Rajaram Venkatesan

828 total citations
35 papers, 616 citations indexed

About

Rajaram Venkatesan is a scholar working on Molecular Biology, Materials Chemistry and Biochemistry. According to data from OpenAlex, Rajaram Venkatesan has authored 35 papers receiving a total of 616 indexed citations (citations by other indexed papers that have themselves been cited), including 24 papers in Molecular Biology, 19 papers in Materials Chemistry and 10 papers in Biochemistry. Recurrent topics in Rajaram Venkatesan's work include Enzyme Structure and Function (19 papers), Amino Acid Enzymes and Metabolism (8 papers) and Protein Structure and Dynamics (6 papers). Rajaram Venkatesan is often cited by papers focused on Enzyme Structure and Function (19 papers), Amino Acid Enzymes and Metabolism (8 papers) and Protein Structure and Dynamics (6 papers). Rajaram Venkatesan collaborates with scholars based in Finland, India and Germany. Rajaram Venkatesan's co-authors include Rik K. Wierenga, Evangelia G. Kapetaniou, J. Kalervo Hiltunen, Alexander J. Kastaniotis, Zhijun Chen, K. Suresh, H.S. Savithri, M.R.N. Murthy, K Sasikala and Ramachandran Chandirasekar and has published in prestigious journals such as Journal of Biological Chemistry, Nature Communications and The Journal of Physical Chemistry B.

In The Last Decade

Rajaram Venkatesan

33 papers receiving 605 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Rajaram Venkatesan Finland 13 370 185 83 70 69 35 616
Takako Mukai Japan 12 385 1.0× 71 0.4× 52 0.6× 34 0.5× 47 0.7× 17 603
María T. Villar United States 18 527 1.4× 36 0.2× 36 0.4× 45 0.6× 42 0.6× 34 837
Michelle A.C. Reed United Kingdom 16 366 1.0× 48 0.3× 35 0.4× 68 1.0× 20 0.3× 21 534
Matthew L. Brown United States 12 463 1.3× 66 0.4× 38 0.5× 52 0.7× 34 0.5× 16 770
Arturo Leone Italy 16 362 1.0× 58 0.3× 23 0.3× 34 0.5× 28 0.4× 22 635
Archie C. Swindell United States 12 282 0.8× 62 0.3× 62 0.7× 26 0.4× 36 0.5× 21 731
Kirby Snell United Kingdom 18 566 1.5× 94 0.5× 167 2.0× 142 2.0× 295 4.3× 31 926
Natasha M. Nesbitt United States 13 537 1.5× 100 0.5× 22 0.3× 10 0.1× 100 1.4× 21 792
Bengt Mannervik Sweden 11 456 1.2× 60 0.3× 36 0.4× 40 0.6× 58 0.8× 20 633
Masahiro Matsushima Japan 12 203 0.5× 64 0.3× 18 0.2× 41 0.6× 74 1.1× 41 465

