Qingping Xu

4.4k total citations
38 papers, 1.4k citations indexed

About

Qingping Xu is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, Qingping Xu has authored 38 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 34 papers in Molecular Biology, 17 papers in Materials Chemistry and 9 papers in Genetics. Recurrent topics in Qingping Xu's work include Enzyme Structure and Function (17 papers), Bacterial Genetics and Biotechnology (9 papers) and Biochemical and Molecular Research (8 papers). Qingping Xu is often cited by papers focused on Enzyme Structure and Function (17 papers), Bacterial Genetics and Biotechnology (9 papers) and Biochemical and Molecular Research (8 papers). Qingping Xu collaborates with scholars based in United States, United Kingdom and China. Qingping Xu's co-authors include Ann H. West, Ashley M. Deacon, Ann Stock, Paul N. Goudreau, Snežana Djordjević, Marc‐André Elsliger, Ian A. Wilson, Scott A. Lesley, Gye Won Han and Raymond C. Stevens and has published in prestigious journals such as Nature, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Qingping Xu

38 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Qingping Xu United States 20 1.1k 291 291 135 123 38 1.4k
Maya Palnitkar United States 9 715 0.7× 157 0.5× 320 1.1× 87 0.6× 49 0.4× 9 1.3k
Theresa M. Kelly United States 16 564 0.5× 66 0.2× 202 0.7× 86 0.6× 66 0.5× 23 1.1k
J. Van Beeumen Belgium 19 811 0.8× 171 0.6× 184 0.6× 115 0.9× 45 0.4× 39 1.6k
Florence Vincent France 23 894 0.8× 273 0.9× 192 0.7× 142 1.1× 52 0.4× 47 1.8k
Joanna Betts United Kingdom 26 1.9k 1.8× 211 0.7× 416 1.4× 137 1.0× 240 2.0× 37 3.9k
Marie‐France Giraud France 25 1.6k 1.5× 60 0.2× 108 0.4× 300 2.2× 49 0.4× 53 2.0k
Adam J. Kuszak United States 16 1.0k 1.0× 258 0.9× 351 1.2× 65 0.5× 29 0.2× 38 1.4k
Erik Chorell Sweden 23 1.2k 1.1× 82 0.3× 165 0.6× 146 1.1× 43 0.3× 55 1.9k
Kazuaki Kitano Japan 16 764 0.7× 67 0.2× 170 0.6× 60 0.4× 230 1.9× 53 1.3k
Oliver Hofnagel Germany 23 826 0.8× 85 0.3× 151 0.5× 34 0.3× 42 0.3× 36 1.6k

