Panadda Boonserm

1.1k total citations
43 papers, 826 citations indexed

About

Panadda Boonserm is a scholar working on Molecular Biology, Insect Science and Immunology. According to data from OpenAlex, Panadda Boonserm has authored 43 papers receiving a total of 826 indexed citations (citations by other indexed papers that have themselves been cited), including 39 papers in Molecular Biology, 30 papers in Insect Science and 11 papers in Immunology. Recurrent topics in Panadda Boonserm's work include Insect Resistance and Genetics (35 papers), Insect and Pesticide Research (28 papers) and Toxin Mechanisms and Immunotoxins (11 papers). Panadda Boonserm is often cited by papers focused on Insect Resistance and Genetics (35 papers), Insect and Pesticide Research (28 papers) and Toxin Mechanisms and Immunotoxins (11 papers). Panadda Boonserm collaborates with scholars based in Thailand, Singapore and Japan. Panadda Boonserm's co-authors include Boonhiang Promdonkoy, David J. Ellar, Jade Li, Paul F. Davis, Chanan Angsuthanasombat, Julien Lescar, Min Mo, Jaume Torres, Gerd Katzenmeier and Kamonnut Singkhamanan and has published in prestigious journals such as SHILAP Revista de lepidopterología, PLoS ONE and Journal of Molecular Biology.

In The Last Decade

Panadda Boonserm

42 papers receiving 807 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Panadda Boonserm Thailand 16 733 620 158 97 93 43 826
Anrui Lu China 10 234 0.3× 367 0.6× 86 0.5× 40 0.4× 315 3.4× 12 590
S. K. Gakhar India 12 195 0.3× 89 0.1× 106 0.7× 178 1.8× 96 1.0× 46 417
Sylwia Stączek Poland 13 144 0.2× 206 0.3× 63 0.4× 33 0.3× 252 2.7× 22 446
Anja Strauß Germany 12 138 0.2× 246 0.4× 103 0.7× 31 0.3× 24 0.3× 16 469
Małgorzata Dawgul Poland 16 306 0.4× 210 0.3× 150 0.9× 27 0.3× 55 0.6× 25 626
Mariola Andrejko Poland 11 150 0.2× 151 0.2× 41 0.3× 32 0.3× 150 1.6× 24 335
Meredith Claire Edwards United States 5 134 0.2× 152 0.2× 93 0.6× 119 1.2× 74 0.8× 9 396
Silas P. Rodrigues Brazil 12 238 0.3× 47 0.1× 188 1.2× 152 1.6× 49 0.5× 23 505
Sergio J. Mijailovsky Argentina 11 346 0.5× 492 0.8× 246 1.6× 192 2.0× 31 0.3× 19 761
Zhen‐Tian Yan China 13 273 0.4× 197 0.3× 158 1.0× 206 2.1× 19 0.2× 30 516

