M. Vijayan

6.2k total citations
223 papers, 5.2k citations indexed

About

M. Vijayan is a scholar working on Molecular Biology, Materials Chemistry and Organic Chemistry. According to data from OpenAlex, M. Vijayan has authored 223 papers receiving a total of 5.2k indexed citations (citations by other indexed papers that have themselves been cited), including 168 papers in Molecular Biology, 87 papers in Materials Chemistry and 52 papers in Organic Chemistry. Recurrent topics in M. Vijayan's work include Enzyme Structure and Function (82 papers), Glycosylation and Glycoproteins Research (60 papers) and Carbohydrate Chemistry and Synthesis (47 papers). M. Vijayan is often cited by papers focused on Enzyme Structure and Function (82 papers), Glycosylation and Glycoproteins Research (60 papers) and Carbohydrate Chemistry and Synthesis (47 papers). M. Vijayan collaborates with scholars based in India, United States and Canada. M. Vijayan's co-authors include Avadhesha Surolia, Nagasuma Chandra, K. Suguna, C.G. Suresh, K. Sekar, Thirumaleshwara N. Bhat, R. Banerjee, R. Ravishankar, Vivek Sharma and Rajan Sankaranarayanan and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

M. Vijayan

219 papers receiving 5.1k citations

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
M. Vijayan 3.7k 1.4k 1.2k 760 681 223 5.2k
Neil W. Isaacs 6.4k 1.7× 566 0.4× 1.9k 1.5× 526 0.7× 567 0.8× 140 9.3k
Matthew P. Crump 3.5k 0.9× 1.9k 1.4× 813 0.7× 658 0.9× 201 0.3× 142 5.9k
David G. Gorenstein 5.6k 1.5× 1.4k 1.0× 706 0.6× 261 0.3× 255 0.4× 257 8.5k
Anders Liljas 5.7k 1.5× 944 0.7× 1.3k 1.0× 269 0.4× 722 1.1× 122 6.7k
M. Chruszcz 4.4k 1.2× 672 0.5× 1.2k 1.0× 349 0.5× 173 0.3× 163 7.2k
Simon E. V. Phillips 5.6k 1.5× 508 0.4× 1.3k 1.0× 501 0.7× 226 0.3× 151 8.4k
J. Feeney 4.4k 1.2× 1.4k 1.0× 1.6k 1.3× 460 0.6× 246 0.4× 241 7.3k
Gerald R. Grimsley 5.5k 1.5× 511 0.4× 1.6k 1.3× 374 0.5× 216 0.3× 31 7.3k
Gerald Zon 6.4k 1.7× 1.8k 1.3× 500 0.4× 638 0.8× 167 0.2× 207 9.3k
Miquel Pons 3.3k 0.9× 1.2k 0.9× 1.0k 0.8× 250 0.3× 206 0.3× 173 5.2k

