K. K. Kannan

2.1k total citations · 1 hit paper
39 papers, 1.6k citations indexed

About

K. K. Kannan is a scholar working on Molecular Biology, Materials Chemistry and Physical and Theoretical Chemistry. According to data from OpenAlex, K. K. Kannan has authored 39 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 26 papers in Molecular Biology, 10 papers in Materials Chemistry and 9 papers in Physical and Theoretical Chemistry. Recurrent topics in K. K. Kannan's work include Enzyme function and inhibition (13 papers), Chemical Reactions and Mechanisms (8 papers) and Enzyme Structure and Function (6 papers). K. K. Kannan is often cited by papers focused on Enzyme function and inhibition (13 papers), Chemical Reactions and Mechanisms (8 papers) and Enzyme Structure and Function (6 papers). K. K. Kannan collaborates with scholars based in India, Sweden and United States. K. K. Kannan's co-authors include Seved Lövgren, K. Fridborg, B. Strandberg, Anders Liljas, M. Ramanadham, M. A. Viswamitra, T. Alwyn Jones, M.V. Hosur, Bindu Pillai and Lina Nyström and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Molecular Biology.

In The Last Decade

K. K. Kannan

37 papers receiving 1.4k citations

Hit Papers

Crystal Structure of Huma... 1972 2026 1990 2008 1972 100 200 300

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
K. K. Kannan India 16 1.2k 402 351 212 212 39 1.6k
R. W. King United Kingdom 23 1.2k 1.0× 466 1.2× 263 0.7× 107 0.5× 420 2.0× 40 1.9k
Carlos H. Faerman United States 16 778 0.7× 478 1.2× 364 1.0× 348 1.6× 296 1.4× 28 1.9k
A.H. Robbins United States 22 1.3k 1.1× 573 1.4× 236 0.7× 202 1.0× 363 1.7× 42 2.4k
Paul Beroza United States 21 1.2k 1.1× 267 0.7× 131 0.4× 193 0.9× 276 1.3× 32 1.8k
S. Zoë Fisher United States 27 1.5k 1.3× 438 1.1× 288 0.8× 173 0.8× 636 3.0× 80 2.0k
Rick L. Ornstein United States 31 1.6k 1.4× 464 1.2× 272 0.8× 85 0.4× 376 1.8× 83 2.6k
M. Tabak Brazil 16 1.1k 1.0× 450 1.1× 173 0.5× 54 0.3× 353 1.7× 41 1.5k
Mikael Peräkylä Finland 28 980 0.9× 497 1.2× 137 0.4× 53 0.3× 237 1.1× 79 2.0k
Michel Rougée France 30 1.6k 1.4× 470 1.2× 273 0.8× 43 0.2× 705 3.3× 51 2.5k
Paul Vigny France 27 1.2k 1.0× 384 1.0× 175 0.5× 133 0.6× 274 1.3× 108 2.1k

