Palaniappa Arjunan

1.2k total citations
25 papers, 1.0k citations indexed

About

Palaniappa Arjunan is a scholar working on Biochemistry, Clinical Biochemistry and Neurology. According to data from OpenAlex, Palaniappa Arjunan has authored 25 papers receiving a total of 1.0k indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Biochemistry, 16 papers in Clinical Biochemistry and 11 papers in Neurology. Recurrent topics in Palaniappa Arjunan's work include Biochemical Acid Research Studies (19 papers), Metabolism and Genetic Disorders (16 papers) and Alcoholism and Thiamine Deficiency (11 papers). Palaniappa Arjunan is often cited by papers focused on Biochemical Acid Research Studies (19 papers), Metabolism and Genetic Disorders (16 papers) and Alcoholism and Thiamine Deficiency (11 papers). Palaniappa Arjunan collaborates with scholars based in United States, Germany and Hungary. Palaniappa Arjunan's co-authors include William Furey, Frank Jordan, Natalia S. Nemeria, Krishnamoorthy Chandrasekhar, Martin Sax, Andrew P. J. Brunskill, Sheng Zhang, M. Sax, John R. Guest and Timothy C. Umland and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

Palaniappa Arjunan

25 papers receiving 1.0k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Palaniappa Arjunan United States 18 736 488 417 384 118 25 1.0k
Gary A. Radke United States 18 433 0.6× 307 0.6× 449 1.1× 38 0.1× 59 0.5× 31 782
Yuko Kawasaki Japan 14 93 0.1× 84 0.2× 330 0.8× 68 0.2× 39 0.3× 33 510
Margaret L. Fonda United States 20 378 0.5× 171 0.4× 589 1.4× 17 0.0× 252 2.1× 43 1.1k
M. Krueger United States 13 63 0.1× 102 0.2× 329 0.8× 232 0.6× 18 0.2× 19 677
U. Redweik Switzerland 13 83 0.1× 208 0.4× 287 0.7× 55 0.1× 22 0.2× 20 479
W. Bruce Rowe United States 8 306 0.4× 103 0.2× 438 1.1× 14 0.0× 96 0.8× 9 775
Maria L. Maccecchini United States 12 62 0.1× 108 0.2× 641 1.5× 70 0.2× 15 0.1× 21 882
R. Seng United States 12 132 0.2× 51 0.1× 317 0.8× 64 0.2× 17 0.1× 12 598
Joseph E. Hayes United States 10 115 0.2× 79 0.2× 573 1.4× 19 0.0× 129 1.1× 14 845
G. Prezioso Italy 12 154 0.2× 293 0.6× 621 1.5× 10 0.0× 20 0.2× 25 789

