Kam‐Bo Wong

5.1k total citations
127 papers, 3.9k citations indexed

About

Kam‐Bo Wong is a scholar working on Molecular Biology, Materials Chemistry and Atomic and Molecular Physics, and Optics. According to data from OpenAlex, Kam‐Bo Wong has authored 127 papers receiving a total of 3.9k indexed citations (citations by other indexed papers that have themselves been cited), including 59 papers in Molecular Biology, 42 papers in Materials Chemistry and 33 papers in Atomic and Molecular Physics, and Optics. Recurrent topics in Kam‐Bo Wong's work include Semiconductor Quantum Structures and Devices (31 papers), Enzyme Structure and Function (23 papers) and Toxin Mechanisms and Immunotoxins (21 papers). Kam‐Bo Wong is often cited by papers focused on Semiconductor Quantum Structures and Devices (31 papers), Enzyme Structure and Function (23 papers) and Toxin Mechanisms and Immunotoxins (21 papers). Kam‐Bo Wong collaborates with scholars based in Hong Kong, United Kingdom and China. Kam‐Bo Wong's co-authors include M. Jaroš, Stefan M.V. Freund, Pang‐Chui Shaw, Alan R. Fersht, Valerie Daggett, Alan R. Fersht, David Chi‐Cheong Wan, Mark Bycroft, M. A. Gell and Jane Clarke and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Physical Review Letters and Nucleic Acids Research.

In The Last Decade

Kam‐Bo Wong

122 papers receiving 3.8k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Kam‐Bo Wong Hong Kong 36 2.0k 938 634 553 514 127 3.9k
Michael G. Prisant United States 13 5.2k 2.6× 1.3k 1.4× 596 0.9× 332 0.6× 402 0.8× 25 7.6k
B.C. Finzel United States 29 4.0k 2.0× 1.2k 1.3× 358 0.6× 129 0.2× 265 0.5× 69 6.4k
An‐Suei Yang Taiwan 38 3.7k 1.9× 1.1k 1.2× 288 0.5× 537 1.0× 110 0.2× 88 5.3k
Albert M. Berghuis Canada 39 4.5k 2.2× 969 1.0× 236 0.4× 308 0.6× 148 0.3× 116 5.9k
Se Won Suh South Korea 40 4.2k 2.1× 906 1.0× 317 0.5× 91 0.2× 494 1.0× 196 5.7k
Demetrius Tsernoglou Italy 37 4.5k 2.2× 1.4k 1.4× 415 0.7× 417 0.8× 296 0.6× 77 6.2k
Robin J. Leatherbarrow United Kingdom 44 3.2k 1.6× 401 0.4× 376 0.6× 81 0.1× 279 0.5× 118 4.7k
Dmitri Beglov United States 30 5.1k 2.5× 626 0.7× 752 1.2× 177 0.3× 282 0.5× 51 6.9k
Oreola Donini United States 15 3.7k 1.8× 549 0.6× 452 0.7× 323 0.6× 100 0.2× 33 5.5k
J. Michael Word United States 14 5.6k 2.8× 1.9k 2.1× 455 0.7× 193 0.3× 358 0.7× 14 7.3k

Countries citing papers authored by Kam‐Bo Wong

Since Specialization
Citations

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

Fields of papers citing papers by Kam‐Bo Wong

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Kam‐Bo Wong. 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 Kam‐Bo Wong. The network helps show where Kam‐Bo Wong may publish in the future.

