Tzu‐Ping Ko

9.3k total citations · 1 hit paper
217 papers, 7.3k citations indexed

About

Tzu‐Ping Ko is a scholar working on Molecular Biology, Materials Chemistry and Pharmacology. According to data from OpenAlex, Tzu‐Ping Ko has authored 217 papers receiving a total of 7.3k indexed citations (citations by other indexed papers that have themselves been cited), including 159 papers in Molecular Biology, 57 papers in Materials Chemistry and 36 papers in Pharmacology. Recurrent topics in Tzu‐Ping Ko's work include Enzyme Structure and Function (57 papers), Plant biochemistry and biosynthesis (46 papers) and Microbial Natural Products and Biosynthesis (33 papers). Tzu‐Ping Ko is often cited by papers focused on Enzyme Structure and Function (57 papers), Plant biochemistry and biosynthesis (46 papers) and Microbial Natural Products and Biosynthesis (33 papers). Tzu‐Ping Ko collaborates with scholars based in Taiwan, China and United States. Tzu‐Ping Ko's co-authors include Andrew H.‐J. Wang, Rey‐Ting Guo, Po‐Huang Liang, Chun‐Chi Chen, Weidong Liu, Ya‐Shan Cheng, Chih‐Jung Kuo, Jian‐Wen Huang, Chun‐Hsiang Huang and Yingying Zheng and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Nucleic Acids Research.

In The Last Decade

Tzu‐Ping Ko

217 papers receiving 7.2k 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.

The opportunistic marine pathogen Vibrio parahaemolyticus becomes virulent by acquiring a plasmid that expresses a deadly toxin

2015 467 citations Tzu‐Ping Ko, Yun-Tzu Huang et al. Proceedings of the National Academy of Sciences profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Tzu‐Ping Ko Taiwan	46	4.4k	971	821	716	704	217	7.3k
Florian Kiefer Switzerland	18	5.1k 1.2×	877 0.9×	374 0.5×	507 0.7×	601 0.9×	29	8.1k
Alexei Savchenko Canada	55	5.4k 1.2×	1.2k 1.2×	375 0.5×	694 1.0×	389 0.6×	215	8.2k
Rafal Gumienny Switzerland	10	6.2k 1.4×	586 0.6×	458 0.6×	615 0.9×	745 1.1×	10	9.9k
Rosalba Lepore Italy	15	5.7k 1.3×	514 0.5×	433 0.5×	581 0.8×	777 1.1×	27	9.3k
Marco Biasini Switzerland	8	4.7k 1.1×	639 0.7×	328 0.4×	528 0.7×	516 0.7×	10	7.2k
Christine Rempfer Germany	5	5.7k 1.3×	481 0.5×	454 0.6×	625 0.9×	725 1.0×	6	9.3k
Florian Heer Switzerland	3	5.3k 1.2×	441 0.5×	418 0.5×	567 0.8×	677 1.0×	4	8.7k
Wim J. Quax Netherlands	53	7.4k 1.7×	570 0.6×	509 0.6×	1.1k 1.5×	758 1.1×	239	9.7k
Mirosław Cygler Canada	59	10.2k 2.3×	1.5k 1.5×	863 1.1×	1.1k 1.5×	706 1.0×	246	13.8k
Kai Hilpert Germany	31	4.3k 1.0×	608 0.6×	522 0.6×	282 0.4×	730 1.0×	71	8.4k

Countries citing papers authored by Tzu‐Ping Ko

Since Specialization

Citations

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

Fields of papers citing papers by Tzu‐Ping Ko

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Tzu‐Ping Ko. 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 Tzu‐Ping Ko. The network helps show where Tzu‐Ping Ko may publish in the future.

Co-authorship network of co-authors of Tzu‐Ping Ko

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

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

Liu, Changyi, Chan‐Pin Lin, Yi‐Ting Liao, et al.. (2024). Structural insights into the molecular mechanism of phytoplasma immunodominant membrane protein. IUCrJ. 11(3). 384–394. 2 indexed citations

Lin, Shin-Jen, Yuan‐Chih Chang, Yu‐Hsuan Chen, et al.. (2024). The QS regulator AphB promotes expression of the AHPND PirA and PirB toxins and may enhance virulence under acidic conditions. International Journal of Biological Macromolecules. 283(Pt 1). 137563–137563. 1 indexed citations

Ho, Meng‐Ru, et al.. (2023). Robust Design of Effective Allosteric Activators for Rsp5 E3 Ligase Using the Machine Learning Tool ProteinMPNN. ACS Synthetic Biology. 12(8). 2310–2319. 4 indexed citations

Huang, Kai-Fa, et al.. (2021). A Unique Carboxylic-Acid Hydrogen-Bond Network (CAHBN) Confers Glutaminyl Cyclase Activity on M28 Family Enzymes. Journal of Molecular Biology. 433(13). 166960–166960. 3 indexed citations

