Lujun Liang

1.3k total citations
33 papers, 957 citations indexed

About

Lujun Liang is a scholar working on Molecular Biology, Oncology and Organic Chemistry. According to data from OpenAlex, Lujun Liang has authored 33 papers receiving a total of 957 indexed citations (citations by other indexed papers that have themselves been cited), including 29 papers in Molecular Biology, 13 papers in Oncology and 7 papers in Organic Chemistry. Recurrent topics in Lujun Liang's work include Ubiquitin and proteasome pathways (22 papers), Protein Degradation and Inhibitors (12 papers) and Peptidase Inhibition and Analysis (12 papers). Lujun Liang is often cited by papers focused on Ubiquitin and proteasome pathways (22 papers), Protein Degradation and Inhibitors (12 papers) and Peptidase Inhibition and Analysis (12 papers). Lujun Liang collaborates with scholars based in China, United States and Canada. Lujun Liang's co-authors include Lei Liu, Qingyun Zheng, Man Pan, Huasong Ai, Ziqing Mei, Guo‐Chao Chu, Yi‐Ming Li, Shan Tang, Yanyan Si and Tian Wang and has published in prestigious journals such as Nature, Angewandte Chemie International Edition and Nature Communications.

In The Last Decade

Lujun Liang

32 papers receiving 942 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Lujun Liang China 17 739 360 235 39 36 33 957
Zhipeng A. Wang United States 14 589 0.8× 192 0.5× 162 0.7× 39 1.0× 14 0.4× 30 680
Gui‐in Lee United States 9 469 0.6× 202 0.6× 102 0.4× 29 0.7× 54 1.5× 10 600
V. Azzarito United Kingdom 7 696 0.9× 409 1.1× 97 0.4× 73 1.9× 11 0.3× 8 795
Balakumar Vijayakrishnan United Kingdom 13 373 0.5× 348 1.0× 147 0.6× 117 3.0× 17 0.5× 20 591
Lining Lu China 9 376 0.5× 127 0.4× 108 0.5× 20 0.5× 37 1.0× 14 462
Kiall F. Suazo United States 10 464 0.6× 195 0.5× 97 0.4× 87 2.2× 10 0.3× 23 626
Suttipong Suttapitugsakul United States 15 541 0.7× 128 0.4× 67 0.3× 68 1.7× 12 0.3× 27 665
Ctirad Hofr Czechia 18 848 1.1× 207 0.6× 289 1.2× 25 0.6× 98 2.7× 27 1.0k
Mark Ruppen United States 15 409 0.6× 188 0.5× 97 0.4× 26 0.7× 36 1.0× 20 666
Richard J. Spears United Kingdom 11 321 0.4× 287 0.8× 97 0.4× 101 2.6× 15 0.4× 22 450

