P. Chitnumsub

2.3k total citations
47 papers, 1.7k citations indexed

About

P. Chitnumsub is a scholar working on Molecular Biology, Infectious Diseases and Epidemiology. According to data from OpenAlex, P. Chitnumsub has authored 47 papers receiving a total of 1.7k indexed citations (citations by other indexed papers that have themselves been cited), including 26 papers in Molecular Biology, 18 papers in Infectious Diseases and 14 papers in Epidemiology. Recurrent topics in P. Chitnumsub's work include HIV/AIDS drug development and treatment (18 papers), Biochemical and Molecular Research (15 papers) and Malaria Research and Control (12 papers). P. Chitnumsub is often cited by papers focused on HIV/AIDS drug development and treatment (18 papers), Biochemical and Molecular Research (15 papers) and Malaria Research and Control (12 papers). P. Chitnumsub collaborates with scholars based in Thailand, United Kingdom and United States. P. Chitnumsub's co-authors include Yongyuth Yuthavong, Sumalee Kamchonwongpaisan, Jarunee Vanichtanankul, Jirundon Yuvaniyama, Worachart Sirawaraporn, Malcolm D. Walkinshaw, Ubolsree Leartsakulpanich, Paul Taylor, Bongkoch Tarnchompoo and Tirayut Vilaivan and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

P. Chitnumsub

45 papers receiving 1.7k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
P. Chitnumsub Thailand	20	838	534	511	391	386	47	1.7k
Namita Surolia India	23	802 1.0×	486 0.9×	198 0.4×	403 1.0×	212 0.5×	64	1.7k
Francisco‐Javier Gamo Spain	23	962 1.1×	1.3k 2.4×	404 0.8×	403 1.0×	628 1.6×	70	2.4k
Martin Schlitzer Germany	23	925 1.1×	763 1.4×	253 0.5×	774 2.0×	364 0.9×	119	2.1k
Jirundon Yuvaniyama Thailand	13	813 1.0×	372 0.7×	279 0.5×	226 0.6×	241 0.6×	29	1.4k
Cátia Teixeira Portugal	25	654 0.8×	358 0.7×	258 0.5×	551 1.4×	178 0.5×	76	1.8k
Paul A. Stocks United Kingdom	23	350 0.4×	756 1.4×	218 0.4×	621 1.6×	279 0.7×	33	1.4k
Silvia Parapini Italy	30	728 0.9×	1.2k 2.2×	239 0.5×	964 2.5×	375 1.0×	113	2.7k
Livia Vivas United Kingdom	23	392 0.5×	802 1.5×	217 0.4×	605 1.5×	331 0.9×	41	1.6k
Radim Nencka Czechia	28	1.1k 1.3×	532 1.0×	936 1.8×	305 0.8×	150 0.4×	90	2.4k
Martin Hintz Germany	23	1.8k 2.1×	552 1.0×	193 0.4×	148 0.4×	185 0.5×	36	2.9k

Countries citing papers authored by P. Chitnumsub

Since Specialization

Citations

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

Fields of papers citing papers by P. Chitnumsub

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of P. Chitnumsub

This figure shows the co-authorship network connecting the top 25 collaborators of P. Chitnumsub. A scholar is included among the top collaborators of P. Chitnumsub 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 P. Chitnumsub. P. Chitnumsub is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Prakinee, Kridsadakorn, Narin Lawan, Aisaraphon Phintha, et al.. (2024). On the Mechanisms of Hypohalous Acid Formation and Electrophilic Halogenation by Non‐Native Halogenases. Angewandte Chemie International Edition. 63(24). e202403858–e202403858. 8 indexed citations

Pimviriyakul, Panu, Ruchanok Tinikul, A. Jaruwat, et al.. (2023). Structure and biochemical characterization of an extradiol 3,4-dihydroxyphenylacetate 2,3-dioxygenase from Acinetobacter baumannii. Archives of Biochemistry and Biophysics. 747. 109768–109768. 3 indexed citations

Maenpuen, Somchart, Panu Pimviriyakul, Thanyada Rungrotmongkol, et al.. (2023). Mangiferin is a new potential antimalarial and anticancer drug for targeting serine hydroxymethyltransferase. Archives of Biochemistry and Biophysics. 745. 109712–109712. 14 indexed citations

Prakinee, Kridsadakorn, Aisaraphon Phintha, Surawit Visitsatthawong, et al.. (2022). Mechanism-guided tunnel engineering to increase the efficiency of a flavin-dependent halogenase. Nature Catalysis. 5(6). 534–544. 76 indexed citations

