Ajit K. Basak

2.4k total citations
33 papers, 1.8k citations indexed

About

Ajit K. Basak is a scholar working on Infectious Diseases, Immunology and Molecular Biology. According to data from OpenAlex, Ajit K. Basak has authored 33 papers receiving a total of 1.8k indexed citations (citations by other indexed papers that have themselves been cited), including 23 papers in Infectious Diseases, 16 papers in Immunology and 12 papers in Molecular Biology. Recurrent topics in Ajit K. Basak's work include Clostridium difficile and Clostridium perfringens research (20 papers), Toxin Mechanisms and Immunotoxins (16 papers) and Antimicrobial Resistance in Staphylococcus (5 papers). Ajit K. Basak is often cited by papers focused on Clostridium difficile and Clostridium perfringens research (20 papers), Toxin Mechanisms and Immunotoxins (16 papers) and Antimicrobial Resistance in Staphylococcus (5 papers). Ajit K. Basak collaborates with scholars based in United Kingdom, United States and France. Ajit K. Basak's co-authors include Richard W. Titball, C.E. Naylor, David S. Moss, Christos G. Savva, Monika Bokori‐Brown, David I. Stuart, Jonathan M. Grimes, Polly Roy, A.R. Cole and Michel R. Popoff and has published in prestigious journals such as Nature, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

Ajit K. Basak

33 papers receiving 1.8k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Ajit K. Basak United Kingdom 23 896 829 370 296 199 33 1.8k
Ron Geller Spain 18 592 0.7× 803 1.0× 274 0.7× 171 0.6× 150 0.8× 46 1.6k
Robert Clubb United States 33 503 0.6× 2.5k 3.0× 266 0.7× 533 1.8× 388 1.9× 91 3.3k
Elke Maier Germany 34 708 0.8× 1.9k 2.3× 550 1.5× 223 0.8× 653 3.3× 80 3.5k
José L. Nieva Spain 36 896 1.0× 2.5k 3.0× 657 1.8× 241 0.8× 235 1.2× 118 4.1k
Paul Liberator United States 32 819 0.9× 817 1.0× 304 0.8× 395 1.3× 102 0.5× 75 3.3k
Navin Khanna India 35 1.1k 1.3× 1.5k 1.8× 286 0.8× 1.2k 4.1× 232 1.2× 115 3.4k
Jade K. Forwood Australia 30 519 0.6× 2.1k 2.5× 239 0.6× 387 1.3× 631 3.2× 153 3.6k
Martijn A. Langereis Netherlands 30 904 1.0× 1.2k 1.5× 679 1.8× 92 0.3× 217 1.1× 40 2.5k
Darren J. Hart France 26 550 0.6× 2.4k 2.9× 757 2.0× 116 0.4× 207 1.0× 63 3.7k

