Zheng‐Qing Fu

520 total citations
22 papers, 398 citations indexed

About

Zheng‐Qing Fu is a scholar working on Molecular Biology, Materials Chemistry and Immunology. According to data from OpenAlex, Zheng‐Qing Fu has authored 22 papers receiving a total of 398 indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 6 papers in Materials Chemistry and 4 papers in Immunology. Recurrent topics in Zheng‐Qing Fu's work include Enzyme Structure and Function (5 papers), Protein Structure and Dynamics (4 papers) and X-ray Diffraction in Crystallography (3 papers). Zheng‐Qing Fu is often cited by papers focused on Enzyme Structure and Function (5 papers), Protein Structure and Dynamics (4 papers) and X-ray Diffraction in Crystallography (3 papers). Zheng‐Qing Fu collaborates with scholars based in United States, China and Germany. Zheng‐Qing Fu's co-authors include Bingdong Sha, Zhongmin Jin, Xiaoqiang Wang, Zhiqiang Pan, Zhenzhan Chang, Lenong Li, Jingzhi Li, Yunkun Wu, Irene T. Weber and Robert W. Harrison and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

Zheng‐Qing Fu

22 papers receiving 396 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Zheng‐Qing Fu United States 11 273 79 48 36 27 22 398
Minghui Wang China 14 244 0.9× 55 0.7× 42 0.9× 23 0.6× 21 0.8× 33 507
Hans‐Georg Beisel Germany 9 225 0.8× 180 2.3× 99 2.1× 33 0.9× 7 0.3× 11 516
Katharine A. Winans United States 9 651 2.4× 88 1.1× 27 0.6× 19 0.5× 28 1.0× 10 786
Luisa Tonella Switzerland 11 477 1.7× 29 0.4× 58 1.2× 25 0.7× 16 0.6× 13 677
Xue Yu China 14 168 0.6× 44 0.6× 60 1.3× 23 0.6× 23 0.9× 34 416
Alain R. Bernard United Kingdom 13 275 1.0× 55 0.7× 43 0.9× 22 0.6× 26 1.0× 17 390
В. Н. Зайцев United Kingdom 8 217 0.8× 126 1.6× 62 1.3× 90 2.5× 71 2.6× 19 638
Helga Wessner Germany 11 378 1.4× 82 1.0× 38 0.8× 9 0.3× 16 0.6× 20 532
Eszter Boros Hungary 7 214 0.8× 115 1.5× 26 0.5× 8 0.2× 26 1.0× 11 414
Geoffrey Allen United Kingdom 11 385 1.4× 137 1.7× 28 0.6× 16 0.4× 23 0.9× 15 592

Countries citing papers authored by Zheng‐Qing Fu

Since Specialization
Citations

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

Fields of papers citing papers by Zheng‐Qing Fu

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Zheng‐Qing Fu. 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 Zheng‐Qing Fu. The network helps show where Zheng‐Qing Fu may publish in the future.

