Kui K. Chan

1.5k total citations · 1 hit paper
19 papers, 928 citations indexed

About

Kui K. Chan is a scholar working on Molecular Biology, Infectious Diseases and Materials Chemistry. According to data from OpenAlex, Kui K. Chan has authored 19 papers receiving a total of 928 indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 8 papers in Infectious Diseases and 8 papers in Materials Chemistry. Recurrent topics in Kui K. Chan's work include SARS-CoV-2 and COVID-19 Research (8 papers), Enzyme Structure and Function (8 papers) and Porphyrin Metabolism and Disorders (6 papers). Kui K. Chan is often cited by papers focused on SARS-CoV-2 and COVID-19 Research (8 papers), Enzyme Structure and Function (8 papers) and Porphyrin Metabolism and Disorders (6 papers). Kui K. Chan collaborates with scholars based in United States, Hungary and China. Kui K. Chan's co-authors include Erik Procko, John M. Dye, David M. Kranz, Danielle E. Dorosky, Shawn A. Abbasi, Andrew S. Herbert, Preeti Sharma, J.A. Gerlt, Tina L. Amyes and B.M. Wood and has published in prestigious journals such as Science, Journal of the American Chemical Society and The Journal of Physical Chemistry B.

In The Last Decade

Kui K. Chan

18 papers receiving 919 citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Engineering human ACE2 to optimize binding to the spike protein of SARS coronavirus 2

2020 389 citations Kui K. Chan, Danielle E. Dorosky et al. Science profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Kui K. Chan United States	13	498	486	191	83	78	19	928
Amarnath Chatterjee India	16	375 0.8×	251 0.5×	81 0.4×	11 0.1×	33 0.4×	28	709
Yasien Sayed South Africa	21	589 1.2×	407 0.8×	28 0.1×	28 0.3×	91 1.2×	78	1.1k
Judith Rittenhouse United States	17	653 1.3×	315 0.6×	143 0.7×	60 0.7×	75 1.0×	24	1.2k
She Zhang United States	13	465 0.9×	176 0.4×	92 0.5×	22 0.3×	68 0.9×	21	769
John O. Hui United States	19	602 1.2×	500 1.0×	56 0.3×	10 0.1×	95 1.2×	42	1.3k
P. Vedantham United States	11	699 1.4×	377 0.8×	19 0.1×	12 0.1×	134 1.7×	16	1.4k
Wai‐Lung Ng Hong Kong	17	450 0.9×	344 0.7×	16 0.1×	6 0.1×	35 0.4×	32	987
Winfried Meining Germany	15	664 1.3×	75 0.2×	361 1.9×	54 0.7×	14 0.2×	24	826
Sameh H. Soror Egypt	15	408 0.8×	66 0.1×	37 0.2×	13 0.2×	36 0.5×	36	650
Laura Cooper United States	17	424 0.9×	396 0.8×	25 0.1×	4 0.0×	149 1.9×	34	1.1k

Countries citing papers authored by Kui K. Chan

Since Specialization

Citations

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

Fields of papers citing papers by Kui K. Chan

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Kui K. Chan

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

All Works

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19 of 19 papers shown

Stepanyuk, Galina A., David F. Thieker, Kui K. Chan, et al.. (2024). Modulation of the pharmacokinetics of soluble ACE2 decoy receptors through glycosylation. Molecular Therapy — Methods & Clinical Development. 32(3). 101301–101301. 1 indexed citations

Chan, Matthew C., Kui K. Chan, Erik Procko, & Diwakar Shukla. (2023). Machine Learning Guided Design of High-Affinity ACE2 Decoys for SARS-CoV-2 Neutralization. The Journal of Physical Chemistry B. 127(9). 1995–2001. 7 indexed citations

Zhang, Lianghui, Soumajit Dutta, Shiqin Xiong, et al.. (2022). Engineered ACE2 decoy mitigates lung injury and death induced by SARS-CoV-2 variants. Nature Chemical Biology. 18(3). 342–351. 53 indexed citations

Zhang, Lianghui, Laura Cooper, Kui K. Chan, et al.. (2022). An ACE2 decoy can be administered by inhalation and potently targets omicron variants of SARS‐CoV ‐2. EMBO Molecular Medicine. 14(11). e16109–e16109. 31 indexed citations

Islam, Mohammad S., et al.. (2022). Computationally engineered ACE2 decoy binds with nanomolar affinity with the SARS-CoV-2 spike protein. Biophysical Journal. 121(3). 422a–422a. 1 indexed citations

Chan, Kui K., et al.. (2021). An engineered decoy receptor for SARS-CoV-2 broadly binds protein S sequence variants. Science Advances. 7(8). 83 indexed citations

Zhong, Linda L. D., Bo Peng, Yi Luo, et al.. (2021). The Effect of Chinese Medicine for Rehabilitation of Discharged COVID-19 Patients: A Protocol for Multi-Center Observational Study. OBM Integrative and Complementary Medicine. 6(3). 1–1.