Countries citing papers authored by Ajit K. Basak

Since Specialization
Citations

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

Fields of papers citing papers by Ajit K. Basak

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Ajit K. Basak

This figure shows the co-authorship network connecting the top 25 collaborators of Ajit K. Basak. A scholar is included among the top collaborators of Ajit K. Basak 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 Ajit K. Basak. Ajit K. Basak 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.
Savva, Christos G., Alice R. Clark, C.E. Naylor, et al.. (2019). The pore structure of Clostridium perfringens epsilon toxin. Nature Communications. 10(1). 2641–2641. 49 indexed citations
2.
Palmer, Rex A., Carina M. C. Lobley, C.E. Naylor, et al.. (2017). Ultra-high resolution X-ray structures of two forms of human recombinant insulin at 100 K. Chemistry Central Journal. 11(1). 73–73. 8 indexed citations
3.
Bokori‐Brown, Monika, Thomas G. Martin, C.E. Naylor, et al.. (2016). Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein. Nature Communications. 7(1). 11293–11293. 108 indexed citations
4.
Yelland, Tamas, C.E. Naylor, Christos G. Savva, et al.. (2014). Structure of a C. perfringens Enterotoxin Mutant in Complex with a Modified Claudin-2 Extracellular Loop 2. Journal of Molecular Biology. 426(18). 3134–3147. 18 indexed citations
5.
Bokori‐Brown, Monika, Christos G. Savva, C.E. Naylor, et al.. (2014). Clostridium perfringens epsilon toxin mutant Y30A-Y196A as a recombinant vaccine candidate against enterotoxemia. Vaccine. 32(23). 2682–2687. 37 indexed citations
6.
Bokori‐Brown, Monika, Christos G. Savva, C.E. Naylor, et al.. (2013). Clostridium perfringens epsilon toxin H149A mutant as a platform for receptor binding studies. Protein Science. 22(5). 650–659. 39 indexed citations
7.
Huyet, J., et al.. (2011). Crystallization and preliminary X-ray diffraction studies of delta-toxin fromClostridium perfringens. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67(3). 369–371. 4 indexed citations
8.
Bokori‐Brown, Monika, et al.. (2011). Molecular basis of toxicity ofClostridium perfringensepsilon toxin. FEBS Journal. 278(23). 4589–4601. 92 indexed citations
9.
Briggs, David C., James G. Smedley, Bruce A. McClane, & Ajit K. Basak. (2010). Crystallization and preliminary crystallographic analysis of theClostridium perfringensenterotoxin. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66(7). 794–797. 2 indexed citations
10.
Cole, A.R., Maryse Gibert, Michel R. Popoff, et al.. (2004). Clostridium perfringens ε-toxin shows structural similarity to the pore-forming toxin aerolysin. Nature Structural & Molecular Biology. 11(8). 797–798. 148 indexed citations
11.
Clark, Graeme C., David C. Briggs, Tadahiro Karasawa, et al.. (2003). Clostridium absonum α-Toxin: New Insights into Clostridial Phospholipase C Substrate Binding and Specificity. Journal of Molecular Biology. 333(4). 759–769. 22 indexed citations
12.
Naylor, C.E., S. Gover, Ajit K. Basak, et al.. (2001). NADP+and NAD+binding to the dual coenzyme specific enzymeLeuconostoc mesenteroidesglucose 6-phosphate dehydrogenase: different interdomain hinge angles are seen in different binary and ternary complexes. Acta Crystallographica Section D Biological Crystallography. 57(5). 635–648. 35 indexed citations
13.
Alape‐Girón, Alberto, Marietta Flores-Dı́az, Isabelle Guillouard, et al.. (2000). Identification of residues critical for toxicity in Clostridium perfringens phospholipase C, the key toxin in gas gangrene. European Journal of Biochemistry. 267(16). 5191–5197. 41 indexed citations
14.
Clout, Naomi J., Ajit K. Basak, Karin Wieligmann, et al.. (2000). The N-terminal domain of βb2-crystallin resembles the putative ancestral homodimer. Journal of Molecular Biology. 304(3). 253–257. 22 indexed citations
15.
Naylor, C.E., Dennis Crane, Richard W. Titball, et al.. (1999). Characterisation of the calcium-binding C-terminal domain of Clostridium perfringens alpha-toxin 1 1Edited by A Klug. Journal of Molecular Biology. 294(3). 757–770. 47 indexed citations
16.
Naylor, C.E., Julian T. Eaton, Angela M. Howells, et al.. (1998). Structure of the key toxin in gas gangrene. Nature Structural & Molecular Biology. 5(8). 738–746. 146 indexed citations
17.
Basak, Ajit K., Jonathan M. Grimes, Patrice Gouet, Polly Roy, & David I. Stuart. (1997). Structures of orbivirus VP7: implications for the role of this protein in the viral life cycle. Structure. 5(7). 871–883. 30 indexed citations
18.
Grimes, Jonathan M., Ajit K. Basak, Polly Roy, & David I. Stuart. (1995). The crystal structure of bluetongue virus VP7. Nature. 373(6510). 167–170. 134 indexed citations
19.
Rowland, Paul, Ajit K. Basak, S. Gover, Haim Levy, & Margaret Adams. (1994). The three–dimensional structure of glucose 6–phosphate dehydrogenase from Leuconostoc mesenteroides refined at 2.0 Å resolution. Structure. 2(11). 1073–1087. 112 indexed citations
20.
Adams, Margaret, Ajit K. Basak, S. Gover, Paul Rowland, & Haim Levy. (1993). Site‐directed mutagenesis to facilitate X‐ray structural studies of leuconostoc mesenteroides glucose 6‐phosphate dehydrogenase. Protein Science. 2(5). 859–862. 8 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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