Countries citing papers authored by Lujun Liang

Since Specialization
Citations

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

Fields of papers citing papers by Lujun Liang

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Lujun Liang

This figure shows the co-authorship network connecting the top 25 collaborators of Lujun Liang. A scholar is included among the top collaborators of Lujun Liang 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 Lujun Liang. Lujun Liang 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.
Deng, Xiangyu, Yan Cui, Xinyue Zhu, et al.. (2025). Superfast Protein Desulfurization Triggered by Low‐Energy Visible Light. Angewandte Chemie. 137(24).
2.
Wu, Xiangwei, Huasong Ai, Lujun Liang, et al.. (2025). Structural visualization of HECT-type E3 ligase Ufd4 accepting and transferring ubiquitin to form K29/K48-branched polyubiquitination. Nature Communications. 16(1). 4313–4313. 8 indexed citations
3.
Ai, Huasong, Zebin Tong, Zhiheng Deng, et al.. (2024). Mechanism of nucleosomal H2A K13/15 monoubiquitination and adjacent dual monoubiquitination by RNF168. Nature Chemical Biology. 21(5). 668–680. 13 indexed citations
4.
Tong, Zebin, Huasong Ai, Guo‐Chao Chu, et al.. (2024). Synovial sarcoma X breakpoint 1 protein uses a cryptic groove to selectively recognize H2AK119Ub nucleosomes. Nature Structural & Molecular Biology. 31(2). 300–310. 21 indexed citations
5.
Zhang, Liying, Zhiheng Deng, Zebin Tong, et al.. (2024). RAD18-catalysed formation of ubiquitination intermediate mimic of proliferating cell nuclear antigen PCNA. Bioorganic & Medicinal Chemistry. 117. 118016–118016. 4 indexed citations
6.
Li, Chuntong, Tian Wang, Lujun Liang, et al.. (2023). Simultaneous capture of ISG15 conjugating and deconjugating enzymes using a semi-synthetic ISG15-Dha probe. Science China Chemistry. 66(3). 837–844. 12 indexed citations
7.
Ai, Huasong, Zebin Tong, Zhiheng Deng, et al.. (2023). Synthetic E2-Ub-nucleosome conjugates for studying nucleosome ubiquitination. Chem. 9(5). 1221–1240. 40 indexed citations
8.
Zhou, Bo, Jing Lv, Mengya Zhu, et al.. (2023). Simulation study of a thin membrane inclined automatic wicking dew-point evaporative cooling device. Journal of Building Engineering. 72. 106601–106601. 8 indexed citations
9.
Ai, Huasong, Aijun Liu, Zixian Sun, et al.. (2022). H2B Lys34 Ubiquitination Induces Nucleosome Distortion to Stimulate Dot1L Activity. Nature Chemical Biology. 18(9). 972–980. 75 indexed citations
10.
Zuo, Chong, et al.. (2022). Chemical tools for E3 ubiquitin ligase study. Chinese Chemical Letters. 34(4). 107781–107781. 2 indexed citations
11.
Lu, Lining, Shuansuo Wang, Lijun Zhang, et al.. (2022). Met1-specific motifs conserved in OTUB subfamily of green plants enable rice OTUB1 to hydrolyse Met1 ubiquitin chains. Nature Communications. 13(1). 4672–4672. 59 indexed citations
12.
Wang, Tian, Chuntong Li, Meijing Wang, et al.. (2022). Expedient Synthesis of Ubiquitin‐like Protein ISG15 Tools through Chemo‐Enzymatic Ligation Catalyzed by a Viral Protease Lbpro. Angewandte Chemie International Edition. 61(40). e202206205–e202206205. 14 indexed citations
13.
Zheng, Qingyun, Tian Wang, Guo‐Chao Chu, et al.. (2022). A bifunctional molecule-assisted synthesis of mimics for use in probing the ubiquitination system. Nature Protocols. 18(2). 530–554. 16 indexed citations
14.
Pan, Man, Qingyun Zheng, Tian Wang, et al.. (2021). Structural insights into Ubr1-mediated N-degron polyubiquitination. Nature. 600(7888). 334–338. 86 indexed citations
15.
Sui, Xin, Yu Wang, Lujun Liang, et al.. (2020). Development and application of ubiquitin-based chemical probes. Chemical Science. 11(47). 12633–12646. 54 indexed citations
16.
Liang, Lujun, Yanyan Si, Shan Tang, et al.. (2018). Biochemical properties of K11,48-branched ubiquitin chains. Chinese Chemical Letters. 29(7). 1155–1159. 16 indexed citations
17.
Tang, Shan, Lujun Liang, Yanyan Si, et al.. (2017). Practical Chemical Synthesis of Atypical Ubiquitin Chains by Using an Isopeptide‐Linked Ub Isomer. Angewandte Chemie International Edition. 56(43). 13333–13337. 103 indexed citations
18.
Tang, Shan, Lujun Liang, Yanyan Si, et al.. (2017). Practical Chemical Synthesis of Atypical Ubiquitin Chains by Using an Isopeptide‐Linked Ub Isomer. Angewandte Chemie. 129(43). 13518–13522. 16 indexed citations
19.
Tan, Xianglong, Man Pan, Yong Zheng, et al.. (2017). Sortase-mediated chemical protein synthesis reveals the bidentate binding of bisphosphorylated p62 with K63 diubiquitin. Chemical Science. 8(10). 6881–6887. 27 indexed citations
20.
Zhang, Zhenqi, Chu‐Ting Yang, Lujun Liang, et al.. (2014). Copper-Catalyzed/Promoted Cross-coupling of gem-Diborylalkanes with Nonactivated Primary Alkyl Halides: An Alternative Route to Alkylboronic Esters. Organic Letters. 16(24). 6342–6345. 142 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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