S. Raghothama

3.0k total citations
104 papers, 2.6k citations indexed

About

S. Raghothama is a scholar working on Molecular Biology, Organic Chemistry and Spectroscopy. According to data from OpenAlex, S. Raghothama has authored 104 papers receiving a total of 2.6k indexed citations (citations by other indexed papers that have themselves been cited), including 76 papers in Molecular Biology, 38 papers in Organic Chemistry and 19 papers in Spectroscopy. Recurrent topics in S. Raghothama's work include Chemical Synthesis and Analysis (55 papers), Carbohydrate Chemistry and Synthesis (24 papers) and Protein Structure and Dynamics (18 papers). S. Raghothama is often cited by papers focused on Chemical Synthesis and Analysis (55 papers), Carbohydrate Chemistry and Synthesis (24 papers) and Protein Structure and Dynamics (18 papers). S. Raghothama collaborates with scholars based in India, United States and United Kingdom. S. Raghothama's co-authors include Padmanabhan Balaram, P. Balaram, N. Shamala, Isabella L. Karle, Satish Kumar Awasthi, Rajkishor Rai, Kenny B. Lipkowitz, Radhakrishnan Mahalakshmi, P. J. Simpson and Michael P. Williamson and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Advanced Materials.

In The Last Decade

S. Raghothama

102 papers receiving 2.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
S. Raghothama India 32 1.9k 940 422 342 321 104 2.6k
R. Scott Lokey United States 35 3.7k 2.0× 1.6k 1.7× 302 0.7× 623 1.8× 327 1.0× 84 5.0k
Jianmin Gao United States 38 2.8k 1.5× 1.3k 1.4× 244 0.6× 111 0.3× 245 0.8× 100 3.8k
Patrick Perlmutter Australia 27 1.4k 0.7× 1.4k 1.5× 347 0.8× 178 0.5× 186 0.6× 156 3.2k
Cristina Nativi Italy 32 2.0k 1.1× 2.0k 2.1× 266 0.6× 167 0.5× 455 1.4× 174 3.7k
Suryanarayanarao Ramakumar India 27 1.4k 0.8× 642 0.7× 292 0.7× 110 0.3× 153 0.5× 71 2.1k
Sébastien Vidal France 34 2.4k 1.3× 2.3k 2.5× 306 0.7× 124 0.4× 267 0.8× 103 3.7k
Paul Boullanger France 28 1.7k 0.9× 1.5k 1.6× 292 0.7× 93 0.3× 122 0.4× 104 2.5k
Juan Luis Asensio Spain 41 3.2k 1.8× 2.1k 2.2× 136 0.3× 128 0.4× 329 1.0× 115 4.1k
Ruthven N.A.H. Lewis Canada 39 3.8k 2.0× 786 0.8× 290 0.7× 802 2.3× 286 0.9× 97 4.4k
Normand Voyer Canada 24 1.3k 0.7× 827 0.9× 274 0.6× 279 0.8× 560 1.7× 119 2.1k

