Wanchao Yin

4.0k total citations
27 papers, 1.1k citations indexed

About

Wanchao Yin is a scholar working on Molecular Biology, Cellular and Molecular Neuroscience and Infectious Diseases. According to data from OpenAlex, Wanchao Yin has authored 27 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 20 papers in Molecular Biology, 10 papers in Cellular and Molecular Neuroscience and 8 papers in Infectious Diseases. Recurrent topics in Wanchao Yin's work include Receptor Mechanisms and Signaling (17 papers), Neuropeptides and Animal Physiology (9 papers) and SARS-CoV-2 and COVID-19 Research (8 papers). Wanchao Yin is often cited by papers focused on Receptor Mechanisms and Signaling (17 papers), Neuropeptides and Animal Physiology (9 papers) and SARS-CoV-2 and COVID-19 Research (8 papers). Wanchao Yin collaborates with scholars based in China, United States and Germany. Wanchao Yin's co-authors include H. Eric Xu, Yi Jiang, Canrong Wu, Xinheng He, Fulai Zhou, Hualiang Jiang, Yan Zhang, Dehua Yang, Ming‐Wei Wang and Peiyu Xu and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Nature Communications.

In The Last Decade

Wanchao Yin

23 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Wanchao Yin China 18 673 312 299 210 94 27 1.1k
Jeffrey Velasquez United States 7 1.0k 1.5× 417 1.3× 179 0.6× 118 0.6× 112 1.2× 8 1.3k
Coralie Di Scala France 18 758 1.1× 201 0.6× 325 1.1× 137 0.7× 23 0.2× 28 1.4k
Minos–Timotheos Matsoukas Greece 19 775 1.2× 134 0.4× 96 0.3× 231 1.1× 112 1.2× 64 1.3k
Andrew Orry United States 17 1.3k 1.9× 248 0.8× 62 0.2× 341 1.6× 83 0.9× 37 1.6k
Christopher Higgs United Kingdom 12 432 0.6× 212 0.7× 80 0.3× 115 0.5× 61 0.6× 18 687
Mattia Sturlese Italy 21 939 1.4× 102 0.3× 162 0.5× 395 1.9× 36 0.4× 85 1.4k
Andrea E. DeBarber United States 23 777 1.2× 117 0.4× 244 0.8× 58 0.3× 18 0.2× 49 1.8k
Per-Olof Markgren Sweden 13 631 0.9× 100 0.3× 169 0.6× 133 0.6× 138 1.5× 13 1.1k
Li-Yin Huang United States 8 680 1.0× 365 1.2× 76 0.3× 68 0.3× 83 0.9× 10 802
John O. Hui United States 19 602 0.9× 60 0.2× 500 1.7× 95 0.5× 102 1.1× 42 1.3k