Lee, Cheng‐Chung, Yu-Cheng Su, Tzu‐Ping Ko, et al.. (2020). Structural basis of polyethylene glycol recognition by antibody. Journal of Biomedical Science. 27(1). 12–12. 45 indexed citations

Chen, Chun‐Chi, Lilan Zhang, Xuejing Yu, et al.. (2020). Versatile cis-isoprenyl Diphosphate Synthase Superfamily Members in Catalyzing Carbon–Carbon Bond Formation. ACS Catalysis. 10(8). 4717–4725. 15 indexed citations

Chen, Chun‐Chi, Jing Xue, Wei Peng, et al.. (2020). Structural insights into thebaine synthase 2 catalysis. Biochemical and Biophysical Research Communications. 529(2). 156–161. 9 indexed citations

Lin, Shin-Jen, Yi‐Fan Chen, Kai‐Cheng Hsu, et al.. (2019). Structural Insights to the Heterotetrameric Interaction between the Vibrio parahaemolyticus PirAvp and PirBvp Toxins and Activation of the Cry-Like Pore-Forming Domain. Toxins. 11(4). 233–233. 33 indexed citations

Liao, Yi‐Ting, Shih‐Shun Lin, Chan‐Pin Lin, et al.. (2019). Structural insights into the interaction between phytoplasmal effector causing phyllody 1 and MADS transcription factors. The Plant Journal. 100(4). 706–719. 18 indexed citations

10.

Xue, Jing, Yunyun Yang, Tzu‐Ping Ko, et al.. (2019). Structural insights into the calcium dependence of Stig cyclases. RSC Advances. 9(23). 13182–13185. 1 indexed citations

11.

Ko, Tzu‐Ping, et al.. (2017). Enzymatic characterization and crystal structure analysis of Chlamydomonas reinhardtii dehydroascorbate reductase and their implications for oxidative stress. Plant Physiology and Biochemistry. 120. 144–155. 14 indexed citations

12.

Ko, Tzu‐Ping, Yun-Tzu Huang, Jiun‐Yan Huang, et al.. (2015). The opportunistic marine pathogen Vibrio parahaemolyticus becomes virulent by acquiring a plasmid that expresses a deadly toxin. Proceedings of the National Academy of Sciences. 112(34). 10798–10803. 467 indexed citations breakdown →

13.

Wang, Hao‐Ching, Kai‐Cheng Hsu, Jinn‐Moon Yang, et al.. (2013). Staphylococcus aureus protein SAUGI acts as a uracil-DNA glycosylase inhibitor. Nucleic Acids Research. 42(2). 1354–1364. 36 indexed citations

14.

Chan, Hsiu‐Chien, Yueming Zhu, Yumei Hu, et al.. (2012). Crystal structures of d-psicose 3-epimerase from Clostridium cellulolyticum H10 and its complex with ketohexose sugars. Protein & Cell. 3(2). 123–131. 79 indexed citations

15.

Chou, Chi‐Chi, et al.. (2010). Protein S-Thiolation by Glutathionylspermidine (Gsp). Journal of Biological Chemistry. 285(33). 25345–25353. 32 indexed citations

16.

Wang, Hao‐Ching, Han‐Ching Wang, Tzu‐Ping Ko, et al.. (2008). White spot syndrome virus protein ICP11: A histone-binding DNA mimic that disrupts nucleosome assembly. Proceedings of the National Academy of Sciences. 105(52). 20758–20763. 74 indexed citations

17.

Ko, Tzu‐Ping, et al.. (2008). Structural Basis for Catalytic and Inhibitory Mechanisms of Human Prostaglandin Reductase PTGR2. Structure. 16(11). 1714–1723. 45 indexed citations

18.

Ko, Tzu‐Ping, et al.. (2003). Crystal Structure of Yeast Cytosine Deaminase. Journal of Biological Chemistry. 278(21). 19111–19117. 105 indexed citations

19.

Huang, Kai-Fa, Shyh‐Horng Chiou, Tzu‐Ping Ko, Jeu‐Ming P. Yuann, & Andrew H.‐J. Wang. (2002). The 1.35 Å structure of cadmium-substituted TM-3, a snake-venom metalloproteinase from Taiwan habu: elucidation of a TNFα-converting enzyme-like active-site structure with a distorted octahedral geometry of cadmium. Acta Crystallographica Section D Biological Crystallography. 58(7). 1118–1128. 26 indexed citations

20.

Safo, Martin K., Faik N. Musayev, Shih‐Hsiung Wu, Donald J. Abraham, & Tzu‐Ping Ko. (2001). Structure of tetragonal crystals of human erythrocyte catalase. Acta Crystallographica Section D Biological Crystallography. 57(1). 1–7. 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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