Cong‐Zhao Zhou

12.9k total citations · 2 hit papers
161 papers, 4.5k citations indexed

About

Cong‐Zhao Zhou is a scholar working on Molecular Biology, Materials Chemistry and Ecology. According to data from OpenAlex, Cong‐Zhao Zhou has authored 161 papers receiving a total of 4.5k indexed citations (citations by other indexed papers that have themselves been cited), including 121 papers in Molecular Biology, 30 papers in Materials Chemistry and 22 papers in Ecology. Recurrent topics in Cong‐Zhao Zhou's work include Enzyme Structure and Function (30 papers), RNA and protein synthesis mechanisms (20 papers) and Photosynthetic Processes and Mechanisms (19 papers). Cong‐Zhao Zhou is often cited by papers focused on Enzyme Structure and Function (30 papers), RNA and protein synthesis mechanisms (20 papers) and Photosynthetic Processes and Mechanisms (19 papers). Cong‐Zhao Zhou collaborates with scholars based in China, France and United States. Cong‐Zhao Zhou's co-authors include Yuxing Chen, Yong‐Liang Jiang, Joël Janin, Fabrice Confalonieri, Roland Perasso, Michel Jacquet, Zhengang Li, Yong‐Xing He, Cheng‐Cai Zhang and Weifang Li and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Nucleic Acids Research and Journal of Biological Chemistry.

In The Last Decade

Cong‐Zhao Zhou

157 papers receiving 4.5k citations

Hit Papers

Silk fibroin: Structural implications of a remarkable ami... 2000 2026 2008 2017 2001 2000 200 400 600

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Cong‐Zhao Zhou China 34 2.5k 1.3k 459 431 383 161 4.5k
Oldřích Benada Czechia 36 1.8k 0.7× 354 0.3× 518 1.1× 389 0.9× 333 0.9× 175 4.1k
Jin He China 36 2.2k 0.9× 769 0.6× 403 0.9× 444 1.0× 1.2k 3.2× 134 5.4k
Wei‐Chiang Shen United States 43 4.5k 1.8× 658 0.5× 791 1.7× 234 0.5× 225 0.6× 131 6.8k
Seong‐Cheol Park South Korea 34 1.9k 0.8× 416 0.3× 457 1.0× 138 0.3× 244 0.6× 150 3.6k
Luciano Paulino Silva Brazil 35 1.3k 0.5× 504 0.4× 636 1.4× 109 0.3× 590 1.5× 208 4.0k
Kiyoshi Yamauchi Japan 40 1.9k 0.8× 1.5k 1.2× 192 0.4× 361 0.8× 318 0.8× 280 6.3k
Tara D. Sutherland Australia 34 1.2k 0.5× 1.0k 0.8× 577 1.3× 186 0.4× 104 0.3× 85 3.4k
Yang Ding China 35 3.4k 1.4× 796 0.6× 1.3k 2.8× 299 0.7× 355 0.9× 108 6.9k
Linglin Fu China 42 1.8k 0.7× 463 0.4× 493 1.1× 171 0.4× 338 0.9× 183 5.3k
Sônia Nair Báo Brazil 41 1.4k 0.5× 497 0.4× 538 1.2× 157 0.4× 294 0.8× 321 5.8k

Countries citing papers authored by Cong‐Zhao Zhou

Since Specialization
Citations

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

Fields of papers citing papers by Cong‐Zhao Zhou

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Cong‐Zhao Zhou. 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 Cong‐Zhao Zhou. The network helps show where Cong‐Zhao Zhou may publish in the future.

