N. Sukumar

1.0k total citations
35 papers, 827 citations indexed

About

N. Sukumar is a scholar working on Molecular Biology, Materials Chemistry and Organic Chemistry. According to data from OpenAlex, N. Sukumar has authored 35 papers receiving a total of 827 indexed citations (citations by other indexed papers that have themselves been cited), including 27 papers in Molecular Biology, 14 papers in Materials Chemistry and 5 papers in Organic Chemistry. Recurrent topics in N. Sukumar's work include Enzyme Structure and Function (14 papers), Porphyrin Metabolism and Disorders (7 papers) and Protein Structure and Dynamics (7 papers). N. Sukumar is often cited by papers focused on Enzyme Structure and Function (14 papers), Porphyrin Metabolism and Disorders (7 papers) and Protein Structure and Dynamics (7 papers). N. Sukumar collaborates with scholars based in United States, India and France. N. Sukumar's co-authors include F. Scott Mathews, M. Vijayan, Paul Langan, Yoshiharu Nishiyama, H. Chanzy, Victor L. Davidson, Marc Delarue, François Rougeon, Jean-Baptiste Boulé and Catherine G. Papanicolaou and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

N. Sukumar

34 papers receiving 818 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
N. Sukumar United States 15 504 180 96 84 77 35 827
Marcin Król Poland 17 456 0.9× 134 0.7× 68 0.7× 63 0.8× 117 1.5× 35 794
Craig T. Armstrong United Kingdom 14 569 1.1× 125 0.7× 122 1.3× 62 0.7× 67 0.9× 15 824
Vu Le United States 18 491 1.0× 104 0.6× 58 0.6× 46 0.5× 107 1.4× 29 802
Hairong Ma United States 21 806 1.6× 123 0.7× 120 1.3× 208 2.5× 117 1.5× 39 1.3k
Zhiyan Li China 19 447 0.9× 223 1.2× 56 0.6× 156 1.9× 245 3.2× 64 1.0k
Michael J. Palte United States 11 733 1.5× 88 0.5× 85 0.9× 155 1.8× 174 2.3× 14 1.3k
Gerald Platzer Austria 12 565 1.1× 215 1.2× 77 0.8× 49 0.6× 118 1.5× 24 905
Yousef Najajreh Israel 18 439 0.9× 203 1.1× 165 1.7× 172 2.0× 497 6.5× 31 1.2k
Jarkko Valjakka Finland 19 813 1.6× 124 0.7× 33 0.3× 116 1.4× 216 2.8× 39 1.3k
Wenjia Zhang China 18 374 0.7× 196 1.1× 131 1.4× 171 2.0× 133 1.7× 38 948

