Yao Cong

4.9k total citations
68 papers, 3.2k citations indexed

About

Yao Cong is a scholar working on Molecular Biology, Materials Chemistry and Infectious Diseases. According to data from OpenAlex, Yao Cong has authored 68 papers receiving a total of 3.2k indexed citations (citations by other indexed papers that have themselves been cited), including 51 papers in Molecular Biology, 18 papers in Materials Chemistry and 12 papers in Infectious Diseases. Recurrent topics in Yao Cong's work include Enzyme Structure and Function (17 papers), Heat shock proteins research (13 papers) and Protein Structure and Dynamics (12 papers). Yao Cong is often cited by papers focused on Enzyme Structure and Function (17 papers), Heat shock proteins research (13 papers) and Protein Structure and Dynamics (12 papers). Yao Cong collaborates with scholars based in China, United States and Germany. Yao Cong's co-authors include Wah Chiu, Steven J. Ludtke, Yifan Wang, Zhong Huang, Liangliang Kong, Yanxing Wang, Caixuan Liu, Cong Xu, Chao Zhang and Judith Frydman and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Yao Cong

66 papers receiving 3.1k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Yao Cong China	30	2.2k	742	430	265	251	68	3.2k
Swati Jain United States	18	2.9k 1.3×	467 0.6×	552 1.3×	270 1.0×	144 0.6×	60	4.2k
Björn Forsberg Sweden	13	3.2k 1.4×	390 0.5×	425 1.0×	376 1.4×	185 0.7×	18	4.8k
Meitian Wang Switzerland	39	2.0k 0.9×	931 1.3×	1.1k 2.5×	82 0.3×	320 1.3×	129	4.1k
Billy K. Poon United States	16	2.7k 1.2×	293 0.4×	833 1.9×	323 1.2×	133 0.5×	31	3.7k
Bradley J. Hintze United States	10	2.2k 1.0×	287 0.4×	473 1.1×	189 0.7×	91 0.4×	22	3.2k
Oleg V. Sobolev Germany	21	2.7k 1.2×	314 0.4×	860 2.0×	330 1.2×	138 0.5×	60	4.4k
Joel Quispe United States	23	2.5k 1.1×	854 1.2×	390 0.9×	186 0.7×	98 0.4×	43	3.9k
Lizbeth L. Videau United States	5	2.0k 0.9×	277 0.4×	448 1.0×	190 0.7×	89 0.4×	6	2.9k
L.N. Deis United States	5	2.0k 0.9×	290 0.4×	430 1.0×	185 0.7×	88 0.4×	5	2.9k
Alexis Rohou United States	18	3.8k 1.7×	392 0.5×	453 1.1×	398 1.5×	271 1.1×	27	5.4k

Countries citing papers authored by Yao Cong

Since Specialization

Citations

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

Fields of papers citing papers by Yao Cong

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Yao Cong

This figure shows the co-authorship network connecting the top 25 collaborators of Yao Cong. A scholar is included among the top collaborators of Yao Cong 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 Yao Cong. Yao Cong 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

Jin, Mingliang, Yunxiang Zang, Huping Wang, & Yao Cong. (2024). The conformational landscape of TRiC ring-opening and its underlying stepwise mechanism revealed by cryo-EM. SHILAP Revista de lepidopterología. 6. e7–e7. 1 indexed citations

Tan, Yangxia, Shiyan Zhang, Yonglei Zhang, et al.. (2024). Cryo-EM structure of PML RBCC dimer reveals CC-mediated octopus-like nuclear body assembly mechanism. Cell Discovery. 10(1). 118–118. 1 indexed citations

Liu, Caixuan, Mingliang Jin, Shutian Wang, et al.. (2023). Pathway and mechanism of tubulin folding mediated by TRiC/CCT along its ATPase cycle revealed using cryo-EM. Communications Biology. 6(1). 531–531. 13 indexed citations

