Jingpeng Ge

1.2k total citations
14 papers, 869 citations indexed

About

Jingpeng Ge is a scholar working on Molecular Biology, Public Health, Environmental and Occupational Health and Infectious Diseases. According to data from OpenAlex, Jingpeng Ge has authored 14 papers receiving a total of 869 indexed citations (citations by other indexed papers that have themselves been cited), including 9 papers in Molecular Biology, 3 papers in Public Health, Environmental and Occupational Health and 2 papers in Infectious Diseases. Recurrent topics in Jingpeng Ge's work include Ion channel regulation and function (4 papers), Hearing, Cochlea, Tinnitus, Genetics (2 papers) and Blood properties and coagulation (2 papers). Jingpeng Ge is often cited by papers focused on Ion channel regulation and function (4 papers), Hearing, Cochlea, Tinnitus, Genetics (2 papers) and Blood properties and coagulation (2 papers). Jingpeng Ge collaborates with scholars based in China, United States and Canada. Jingpeng Ge's co-authors include Maojun Yang, Ning Gao, Qiancheng Zhao, Wanqiu Li, Ningning Li, Bailong Xiao, Jie Yu, Johannes Elferich, Eric Gouaux and Yue Feng and has published in prestigious journals such as Nature, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Jingpeng Ge

14 papers receiving 862 citations

Peers

Jingpeng Ge
Marco Lolicato United States
Janet E. McCombs United States
Ana M. Rossi United Kingdom
Zhu Fu United States
Héctor Rojas Venezuela
Jonas Protze Germany
Marie M. Phelan United Kingdom
Jun Liao China
Marco Lolicato United States
Jingpeng Ge
Citations per year, relative to Jingpeng Ge Jingpeng Ge (= 1×) peers Marco Lolicato

Countries citing papers authored by Jingpeng Ge

Since Specialization
Citations

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

Fields of papers citing papers by Jingpeng Ge

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Jingpeng Ge

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

All Works

14 of 14 papers shown
1.
Ning, Yingjie, Zheng‐Jiang Zhu, Xuefang Pan, et al.. (2024). Structure and mechanism of lysosome transmembrane acetylation by HGSNAT. Nature Structural & Molecular Biology. 31(10). 1502–1508. 4 indexed citations
2.
Ge, Jingpeng, Johannes Elferich, Sepehr Dehghani‐Ghahnaviyeh, et al.. (2021). Molecular mechanism of prestin electromotive signal amplification. Cell. 184(18). 4669–4679.e13. 62 indexed citations
3.
Ge, Jingpeng, Johannes Elferich, April Goehring, et al.. (2018). Structure of mouse protocadherin 15 of the stereocilia tip link in complex with LHFPL5. eLife. 7. 57 indexed citations
4.
Yang, Yiqing, You Yu, Xiaolu Li, et al.. (2017). Target Elucidation by Cocrystal Structures of NADH-Ubiquinone Oxidoreductase of Plasmodium falciparum (PfNDH2) with Small Molecule To Eliminate Drug-Resistant Malaria. Journal of Medicinal Chemistry. 60(5). 1994–2005. 64 indexed citations
5.
Yu, Jie, Bing Zhang, Yixiao Zhang, et al.. (2017). A binding-block ion selective mechanism revealed by a Na/K selective channel. Protein & Cell. 9(7). 629–639. 16 indexed citations
6.
Ge, Jingpeng, Wanqiu Li, Qiancheng Zhao, et al.. (2015). Architecture of the mammalian mechanosensitive Piezo1 channel. Nature. 527(7576). 64–69. 372 indexed citations
7.
Wu, Meng, Wei Zhuo, Jinke Gu, et al.. (2015). Crystal structures of Bbp from Staphylococcus aureus reveal the ligand binding mechanism with Fibrinogen α. Protein & Cell. 6(10). 757–766. 13 indexed citations
8.
Yu, Jie, Jingpeng Ge, Johanna Heuveling, Erwin Schneider, & Maojun Yang. (2015). Structural basis for substrate specificity of an amino acid ABC transporter. Proceedings of the National Academy of Sciences. 112(16). 5243–5248. 48 indexed citations
9.
Yu, Jie, Yaya Pian, Jingpeng Ge, et al.. (2015). Functional and Structural Characterization of the Antiphagocytic Properties of a Novel Transglutaminase from Streptococcus suis. Journal of Biological Chemistry. 290(31). 19081–19092. 26 indexed citations
10.
Zhang, Yi, Jingpeng Ge, Yang Li, et al.. (2013). Structural Insight into Caenorhabditis elegans Sex-determining Protein FEM-2*. Journal of Biological Chemistry. 288(30). 22058–22066. 13 indexed citations
12.
Li, Xiaolu, Wei Zhuo, Jie Yu, et al.. (2013). Structure of the nucleotide-binding domain of a dipeptide ABC transporter reveals a novel iron–sulfur cluster-binding domain. Acta Crystallographica Section D Biological Crystallography. 69(2). 256–265. 11 indexed citations
13.
Zhang, Xiaozhe, Jingjing Wang, Yue Feng, et al.. (2012). Structure and molecular mechanism of an anion-selective mechanosensitive channel of small conductance. Proceedings of the National Academy of Sciences. 109(44). 18180–18185. 49 indexed citations
14.
Feng, Yue, Wenfei Li, Jian Li, et al.. (2012). Structural insight into the type-II mitochondrial NADH dehydrogenases. Nature. 491(7424). 478–482. 103 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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