Co-authorship network of co-authors of Zheng‐Qing Fu

This figure shows the co-authorship network connecting the top 25 collaborators of Zheng‐Qing Fu. A scholar is included among the top collaborators of Zheng‐Qing Fu 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 Zheng‐Qing Fu. Zheng‐Qing Fu 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.
Mishra, Nitin, Timothy J. Herdendorf, Michal Hammel, et al.. (2024). S. aureus Eap is a polyvalent inhibitor of neutrophil serine proteases. Journal of Biological Chemistry. 300(9). 107627–107627. 2 indexed citations
2.
Thompson, Stephen, et al.. (2023). Methods for Viewing Plant Stomata Responses. The American Biology Teacher. 85(1). 33–37. 2 indexed citations
3.
Sun, Lifang, et al.. (2016). Crystal Structure of Major Envelope Protein VP24 from White Spot Syndrome Virus. Scientific Reports. 6(1). 32309–32309. 16 indexed citations
4.
Mohan, Rajinikanth, et al.. (2016). Overexpression of Arabidopsis NIMIN1 results in salicylate intolerance. Plant Signaling & Behavior. 11(10). e1211222–e1211222. 5 indexed citations
5.
Zhu, J., Zheng‐Qing Fu, Lirong Chen, et al.. (2012). Structure of theArchaeoglobus fulgidusorphan ORF AF1382 determined by sulfur SAD from a moderately diffracting crystal. Acta Crystallographica Section D Biological Crystallography. 68(9). 1242–1252. 5 indexed citations
6.
Garcia, Brandon L., Brady J. Summers, Zhuoer Lin, et al.. (2011). Diversity in the C3b Convertase Contact Residues and Tertiary Structures of the Staphylococcal Complement Inhibitor (SCIN) Protein Family. Journal of Biological Chemistry. 287(1). 628–640. 23 indexed citations
7.
Li, Jingzhi, et al.. (2011). Membrane Binding Mechanism of Yeast Mitochondrial Peripheral Membrane Protzein TIM44. Protein and Peptide Letters. 18(7). 718–725. 5 indexed citations
8.
Fu, Zheng‐Qing, et al.. (2011). The Crystal Structure Analysis of Group B Streptococcus Sortase C1: A Model for the “Lid” Movement upon Substrate Binding. Journal of Molecular Biology. 414(4). 563–577. 20 indexed citations
9.
Li, Jingzhi, et al.. (2009). Preliminary X-ray crystallographic studies of yeast Get3. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65(5). 489–491. 1 indexed citations
10.
Wu, Yunkun, et al.. (2008). The crystal structure of the putative peptide-binding fragment from the human Hsp40 protein Hdj1. BMC Structural Biology. 8(1). 3–3. 29 indexed citations
11.
Li, Lenong, Zhenzhan Chang, Zhiqiang Pan, Zheng‐Qing Fu, & Xiaoqiang Wang. (2008). Modes of heme binding and substrate access for cytochrome P450 CYP74A revealed by crystal structures of allene oxide synthase. Proceedings of the National Academy of Sciences. 105(37). 13883–13888. 85 indexed citations
12.
Fu, Zheng‐Qing, et al.. (2007). A parallel program usingSHELXDfor quick heavy-atom partial structural solution on high-performance computers. Journal of Applied Crystallography. 40(2). 387–390. 3 indexed citations
13.
Das, Amaresh, Zheng‐Qing Fu, W. Tempel, et al.. (2007). Characterization of a corrinoid protein involved in the C1 metabolism of strict anaerobic bacterium Moorella thermoacetica. Proteins Structure Function and Bioinformatics. 67(1). 167–176. 30 indexed citations
14.
Jin, Zhongmin, et al.. (2006). Crystal Structure of Yeast Mitochondrial Peripheral Membrane Protein Tim44p C-terminal Domain. Journal of Molecular Biology. 359(3). 798–804. 28 indexed citations
15.
Wu, Yunkun, Jingzhi Li, Zhongmin Jin, Zheng‐Qing Fu, & Bingdong Sha. (2004). The Crystal Structure of the C-terminal Fragment of Yeast Hsp40 Ydj1 Reveals Novel Dimerization Motif for Hsp40. Journal of Molecular Biology. 346(4). 1005–1011. 47 indexed citations
16.
Fu, Zheng‐Qing, John P. Rose, & Bi‐Cheng Wang. (2004). Monitoring the anomalous scattering signal and noise levels in X-ray diffraction of crystals. Acta Crystallographica Section D Biological Crystallography. 60(3). 499–506. 5 indexed citations
17.
Fu, Zheng‐Qing, et al.. (1999). Improving the diffraction quality of MTCP-1 crystals by post-crystallization soaking. Acta Crystallographica Section D Biological Crystallography. 55(1). 5–7. 4 indexed citations
18.
Reed, Charles C., Zheng‐Qing Fu, Juan Wu, et al.. (1997). Crystal structure of TNF-alpha mutant R31D with greater affinity for receptor R1 compared with R2. Protein Engineering Design and Selection. 10(10). 1101–1107. 41 indexed citations
19.
Fu, Zheng‐Qing & Huayu Fan. (1997). A computer program to derive (3+1)-dimensional symmetry operations from two-line symbols. Journal of Applied Crystallography. 30(1). 73–78. 4 indexed citations
20.
Fu, Zheng‐Qing, Robert W. Harrison, Charles C. Reed, et al.. (1995). Model complexes of tumor necrosis factor-α with receptors Rl and R2. Protein Engineering Design and Selection. 8(12). 1233–1241. 10 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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