Countries citing papers authored by Qingping Xu

Since Specialization
Citations

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

Fields of papers citing papers by Qingping Xu

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Qingping Xu

This figure shows the co-authorship network connecting the top 25 collaborators of Qingping Xu. A scholar is included among the top collaborators of Qingping Xu 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 Qingping Xu. Qingping Xu 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.
Selim, Khaled A., et al.. (2021). The exo-β-N-acetylmuramidase NamZ from Bacillus subtilis is the founding member of a family of exo-lytic peptidoglycan hexosaminidases. Journal of Biological Chemistry. 296. 100519–100519. 13 indexed citations
2.
Shao, Zhenhua, Wei Yan, Karen Chapman, et al.. (2019). Structure of an allosteric modulator bound to the CB1 cannabinoid receptor. Nature Chemical Biology. 15(12). 1199–1205. 135 indexed citations
3.
Pal, Kuntal, Abhishek Bandyopadhyay, X. Edward Zhou, et al.. (2017). Structural Basis of TPR-Mediated Oligomerization and Activation of Oncogenic Fusion Kinases. Structure. 25(6). 867–877.e3. 18 indexed citations
4.
Horowitz, Scott, Loïc Salmon, Philipp Koldewey, et al.. (2016). Visualizing chaperone-assisted protein folding. Nature Structural & Molecular Biology. 23(7). 691–697. 43 indexed citations
5.
Xu, Qingping, Marc C. Deller, Tine Nielsen, et al.. (2014). Structural Insights into the Recognition of Phosphopeptide by the FHA Domain of Kanadaptin. PLoS ONE. 9(9). e107309–e107309. 8 indexed citations
6.
Rigden, Daniel J., Ruth Y. Eberhardt, Harry J. Gilbert, et al.. (2014). Structure- and context-based analysis of the GxGYxYP family reveals a new putative class of Glycoside Hydrolase. BMC Bioinformatics. 15(1). 196–196. 9 indexed citations
7.
Xu, Qingping, Dominique Mengin‐Lecreulx, Delphine Patin, et al.. (2014). Structure-Guided Functional Characterization of DUF1460 Reveals a Highly Specific NlpC/P60 Amidase Family. Structure. 22(12). 1799–1809. 11 indexed citations
8.
Childers, W. Seth, Qingping Xu, Thomas H. Mann, et al.. (2014). Cell Fate Regulation Governed by a Repurposed Bacterial Histidine Kinase. PLoS Biology. 12(10). e1001979–e1001979. 52 indexed citations
9.
Blair, Jimmy A., Qingping Xu, W. Seth Childers, et al.. (2013). Branched Signal Wiring of an Essential Bacterial Cell-Cycle Phosphotransfer Protein. Structure. 21(9). 1590–1601. 20 indexed citations
10.
Xu, Qingping, Hsiu‐Ju Chiu, Carol L. Farr, et al.. (2013). Structures of a Bifunctional Cell Wall Hydrolase CwlT Containing a Novel Bacterial Lysozyme and an NlpC/P60 dl-Endopeptidase. Journal of Molecular Biology. 426(1). 169–184. 23 indexed citations
11.
Levisson, Mark, Gye Won Han, Marc C. Deller, et al.. (2012). Functional and structural characterization of a thermostable acetyl esterase from Thermotoga maritima. Proteins Structure Function and Bioinformatics. 80(6). 1545–1559. 44 indexed citations
12.
Xu, Qingping, Beat Christen, Hsiu‐Ju Chiu, et al.. (2011). Structure of the pilus assembly protein TadZ from Eubacterium rectale: implications for polar localization. Molecular Microbiology. 83(4). 712–727. 23 indexed citations
13.
Bedem, Henry van den, Guenter Wolf, Qingping Xu, & Ashley M. Deacon. (2011). Distributed structure determination at the JCSG. Acta Crystallographica Section D Biological Crystallography. 67(4). 368–375. 20 indexed citations
14.
Xu, Qingping, Neil D. Rawlings, Carol L. Farr, et al.. (2011). Structural and Sequence Analysis of Imelysin-Like Proteins Implicated in Bacterial Iron Uptake. PLoS ONE. 6(7). e21875–e21875. 17 indexed citations
15.
Han, Gye Won, Jaeju Ko, Carol L. Farr, et al.. (2011). Crystal structure of a metal‐dependent phosphoesterase (YP_910028.1) from Bifidobacterium adolescentis: Computational prediction and experimental validation of phosphoesterase activity. Proteins Structure Function and Bioinformatics. 79(7). 2146–2160. 13 indexed citations
16.
Matsumoto, Yasuhiko, Qingping Xu, Shinya Miyazaki, et al.. (2010). Structure of a Virulence Regulatory Factor CvfB Reveals a Novel Winged Helix RNA Binding Module. Structure. 18(4). 537–547. 19 indexed citations
17.
18.
Xu, Qingping, et al.. (2003). Ssk1p Response Regulator Binding Surface on Histidine- Containing Phosphotransfer Protein Ypd1p. Eukaryotic Cell. 2(1). 27–33. 19 indexed citations
19.
Xu, Qingping, et al.. (2003). The Yeast YPD1/SLN1 Complex. Structure. 11(12). 1569–1581. 59 indexed citations
20.
Xu, Qingping, et al.. (1999). Purification, crystallization and preliminary X-ray diffraction analysis of the yeast phosphorelay protein YPD1. Acta Crystallographica Section D Biological Crystallography. 55(1). 291–293. 11 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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