Siddhartha Roy

3.8k total citations
136 papers, 3.1k citations indexed

About

Siddhartha Roy is a scholar working on Molecular Biology, Materials Chemistry and Oncology. According to data from OpenAlex, Siddhartha Roy has authored 136 papers receiving a total of 3.1k indexed citations (citations by other indexed papers that have themselves been cited), including 110 papers in Molecular Biology, 27 papers in Materials Chemistry and 22 papers in Oncology. Recurrent topics in Siddhartha Roy's work include RNA and protein synthesis mechanisms (37 papers), DNA and Nucleic Acid Chemistry (35 papers) and Protein Structure and Dynamics (26 papers). Siddhartha Roy is often cited by papers focused on RNA and protein synthesis mechanisms (37 papers), DNA and Nucleic Acid Chemistry (35 papers) and Protein Structure and Dynamics (26 papers). Siddhartha Roy collaborates with scholars based in India, United States and Japan. Siddhartha Roy's co-authors include Sankar Adhya, Ettore Appella, M. Vijayan, Gordon A. Vehar, Alfred G. Redfield, Kazuyasu Sakaguchi, Tapas K. Kundu, Carl W. Anderson, Yuichiro Higashimoto and Shinichi Saito and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Nucleic Acids Research.

In The Last Decade

Siddhartha Roy

132 papers receiving 3.0k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Siddhartha Roy India 33 2.3k 501 432 367 269 136 3.1k
Lanette Fee United States 10 2.9k 1.3× 372 0.7× 330 0.8× 717 2.0× 358 1.3× 12 4.0k
Steven R. Jordan United States 24 2.2k 0.9× 501 1.0× 406 0.9× 280 0.8× 131 0.5× 46 3.2k
F. Niesen United Kingdom 19 2.7k 1.1× 422 0.8× 261 0.6× 443 1.2× 401 1.5× 25 3.5k
James G. Omichinski United States 38 3.7k 1.6× 806 1.6× 374 0.9× 506 1.4× 217 0.8× 106 4.8k
Marc Whitlow United States 34 3.9k 1.6× 803 1.6× 216 0.5× 720 2.0× 194 0.7× 63 5.9k
John Spurlino United States 24 1.6k 0.7× 538 1.1× 485 1.1× 707 1.9× 177 0.7× 42 2.8k
J. Günter Grossmann United Kingdom 35 2.4k 1.0× 205 0.4× 345 0.8× 705 1.9× 465 1.7× 61 3.4k
Petr Kuzmič United States 26 2.3k 1.0× 569 1.1× 188 0.4× 420 1.1× 134 0.5× 65 3.5k
F.K. Winkler Switzerland 18 2.5k 1.1× 432 0.9× 385 0.9× 350 1.0× 278 1.0× 32 4.1k
Martin Högbom Sweden 31 2.3k 1.0× 476 1.0× 378 0.9× 499 1.4× 111 0.4× 103 3.3k

