Hanqin Peng

4.7k total citations · 3 hit papers
20 papers, 2.5k citations indexed

About

Hanqin Peng is a scholar working on Infectious Diseases, Virology and Molecular Biology. According to data from OpenAlex, Hanqin Peng has authored 20 papers receiving a total of 2.5k indexed citations (citations by other indexed papers that have themselves been cited), including 10 papers in Infectious Diseases, 10 papers in Virology and 6 papers in Molecular Biology. Recurrent topics in Hanqin Peng's work include HIV Research and Treatment (10 papers), SARS-CoV-2 and COVID-19 Research (8 papers) and Monoclonal and Polyclonal Antibodies Research (5 papers). Hanqin Peng is often cited by papers focused on HIV Research and Treatment (10 papers), SARS-CoV-2 and COVID-19 Research (8 papers) and Monoclonal and Polyclonal Antibodies Research (5 papers). Hanqin Peng collaborates with scholars based in United States, China and Poland. Hanqin Peng's co-authors include Bing Chen, Sophia Rits‐Volloch, Yongfei Cai, Jun Zhang, Tianshu Xiao, Richard M. Walsh, Sarah M. Sterling, Shaun Rawson, Michael S. Seaman and Jianming Lü and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Hanqin Peng

19 papers receiving 2.5k citations

Hit Papers

Distinct conformational states of SARS-CoV-2 spike protein 2020 2026 2022 2024 2020 2021 2021 250 500 750

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Hanqin Peng United States 17 1.8k 936 732 478 413 20 2.5k
Sophia Rits‐Volloch United States 20 1.8k 1.0× 1.0k 1.1× 906 1.2× 590 1.2× 504 1.2× 35 2.9k
Priyamvada Acharya United States 23 1.2k 0.7× 1.1k 1.2× 684 0.9× 417 0.9× 431 1.0× 56 2.3k
Christopher A. Cottrell United States 15 1.2k 0.7× 742 0.8× 576 0.8× 380 0.8× 340 0.8× 19 2.0k
Christopher O. Barnes United States 20 1.4k 0.8× 1.1k 1.1× 282 0.4× 327 0.7× 398 1.0× 37 2.4k
Jesper Pallesen United States 17 1.5k 0.8× 897 1.0× 245 0.3× 248 0.5× 231 0.6× 23 2.4k
Adam S. Dingens United States 19 3.2k 1.8× 1.4k 1.5× 288 0.4× 437 0.9× 540 1.3× 27 4.0k
Jianhui Nie China 20 2.1k 1.2× 667 0.7× 316 0.4× 272 0.6× 179 0.4× 90 2.7k
Zizhang Sheng United States 28 2.2k 1.2× 1.0k 1.1× 317 0.4× 725 1.5× 491 1.2× 61 3.8k
Mirko Cortese Germany 23 2.0k 1.2× 971 1.0× 235 0.3× 424 0.9× 133 0.3× 43 3.5k
Yongfei Cai United States 20 2.2k 1.2× 1.2k 1.3× 135 0.2× 309 0.6× 299 0.7× 30 2.9k