Countries citing papers authored by N. Sukumar

Since Specialization
Citations

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

Fields of papers citing papers by N. Sukumar

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of N. Sukumar

This figure shows the co-authorship network connecting the top 25 collaborators of N. Sukumar. A scholar is included among the top collaborators of N. Sukumar 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 N. Sukumar. N. Sukumar 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.
2.
Li, Shuang, et al.. (2020). Structural basis of antagonizing the vitamin K catalytic cycle for anticoagulation. Science. 371(6524). 47 indexed citations
3.
Sukumar, N., Jason O. Matos, Moonsung Choi, et al.. (2014). The sole tryptophan of amicyanin enhances its thermal stability but does not influence the electronic properties of the type 1 copper site. Archives of Biochemistry and Biophysics. 550-551. 20–27. 8 indexed citations
4.
Sukumar, N.. (2013). Crystallographic studies on B12 binding proteins in eukaryotes and prokaryotes. Biochimie. 95(5). 976–988. 9 indexed citations
5.
Sukumar, N., Moonsung Choi, & Victor L. Davidson. (2011). Replacement of the axial copper ligand methionine with lysine in amicyanin converts it to a zinc-binding protein that no longer binds copper. Journal of Inorganic Biochemistry. 105(12). 1638–1644. 4 indexed citations
6.
Choi, Moonsung, N. Sukumar, F. Scott Mathews, Aimin Liu, & Victor L. Davidson. (2011). Proline 96 of the Copper Ligand Loop of Amicyanin Regulates Electron Transfer from Methylamine Dehydrogenase by Positioning Other Residues at the Protein−Protein Interface. Biochemistry. 50(7). 1265–1273. 7 indexed citations
7.
Sukumar, N., F. Scott Mathews, Paul Langan, & Victor L. Davidson. (2010). A joint x-ray and neutron study on amicyanin reveals the role of protein dynamics in electron transfer. Proceedings of the National Academy of Sciences. 107(15). 6817–6822. 29 indexed citations
8.
Kovalevsky, Andrey, S. Zoë Fisher, Marat Mustyakimov, et al.. (2010). Preliminary neutron and X-ray crystallographic studies of equine cyanomethemoglobin. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66(4). 474–477. 4 indexed citations
9.
Sukumar, N., et al.. (2009). Structures of the G81A mutant form of the active chimera of (S)-mandelate dehydrogenase and its complex with two of its substrates. Acta Crystallographica Section D Biological Crystallography. 65(6). 543–552. 9 indexed citations
10.
Garavilla, Lawrence de, Michael N. Greco, N. Sukumar, et al.. (2005). A Novel, Potent Dual Inhibitor of the Leukocyte Proteases Cathepsin G and Chymase. Journal of Biological Chemistry. 280(18). 18001–18007. 75 indexed citations
11.
Sukumar, N., Paul Langan, F. Scott Mathews, et al.. (2005). A preliminary time-of-flight neutron diffraction study on amicyanin fromParacoccus denitrificans. Acta Crystallographica Section D Biological Crystallography. 61(5). 640–642. 12 indexed citations
12.
Sukumar, N., et al.. (2004). High Resolution Structures of an Oxidized and Reduced Flavoprotein. Journal of Biological Chemistry. 279(5). 3749–3757. 23 indexed citations
13.
Angaiah, Subramania, et al.. (2004). Development of PVA based micro-porous polymer electrolyte by a novel preferential polymer dissolution process. Journal of Power Sources. 141(1). 188–192. 38 indexed citations
14.
Delarue, Marc, Jean-Baptiste Boulé, Julien Lescar, et al.. (2002). Crystal structures of a template-independent DNA polymerase: murine terminal deoxynucleotidyltransferase. The EMBO Journal. 21(3). 427–439. 142 indexed citations
15.
Sukumar, N., Jean-Baptiste Boulé, Julien Lescar, et al.. (2000). Crystallization of the catalytic domain of murine terminal deoxynucleotidyl transferase. Acta Crystallographica Section D Biological Crystallography. 56(12). 1662–1664. 8 indexed citations
16.
Biswal, B.K., N. Sukumar, & M. Vijayan. (2000). Hydration, mobility and accessibility of lysozyme: structures of a pH 6.5 orthorhombic form and its low-humidity variant and a comparative study involving 20 crystallographically independent molecules. Acta Crystallographica Section D Biological Crystallography. 56(9). 1110–1119. 28 indexed citations
17.
Sukumar, N., et al.. (1998). Role of water in plasticity, stability, and action of proteins: The crystal structures of lysozyme at very low levels of hydration. Proteins Structure Function and Bioinformatics. 32(2). 229–240. 87 indexed citations
18.
19.
Pattabhi, V., N. Sukumar, & O. P. Sharma. (1991). ChemInform Abstract: Structure of Lantadene A, the Major Triterpenoid of Lantana Camara, Red Variety.. ChemInform. 22(29). 1 indexed citations
20.
Sukumar, N. & M L Gulrajani. (1985). Kinetics of Bleaching Agent Decomposition in a Single-Stage Preparatory Process. Textile Research Journal. 55(6). 367–371. 3 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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