Chan, Kui K., et al.. (2021). Computationally Designed ACE2 Decoy Receptor Binds SARS-CoV-2 Spike (S) Protein with Tight Nanomolar Affinity. Journal of Chemical Information and Modeling. 61(9). 4656–4669. 21 indexed citations

Chan, Kui K., Danielle E. Dorosky, Preeti Sharma, et al.. (2020). Engineering human ACE2 to optimize binding to the spike protein of SARS coronavirus 2. Science. 369(6508). 1261–1265. 389 indexed citations breakdown →

10.

Basanta, Benjamin, Kui K. Chan, Patrick Barth, et al.. (2016). Introduction of a polar core into the de novo designed protein Top7. Protein Science. 25(7). 1299–1307. 5 indexed citations

11.

Shah, Amit, Wayne Liu, Kui K. Chan, et al.. (2015). Protein Engineering of Coenzyme‐A‐Dependent Aldehyde Dehydrogenase for Commercial Scale 1,4‐Butanediol Production in Escherichia coli. The FASEB Journal. 29(S1). 1 indexed citations

12.

Tóth, K, Tina L. Amyes, B.M. Wood, et al.. (2010). Product Deuterium Isotope Effects for Orotidine 5′-Monophosphate Decarboxylase: Effect of Changing Substrate and Enzyme Structure on the Partitioning of the Vinyl Carbanion Reaction Intermediate. Journal of the American Chemical Society. 132(20). 7018–7024. 21 indexed citations

13.

Wood, B.M., Kui K. Chan, Tina L. Amyes, John P. Richard, & J.A. Gerlt. (2009). Mechanism of the Orotidine 5′-Monophosphate Decarboxylase-Catalyzed Reaction: Effect of Solvent Viscosity on Kinetic Constants. Biochemistry. 48(24). 5510–5517. 31 indexed citations

14.

Chan, Kui K., B.M. Wood, А.А. Федоров, et al.. (2009). Mechanism of the Orotidine 5′-Monophosphate Decarboxylase-Catalyzed Reaction: Evidence for Substrate Destabilization^,. Biochemistry. 48(24). 5518–5531. 55 indexed citations

15.

Tóth, K, Tina L. Amyes, B.M. Wood, et al.. (2009). An Examination of the Relationship between Active Site Loop Size and Thermodynamic Activation Parameters for Orotidine 5′-Monophosphate Decarboxylase from Mesophilic and Thermophilic Organisms. Biochemistry. 48(33). 8006–8013. 30 indexed citations

16.

Amyes, Tina L., B.M. Wood, Kui K. Chan, J.A. Gerlt, & John P. Richard. (2008). Formation and Stability of a Vinyl Carbanion at the Active Site of Orotidine 5‘-Monophosphate Decarboxylase: p K _a of the C-6 Proton of Enzyme-Bound UMP. Journal of the American Chemical Society. 130(5). 1574–1575. 69 indexed citations

17.

Chan, Kui K., А.А. Федоров, E.V. Fedorov, Steven C. Almo, & J.A. Gerlt. (2008). Structural Basis for Substrate Specificity in Phosphate Binding (β/α)₈-Barrels: d-Allulose 6-Phosphate 3-Epimerase from Escherichia coli K-12. Biochemistry. 47(36). 9608–9617. 16 indexed citations

18.

Tóth, K, Tina L. Amyes, B.M. Wood, et al.. (2007). Product Deuterium Isotope Effect for Orotidine 5‘-Monophosphate Decarboxylase: Evidence for the Existence of a Short-Lived Carbanion Intermediate. Journal of the American Chemical Society. 129(43). 12946–12947. 41 indexed citations

19.

Moran, R G, Paul D. Colman, A. Rosowsky, Ronald A. Forsch, & Kui K. Chan. (1985). Structural features of 4-amino antifolates required for substrate activity with mammalian folylpolyglutamate synthetase.. Molecular Pharmacology. 27(1). 156–166. 73 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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