Countries citing papers authored by Hanqin Peng

Since Specialization
Citations

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

Fields of papers citing papers by Hanqin Peng

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Hanqin Peng

This figure shows the co-authorship network connecting the top 25 collaborators of Hanqin Peng. A scholar is included among the top collaborators of Hanqin Peng 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 Hanqin Peng. Hanqin Peng 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.
Shi, Wei, Hanqin Peng, Sophia Rits‐Volloch, et al.. (2025). Effect of the S2’ site cleavage on SARS-CoV-2 spike. Nature Communications. 16(1). 11675–11675.
2.
Shi, Wei, Yongfei Cai, Haisun Zhu, et al.. (2023). Cryo-EM structure of SARS-CoV-2 postfusion spike in membrane. Nature. 619(7969). 403–409. 55 indexed citations
3.
Lavine, Christy L., Weichun Tang, Shaowei Wang, et al.. (2023). Antibody‐mediated SARS‐CoV ‐2 entry in cultured cells. EMBO Reports. 24(12). e57724–e57724. 6 indexed citations
4.
Zhang, Jun, Yongfei Cai, Christy L. Lavine, et al.. (2022). Structural and functional impact by SARS-CoV-2 Omicron spike mutations. Cell Reports. 39(4). 110729–110729. 97 indexed citations
5.
Zhang, Jun, Yongfei Cai, Tianshu Xiao, et al.. (2021). Structural impact on SARS-CoV-2 spike protein by D614G substitution. Science. 372(6541). 525–530. 270 indexed citations breakdown →
6.
Cai, Yongfei, Jun Zhang, Tianshu Xiao, et al.. (2021). Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants. Science. 373(6555). 642–648. 154 indexed citations
7.
Zhang, Jun, Tianshu Xiao, Yongfei Cai, et al.. (2021). Membrane fusion and immune evasion by the spike protein of SARS-CoV-2 Delta variant. Science. 374(6573). 1353–1360. 190 indexed citations breakdown →
8.
Xiao, Tianshu, Jianming Lü, Jun Zhang, et al.. (2021). A trimeric human angiotensin-converting enzyme 2 as an anti-SARS-CoV-2 agent. Nature Structural & Molecular Biology. 28(2). 202–209. 88 indexed citations
9.
Cai, Yongfei, Jun Zhang, Tianshu Xiao, et al.. (2020). Distinct conformational states of SARS-CoV-2 spike protein. Science. 369(6511). 1586–1592. 765 indexed citations breakdown →
10.
Piai, Alessandro, Qingshan Fu, Yongfei Cai, et al.. (2020). Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein. Nature Communications. 11(1). 2317–2317. 33 indexed citations
11.
Pan, Junhua, Hanqin Peng, Bing Chen, & Stephen C. Harrison. (2020). Cryo-EM Structure of Full-length HIV-1 Env Bound With the Fab of Antibody PG16. Journal of Molecular Biology. 432(4). 1158–1168. 41 indexed citations
12.
Shaik, Md Munan, Hanqin Peng, Jianming Lü, et al.. (2018). Structural basis of coreceptor recognition by HIV-1 envelope spike. Nature. 565(7739). 318–323. 147 indexed citations
13.
Fu, Qingshan, Md Munan Shaik, Yongfei Cai, et al.. (2018). Structure of the membrane proximal external region of HIV-1 envelope glycoprotein. Proceedings of the National Academy of Sciences. 115(38). E8892–E8899. 62 indexed citations
14.
Chen, Jia, James M. Kovacs, Hanqin Peng, et al.. (2015). Effect of the cytoplasmic domain on antigenic characteristics of HIV-1 envelope glycoprotein. Science. 349(6244). 191–195. 96 indexed citations
15.
Kovacs, James M., et al.. (2014). Stable, uncleaved HIV-1 envelope glycoprotein gp140 forms a tightly folded trimer with a native-like structure. Proceedings of the National Academy of Sciences. 111(52). 18542–18547. 52 indexed citations
16.
Chen, Jia, Gary Frey, Hanqin Peng, et al.. (2013). Mechanism of HIV-1 Neutralization by Antibodies Targeting a Membrane-Proximal Region of gp41. Journal of Virology. 88(2). 1249–1258. 81 indexed citations
17.
Kovacs, James M., Joseph P. Nkolola, Hanqin Peng, et al.. (2012). HIV-1 envelope trimer elicits more potent neutralizing antibody responses than monomeric gp120. Proceedings of the National Academy of Sciences. 109(30). 12111–12116. 136 indexed citations
18.
Peng, Hanqin, et al.. (2012). HIV-1 envelope trimer elicits higher neutralizing antibody responses than monomeric gp120. Retrovirology. 9(S2). 2 indexed citations
19.
Nkolola, Joseph P., Hanqin Peng, Ethan C. Settembre, et al.. (2010). Breadth of Neutralizing Antibodies Elicited by Stable, Homogeneous Clade A and Clade C HIV-1 gp140 Envelope Trimers in Guinea Pigs. Journal of Virology. 84(7). 3270–3279. 74 indexed citations
20.
Frey, Gary, Hanqin Peng, Sophia Rits‐Volloch, et al.. (2008). A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodies. Proceedings of the National Academy of Sciences. 105(10). 3739–3744. 189 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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