Countries citing papers authored by Panadda Boonserm

Since Specialization
Citations

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

Fields of papers citing papers by Panadda Boonserm

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Panadda Boonserm

This figure shows the co-authorship network connecting the top 25 collaborators of Panadda Boonserm. A scholar is included among the top collaborators of Panadda Boonserm 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 Panadda Boonserm. Panadda Boonserm 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.
Promdonkoy, Boonhiang, et al.. (2025). Rational protein design to improve the thermal stability of a Bacillus thuringiensis Vip3A protein. Journal of Invertebrate Pathology. 213. 108429–108429.
2.
Surya, Wahyu, et al.. (2024). Biophysical Analysis of Vip3Aa Toxin Mutants Before and After Activation. International Journal of Molecular Sciences. 25(22). 11970–11970. 1 indexed citations
3.
Boonserm, Panadda, et al.. (2024). Anticancer efficacy of biosynthesized silver nanoparticles loaded with recombinant truncated parasporin-2 protein. Scientific Reports. 14(1). 15544–15544. 8 indexed citations
4.
Boonserm, Panadda, et al.. (2024). A fusion protein designed for soluble expression, rapid purification, and enhanced stability of parasporin-2 with potential therapeutic applications. Biotechnology Reports. 43. e00851–e00851. 1 indexed citations
5.
Boonserm, Panadda, et al.. (2023). Biosynthesized Silver Nanoparticles Using Morus alba (White Mulberry) Leaf Extract as Potential Antibacterial and Anticancer Agents. Molecules. 28(3). 1213–1213. 31 indexed citations
6.
Promdonkoy, Boonhiang, et al.. (2023). Screening and characterization of Bacillus thuringiensis isolates for high production of Vip3A and Cry proteins and high thermostability to control Spodoptera spp. Journal of Invertebrate Pathology. 201. 108020–108020. 4 indexed citations
7.
Torres, Jaume, Wahyu Surya, & Panadda Boonserm. (2023). Channel Formation in Cry Toxins: An Alphafold-2 Perspective. International Journal of Molecular Sciences. 24(23). 16809–16809. 1 indexed citations
8.
Surachat, Komwit, et al.. (2023). Effects of Postbiotic from Bacteriocin-Like Inhibitory Substance Producing Enterococcus faecalis on Toxigenic Clostridioides difficile. SHILAP Revista de lepidopterología. 1–1. 6 indexed citations
9.
Boonserm, Panadda, et al.. (2020). Local conformations affect the histidine tag-Ni<sup>2+</sup> binding affinity of BinA and BinB proteins. AIMS Biophysics. 7(3). 133–143. 1 indexed citations
10.
Surya, Wahyu, et al.. (2018). An aromatic cluster in Lysinibacillus sphaericus BinB involved in toxicity and proper in-membrane folding. Archives of Biochemistry and Biophysics. 660. 29–35. 5 indexed citations
11.
Watanabe, Hirokazu, Ryuji Kawano, Yoshikazu Tanaka, et al.. (2017). pH regulates pore formation of a protease activated Vip3Aa from Bacillus thuringiensis. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1859(11). 2234–2241. 30 indexed citations
12.
Surya, Wahyu, et al.. (2016). Conditions for homogeneous preparation of stable monomeric and oligomeric forms of activated Vip3A toxin from Bacillus thuringiensis. European Biophysics Journal. 46(3). 257–264. 20 indexed citations
13.
Promdonkoy, Boonhiang, et al.. (2015). Lysinibacillus sphaericus binary toxin induces apoptosis in susceptible Culex quinquefasciatus larvae. Journal of Invertebrate Pathology. 128. 57–63. 31 indexed citations
14.
Yao, Min, et al.. (2013). Crystallization and preliminary X-ray crystallographic analysis of the functional form of BinB binary toxin fromBacillus sphaericus. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 69(2). 170–173. 2 indexed citations
15.
Soonsanga, Sumarin, et al.. (2010). Role of cysteine at positions 67, 161 and 241 of a Bacillus sphaericus binary toxin BinB. BMB Reports. 43(1). 23–28. 13 indexed citations
16.
Singkhamanan, Kamonnut, Boonhiang Promdonkoy, Urai Chaisri, & Panadda Boonserm. (2009). Identification of amino acids required for receptor binding and toxicity of theBacillus sphaericusâbinary toxin. FEMS Microbiology Letters. 303(1). 84–91. 15 indexed citations
17.
Promdonkoy, Boonhiang, et al.. (2008). Targeted Mutagenesis at Charged Residues in Bacillus sphaericus BinA Toxin Affects Mosquito-Larvicidal Activity. Current Microbiology. 57(3). 230–234. 10 indexed citations
18.
Promdonkoy, Boonhiang, et al.. (2008). Cys31, Cys47, and Cys195 in BinA Are Essential for Toxicity of a Binary Toxin from Bacillus sphaericus. Current Microbiology. 56(4). 334–338. 12 indexed citations
19.
Boonserm, Panadda, et al.. (2004). Targeted mutagenesis of loop residues in the receptor-binding domain of theBacillus thuringiensisCry4Ba toxin affects larvicidal activity. FEMS Microbiology Letters. 242(2). 325–332. 28 indexed citations
20.
Boonserm, Panadda, Walairat Pornwiroon, Gerd Katzenmeier, Sakol Panyim, & Chanan Angsuthanasombat. (2004). Optimised expression in Escherichia coli and purification of the functional form of the Bacillus thuringiensis Cry4Aa δ-endotoxin. Protein Expression and Purification. 35(2). 397–403. 21 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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