Chingkuang Tu

3.9k total citations
101 papers, 3.2k citations indexed

About

Chingkuang Tu is a scholar working on Molecular Biology, Organic Chemistry and Physical and Theoretical Chemistry. According to data from OpenAlex, Chingkuang Tu has authored 101 papers receiving a total of 3.2k indexed citations (citations by other indexed papers that have themselves been cited), including 91 papers in Molecular Biology, 42 papers in Organic Chemistry and 32 papers in Physical and Theoretical Chemistry. Recurrent topics in Chingkuang Tu's work include Enzyme function and inhibition (81 papers), Chemical Reactions and Mechanisms (31 papers) and Synthesis and Catalytic Reactions (24 papers). Chingkuang Tu is often cited by papers focused on Enzyme function and inhibition (81 papers), Chemical Reactions and Mechanisms (31 papers) and Synthesis and Catalytic Reactions (24 papers). Chingkuang Tu collaborates with scholars based in United States, China and South Africa. Chingkuang Tu's co-authors include David N. Silverman, Robert McKenna, Philip J. Laipis, B Jönsson, Cecilia Forsman, Sven Lindskog, S. Zoë Fisher, L. Govindasamy, Mavis Agbandje‐McKenna and David M. Duda and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Chingkuang Tu

100 papers receiving 3.1k citations

Peers

Chingkuang Tu

PTC

PHARM

Fabrizio Briganti Italy

Y. Pocker United States

Michael J. Gresser Canada

Yuichi Kanaoka Japan

Sam Hay United Kingdom

Jan Bergman Sweden

Jasmin Mecinović Netherlands

Vincenzo Alterio Italy

E.M. Fielden United Kingdom

Kent S. Gates United States

Fabrizio Briganti Italy

Chingkuang Tu

2.5k ×0.9

1.6k ×1.4

544 ×0.7

PTC

675 ×1.4

PHARM

146 ×0.5

Citations per year, relative to Chingkuang Tu Chingkuang Tu (= 1×) peers Fabrizio Briganti

Countries citing papers authored by Chingkuang Tu

Since Specialization

Citations

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

Fields of papers citing papers by Chingkuang Tu

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Chingkuang Tu

This figure shows the co-authorship network connecting the top 25 collaborators of Chingkuang Tu. A scholar is included among the top collaborators of Chingkuang Tu 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 Chingkuang Tu. Chingkuang Tu 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

Xiao, Shengxiang, et al.. (2025). Real-world safety of deucravacitinib: insights from the Food and Drug Administration Adverse Event Reporting System. International Journal of Clinical Pharmacy. 47(5). 1215–1223. 9 indexed citations

Mboge, Mam Y., Srishti Singh, Jacob T. Andring, et al.. (2021). Inhibition of Carbonic Anhydrase Using SLC-149: Support for a Noncatalytic Function of CAIX in Breast Cancer. Journal of Medicinal Chemistry. 64(3). 1713–1724. 26 indexed citations

Chen, Zhijuan, Lingbao Ai, Mam Y. Mboge, et al.. (2018). Differential expression and function of CAIX and CAXII in breast cancer: A comparison between tumorgraft models and cells. PLoS ONE. 13(7). e0199476–e0199476. 51 indexed citations

Pinard, Melissa A., Mayank Aggarwal, Brian P. Mahon, Chingkuang Tu, & Robert McKenna. (2015). A sucrose-binding site provides a lead towards an isoform-specific inhibitor of the cancer-associated enzyme carbonic anhydrase IX. Acta Crystallographica Section F Structural Biology Communications. 71(10). 1352–1358. 24 indexed citations

Pinard, Melissa A., et al.. (2014). Human carbonic anhydrase II–cyanate inhibitor complex: putting the debate to rest. Acta Crystallographica Section F Structural Biology Communications. 70(10). 1324–1327. 5 indexed citations