Countries citing papers authored by Wanchao Yin

Since Specialization
Citations

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

Fields of papers citing papers by Wanchao Yin

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Wanchao Yin

This figure shows the co-authorship network connecting the top 25 collaborators of Wanchao Yin. A scholar is included among the top collaborators of Wanchao Yin 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 Wanchao Yin. Wanchao Yin 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.
Liu, Hongli, Chongzhao You, Yixiao Zhang, et al.. (2025). Structural insights into antagonist recognition by the vasopressin V2 receptor. Nature Communications. 16(1). 9734–9734.
2.
Xie, Wenqin, et al.. (2024). Structural features of arrestin-mediated GPCR signaling. SHILAP Revista de lepidopterología. 24. 100201–100201.
3.
Liu, Heng, Qing Zhang, Xinheng He, et al.. (2023). Structural insights into ligand recognition and activation of the medium-chain fatty acid-sensing receptor GPR84. Nature Communications. 14(1). 3271–3271. 32 indexed citations
4.
Sun, Wenjing, Fan Yang, Huanhuan Zhang, et al.. (2023). Structural insights into neurokinin 3 receptor activation by endogenous and analogue peptide agonists. Cell Discovery. 9(1). 66–66. 9 indexed citations
5.
Duan, Jia, Heng Liu, Fenghui Zhao, et al.. (2023). GPCR activation and GRK2 assembly by a biased intracellular agonist. Nature. 620(7974). 676–681. 58 indexed citations
6.
Duan, Jia, Dandan Shen, Tingting Zhao, et al.. (2022). Molecular basis for allosteric agonism and G protein subtype selectivity of galanin receptors. Nature Communications. 13(1). 1364–1364. 36 indexed citations
7.
Luan, Xiaodong, Xinming Li, Yufan Li, et al.. (2022). Antiviral drug design based on structural insights into the N-terminal domain and C-terminal domain of the SARS-CoV-2 nucleocapsid protein. Science Bulletin. 67(22). 2327–2335. 17 indexed citations
8.
Wu, Canrong, Wanchao Yin, Yi Jiang, & H. Eric Xu. (2022). Structure genomics of SARS-CoV-2 and its Omicron variant: drug design templates for COVID-19. Acta Pharmacologica Sinica. 43(12). 3021–3033. 77 indexed citations
9.
Luan, Xiaodong, Weijuan Shang, Wanchao Yin, et al.. (2022). Structure basis for inhibition of SARS-CoV-2 by the feline drug GC376. Acta Pharmacologica Sinica. 44(1). 255–257. 10 indexed citations
10.
You, Chongzhao, Peiyu Xu, Sijie Huang, et al.. (2022). Structural insights into the peptide selectivity and activation of human neuromedin U receptors. Nature Communications. 13(1). 2045–2045. 18 indexed citations
11.
Xu, Youwei, Canrong Wu, Xiaodan Cao, et al.. (2022). Structural and biochemical mechanism for increased infectivity and immune evasion of Omicron BA.2 variant compared to BA.1 and their possible mouse origins. Cell Research. 32(7). 609–620. 56 indexed citations
12.
Duan, Jia, Peiyu Xu, Xi Cheng, et al.. (2021). Structures of full-length glycoprotein hormone receptor signalling complexes. Nature. 598(7882). 688–692. 69 indexed citations
13.
Zhao, Fenghui, Chao Zhang, Qingtong Zhou, et al.. (2021). Structural insights into hormone recognition by the human glucose-dependent insulinotropic polypeptide receptor. eLife. 10. 30 indexed citations
14.
Yin, Wanchao, Xiaodong Luan, Zhihai Li, et al.. (2021). Structural basis for inhibition of the SARS-CoV-2 RNA polymerase by suramin. Nature Structural & Molecular Biology. 28(3). 319–325. 118 indexed citations
15.
Wang, Yue, Shimeng Guo, Youwen Zhuang, et al.. (2021). Molecular recognition of an acyl-peptide hormone and activation of ghrelin receptor. Nature Communications. 12(1). 5064–5064. 51 indexed citations
16.
Yin, Yu-Ling, Chenyu Ye, Fulai Zhou, et al.. (2021). Molecular basis for kinin selectivity and activation of the human bradykinin receptors. Nature Structural & Molecular Biology. 28(9). 755–761. 36 indexed citations
17.
Liu, Qiufeng, Dehua Yang, Youwen Zhuang, et al.. (2021). Ligand recognition and G-protein coupling selectivity of cholecystokinin A receptor. Nature Chemical Biology. 17(12). 1238–1244. 67 indexed citations
18.
Zhou, Yu, Yan Fu, Wanchao Yin, et al.. (2021). Kinetics-Driven Drug Design Strategy for Next-Generation Acetylcholinesterase Inhibitors to Clinical Candidate. Journal of Medicinal Chemistry. 64(4). 1844–1855. 52 indexed citations
19.
Jiang, Yi, Wanchao Yin, & H. Eric Xu. (2020). RNA-dependent RNA polymerase: Structure, mechanism, and drug discovery for COVID-19. Biochemical and Biophysical Research Communications. 538. 47–53. 115 indexed citations
20.
Yin, Wanchao, Zhihai Li, Mingliang Jin, et al.. (2019). A complex structure of arrestin-2 bound to a G protein-coupled receptor. Cell Research. 29(12). 971–983. 148 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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