Countries citing papers authored by M. Vijayan

Since Specialization
Citations

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

Fields of papers citing papers by M. Vijayan

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of M. Vijayan

This figure shows the co-authorship network connecting the top 25 collaborators of M. Vijayan. A scholar is included among the top collaborators of M. Vijayan 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 M. Vijayan. M. Vijayan 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.
Vijayan, M., et al.. (2017). A Mutation Directs the Structural Switch of DNA Binding Proteins under Starvation to a Ferritin-like Protein Cage. Structure. 25(9). 1449–1454.e3. 7 indexed citations
2.
Varshney, Umesh, et al.. (2017). Hydrolysis of diadenosine polyphosphates. Exploration of an additional role of Mycobacterium smegmatis MutT1. Journal of Structural Biology. 199(3). 165–176. 14 indexed citations
3.
Kumar, Pradeep, et al.. (2017). Biochemical and structural studies of mutants indicate concerted movement of the dimer interface and ligand-binding region ofMycobacterium tuberculosispantothenate kinase. Acta Crystallographica Section F Structural Biology Communications. 73(11). 635–643. 3 indexed citations
4.
Varshney, Umesh, et al.. (2017). Biochemical and structural studies ofMycobacterium smegmatisMutT1, a sanitization enzyme with unusual modes of association. Acta Crystallographica Section D Structural Biology. 73(4). 349–364. 14 indexed citations
5.
Varshney, Umesh, et al.. (2016). Structure of the second Single Stranded DNA Binding protein (SSBb) from Mycobacterium smegmatis. Journal of Structural Biology. 196(3). 448–454. 7 indexed citations
6.
Prabu, J. Rajan, et al.. (2015). Structural studies on Mycobacterium tuberculosis RecA: Molecular plasticity and interspecies variability. Journal of Biosciences. 40(1). 13–30. 11 indexed citations
7.
Patra, Dhabaleswar, et al.. (2014). Structure, interactions and evolutionary implications of a domain-swapped lectin dimer from Mycobacterium smegmatis. Glycobiology. 24(10). 956–965. 13 indexed citations
8.
Vijayan, M., et al.. (2013). Generation of Ligand Specificity and Modes of Oligomerization in β-Prism I Fold Lectins. Advances in protein chemistry and structural biology. 92. 135–178. 10 indexed citations
9.
Saikrishnan, K., G. Manjunath, Pawan Singh, et al.. (2005). STRUCTURE OF MYCOBACTERIUM SMEGMATIS SINGLE-STRANDED DNA-BINDING PROTEIN AND A COMPARATIVE STUDY INVOLVING HOMOLOGUS SSBS: BIOLOGICAL IMPLICATIONS OF STRUCTURAL PLASTICITY AND VARIABILITY IN QUATERNARY ASSOCIATION. Structure. 12. 1 indexed citations
10.
Muniyappa, K., N. Ganesh, Pawan Singh, et al.. (2004). Homologous recombination in mycobacteria. Current Science. 86(1). 141–148. 2 indexed citations
11.
Vijayan, M.. (2003). Structural genomics of microbial pathogens – An Indian programme. NOT FOUND REPOSITORY (Indian Institute of Science Bangalore). 2 indexed citations
12.
Saraswathi, N.T., Siddhartha Roy, & M. Vijayan. (2003). X-ray studies on crystalline complexes involving amino acids and peptides. XLI. Commonalities in aggregation and conformation revealed by the crystal structures of the pimelic acid complexes of L-arginine and DL-lysine. Acta Crystallographica Section B Structural Science. 59(5). 641–646. 15 indexed citations
13.
Saikrishnan, K., R. Ravishankar, Siddhartha Roy, et al.. (2002). Domain closure and action of uracil DNA glycosylase (UDG): structures of new crystal forms containing the Escherichia coli enzyme and a comparative study of the known structures involving UDG. Acta Crystallographica Section D Biological Crystallography. 58(8). 1269–1276. 16 indexed citations
14.
Jeyaprakash, A. Arockia, G. Bhanuprakash Reddy, Christian Betzel, et al.. (2002). Crystal Structure of the Jacalin–T-antigen Complex and a Comparative Study of Lectin–T-antigen Complexes. Journal of Molecular Biology. 321(4). 637–645. 76 indexed citations
15.
16.
Manoj, N., V. R. Srinivas, Avadhesha Surolia, M. Vijayan, & K. Suguna. (2000). Carbohydrate specificity and salt-bridge mediated conformational change in acidic winged bean agglutinin 1 1Edited by A. Klug. Journal of Molecular Biology. 302(5). 1129–1137. 33 indexed citations
17.
Baker, Edward N., Tom L. Blundell, E.J. Dodson, et al.. (1996). Diffraction data deposition. Structure. 4(2). 217–217. 1 indexed citations
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20.
Vijayan, M.. (1988). Molecular interactions and aggregation involving amino acids and peptides and their role in chemical evolution. Progress in Biophysics and Molecular Biology. 52(2). 71–99. 54 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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