Pimviriyakul, Panu, A. Jaruwat, P. Chitnumsub, & Pimchai Chaiyen. (2021). Structural insights into a flavin-dependent dehalogenase HadA explain catalysis and substrate inhibition via quadruple π-stacking. Journal of Biological Chemistry. 297(2). 100952–100952. 13 indexed citations

Jaruwat, A., Narin Lawan, Juthamas Jaroensuk, et al.. (2021). Catalytic and structural insights into a stereospecific and thermostable Class II aldolase HpaI from Acinetobacter baumannii. Journal of Biological Chemistry. 297(5). 101280–101280. 5 indexed citations

Phintha, Aisaraphon, Kridsadakorn Prakinee, A. Jaruwat, et al.. (2020). Dissecting the low catalytic capability of flavin-dependent halogenases. Journal of Biological Chemistry. 296. 100068–100068. 41 indexed citations

Jaroensuk, Juthamas, Wichai Pornthanakasem, Nuntaporn Kamonsutthipaijit, et al.. (2019). A flap motif in human serine hydroxymethyltransferase is important for structural stabilization, ligand binding, and control of product release. Journal of Biological Chemistry. 294(27). 10490–10502. 11 indexed citations

Jaruwat, A., et al.. (2019). Crystal structure of Plasmodium falciparum adenosine deaminase reveals a novel binding pocket for inosine. Archives of Biochemistry and Biophysics. 667. 6–13. 3 indexed citations

10.

Maenpuen, Somchart, et al.. (2017). Human and Plasmodium serine hydroxymethyltransferases differ in rate-limiting steps and pH-dependent substrate inhibition behavior. Archives of Biochemistry and Biophysics. 630. 91–100. 12 indexed citations

11.

Maenpuen, Somchart, Jeerus Sucharitakul, Bruce A. Palfey, et al.. (2015). Kinetic Mechanism and the Rate-limiting Step of Plasmodium vivax Serine Hydroxymethyltransferase. Journal of Biological Chemistry. 290(13). 8656–8665. 10 indexed citations

12.

Chitnumsub, P., A. Jaruwat, Phimonphan Chuankhayan, et al.. (2014). Structures ofPlasmodium vivaxserine hydroxymethyltransferase: implications for ligand-binding specificity and functional control. Acta Crystallographica Section D Biological Crystallography. 70(12). 3177–3186. 19 indexed citations

13.

Shaw, Philip J., et al.. (2010). Formation of catalytically active cross-species heterodimers of thymidylate synthase from Plasmodium falciparum and Plasmodium vivax. Molecular Biology Reports. 38(2). 1029–1037. 6 indexed citations

14.

Dasgupta, Tina, P. Chitnumsub, Sumalee Kamchonwongpaisan, et al.. (2009). Exploiting Structural Analysis, in Silico Screening, and Serendipity To Identify Novel Inhibitors of Drug-Resistant Falciparum Malaria. ACS Chemical Biology. 4(1). 29–40. 52 indexed citations

15.

Kamchonwongpaisan, Sumalee, Jarunee Vanichtanankul, Supannee Taweechai, P. Chitnumsub, & Yongyuth Yuthavong. (2007). The role of tryptophan-48 in catalysis and binding of inhibitors of Plasmodium falciparum dihydrofolate reductase. International Journal for Parasitology. 37(7). 787–793. 9 indexed citations

16.

Yuthavong, Yongyuth, Jirundon Yuvaniyama, P. Chitnumsub, et al.. (2004). Malarial (Plasmodium falciparum) dihydrofolate reductase-thymidylate synthase: structural basis for antifolate resistance and development of effective inhibitors. Parasitology. 130(3). 249–259. 86 indexed citations

17.

Chitnumsub, P., et al.. (2004). Subunit complementation of thymidylate synthase in Plasmodium falciparum bifunctional dihydrofolate reductase-thymidylate synthase. Molecular and Biochemical Parasitology. 139(1). 83–90. 6 indexed citations

18.

Yuvaniyama, Jirundon, P. Chitnumsub, Sumalee Kamchonwongpaisan, et al.. (2003). Insights into antifolate resistance from malarial DHFR-TS structures. Nature Structural & Molecular Biology. 10(5). 357–365. 324 indexed citations

19.

Sardarian, Ali Reza, Kenneth T. Douglas, Martin Read, et al.. (2003). Pyrimethamine analogs as strong inhibitors of double and quadruple mutants of dihydrofolate reductase in human malaria parasites. Organic & Biomolecular Chemistry. 1(6). 960–964. 47 indexed citations

20.

Li, Rongbao, Rachada Sirawaraporn, P. Chitnumsub, et al.. (2000). Three-dimensional structure of M. tuberculosis dihydrofolate reductase reveals opportunities for the design of novel tuberculosis drugs. Journal of Molecular Biology. 295(2). 307–323. 170 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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