Rahul S. Rajan

2.1k total citations
24 papers, 1.7k citations indexed

About

Rahul S. Rajan is a scholar working on Molecular Biology, Materials Chemistry and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, Rahul S. Rajan has authored 24 papers receiving a total of 1.7k indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 7 papers in Materials Chemistry and 4 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in Rahul S. Rajan's work include Protein purification and stability (6 papers), Monoclonal and Polyclonal Antibodies Research (4 papers) and Magnetism in coordination complexes (4 papers). Rahul S. Rajan is often cited by papers focused on Protein purification and stability (6 papers), Monoclonal and Polyclonal Antibodies Research (4 papers) and Magnetism in coordination complexes (4 papers). Rahul S. Rajan collaborates with scholars based in India, United States and France. Rahul S. Rajan's co-authors include Ron R. Kopito, Michelle Illing, Neil Bence, Nitin Rathore, P. Balaram, K. S. Gandhi, Rajeev Kumar, Stephen R. Brych, Michael J. Treuheit and Tiansheng Li and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and The Journal of Chemical Physics.

In The Last Decade

Rahul S. Rajan

23 papers receiving 1.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Rahul S. Rajan India 14 1.2k 315 289 253 193 24 1.7k
Rosaria P. Haugland United States 15 826 0.7× 156 0.5× 226 0.8× 91 0.4× 144 0.7× 20 1.5k
Ying‐Xin Fan China 16 1.0k 0.9× 264 0.8× 157 0.5× 101 0.4× 421 2.2× 28 1.5k
Theodore L. Hazlett United States 25 1.5k 1.3× 115 0.4× 114 0.4× 206 0.8× 199 1.0× 43 2.1k
Feng He United States 26 1.4k 1.2× 542 1.7× 100 0.3× 210 0.8× 147 0.8× 60 1.7k
Virender K. Sarin United States 18 1.4k 1.2× 247 0.8× 106 0.4× 149 0.6× 86 0.4× 25 2.0k
Catherine Vénien‐Bryan France 29 1.8k 1.6× 89 0.3× 271 0.9× 193 0.8× 201 1.0× 79 2.5k
László Mátyus Hungary 21 1.0k 0.9× 139 0.4× 126 0.4× 119 0.5× 181 0.9× 54 1.7k
Tudor Arvinte Switzerland 26 1.5k 1.3× 394 1.3× 176 0.6× 87 0.3× 94 0.5× 60 2.1k
Masanori Osawa Japan 27 1.6k 1.4× 85 0.3× 324 1.1× 410 1.6× 223 1.2× 70 2.3k
Holger Eickhoff Germany 20 1.3k 1.1× 262 0.8× 70 0.2× 290 1.1× 95 0.5× 36 2.1k

Countries citing papers authored by Rahul S. Rajan

Since Specialization
Citations

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

Fields of papers citing papers by Rahul S. Rajan

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Rahul S. Rajan. 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 Rahul S. Rajan. The network helps show where Rahul S. Rajan may publish in the future.

Co-authorship network of co-authors of Rahul S. Rajan

This figure shows the co-authorship network connecting the top 25 collaborators of Rahul S. Rajan. A scholar is included among the top collaborators of Rahul S. Rajan 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 Rahul S. Rajan. Rahul S. Rajan 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
2.
Rajan, Rahul S., et al.. (2023). Ecological Insights from Phytoplankton Diversity Off Veraval, Gujarat Coast, India. Ecology Environment and Conservation. 29. S314–S320.
3.
Rajan, Rahul S., et al.. (2023). Barcoding Mullets (Mugilidae): Genetic Characterization of Exploited Species in Southern Peninsular India. Diversity. 15(12). 1193–1193. 2 indexed citations
5.
Brych, Stephen R., et al.. (2010). Increased aggregation propensity of IgG2 subclass over IgG1: Role of conformational changes and covalent character in isolated aggregates. Protein Science. 19(9). 1601–1615. 54 indexed citations
6.
Rajan, Rahul S., et al.. (2010). Chemical and Pharmacological Chaperones: Application for Recombinant Protein Production and Protein Folding Diseases. Current Medicinal Chemistry. 18(1). 1–15. 70 indexed citations
7.
Brych, Stephen R., et al.. (2009). Characterization of antibody aggregation: Role of buried, unpaired cysteines in particle formation. Journal of Pharmaceutical Sciences. 99(2). 764–781. 79 indexed citations
8.
Rathore, Nitin & Rahul S. Rajan. (2008). Current Perspectives on Stability of Protein Drug Products during Formulation, Fill and Finish Operations. Biotechnology Progress. 24(3). 504–514. 220 indexed citations
9.
Rajan, Rahul S., Tiansheng Li, Mohini Aras, et al.. (2006). Modulation of protein aggregation by polyethylene glycol conjugation: GCSF as a case study. Protein Science. 15(5). 1063–1075. 95 indexed citations
10.
Chelius, Dirk, Douglas S. Rehder, Thomas M. Dillon, et al.. (2006). Formation of Pyroglutamic Acid from N-Terminal Glutamic Acid in Immunoglobulin Gamma Antibodies. Analytical Chemistry. 78(7). 2370–2376. 160 indexed citations
11.
Rajan, Rahul S. & Ron R. Kopito. (2004). Suppression of Wild-type Rhodopsin Maturation by Mutants Linked to Autosomal Dominant Retinitis Pigmentosa. Journal of Biological Chemistry. 280(2). 1284–1291. 67 indexed citations
12.
Illing, Michelle, Rahul S. Rajan, Neil Bence, & Ron R. Kopito. (2002). A Rhodopsin Mutant Linked to Autosomal Dominant Retinitis Pigmentosa Is Prone to Aggregate and Interacts with the Ubiquitin Proteasome System. Journal of Biological Chemistry. 277(37). 34150–34160. 266 indexed citations
13.
Rajan, Rahul S., Michelle Illing, Neil Bence, & Ron R. Kopito. (2001). Specificity in intracellular protein aggregation and inclusion body formation. Proceedings of the National Academy of Sciences. 98(23). 13060–13065. 185 indexed citations
14.
Rajan, Rahul S., Satish Kumar Awasthi, Surajit Bhattacharjya, & P. Balaram. (1997). “Teflon-coated peptides”: Hexafluoroacetone trihydrate as a structure stabilizer for peptides. Biopolymers. 42(2). 125–128. 62 indexed citations
15.
Rajan, Rahul S. & P. Balaram. (1996). A model for the interaction of trifluoroethanol with peptides and proteins. International journal of peptide & protein research. 48(4). 328–336. 174 indexed citations
16.
Rajan, Rahul S., et al.. (1963). Electron Spin Resonance in Ethylenediamine Complexes of Copper (II) Sulfate. The Journal of Chemical Physics. 39(4). 1140–1142. 13 indexed citations
17.
Rajan, Rahul S.. (1963). Electron spin resonance in copper (II) monoethylenediamine chloride. Physica. 29(11). 1191–1195. 5 indexed citations
18.
Rajan, Rahul S.. (1962). Electron spin resonance in cupric acid fluoride. Physica. 28(12). 1329–1334. 3 indexed citations
19.
Rajan, Rahul S.. (1962). Electron Spin Resonance in Ethylene Diamine Copper (II) Nitrate. The Journal of Chemical Physics. 37(8). 1901–1902. 8 indexed citations
20.
Rajan, Rahul S.. (1962). Electron Spin Resonance in Copper(II) Malonate. The Journal of Chemical Physics. 37(2). 460–461. 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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