Co-authorship network of co-authors of Cong‐Zhao Zhou

This figure shows the co-authorship network connecting the top 25 collaborators of Cong‐Zhao Zhou. A scholar is included among the top collaborators of Cong‐Zhao Zhou 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 Cong‐Zhao Zhou. Cong‐Zhao Zhou 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.
Xing, Zheng, et al.. (2025). Pdr15 ABC Transporter of Phyllospheric Yeast Enhances Plant Tolerance to 4-Monobrominated Diphenyl Ether, Chromium, and Cadmium Stress. Journal of Agricultural and Food Chemistry. 73(45). 28735–28744.
2.
Yang, Feng, Hongyan Zhang, Ning Cui, et al.. (2024). Structure of the intact tail machine of Anabaena myophage A-1(L). Nature Communications. 15(1). 2654–2654. 12 indexed citations
3.
Ain, Qurat Ul, Xuan Wu, Qing Bai, et al.. (2024). Cyanophage-encoded auxiliary metabolic genes in modulating cyanobacterial metabolism and algal bloom dynamics. SHILAP Revista de lepidopterología. 4. 5 indexed citations
4.
Li, Bo, Xiaoqian Wang, Da Xu, et al.. (2024). Allosteric regulation of nitrate transporter NRT via the signaling protein PII. Proceedings of the National Academy of Sciences. 121(11). e2318320121–e2318320121. 4 indexed citations
5.
Zhao, Dandan, Yuhao Qin, Jiaqi Liu, et al.. (2023). Orally administered BZL-sRNA-20 oligonucleotide targeting TLR4 effectively ameliorates acute lung injury in mice. Science China Life Sciences. 66(7). 1589–1599. 11 indexed citations
6.
Wang, Liang, et al.. (2023). Structural insights into human ABCC4-mediated transport of platelet agonist and antagonist. Nature Cardiovascular Research. 2(7). 693–701. 12 indexed citations
7.
Yang, Feng, Qingfa Wu, Yuxing Chen, et al.. (2023). Phylogenomics of five Pseudanabaena cyanophages and evolutionary traces of horizontal gene transfer. Environmental Microbiome. 18(1). 3–3. 6 indexed citations
8.
Chen, Zhipeng, et al.. (2022). Structural insights into the activation of autoinhibited human lipid flippase ATP8B1 upon substrate binding. Proceedings of the National Academy of Sciences. 119(14). e2118656119–e2118656119. 27 indexed citations
9.
Haubrich, Brad A., Caroline Williams, Tahl Zimmerman, et al.. (2022). Inhibition of Streptococcus pneumoniae growth by masarimycin. Microbiology. 168(4).
10.
Cai, Kun, Yong‐Liang Jiang, Yue Chen, et al.. (2022). Biochemical and structural characterization of the cyanophage‐encoded phosphate‐binding protein: implications for enhanced phosphate uptake of infected cyanobacteria. Environmental Microbiology. 24(7). 3037–3050. 15 indexed citations
11.
Xu, Tingting, Cong‐Zhao Zhou, Jianxi Xiao, & Jinsong Liu. (2018). Unique Conformation in a Natural Interruption Sequence of Type XIX Collagen Revealed by Its High-Resolution Crystal Structure. Biochemistry. 57(7). 1087–1095. 7 indexed citations
12.
Ruan, Lingwei, et al.. (2018). Cloning, identification and function analysis of a Chibby homolog from Litopenaeus vannamei. Fish & Shellfish Immunology. 78. 114–120. 8 indexed citations
13.
Chi, Changbiao, Yajun Tang, Jiahai Zhang, et al.. (2018). Structural and Biochemical Insights into the Multiple Functions of Yeast Grx3. Journal of Molecular Biology. 430(8). 1235–1248. 18 indexed citations
14.
Tan, Xiao-Feng, Ya-Nan Dai, Kang Zhou, et al.. (2015). Structure of the adenylation–peptidyl carrier protein didomain of theMicrocystis aeruginosamicrocystin synthetase McyG. Acta Crystallographica Section D Biological Crystallography. 71(4). 873–881. 20 indexed citations
15.
Yang, Yihu, Yong‐Liang Jiang, Juan Zhang, et al.. (2014). Structural Insights into SraP-Mediated Staphylococcus aureus Adhesion to Host Cells. PLoS Pathogens. 10(6). e1004169–e1004169. 84 indexed citations
16.
Bao, Rui, Cong‐Zhao Zhou, Chunhui Jiang, et al.. (2009). The Ternary Structure of the Double-headed Arrowhead Protease Inhibitor API-A Complexed with Two Trypsins Reveals a Novel Reactive Site Conformation. Journal of Biological Chemistry. 284(39). 26676–26684. 49 indexed citations
17.
Tang, Jie, Weifang Li, Xuan Zhang, & Cong‐Zhao Zhou. (2007). The gene expression profile of Bombyx mori silkgland. Gene. 396(2). 369–372. 7 indexed citations
18.
Bao, Rui, Yuxing Chen, Yajun Tang, Joël Janin, & Cong‐Zhao Zhou. (2006). Crystal structure of the yeast cytoplasmic thioredoxin Trx2. Proteins Structure Function and Bioinformatics. 66(1). 246–249. 22 indexed citations
19.
Bao, Rui, et al.. (2006). Expression, purification, crystallization and preliminary X-ray diffraction analysis of mitochondrial thioredoxin Trx3 fromSaccharomyces cerevisiae. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62(11). 1161–1163. 3 indexed citations
20.
Zhou, Cong‐Zhao, Fabrice Confalonieri, Michel Jacquet, et al.. (2001). Silk fibroin: Structural implications of a remarkable amino acid sequence. Proteins Structure Function and Bioinformatics. 44(2). 119–122. 617 indexed citations breakdown →

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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