Wang, Selene Nuñez-Cruz, et al.. (2022). Induction of Transcriptional Inhibitor HES1 and the Related Repression of Tumor-Suppressor TXNIP Are Important Components of Cell-Transformation Program Imposed by Oncogenic Kinase NPM-ALK. American Journal Of Pathology. 192(8). 1186–1198. 2 indexed citations
3.
Lee, Jonathan, Xiaoman Luo, Raymond A. Smith, et al.. (2018). A Heparan Sulfate Device for the Regeneration of Osteochondral Defects. Tissue Engineering Part A. 25(5-6). 352–363. 18 indexed citations
4.
Hameed, Umar F. Shahul, Oana Sanislav, Sarah J. Annesley, et al.. (2018). Proteobacterial Origin of Protein Arginine Methylation and Regulation of Complex I Assembly by MidA. Cell Reports. 24(8). 1996–2004. 8 indexed citations
5.
Lee, Wei Lin, Sheena Wee, Umesh Ghoshdastider, et al.. (2017). Yersinia effector protein (YopO)-mediated phosphorylation of host gelsolin causes calcium-independent activation leading to disruption of actin dynamics. Journal of Biological Chemistry. 292(19). 8092–8100. 14 indexed citations
6.
Ling, Ling, Sadasivam Murali, Simon F.R. Hinkley, et al.. (2016). Affinity Selection of FGF2-Binding Heparan Sulfates for Ex Vivo Expansion of Human Mesenchymal Stem Cells. Journal of Cellular Physiology. 232(3). 566–575. 31 indexed citations
7.
Siveen, Kodappully Sivaraman, Tuan Zea Tan, Jean Paul Thiery, et al.. (2016). Functional characterization of selective exosite-binding inhibitors of matrix metalloproteinase-13 (MMP-13) – experimental validation in human breast and colon cancer. Bioscience Biotechnology and Biochemistry. 80(11). 2122–2131. 8 indexed citations
8.
Zhao, Yongqian, Jie Zheng, Kitti Wing Ki Chan, et al.. (2015). A Crystal Structure of the Dengue Virus NS5 Protein Reveals a Novel Inter-domain Interface Essential for Protein Flexibility and Virus Replication. PLoS Pathogens. 11(3). e1004682–e1004682. 214 indexed citations
9.
Johnson, John E., et al.. (2014). Hibiscus Chlorotic Ringspot Virus Coat Protein Is Essential for Cell-to-Cell and Long-Distance Movement but Not for Viral RNA Replication. PLoS ONE. 9(11). e113347–e113347. 8 indexed citations
10.
Kovach, Amanda, Yang Zhao, Jian‐Kang Zhu, et al.. (2014). H2O2 Inhibits ABA-Signaling Protein Phosphatase HAB1. PLoS ONE. 9(12). e113643–e113643. 23 indexed citations
11.
Swaminathan, Kunchithapadam. (2012). Frequency distribution of the reduced unit cells of centred lattices from the Protein Data Bank. Acta Crystallographica Section A Foundations of Crystallography. 68(2). 295–297. 1 indexed citations
12.
Hotta, Kinya, Xi Chen, Robert S. Paton, et al.. (2012). Enzymatic catalysis of anti-Baldwin ring closure in polyether biosynthesis. Nature. 483(7389). 355–358. 90 indexed citations
13.
Pal, Kuntal, Kunchithapadam Swaminathan, H. Eric Xu, & Augen A. Pioszak. (2010). Structural Basis for Hormone Recognition by the Human CRFR2α G Protein-coupled Receptor. Journal of Biological Chemistry. 285(51). 40351–40361. 63 indexed citations
14.
Saxena, Anand, et al.. (2009). Structural basis of typhoid: Salmonella typhi type IVb pilin (PilS) and cystic fibrosis transmembrane conductance regulator interaction. Proteins Structure Function and Bioinformatics. 77(2). 253–261. 12 indexed citations
15.
Anand, R., et al.. (2009). Production of ethanol from Ipomoea batatas using Saccharomyces cerevisiae.. Asian Journal of Biological Sciences. 4(2). 266–269. 1 indexed citations
16.
Thwin, M.M., et al.. (2007). Structural and pharmacological comparison of daboiatoxin fromDaboia russelli siamensiswith viperotoxin F and vipoxin from other vipers. Acta Crystallographica Section D Biological Crystallography. 63(6). 722–729. 14 indexed citations
17.
Saxena, Sandeep, Ping Yuan, Suman Kumar Dhar, et al.. (2004). A Dimerized Coiled-Coil Domain and an Adjoining Part of Geminin Interact with Two Sites on Cdt1 for Replication Inhibition. Molecular Cell. 15(2). 245–258. 70 indexed citations
18.
Zhang, Daohai, et al.. (2003). A motif rich in charged residues determines product specificity in isomaltulose synthase. FEBS Letters. 534(1-3). 151–155. 21 indexed citations
19.
Li, Nan, Bharat Patel, Benjamin N. Mijts, & Kunchithapadam Swaminathan. (2002). Crystallization of an α-amylase, AmyA, from the thermophilic halophileHalothermothrix orenii. Acta Crystallographica Section D Biological Crystallography. 58(12). 2125–2126. 9 indexed citations
20.
Li, Nan, Daohai Zhang, Lian‐Hui Zhang, & Kunchithapadam Swaminathan. (2002). Expression, crystallization and preliminary X-ray analysis of isomaltulose synthase (PalI) fromKlebsiellasp. LX3. Acta Crystallographica Section D Biological Crystallography. 59(1). 150–151. 5 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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