Countries citing papers authored by K. K. Kannan

Since Specialization
Citations

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

Fields of papers citing papers by K. K. Kannan

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of K. K. Kannan

This figure shows the co-authorship network connecting the top 25 collaborators of K. K. Kannan. A scholar is included among the top collaborators of K. K. Kannan 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 K. K. Kannan. K. K. Kannan 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.
Kannan, K. K., et al.. (2025). Dithiocarbamate-Based Sequence-Defined Oligomers as Promising Membrane-Disrupting Antibacterial Agents: Design, Activity, and Mechanism. ACS Applied Bio Materials. 8(2). 1547–1558. 2 indexed citations
2.
Kannan, K. K., et al.. (2024). Lipophilic derivatives of EGCG as potent α-amylase and α-glucosidase inhibitors ameliorating oxidative stress and inflammation. Bioorganic Chemistry. 153. 107786–107786. 1 indexed citations
4.
Kannan, K. K., et al.. (2024). Insights into one drug, multi-target aspects of polyphenols for diabetes management: in vitro, in vivo, and clinical evidence. Phytochemistry Reviews. 24(5). 4545–4593. 4 indexed citations
5.
Pillai, Bindu, K. K. Kannan, Sujata V. Bhat, & M.V. Hosur. (2004). Rapid screening for HIV-1 protease inhibitor leads through X-ray diffraction. Acta Crystallographica Section D Biological Crystallography. 60(3). 594–596. 7 indexed citations
6.
Kumar, Mukesh, K. K. Kannan, M.V. Hosur, et al.. (2002). Effects of remote mutation on the autolysis of HIV-1 PR: X-ray and NMR investigations. Biochemical and Biophysical Research Communications. 294(2). 395–401. 29 indexed citations
7.
Pillai, Bindu, K. K. Kannan, & M.V. Hosur. (2001). 1.9 � x-ray study shows closed flap conformation in crystals of tethered HIV-1 PR. Proteins Structure Function and Bioinformatics. 43(1). 57–64. 53 indexed citations
8.
Kumar, Mukesh, et al.. (1999). Purification, crystallisation and preliminary X-ray diffraction study of ribosome inactivating protein: saporin. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1429(2). 506–511. 1 indexed citations
9.
Kannan, K. K., et al.. (1994). Drug-Protein Interactions. Journal of Molecular Biology. 243(2). 298–309. 146 indexed citations
10.
Kannan, K. K., et al.. (1994). Enzyme-Substrate Interactions. Journal of Molecular Biology. 241(2). 226–232. 46 indexed citations
11.
Hosur, M.V., et al.. (1994). Crystallization of a scRIP—gelonin isolated from plant seeds Gelonium multiforum. Proteins Structure Function and Bioinformatics. 19(4). 340–342. 1 indexed citations
12.
Hosur, M.V., Jayashree K. Sainis, & K. K. Kannan. (1993). Crystallization and X-ray Analysis of a Multienzyme Complex Containing RUBISCO and RuBP. Journal of Molecular Biology. 234(4). 1274–1278. 4 indexed citations
13.
Hosur, Ramakrishna V., et al.. (1989). Solution conformation of d-CTCGAGCTCGAG by two-dimensional NMR: conformational heterogeneity at XhoI cleavage site. Biochemistry. 28(18). 7275–7282. 12 indexed citations
14.
Kumar, Vinay, et al.. (1987). Human carbonic anhydrase I–iodide complex: structure and inhibition mechanism. Acta Crystallographica Section A Foundations of Crystallography. 43(a1). C23–C24. 2 indexed citations
15.
Kannan, K. K. & M. Ramanadham. (1981). Structure, refinement, and function of human carbonic anhydrase‐B. International Journal of Quantum Chemistry. 20(1). 199–209. 4 indexed citations
16.
Carlsson, Lars, Lina Nyström, Uno Lindberg, et al.. (1976). Crystallization of a non-muscle actin. Journal of Molecular Biology. 105(3). 353–366. 127 indexed citations
17.
Strandberg, B., Michael G. Rossmann, K. Fridborg, et al.. (1972). X-Ray Diffraction Studies of the Structure of Satellite Tobacco Necrosis Virus. Cold Spring Harbor Symposia on Quantitative Biology. 36(0). 469–483. 11 indexed citations
18.
Kannan, K. K., Anders Liljas, Seved Lövgren, et al.. (1972). Crystal Structure of Human Erythrocyte Carbonic Anhydrase C. VI. The Three-dimensional Structure at High Resolution in Relation to Other Mammalian Carbonic Anhydrases. Cold Spring Harbor Symposia on Quantitative Biology. 36(0). 221–231. 48 indexed citations
19.
Fridborg, K., K. K. Kannan, Anders Liljas, et al.. (1967). Crystal structure of human erythrocyte carbonic anhydrase C. Journal of Molecular Biology. 25(3). 505–516. 116 indexed citations
20.
Viswamitra, M. A. & K. K. Kannan. (1962). Simple gas-cooling device for low temperature investigations with Weissenberg cameras. Journal of Scientific Instruments. 39(6). 318–319. 1 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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