Countries citing papers authored by Siddhartha Roy

Since Specialization
Citations

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

Fields of papers citing papers by Siddhartha Roy

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Siddhartha Roy

This figure shows the co-authorship network connecting the top 25 collaborators of Siddhartha Roy. A scholar is included among the top collaborators of Siddhartha 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 Siddhartha Roy. Siddhartha 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.
2.
Mukherjee, Shatavisa, et al.. (2024). Safety incident reporting and barriers (SIRaB) study: Strategies and approaches for investigating patient safety events in a hospital set‐up. Journal of Evaluation in Clinical Practice. 30(4). 651–659.
3.
Ghosh, Mrinal K., et al.. (2023). A small HDM2 antagonist peptide and a USP7 inhibitor synergistically inhibit the p53‐HDM2‐USP7 circuit. Chemical Biology & Drug Design. 102(1). 126–136. 1 indexed citations
4.
Mukherjee, Sujoy, et al.. (2021). DNA-Bound p53-DNA-Binding Domain Interconverts between Multiple Conformations: Implications for Partner Protein Recognition. The Journal of Physical Chemistry B. 125(22). 5832–5837. 5 indexed citations
5.
Chakraborty, Prasenjit, Dhrubajyoti Chattopadhyay, & Siddhartha Roy. (2021). N-protein-RNA interaction is a drug target in a negative strand RNA virus. Virus Research. 295. 198298–198298. 4 indexed citations
6.
Dhar, Amlanjyoti, et al.. (2020). A Peptide‐PNA Hybrid Beacon for Sensitive Detection of Protein Biomarkers in Biological Fluids. ChemBioChem. 21(15). 2121–2125. 4 indexed citations
7.
Banik, Suman Kumar, et al.. (2020). Bi‐stability of the master gene regulatory network of the common dendritic precursor cell: Implications for cell differentiation. IUBMB Life. 72(10). 2225–2232. 2 indexed citations
8.
Kundu, Tapas K., et al.. (2019). Tumor Suppressor p53-Mediated Structural Reorganization of the Transcriptional Coactivator p300. Biochemistry. 58(32). 3434–3443. 16 indexed citations
9.
Roy, Koushik, et al.. (2018). A peptide-based synthetic transcription factor selectively activates transcription in a mammalian cell. Chemical Communications. 54(13). 1611–1614. 2 indexed citations
10.
Debnath, Subrata, et al.. (2018). Enhanced basepair dynamics pre-disposes protein-assisted flips of key bases in DNA strand separation during transcription initiation. Physical Chemistry Chemical Physics. 20(14). 9449–9459. 2 indexed citations
11.
Choudhury, Susobhan, et al.. (2018). A Potent Conformation-Constrained Synthetic Peptide Mimic of a Homeodomain Selectively Regulates Target Genes in Cells. ACS Chemical Biology. 13(8). 2003–2009. 2 indexed citations
12.
Mazumder, Abhishek, Subrata Batabyal, Susobhan Choudhury, et al.. (2017). Specific DNA sequences allosterically enhance protein–protein interaction in a transcription factor through modulation of protein dynamics: implications for specificity of gene regulation. Physical Chemistry Chemical Physics. 19(22). 14781–14792. 1 indexed citations
13.
Debnath, Subrata, Snehajyoti Chatterjee, Arif Mohammed, Tapas K. Kundu, & Siddhartha Roy. (2011). Peptide-Protein Interactions Suggest That Acetylation of Lysines 381 and 382 of p53 Is Important for Positive Coactivator 4-p53 Interaction. Journal of Biological Chemistry. 286(28). 25076–25087. 13 indexed citations
14.
Roy, Siddhartha, Catherine A. Musselman, Ioulia Kachirskaia, et al.. (2010). Structural Insight into p53 Recognition by the 53BP1 Tandem Tudor Domain. Journal of Molecular Biology. 398(4). 489–496. 48 indexed citations
15.
Selvaraj, Muniyandi, N. Sadananda Singh, Siddhartha Roy, et al.. (2006). Cloning, expression, purification, crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase fromMycobacterium tuberculosis. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62(9). 913–915. 7 indexed citations
16.
Liu, Mo‐Fang, et al.. (2003). Kinetics of Transcription Initiation at lacP1. Journal of Biological Chemistry. 278(41). 39755–39761. 19 indexed citations
17.
Manna, Tapas, et al.. (2000). Sulfhydryls of tubulin. European Journal of Biochemistry. 267(12). 3469–3476. 41 indexed citations
18.
Roy, Siddhartha, et al.. (1998). An apyrase from Mimosa pudica contains N5,N10‐methenyl tetrahydrofolate and is stimulated by light. European Journal of Biochemistry. 258(3). 1009–1013. 14 indexed citations
19.
Sengupta, Suparna, Kamal D. Puri, Avadhesha Surolia, Siddhartha Roy, & Bhabatarak Bhattacharyya. (1993). N‐(7‐Nitrobenz‐2‐oxa‐1,3‐diazol‐4‐yI)colcemid, a probe for different classes of colchincine‐binding site on tubulin. European Journal of Biochemistry. 212(2). 387–393. 8 indexed citations
20.
Bhattacharyya, Bhabatarak, et al.. (1992). Multiphasic denaturation of the λ repressor by urea and its implications for the repressor structure. European Journal of Biochemistry. 206(1). 15–21. 34 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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