Rajendra P. Roy

810 total citations
38 papers, 694 citations indexed

About

Rajendra P. Roy is a scholar working on Molecular Biology, Cell Biology and Genetics. According to data from OpenAlex, Rajendra P. Roy has authored 38 papers receiving a total of 694 indexed citations (citations by other indexed papers that have themselves been cited), including 28 papers in Molecular Biology, 11 papers in Cell Biology and 4 papers in Genetics. Recurrent topics in Rajendra P. Roy's work include Hemoglobin structure and function (10 papers), Biochemical and Structural Characterization (9 papers) and Protein Structure and Dynamics (6 papers). Rajendra P. Roy is often cited by papers focused on Hemoglobin structure and function (10 papers), Biochemical and Structural Characterization (9 papers) and Protein Structure and Dynamics (6 papers). Rajendra P. Roy collaborates with scholars based in India, United States and Poland. Rajendra P. Roy's co-authors include A. Seetharama Acharya, Vinay Kumar Nandicoori, Sayani Dasgupta, S. Kumaran, Sandip K. Basu, Amitabha Mukhopadhyay, Manoj Raje, Shantanu Sengupta, Ruchi Tandon and Amitabha Mukhopadhyay and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and The Journal of Immunology.

In The Last Decade

Rajendra P. Roy

37 papers receiving 684 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Rajendra P. Roy India 18 468 112 80 77 70 38 694
I. Feil United States 10 342 0.7× 64 0.6× 128 1.6× 59 0.8× 43 0.6× 12 599
Marisa E. McGrath United States 12 284 0.6× 187 1.7× 84 1.1× 148 1.9× 31 0.4× 19 655
Richard Benarous France 16 572 1.2× 242 2.2× 118 1.5× 263 3.4× 46 0.7× 37 992
C. Mark Fletcher United States 13 1.1k 2.3× 56 0.5× 129 1.6× 48 0.6× 57 0.8× 15 1.3k
Todd Mayhood United States 14 592 1.3× 79 0.7× 143 1.8× 145 1.9× 67 1.0× 19 931
Rebeca Kawahara Brazil 19 546 1.2× 125 1.1× 160 2.0× 90 1.2× 94 1.3× 43 895
Shozo Shoji Japan 19 636 1.4× 86 0.8× 172 2.1× 169 2.2× 112 1.6× 73 971
Brandi Levin United States 12 443 0.9× 105 0.9× 132 1.6× 129 1.7× 18 0.3× 20 939
Mai B. Margetts Australia 13 741 1.6× 75 0.7× 109 1.4× 28 0.4× 44 0.6× 19 1.1k
Jessica L. Bridgford Australia 9 308 0.7× 123 1.1× 113 1.4× 87 1.1× 61 0.9× 9 866

Countries citing papers authored by Rajendra P. Roy

Since Specialization
Citations

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

Fields of papers citing papers by Rajendra P. Roy

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Rajendra P. Roy. 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 Rajendra P. Roy. The network helps show where Rajendra P. Roy may publish in the future.