Aggarwal, Mayank, et al.. (2014). Structural insight into activity enhancement and inhibition of H64A carbonic anhydrase II by imidazoles. IUCrJ. 1(2). 129–135. 29 indexed citations

Shenderovich, Ilya G., Chingkuang Tu, David N. Silverman, et al.. (2014). NMR Studies of Active‐Site Properties of Human Carbonic Anhydrase II by Using ¹⁵N‐Labeled 4‐Methylimidazole as a Local Probe and Histidine Hydrogen‐Bond Correlations. Chemistry - A European Journal. 21(7). 2915–2929. 17 indexed citations

Stander, André, Fourie Joubert, Chingkuang Tu, et al.. (2013). Signaling Pathways of ESE-16, an Antimitotic and Anticarbonic Anhydrase Estradiol Analog, in Breast Cancer Cells. PLoS ONE. 8(1). e53853–e53853. 22 indexed citations

Boone, Christopher D., et al.. (2013). Structural and catalytic characterization of a thermally stable and acid-stable variant of human carbonic anhydrase II containing an engineered disulfide bond. Acta Crystallographica Section D Biological Crystallography. 69(8). 1414–1422. 32 indexed citations

10.

Tu, Chingkuang, et al.. (2011). Detection of nitroxyl (HNO) by membrane inlet mass spectrometry. Free Radical Biology and Medicine. 50(10). 1274–1279. 91 indexed citations

11.

Tu, Chingkuang, et al.. (2011). Membrane inlet for mass spectrometric measurement of catalysis by enzymatic decarboxylases. Analytical Biochemistry. 418(1). 73–77. 13 indexed citations

12.

Tu, Chingkuang, Hai Wang, Kathleen T. Shiverick, et al.. (2010). Detecting extracellular carbonic anhydrase activity using membrane inlet mass spectrometry. Analytical Biochemistry. 403(1-2). 74–78. 10 indexed citations

13.

Tu, Chingkuang, et al.. (2009). Reactions of nitrite in erythrocyte suspensions measured by membrane inlet mass spectrometry. Free Radical Biology and Medicine. 48(2). 325–331. 12 indexed citations

14.

Tu, Chingkuang, et al.. (2005). Proton transfer in a Thr200His mutant of human carbonic anhydrase II. Proteins Structure Function and Bioinformatics. 61(2). 239–245. 13 indexed citations

15.

Tu, Chingkuang, Patrick Quint, & David N. Silverman. (2004). Exchange of 18O in the reaction of peroxynitrite with CO2. Free Radical Biology and Medicine. 38(1). 93–97. 5 indexed citations

16.

Wright, S. Kirk, et al.. (1999). Introduction of Histidine Analogs Leads to Enhanced Proton Transfer in Carbonic Anhydrase V. Archives of Biochemistry and Biophysics. 361(2). 264–270. 15 indexed citations

17.

Tu, Chingkuang, et al.. (1998). Isolation and Expression of Murine Carbonic Anhydrase IV. Protein Expression and Purification. 12(1). 7–16. 4 indexed citations

18.

Peterson, Robert E., Chingkuang Tu, & Paul J. Linser. (1997). Isolation and Characterization of a Carbonic Anhydrase Homologue from the Zebrafish (Danio rerio). Journal of Molecular Evolution. 44(4). 432–439. 40 indexed citations

19.

Tu, Chingkuang, et al.. (1993). Interaction and influence of phenylalanine-198 and threonine-199 on catalysis by human carbonic anhydrase III. Biochemistry. 32(31). 7861–7865. 16 indexed citations

20.

Tu, Chingkuang, Mildred Acevedo‐Duncan, George C. Wynns, & David N. Silverman. (1986). Oxygen-18 Exchange as a Measure of Accessibility of CO₂ and HCO₃⁻ to Carbonic Anhydrase in Chlorella vulgaris (UTEX 263). PLANT PHYSIOLOGY. 80(4). 997–1001. 22 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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