Countries citing papers authored by S. Raghothama

Since Specialization
Citations

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

Fields of papers citing papers by S. Raghothama

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of S. Raghothama

This figure shows the co-authorship network connecting the top 25 collaborators of S. Raghothama. A scholar is included among the top collaborators of S. Raghothama 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 S. Raghothama. S. Raghothama 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.
Singh, Manmeet, Bankala Krishnarjuna, S. Raghothama, et al.. (2019). A proline insertion-deletion in the spike glycoprotein fusion peptide of mouse hepatitis virus strongly alters neuropathology. Journal of Biological Chemistry. 294(20). 8064–8087. 24 indexed citations
2.
Brahmkhatri, Varsha, et al.. (2018). Curcumin nanoconjugate inhibits aggregation of N-terminal region (Aβ-16) of an amyloid beta peptide. New Journal of Chemistry. 42(24). 19881–19892. 37 indexed citations
3.
Reid, Korey M., et al.. (2017). Ensemble characterization of an intrinsically disordered FG‐Nup peptide and its F>A mutant in DMSO‐d6. Biopolymers. 108(6). 1 indexed citations
4.
Dey, Debayan, et al.. (2017). Conformational heterogeneity in tails of DNA-binding proteins is augmented by proline containing repeats. Molecular BioSystems. 13(12). 2531–2544. 2 indexed citations
5.
Krishnarjuna, Bankala, Christopher A. MacRaild, Rodrigo A. V. Morales, et al.. (2017). Structure, folding and stability of a minimal homologue from Anemonia sulcata of the sea anemone potassium channel blocker ShK. Peptides. 99. 169–178. 23 indexed citations
6.
7.
Sonti, Rajesh, et al.. (2014). Conformational Analysis of a 20‐Membered Cyclic Peptide Disulfide from Conus virgo with a WPW Segment: Evidence for an Aromatic–Proline Sandwich. Chemistry - A European Journal. 20(17). 5075–5086. 5 indexed citations
8.
Makwana, Kamlesh M., S. Raghothama, & Radhakrishnan Mahalakshmi. (2013). Stabilizing effect of electrostatic vs. aromatic interactions in diproline nucleated peptide β-hairpins. Physical Chemistry Chemical Physics. 15(37). 15321–15321. 8 indexed citations
9.
Chandrappa, S., S. Aravinda, S. Raghothama, et al.. (2012). Helix and hairpin nucleation in short peptides using centrally positioned conformationally constrained dipeptide segments. Organic & Biomolecular Chemistry. 10(14). 2815–2815. 4 indexed citations
10.
Jayanthi, S., Bhaswati Chatterjee, & S. Raghothama. (2009). Natural abundant solid state NMR studies in designed tripeptides for differentiation of multiple conformers. Biopolymers. 91(10). 851–860. 4 indexed citations
11.
Chatterjee, Bhaswati, Indranil Saha, S. Raghothama, et al.. (2008). Designed Peptides with Homochiral and Heterochiral Diproline Templates as Conformational Constraints. Chemistry - A European Journal. 14(20). 6192–6204. 60 indexed citations
12.
Rai, Rajkishor, Prema G. Vasudev, Kuppanna Ananda, et al.. (2007). Hybrid Peptides: Expanding the β Turn in Peptide Hairpins by the Insertion of β‐, γ‐, and δ‐Residues. Chemistry - A European Journal. 13(20). 5917–5926. 54 indexed citations
13.
14.
Mahalakshmi, Radhakrishnan, Anindita Sengupta, S. Raghothama, N. Shamala, & P. Balaram. (2005). Tryptophan‐containing peptide helices: interactions involving the indole side chain*. Journal of Peptide Research. 66(5). 277–296. 19 indexed citations
15.
Raghothama, S., et al.. (2004). Two Novel Hexadepsipeptides with Several Modified Amino Acid Residues Isolated from the Fungus Isaria. Chemistry & Biodiversity. 1(3). 489–504. 31 indexed citations
16.
Awasthi, Satish Kumar, et al.. (2001). Solvent-induced ?-hairpin to helix conformational transition in a designed peptide. Biopolymers. 58(5). 465–476. 30 indexed citations
17.
Das, Chittaranjan, P. Balaram, Vijayashree Nayak, & S. Raghothama. (2000). Synthetic protein design: construction of a four‐stranded β‐sheet structure and evaluation of its integrity in methanol–water systems. Journal of Peptide Research. 56(5). 307–317. 14 indexed citations
18.
Banerjee, Arindam, et al.. (1998). Ambidextrous molecules: Cylindrical peptide structures formed by fusing left- and right-handed helices. Biopolymers. 39(3). 279–285. 22 indexed citations
19.
Awasthi, Satish Kumar, S. Raghothama, & P. Balaram. (1995). A Designed β-Hairpin Peptide. Biochemical and Biophysical Research Communications. 216(1). 375–381. 74 indexed citations
20.
Kishore, R., S. Raghothama, & P. Balaram. (1988). Synthetic peptide models for the redox-active disulfide loop of glutaredoxin. Conformational studies. Biochemistry. 27(7). 2462–2471. 28 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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