E. Subramanian

1.9k total citations
89 papers, 1.5k citations indexed

About

E. Subramanian is a scholar working on Molecular Biology, Organic Chemistry and Materials Chemistry. According to data from OpenAlex, E. Subramanian has authored 89 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 42 papers in Molecular Biology, 39 papers in Organic Chemistry and 19 papers in Materials Chemistry. Recurrent topics in E. Subramanian's work include Chemical Synthesis and Analysis (20 papers), Enzyme Structure and Function (17 papers) and Carbohydrate Chemistry and Synthesis (15 papers). E. Subramanian is often cited by papers focused on Chemical Synthesis and Analysis (20 papers), Enzyme Structure and Function (17 papers) and Carbohydrate Chemistry and Synthesis (15 papers). E. Subramanian collaborates with scholars based in India, United States and Canada. E. Subramanian's co-authors include R. Bott, David R. Davies, K. Suguna, F. L. Suddath, Howard Einspahr, David Hunt, Eduardo A. Padlan, Gerson H. Cohen, Ian D.A. Swan and S. Sheriff and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

E. Subramanian

88 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
E. Subramanian India 21 950 404 272 171 145 89 1.5k
M. A. Viswamitra India 24 1.6k 1.7× 497 1.2× 447 1.6× 284 1.7× 326 2.2× 120 2.5k
Jindřich Hašek Czechia 18 428 0.5× 234 0.6× 202 0.7× 99 0.6× 98 0.7× 87 1.1k
A.W. Roszak United Kingdom 25 1.4k 1.5× 445 1.1× 344 1.3× 77 0.5× 108 0.7× 71 2.1k
L. K. Steinrauf United States 25 997 1.0× 379 0.9× 358 1.3× 402 2.4× 145 1.0× 59 2.0k
Tatzuo Ueki Japan 20 906 1.0× 558 1.4× 211 0.8× 109 0.6× 57 0.4× 58 1.5k
Bret A. Shirley United States 11 1.4k 1.5× 563 1.4× 120 0.4× 153 0.9× 76 0.5× 11 1.9k
Watson J. Lees United States 26 1.2k 1.2× 611 1.5× 877 3.2× 101 0.6× 124 0.9× 61 2.2k
M. Vijayan India 19 651 0.7× 340 0.8× 200 0.7× 137 0.8× 134 0.9× 46 1.1k
Yoshimasa Kyogoku Japan 32 2.3k 2.4× 402 1.0× 411 1.5× 536 3.1× 335 2.3× 84 3.0k
Clifford E. Felder Israel 21 1.3k 1.4× 565 1.4× 304 1.1× 543 3.2× 103 0.7× 36 2.3k

Countries citing papers authored by E. Subramanian

Since Specialization
Citations

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

Fields of papers citing papers by E. Subramanian

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of E. Subramanian

This figure shows the co-authorship network connecting the top 25 collaborators of E. Subramanian. A scholar is included among the top collaborators of E. Subramanian 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 E. Subramanian. E. Subramanian 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.
Subramanian, E., et al.. (2017). Combined effect of adsorbent chitosan and photosensitizer polypyrrole in ternary chitosan-polypyrrole-TiO 2 photocatalyst leading to visible light activity and superior functionality. 56(3). 287–296. 2 indexed citations
2.
Zucker, Frank, Jessica Kim, Li Zhang, et al.. (2010). Prediction of protein crystallization outcome using a hybrid method. Journal of Structural Biology. 171(1). 64–73. 14 indexed citations
3.
Jayakumar, Arumugam R., et al.. (2002). Evidence that nitric oxide production increases γ-amino butyric acid permeability of blood-brain barrier. Brain Research Bulletin. 57(2). 231–236. 46 indexed citations
4.
Jayakumar, Arumugam, Karthik Rajasekaran, E. Subramanian, & V.I. Paul. (1999). Possible involvement of nitric oxide in locomotor behaviour in rats. 19(3). 215–219. 1 indexed citations
6.
Subramanian, E., et al.. (1993). Structure and conformation of linear peptides. International journal of peptide & protein research. 41(4). 319–322. 1 indexed citations
7.
Maruthamuthu, P., K. Gurunathan, E. Subramanian, & M SASTRI. (1993). Visible light induced hydrogen production with Cu(II)/Bi2O3 and Pt/Bi2O3/RuO2 from aqueous methyl viologen solution. International Journal of Hydrogen Energy. 18(1). 9–13. 10 indexed citations
8.
Sivaraman, J., K. Subramanian, D. Velmurugan, E. Subramanian, & K. Balakrishna. (1993). Structure of vicogenin. Acta Crystallographica Section C Crystal Structure Communications. 49(6). 1240–1242. 6 indexed citations
9.
Subramanian, E., et al.. (1992). Polymer-ligand interaction studies. Part I. Binding of some drugs to poly(N-vinyl-2-pyrrolidone). Journal of Chemical Sciences. 104(3). 417–424. 7 indexed citations
10.
Subramanian, E.. (1990). PROTEIN CRYSTALLOGRAPHY AND PROTEIN ENGINEERING. Current Science. 59(15). 728–732. 2 indexed citations
11.
Subramanian, E. & R. Parthasarathy. (1989). Crystal structure and conformation of glycyl‐glycyl‐sarcosine. International journal of peptide & protein research. 33(5). 345–347. 2 indexed citations
12.
Subramanian, E., et al.. (1989). Structure and conformation of linear peptides XII. Structure of tryptophanyl‐glycyl‐glycine dihydrate. International journal of peptide & protein research. 34(2). 134–138. 9 indexed citations
13.
Suguna, K., R. Bott, Eduardo A. Padlan, et al.. (1987). Structure and refinement at 1.8 Å resolution of the aspartic proteinase from Rhizopus chinensis. Journal of Molecular Biology. 196(4). 877–900. 150 indexed citations
14.
Murali, Ramachandran & E. Subramanian. (1987). Structure and conformation of linear peptides. X. Structure of glycyl‐glycyl‐L‐phenylalanine hydrochloride. International journal of peptide & protein research. 29(3). 374–380. 5 indexed citations
15.
Jagannathan, N. R., E. Subramanian, R. Srinivasan, & J. Trotter. (1984). Structure of hexamethylenediammonium phthalate trihydrate, C6H18N22+.C8H4O42−.3H2O. Acta Crystallographica Section C Crystal Structure Communications. 40(10). 1743–1744. 1 indexed citations
16.
Rosati, Robert L., et al.. (1982). Photochemical transformation of cephalosporins into carbapenems. Journal of the American Chemical Society. 104(15). 4262–4264. 10 indexed citations
17.
Srinivasan, R., E. Subramanian, & N. Yathindra. (1981). Diffraction and related studies. Pergamon Press eBooks. 2 indexed citations
18.
Hingerty, Brian E., E. Subramanian, Steven D. Stellman, et al.. (1975). Structure of guanylyl‐3′,5′‐cytidine monophosphate. II. Description of the molecular and crystal structure of the calcium derivative in space group P21. Biopolymers. 14(1). 227–236. 21 indexed citations
19.
Subramanian, E.. (1967). The crystal structure of L-leucine hydrobromide. Acta Crystallographica. 22(6). 910–917. 22 indexed citations
20.
Subramanian, E., et al.. (1966). Structure of Nazarov's compound*. Zeitschrift für Kristallographie. 123(3-4). 206–221. 1 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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