C.S. Raman

5.8k total citations · 1 hit paper
42 papers, 3.2k citations indexed

About

C.S. Raman is a scholar working on Molecular Biology, Physiology and Cell Biology. According to data from OpenAlex, C.S. Raman has authored 42 papers receiving a total of 3.2k indexed citations (citations by other indexed papers that have themselves been cited), including 22 papers in Molecular Biology, 14 papers in Physiology and 11 papers in Cell Biology. Recurrent topics in C.S. Raman's work include Nitric Oxide and Endothelin Effects (14 papers), Hemoglobin structure and function (10 papers) and Metal-Catalyzed Oxygenation Mechanisms (6 papers). C.S. Raman is often cited by papers focused on Nitric Oxide and Endothelin Effects (14 papers), Hemoglobin structure and function (10 papers) and Metal-Catalyzed Oxygenation Mechanisms (6 papers). C.S. Raman collaborates with scholars based in United States, Czechia and France. C.S. Raman's co-authors include Barry T. Nall, T.L. Poulos, Pavel Martásek, Michael Pierce, Bettie Sue Siler Masters, Huiying Li, Vladimı́r Král, Pierre Nioche, Mats Hámberg and Dong‐Sun Lee and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

C.S. Raman

41 papers receiving 3.1k citations

Hit Papers

Crystal Structure of Constitutive Endothelial Nitric Oxid... 1998 2026 2007 2016 1998 100 200 300 400 500

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
C.S. Raman United States 24 1.5k 1.1k 512 396 394 42 3.2k
Haitao Ji United States 35 2.7k 1.8× 534 0.5× 235 0.5× 99 0.3× 190 0.5× 97 4.8k
Ikuko Sagami Japan 29 1.6k 1.1× 712 0.7× 742 1.4× 357 0.9× 48 0.1× 93 2.7k
Debkumar Pain United States 37 3.5k 2.3× 294 0.3× 388 0.8× 183 0.5× 501 1.3× 75 5.1k
Francesca Cutruzzolà Italy 37 3.1k 2.1× 559 0.5× 1.2k 2.3× 309 0.8× 166 0.4× 145 4.6k
Richard Wynn United States 43 3.4k 2.3× 562 0.5× 454 0.9× 217 0.5× 146 0.4× 140 5.1k
Hidehiko Nakagawa Japan 40 2.4k 1.6× 778 0.7× 163 0.3× 125 0.3× 131 0.3× 170 4.9k
Sue Goo Rhee United States 20 3.6k 2.5× 604 0.6× 925 1.8× 244 0.6× 100 0.3× 33 5.0k
Aleksandra Filipovska Australia 46 5.2k 3.5× 504 0.5× 224 0.4× 251 0.6× 93 0.2× 121 7.0k
Yoram Shechter Israel 43 3.6k 2.4× 858 0.8× 703 1.4× 363 0.9× 115 0.3× 124 7.0k
Ewald Schröder United Kingdom 19 2.9k 2.0× 566 0.5× 530 1.0× 88 0.2× 98 0.2× 22 4.2k