Countries citing papers authored by Rajaram Venkatesan

Since Specialization
Citations

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

Fields of papers citing papers by Rajaram Venkatesan

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Rajaram Venkatesan

This figure shows the co-authorship network connecting the top 25 collaborators of Rajaram Venkatesan. A scholar is included among the top collaborators of Rajaram Venkatesan 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 Rajaram Venkatesan. Rajaram Venkatesan 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.
Rahman, Mohammad Asadur, et al.. (2025). Structural enzymological studies of the long chain fatty acyl-CoA synthetase FadD5 from the mce1 operon of Mycobacterium tuberculosis. Biochemical and Biophysical Research Communications. 769. 151960–151960.
2.
Sharma, Rajni, Anil Kumar, Pamali Mahasweta Nanda, et al.. (2022). Molecular Characterization and Management of Congenital Hyperinsulinism: A Tertiary Centre Experience.. PubMed. 59(2). 105–109. 3 indexed citations
3.
Maksimainen, Mirko M., Neil Smith, Ekaterina Biterova, et al.. (2021). IceBear: an intuitive and versatile web application for research-data tracking from crystallization experiment to PDB deposition. Acta Crystallographica Section D Structural Biology. 77(2). 151–163. 17 indexed citations
4.
Pedersen, Jan Skov, et al.. (2021). Structural insights into the substrate-binding proteins Mce1A and Mce4A from Mycobacterium tuberculosis. IUCrJ. 8(5). 757–774. 7 indexed citations
5.
Schmitz, Werner, et al.. (2021). Substrate specificity and conformational flexibility properties of the Mycobacterium tuberculosis β-oxidation trifunctional enzyme. Journal of Structural Biology. 213(3). 107776–107776. 5 indexed citations
6.
Schmitz, Werner, J. Kalervo Hiltunen, Rajaram Venkatesan, et al.. (2020). Crystallographic binding studies of rat peroxisomal multifunctional enzyme type 1 with 3-ketodecanoyl-CoA: capturing active and inactive states of its hydratase and dehydrogenase catalytic sites. Acta Crystallographica Section D Structural Biology. 76(12). 1256–1269. 4 indexed citations
7.
Schmitz, Werner, et al.. (2020). Insights into the stability and substrate specificity of the E. coli aerobic β-oxidation trifunctional enzyme complex. Journal of Structural Biology. 210(3). 107494–107494. 10 indexed citations
8.
Schmitz, Werner, Jani Seitsonen, Jan Skov Pedersen, et al.. (2019). Complementary substrate specificity and distinct quaternary assembly of the Escherichia coli aerobic and anaerobic β-oxidation trifunctional enzyme complexes. Biochemical Journal. 476(13). 1975–1994. 11 indexed citations
9.
Fukao, Toshiyuki, Masahiro Goto, Tomohiro Hori, et al.. (2014). The first case in Asia of 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency (HSD10 disease) with atypical presentation. Journal of Human Genetics. 59(11). 609–614. 17 indexed citations
10.
Chandirasekar, Ramachandran, B. Kumar, K Sasikala, et al.. (2014). Assessment of genotoxic and molecular mechanisms of cancer risk in smoking and smokeless tobacco users. Mutation Research/Genetic Toxicology and Environmental Mutagenesis. 767. 21–27. 36 indexed citations
11.
Venkatesan, Rajaram, et al.. (2013). Effect of glycemic control on the incidence of microalbuminuria in type II diabetes mellitus Individuals. National Journal of Physiology Pharmacy and Pharmacology. 4(2). 132–132. 3 indexed citations
12.
Venkatesan, Rajaram, et al.. (2012). Role of community pharmacists in improving knowledge and glycemic control of type 2 diabetes. Perspectives in Clinical Research. 3(1). 26–26. 31 indexed citations
13.
Sharma, Satyan, Prasenjit Bhaumik, Werner Schmitz, et al.. (2012). The Enolization Chemistry of a Thioester-Dependent Racemase: The 1.4 Å Crystal Structure of a Reaction Intermediate Complex Characterized by Detailed QM/MM Calculations. The Journal of Physical Chemistry B. 116(11). 3619–3629. 17 indexed citations
14.
Suresh, K., et al.. (2011). Association of Trp53 arg72pro polymorphic variants with breast cancer - a case control study in south Indian population. 3(1). 0–0. 7 indexed citations
15.
Chandirasekar, Ramachandran, K. Suresh, Jayakumar Rajarajeswaran, et al.. (2011). XRCC1 gene variants and possible links with chromosome aberrations and micronucleus in active and passive smokers. Environmental Toxicology and Pharmacology. 32(2). 185–192. 22 indexed citations
16.
Venkatesan, Rajaram, Markus Alahuhta, Petri M. Pihko, & Rik K. Wierenga. (2011). High resolution crystal structures of triosephosphate isomerase complexed with its suicide inhibitors: The conformational flexibility of the catalytic glutamate in its closed, liganded active site. Protein Science. 20(8). 1387–1397. 11 indexed citations
17.
Kasaragod, P., Rajaram Venkatesan, Tiila R. Kiema, J. Kalervo Hiltunen, & Rik K. Wierenga. (2010). Crystal Structure of Liganded Rat Peroxisomal Multifunctional Enzyme Type 1. Journal of Biological Chemistry. 285(31). 24089–24098. 22 indexed citations
18.
19.
Venkatesan, Rajaram, et al.. (2003). Crystallization and preliminary X-ray diffraction studies on recombinant diaminopropionate ammonia lyase fromEscherichia coli. Acta Crystallographica Section D Biological Crystallography. 59(9). 1668–1669. 2 indexed citations
20.
Venkatesan, Rajaram, et al.. (1980). Heritability Estimates Of Plasma Alkaline Phosphatase Activity and Economic Traits in Meyer Strain White Leghorn Chicks. 9(6). 329–333. 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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