Countries citing papers authored by Palaniappa Arjunan

Since Specialization
Citations

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

Fields of papers citing papers by Palaniappa Arjunan

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Palaniappa Arjunan

This figure shows the co-authorship network connecting the top 25 collaborators of Palaniappa Arjunan. A scholar is included among the top collaborators of Palaniappa Arjunan 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 Palaniappa Arjunan. Palaniappa Arjunan 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.
Szabó, Eszter, P. Wilk, Bálint Nagy, et al.. (2019). Underlying molecular alterations in human dihydrolipoamide dehydrogenase deficiency revealed by structural analyses of disease-causing enzyme variants. Human Molecular Genetics. 28(20). 3339–3354. 22 indexed citations
2.
Zhou, Jieyu, Luying Yang, Olivér Ozohanics, et al.. (2018). A multipronged approach unravels unprecedented protein–protein interactions in the human 2-oxoglutarate dehydrogenase multienzyme complex. Journal of Biological Chemistry. 293(50). 19213–19227. 21 indexed citations
3.
Arjunan, Palaniappa, et al.. (2018). Structural basis of neurosteroid anesthetic action on GABAA receptors. Nature Communications. 9(1). 3972–3972. 56 indexed citations
4.
Whitley, Matthew J., Palaniappa Arjunan, Natalia S. Nemeria, et al.. (2018). Pyruvate dehydrogenase complex deficiency is linked to regulatory loop disorder in the αV138M variant of human pyruvate dehydrogenase. Journal of Biological Chemistry. 293(34). 13204–13213. 11 indexed citations
5.
Chen, Qiang, et al.. (2015). Direct Pore Binding as a Mechanism for Isoflurane Inhibition of the Pentameric Ligand-gated Ion Channel ELIC. Scientific Reports. 5(1). 13833–13833. 24 indexed citations
6.
Wang, Junjie, Natalia S. Nemeria, Krishnamoorthy Chandrasekhar, et al.. (2014). Structure and Function of the Catalytic Domain of the Dihydrolipoyl Acetyltransferase Component in Escherichia coli Pyruvate Dehydrogenase Complex. Journal of Biological Chemistry. 289(22). 15215–15230. 35 indexed citations
7.
Arjunan, Palaniappa, Junjie Wang, Natalia S. Nemeria, et al.. (2014). Novel Binding Motif and New Flexibility Revealed by Structural Analyses of a Pyruvate Dehydrogenase-Dihydrolipoyl Acetyltransferase Subcomplex from the Escherichia coli Pyruvate Dehydrogenase Multienzyme Complex. Journal of Biological Chemistry. 289(43). 30161–30176. 18 indexed citations
8.
Chandrasekhar, Krishnamoorthy, Junjie Wang, Palaniappa Arjunan, et al.. (2013). Insight to the Interaction of the Dihydrolipoamide Acetyltransferase (E2) Core with the Peripheral Components in the Escherichia coli Pyruvate Dehydrogenase Complex via Multifaceted Structural Approaches. Journal of Biological Chemistry. 288(21). 15402–15417. 43 indexed citations
9.
Nemeria, Natalia S., Palaniappa Arjunan, Krishnamoorthy Chandrasekhar, et al.. (2010). Communication between Thiamin Cofactors in the Escherichia coli Pyruvate Dehydrogenase Complex E1 Component Active Centers. Journal of Biological Chemistry. 285(15). 11197–11209. 26 indexed citations
10.
Jordan, Frank, et al.. (2009). Multiple roles of mobile active center loops in the E1 component of the Escherichia coli pyruvate dehydrogenase complex—Linkage of protein dynamics to catalysis. Journal of Molecular Catalysis B Enzymatic. 61(1-2). 14–22. 9 indexed citations
11.
12.
13.
Arjunan, Palaniappa, et al.. (2005). TheE. coliPDHc E1 component complex with a reaction intermediate analogue. Acta Crystallographica Section A Foundations of Crystallography. 61(a1). c202–c202. 1 indexed citations
14.
Nemeria, Natalia S., Kai Tittmann, Leon Zhou, et al.. (2005). Glutamate 636 of the Escherichia coli Pyruvate Dehydrogenase-E1 Participates in Active Center Communication and Behaves as an Engineered Acetolactate Synthase with Unusual Stereoselectivity. Journal of Biological Chemistry. 280(22). 21473–21482. 29 indexed citations
15.
Nemeria, Natalia S., Yan Yan, Zhen Zhang, et al.. (2001). Inhibition of the Escherichia coli Pyruvate Dehydrogenase Complex E1 Subunit and Its Tyrosine 177 Variants by Thiamin 2-Thiazolone and Thiamin 2-Thiothiazolone Diphosphates. Journal of Biological Chemistry. 276(49). 45969–45978. 94 indexed citations
16.
Furey, William, et al.. (1998). Structure-function relationships and flexible tetramer assembly in pyruvate decarboxylase revealed by analysis of crystal structures. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1385(2). 253–270. 28 indexed citations
17.
Arjunan, Palaniappa, Timothy C. Umland, Fred Dyda, et al.. (1996). Crystal Structure of the Thiamin Diphosphate-dependent Enzyme Pyruvate Decarboxylase from the YeastSaccharomyces cerevisiaeat 2.3 Å Resolution. Journal of Molecular Biology. 256(3). 590–600. 195 indexed citations
18.
Arora, S. K. & Palaniappa Arjunan. (1992). Molecular structure and conformation of rifamycin S, a potent inhibitor of DNA-dependent RNA polymerase.. The Journal of Antibiotics. 45(3). 428–431. 13 indexed citations
19.
Arjunan, Palaniappa, et al.. (1991). Naphthyridinomycin-DNA adducts: A molecular modeling study.. The Journal of Antibiotics. 44(8). 885–894. 5 indexed citations
20.
Arjunan, Palaniappa, et al.. (1990). Structural and Conformational Analysis of Pentostatin (2′-deoxycoformycin), a Potent Inhibitor of Adenosine Deaminase. Journal of Biomolecular Structure and Dynamics. 8(1). 199–212. 2 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.

Explore authors with similar magnitude of impact

Breakdown of academic impact, for papers by Gary A. Radke Breakdown of academic impact, for papers by Yuko Kawasaki Breakdown of academic impact, for papers by Margaret L. Fonda Breakdown of academic impact, for papers by M. Krueger Breakdown of academic impact, for papers by U. Redweik Breakdown of academic impact, for papers by W. Bruce Rowe Breakdown of academic impact, for papers by Maria L. Maccecchini Breakdown of academic impact, for papers by R. Seng Breakdown of academic impact, for papers by Joseph E. Hayes Breakdown of academic impact, for papers by G. Prezioso
Rankless by CCL
2026