Countries citing papers authored by C.S. Raman

Since Specialization
Citations

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

Fields of papers citing papers by C.S. Raman

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of C.S. Raman

This figure shows the co-authorship network connecting the top 25 collaborators of C.S. Raman. A scholar is included among the top collaborators of C.S. Raman 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 C.S. Raman. C.S. Raman 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.
Yoo, Byung‐Kuk, Sergei G. Kruglik, Jean‐Christophe Lambry, et al.. (2023). The H-NOX protein structure adapts to different mechanisms in sensors interacting with nitric oxide. Chemical Science. 14(31). 8408–8420. 1 indexed citations
2.
Raman, C.S., et al.. (2019). Measuring Industry Readiness of Engineering Students of Nagpur Region with Reference to Social Skills. International Journal of Innovative Technology and Exploring Engineering. 8(9S3). 1293–1305. 1 indexed citations
3.
Cho, Kyung‐Bin, Wenzhen Lai, Mats Hámberg, C.S. Raman, & Sason Shaik. (2010). The reaction mechanism of allene oxide synthase: Interplay of theoretical QM/MM calculations and experimental investigations. Archives of Biochemistry and Biophysics. 507(1). 14–25. 16 indexed citations
4.
Lee, Dong‐Sun, Pierre Nioche, Mats Hámberg, & C.S. Raman. (2008). Structural insights into the evolutionary paths of oxylipin biosynthetic enzymes. Nature. 455(7211). 363–368. 241 indexed citations
5.
Verma, I. C., Renu Saxena, J Zeman, et al.. (2007). A New Mutation within the Porphobilinogen Deaminase Gene Leading to a Truncated Protein as a Cause of Acute Intermittent Porphyria in an Extended Indian Family. Folia Biologica. 53(6). 194–201. 3 indexed citations
6.
Pannu, H., Van Tran‐Fadulu, Christina L. Papke, et al.. (2007). MYH11 mutations result in a distinct vascular pathology driven by insulin-like growth factor 1 and angiotensin II. Human Molecular Genetics. 16(20). 2453–2462. 195 indexed citations
7.
Rekka, Eleni A., Jean‐Luc Boucher, Pierre Nioche, et al.. (2006). Analogies and surprising differences between recombinant nitric oxide synthase-like proteins from Staphylococcus aureus and Bacillus anthracis in their interactions with l-arginine analogs and iron ligands. Journal of Inorganic Biochemistry. 100(12). 2024–2033. 21 indexed citations
8.
Hrdinka, Matouš, et al.. (2006). De novo mutation found in the porphobilinogen deaminase gene in Slovak acute intermittent porphyria patient: Molecular biochemical study. Physiological Research. 55 Suppl 2. S145–S154. 8 indexed citations
9.
Berka, Vladimír, et al.. (2004). Femtomolar Sensitivity of a NO Sensor from Clostridium botulinum. Science. 306(5701). 1550–1553. 150 indexed citations
10.
Raman, C.S., Huiying Li, Pavel Martásek, et al.. (2001). Implications for Isoform-selective Inhibitor Design Derived from the Binding Mode of Bulky Isothioureas to the Heme Domain of Endothelial Nitric-oxide Synthase. Journal of Biological Chemistry. 276(28). 26486–26491. 24 indexed citations
11.
Li, Huiying, C.S. Raman, Pavel Martásek, et al.. (2000). Mapping the active site polarity in structures of endothelial nitric oxide synthase heme domain complexed with isothioureas. Journal of Inorganic Biochemistry. 81(3). 133–139. 25 indexed citations
12.
Pierce, Michael, C.S. Raman, & Barry T. Nall. (1999). Isothermal Titration Calorimetry of Protein–Protein Interactions. Methods. 19(2). 213–221. 418 indexed citations
13.
Souza, José M., Evgueni Daikhin, Marc Yudkoff, C.S. Raman, & Harry Ischiropoulos. (1999). Factors Determining the Selectivity of Protein Tyrosine Nitration. Archives of Biochemistry and Biophysics. 371(2). 169–178. 264 indexed citations
14.
Li, Huiying, C.S. Raman, Charles B. Glaser, et al.. (1999). Crystal Structures of Zinc-free and -bound Heme Domain of Human Inducible Nitric-oxide Synthase. Journal of Biological Chemistry. 274(30). 21276–21284. 179 indexed citations
15.
Martásek, Pavel, R. Timothy Miller, Qing Liu, et al.. (1998). The C331A Mutant of Neuronal Nitric-Oxide Synthase Is Defective in Arginine Binding. Journal of Biological Chemistry. 273(52). 34799–34805. 52 indexed citations
16.
Raman, C.S., Huiying Li, Pavel Martásek, et al.. (1998). Crystal Structure of Constitutive Endothelial Nitric Oxide Synthase. Cell. 95(7). 939–950. 508 indexed citations breakdown →
17.
Raaphorst, Frank M., C.S. Raman, Barry T. Nall, & Judy M. Teale. (1997). Molecular mechanisms governing reading frame choice of immunoglobulin diversity genes. Immunology Today. 18(1). 37–43. 37 indexed citations
18.
Gorovits, Boris, C.S. Raman, & Paul M. Horowitz. (1995). High Hydrostatic Pressure Induces the Dissociation of cpn60 Tetradecamers and Reveals a Plasticity of the Monomers. Journal of Biological Chemistry. 270(5). 2061–2066. 56 indexed citations
19.
Raman, C.S., Ronald Jemmerson, Barry T. Nall, & Michael J. Allen. (1992). Diffusion-limited rates for monoclonal antibody binding to cytochrome c. Biochemistry. 31(42). 10370–10379. 66 indexed citations
20.
Raman, C.S. & Katherine L. Knight. (1992). CD5+ B cells predominate in peripheral tissues of rabbit. The Journal of Immunology. 149(12). 3858–3864. 70 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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