Co-authorship network of co-authors of Rajendra P. Roy

This figure shows the co-authorship network connecting the top 25 collaborators of Rajendra P. Roy. A scholar is included among the top collaborators of Rajendra P. Roy 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 Rajendra P. Roy. Rajendra P. Roy 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.
Dhanasekaran, Karthigeyan, et al.. (2024). Unravelling HDAC Selectivity for Erasing Acetyl Mark on Lys‐5 of Histone H2B. ChemBioChem. 25(5). e202300875–e202300875.
2.
Misra, Anurag, et al.. (2020). Interrogation of 3D-swapped structure and functional attributes of quintessential Sortase A from Streptococcus pneumoniae. Biochemical Journal. 477(24). 4711–4728. 1 indexed citations
3.
Singh, Shikha, et al.. (2019). Sortase-click strategy for defined protein conjugation on a heptavalent cyclodextrin scaffold. PLoS ONE. 14(5). e0217369–e0217369. 11 indexed citations
4.
Roy, Rajendra P., et al.. (2018). Facile One‐Step Assembly of Bona Fide SUMO Conjugates by Chemoenzymatic Ligation. ChemBioChem. 19(11). 1137–1141. 4 indexed citations
5.
6.
Gupta, Kanchan, et al.. (2016). Asymmetric DNA methylation by dimeric EcoP15I DNA methyltransferase. Biochimie. 128-129. 70–82. 3 indexed citations
7.
Dasgupta, Sayani, et al.. (2011). Isopeptide Ligation Catalyzed by Quintessential Sortase A. Journal of Biological Chemistry. 286(27). 23996–24006. 26 indexed citations
8.
Misra, Anurag, et al.. (2011). Crystallization and preliminary X-ray diffraction studies of sortase A fromStreptococcus pneumoniae. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67(10). 1195–1198. 4 indexed citations
9.
Khan, Shazia, Albel Singh, Devanand Kumar, et al.. (2010). Phosphorylation of Enoyl-Acyl Carrier Protein Reductase InhA Impacts Mycobacterial Growth and Survival. Journal of Biological Chemistry. 285(48). 37860–37871. 65 indexed citations
10.
Mondal, Kalyani, H. B. Bohidar, Rajendra P. Roy, & Munishwar Nath Gupta. (2006). Alginate-chaperoned facile refolding of Chromobacterium viscosum lipase. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1764(5). 877–886. 20 indexed citations
11.
Choudhury, Devapriya, et al.. (2004). Linkage of Interactions in Sickle Hemoglobin Fiber Assembly. Journal of Biological Chemistry. 279(19). 20018–20027. 3 indexed citations
12.
Roy, Rajendra P., et al.. (2002). Volume Exclusion Effect as a Driving Force for Reverse Proteolysis. Journal of Biological Chemistry. 277(45). 43253–43261. 33 indexed citations
13.
Roy, Rajendra P., et al.. (2001). A Role for the α113 (GH1) Amino Acid Residue in the Polymerization of Sickle Hemoglobin. Journal of Biological Chemistry. 276(21). 18209–18215. 9 indexed citations
14.
Sengupta, Shantanu, Ruchi Tandon, Manoj Raje, et al.. (1999). Hemoglobin Endocytosis in Leishmania Is Mediated through a 46-kDa Protein Located in the Flagellar Pocket. Journal of Biological Chemistry. 274(5). 2758–2765. 67 indexed citations
15.
Nayak, Bishnu P., Renu Tuteja, Venkatasamy Manivel, et al.. (1998). B Cell Responses to a Peptide Epitope. V. Kinetic Regulation of Repertoire Discrimination and Antibody Optimization for Epitope. The Journal of Immunology. 161(7). 3510–3519. 24 indexed citations
16.
17.
Vijayakrishnan, Lalitha, et al.. (1997). B cell responses to a peptide epitope: IV. Subtle sequence changes in flanking residues modulate immunogenicity. The Journal of Immunology. 159(4). 1809–1819. 20 indexed citations
18.
Nacharaju, Parimala, Rajendra P. Roy, Steven P. White, Ronald L. Nagel, & A. Seetharama Acharya. (1997). Inhibition of Sickle β-Chain (βS)-dependent Polymerization by Nonhuman α-Chains. Journal of Biological Chemistry. 272(44). 27869–27876. 12 indexed citations
19.
Roy, Rajendra P. & A. Seetharama Acharya. (1994). [12] Semisynthesis of hemoglobin. Methods in enzymology on CD-ROM/Methods in enzymology. 231. 194–215. 17 indexed citations
20.
Roy, Rajendra P., Kiran Khandke, Belur N. Manjula, & A. Seetharama Acharya. (1992). Helix formation in enzymically ligated peptides as a driving force for the synthetic reaction: example of .alpha.-globin semisynthetic reaction. Biochemistry. 31(32). 7249–7255. 12 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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