Co-authorship network of co-authors of Kam‐Bo Wong

This figure shows the co-authorship network connecting the top 25 collaborators of Kam‐Bo Wong. A scholar is included among the top collaborators of Kam‐Bo Wong 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 Kam‐Bo Wong. Kam‐Bo Wong 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.
Ma, Juncai, Ruben Shrestha, Lei Feng, et al.. (2025). Biomolecular condensation of ERC1 recruits ATG8 and NBR1 to drive autophagosome formation for plant heat tolerance. Proceedings of the National Academy of Sciences. 122(46). e2425689122–e2425689122.
2.
Yang, Meijing, Shuai Chen, Jia Zhong, et al.. (2024). A converged ubiquitin‐proteasome pathway for the degradation of TOC and TOM tail‐anchored receptors. Journal of Integrative Plant Biology. 66(5). 1007–1023. 2 indexed citations
3.
Wong, Kam‐Bo, et al.. (2024). Using AlphaFold2 and Molecular Dynamics Simulation to Model Protein Recognition. Methods in molecular biology. 2841. 49–66.
4.
Zeng, Yonglun, Zizhen Liang, Zhiqi Liu, et al.. (2023). Recent advances in plant endomembrane research and new microscopical techniques. New Phytologist. 240(1). 41–60. 11 indexed citations
5.
Zeng, Yonglun, Baiying Li, Lei Feng, et al.. (2021). A unique AtSar1D-AtRabD2a nexus modulates autophagosome biogenesis in Arabidopsis thaliana. Proceedings of the National Academy of Sciences. 118(17). 38 indexed citations
6.
Mukherjee, Rukmini, Anshu Bhattacharya, Denisa Bojková, et al.. (2021). Famotidine inhibits toll-like receptor 3-mediated inflammatory signaling in SARS-CoV-2 infection. Journal of Biological Chemistry. 297(2). 100925–100925. 40 indexed citations
7.
Chen, Shuai, et al.. (2021). Structural insights into how vacuolar sorting receptors recognize the sorting determinants of seed storage proteins. Proceedings of the National Academy of Sciences. 119(1). 14 indexed citations
8.
Chen, Shuai, et al.. (2018). FdC1 and Leaf-Type Ferredoxins Channel Electrons From Photosystem I to Different Downstream Electron Acceptors. Frontiers in Plant Science. 9. 410–410. 25 indexed citations
9.
Fong, Y.H., et al.. (2017). Structural insights into how GTP-dependent conformational changes in a metallochaperone UreG facilitate urease maturation. Proceedings of the National Academy of Sciences. 114(51). E10890–E10898. 40 indexed citations
10.
Law, Yee-Song, et al.. (2016). AtPAP2 modulates the import of the small subunit of Rubisco into chloroplasts. Plant Signaling & Behavior. 11(10). e1239687–e1239687. 14 indexed citations
11.
Wang, Ruirui, Hong‐Yi Zheng, Liangmin Gao, et al.. (2015). The Recombinant Maize Ribosome-Inactivating Protein Transiently Reduces Viral Load in SHIV89.6 Infected Chinese Rhesus Macaques. Toxins. 7(1). 156–169. 9 indexed citations
12.
Cheung, Ming-Yan, Rui Miao, Meihui Yu, et al.. (2015). Site-directed Mutagenesis Shows the Significance of Interactions with Phospholipids and the G-protein OsYchF1 for the Physiological Functions of the Rice GTPase-activating Protein 1 (OsGAP1). Journal of Biological Chemistry. 290(39). 23984–23996. 13 indexed citations
13.
14.
Chan, Kwok-Ho, et al.. (2012). Structural Basis for GTP-Dependent Dimerization of Hydrogenase Maturation Factor HypB. PLoS ONE. 7(1). e30547–e30547. 24 indexed citations
15.
Sze, Kong‐Hung, et al.. (2011). A Rigidifying Salt-Bridge Favors the Activity of Thermophilic Enzyme at High Temperatures at the Expense of Low-Temperature Activity. PLoS Biology. 9(3). e1001027–e1001027. 61 indexed citations
16.
Chan, Kwok-Ho & Kam‐Bo Wong. (2011). Structure of an essential GTPase, YsxC, fromThermotoga maritima. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67(6). 640–646. 4 indexed citations
17.
Yu, C., Denise Chan, Guang Zhu, et al.. (2010). Solution structure of the dimerization domain of ribosomal protein P2 provides insights for the structural organization of eukaryotic stalk. Nucleic Acids Research. 38(15). 5206–5216. 36 indexed citations
18.
19.
Ding, Yi, Zhichen Wang, Yiwei Liu, et al.. (2003). The structural basis of Trp192 and the C-terminal region in trichosanthin for activity and conformational stability. Protein Engineering Design and Selection. 16(5). 351–356. 8 indexed citations
20.
Wong, Kam‐Bo, Alan R. Fersht, & Stefan M.V. Freund. (1997). NMR 15 N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A 1 1Edited by P. E. Wright. Journal of Molecular Biology. 268(2). 494–511. 35 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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