Zhao, Qiaoyu, Yifan Wang, Wenyu Han, et al.. (2023). Structural insights into constitutive activity of 5-HT ₆ receptor. Proceedings of the National Academy of Sciences. 120(14). e2209917120–e2209917120. 9 indexed citations

Qin, Hong, Wenyu Han, Jiawei Li, et al.. (2022). Molecular basis of receptor binding and antibody neutralization of Omicron. Nature. 604(7906). 546–552. 116 indexed citations

Wang, Yifan, Caixuan Liu, Chao Zhang, et al.. (2022). Structural basis for SARS-CoV-2 Delta variant recognition of ACE2 receptor and broadly neutralizing antibodies. Nature Communications. 13(1). 871–871. 117 indexed citations

Zheng, Wei, Zhanyu Ding, Hao Liu, et al.. (2021). Distinct architecture and composition of mouse axonemal radial spoke head revealed by cryo-EM. Proceedings of the National Academy of Sciences. 118(4). 20 indexed citations

Sahu, Indrajit, Sachitanand M. Mali, Prasad Sulkshane, et al.. (2021). The 20S as a stand-alone proteasome in cells can degrade the ubiquitin tag. Nature Communications. 12(1). 6173–6173. 94 indexed citations

Wang, Yifan, Cong Xu, Yanxing Wang, et al.. (2021). Conformational dynamics of the Beta and Kappa SARS-CoV-2 spike proteins and their complexes with ACE2 receptor revealed by cryo-EM. Nature Communications. 12(1). 7345–7345. 66 indexed citations

10.

Wang, Ning, Yifan Wang, Qian Zhao, et al.. (2021). The cryo-EM structure of the chloroplast ClpP complex. Nature Plants. 7(11). 1505–1515. 6 indexed citations

11.

Zhang, Xiang, Xuan Zhou, Jialin Fan, et al.. (2021). Cryo-EM study of patched in lipid nanodisc suggests a structural basis for its clustering in caveolae. Structure. 29(11). 1286–1294.e6. 6 indexed citations

12.

Zhang, Chao, Cong Xu, Yifan Wang, et al.. (2021). Functional and structural characterization of a two-MAb cocktail for delayed treatment of enterovirus D68 infections. Nature Communications. 12(1). 2904–2904. 26 indexed citations

13.

Xu, Cong, Yanxing Wang, Caixuan Liu, et al.. (2020). Conformational dynamics of SARS-CoV-2 trimeric spike glycoprotein in complex with receptor ACE2 revealed by cryo-EM. Science Advances. 7(1). 262 indexed citations

14.

Zhao, Qian, Xiang Zhang, Frederik Sommer, et al.. (2019). Hetero‐oligomeric CPN60 resembles highly symmetric group‐I chaperonin structure revealed by Cryo‐EM. The Plant Journal. 98(5). 798–812. 9 indexed citations

15.

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

16.

Wu, Zhongshan, Zhicheng Cui, Hao Cheng, et al.. (2015). High yield and efficient expression and purification of the human 5-HT3A receptor. Acta Pharmacologica Sinica. 36(8). 1024–1032. 5 indexed citations

17.

Zhang, Qinfen, Xinghong Dai, Yao Cong, et al.. (2013). Cryo-EM Structure of a Molluscan Hemocyanin Suggests Its Allosteric Mechanism. Structure. 21(4). 604–613. 30 indexed citations

18.

Feng, Miao, Zhanyu Ding, Liang Xu, et al.. (2012). Structural and biochemical studies of RIG-I antiviral signaling. Protein & Cell. 4(2). 142–154. 21 indexed citations

19.

Cong, Yao, Matthew L. Baker, Joanita Jakana, et al.. (2010). 4.0-Å resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement. Proceedings of the National Academy of Sciences. 107(11). 4967–4972. 139 indexed citations

20.

Booth, Christopher R., Anne S. Meyer, Yao Cong, et al.. (2008). Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT. Nature Structural & Molecular Biology. 15(7). 746–753. 71 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.

Explore authors with similar magnitude of impact