Paul Thompson

872 total citations
22 papers, 660 citations indexed

About

Paul Thompson is a scholar working on Molecular Biology, Materials Chemistry and Ecology. According to data from OpenAlex, Paul Thompson has authored 22 papers receiving a total of 660 indexed citations (citations by other indexed papers that have themselves been cited), including 20 papers in Molecular Biology, 7 papers in Materials Chemistry and 6 papers in Ecology. Recurrent topics in Paul Thompson's work include Enzyme Structure and Function (7 papers), Bacteriophages and microbial interactions (6 papers) and Protein Structure and Dynamics (5 papers). Paul Thompson is often cited by papers focused on Enzyme Structure and Function (7 papers), Bacteriophages and microbial interactions (6 papers) and Protein Structure and Dynamics (5 papers). Paul Thompson collaborates with scholars based in United Kingdom, Spain and United States. Paul Thompson's co-authors include Alastair R. Hawkins, Jakob Fuhrmann, Venkataraman Subramanian, Arnaud Baslé, Bernard Henrissat, Carl Morland, Eric C. Martens, Madhav P. Yadav, Artur Rogowski and Alison M. Day and has published in prestigious journals such as Journal of the American Chemical Society, Nucleic Acids Research and Journal of Biological Chemistry.

In The Last Decade

Paul Thompson

21 papers receiving 655 citations

Peers

Paul Thompson

Hong‐Hsiang Guan Taiwan

Folmer Fredslund Denmark

B. Pluvinage Canada

Maurien M. A. Olsthoorn Netherlands

Faping Duan United States

Juan M. Mesas Spain

Vu Van Loi Germany

Olga Fierro Italy

Young Jun An South Korea

Trevor S. Loo New Zealand

Hong‐Hsiang Guan Taiwan

Paul Thompson

354 ×0.8

93 ×0.6

80 ×0.7

87 ×0.8

39 ×0.4

Citations per year, relative to Paul Thompson Paul Thompson (= 1×) peers Hong‐Hsiang Guan

Countries citing papers authored by Paul Thompson

Since Specialization

Citations

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

Fields of papers citing papers by Paul Thompson

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Paul Thompson

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

All Works

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20 of 20 papers shown

Yu, Xin, Yujing Song, Tao Dong, et al.. (2025). Citrullination of NF‐κB p65 by PAD2 as a Novel Therapeutic Target for Modulating Macrophage Polarization in Acute Lung Injury. Advanced Science. 12(18). e2413253–e2413253. 3 indexed citations

Maneiro, Marı́a, Emilio Lence, José M. Otero, et al.. (2023). Quinate-based ligands for irreversible inactivation of the bacterial virulence factor DHQ1 enzyme—A molecular insight†. Frontiers in Molecular Biosciences. 10. 1111598–1111598.

Rostami, Nadia, Robert C. Shields, Jane L. Brittan, et al.. (2022). Interspecies competition in oral biofilms mediated by Streptococcus gordonii extracellular deoxyribonuclease SsnA. npj Biofilms and Microbiomes. 8(1). 96–96. 13 indexed citations

Lence, Emilio, Marı́a Maneiro, Mark J. van Raaij, et al.. (2020). Self‐Immolation of a Bacterial Dehydratase Enzyme by its Epoxide Product. Chemistry - A European Journal. 26(36). 8035–8044. 3 indexed citations

Lence, Emilio, et al.. (2019). Synthesis of rigidified shikimic acid derivatives by ring-closing metathesis to imprint inhibitor efficacy against shikimate kinase enzyme. Organic Chemistry Frontiers. 6(14). 2514–2528. 7 indexed citations

Maneiro, Marı́a, Emilio Lence, José M. Otero, et al.. (2019). Hydroxylammonium derivatives for selective active-site lysine modification in the anti-virulence bacterial target DHQ1 enzyme. Organic Chemistry Frontiers. 6(17). 3127–3135. 5 indexed citations

Convertino, Marino, et al.. (2017). Reducing the Flexibility of Type II Dehydroquinase for Inhibition: A Fragment‐Based Approach and Molecular Dynamics Study. ChemMedChem. 12(18). 1512–1524. 4 indexed citations

Baslé, Arnaud, Lorraine Hewitt, Alan Koh, et al.. (2017). Crystal structure of NucB, a biofilm-degrading endonuclease. Nucleic Acids Research. 46(1). 473–484. 20 indexed citations

Wilkinson, D., Antoine Désilets, Hua Lin, et al.. (2017). The serine proteinase hepsin is an activator of pro-matrix metalloproteinases: molecular mechanisms and implications for extracellular matrix turnover. Scientific Reports. 7(1). 16693–16693. 23 indexed citations

10.

Lence, Emilio, et al.. (2016). Freezing the Dynamic Gap for Selectivity: Motion‐Based Design of Inhibitors of the Shikimate Kinase Enzyme. Chemistry - A European Journal. 22(50). 17988–18000. 4 indexed citations

11.

Lence, Emilio, Juán A. Vallejo, Alejandro Beceiro, et al.. (2016). Study of the Phosphoryl‐Transfer Mechanism of Shikimate Kinase by NMR Spectroscopy. Chemistry - A European Journal. 22(8). 2758–2768. 13 indexed citations

12.

Lence, Emilio, Marı́a Maneiro, Juan Carlos Vázquez-Ucha, et al.. (2016). Targeting the Motion of Shikimate Kinase: Development of Competitive Inhibitors that Stabilize an Inactive Open Conformation of the Enzyme. Journal of Medicinal Chemistry. 59(11). 5471–5487. 17 indexed citations

13.

Fuhrmann, Jakob, Venkataraman Subramanian, Douglas J. Kojetin, & Paul Thompson. (2016). Activity-Based Profiling Reveals a Regulatory Link between Oxidative Stress and Protein Arginine Phosphorylation. Cell chemical biology. 23(8). 967–977. 32 indexed citations

14.

Rogowski, Artur, Jonathon A. Briggs, Jenny C. Mortimer, et al.. (2015). Glycan complexity dictates microbial resource allocation in the large intestine. Nature Communications. 6(1). 7481–7481. 321 indexed citations

15.

Fuhrmann, Jakob, Venkataraman Subramanian, & Paul Thompson. (2015). Synthesis and Use of a Phosphonate Amidine to Generate an Anti‐Phosphoarginine‐Specific Antibody. Angewandte Chemie International Edition. 54(49). 14715–14718. 36 indexed citations

16.

Maneiro, Marı́a, José M. Otero, Emilio Lence, et al.. (2014). Irreversible covalent modification of type I dehydroquinase with a stable Schiff base. Organic & Biomolecular Chemistry. 13(3). 706–716. 9 indexed citations

17.

Maneiro, Marı́a, Emilio Lence, José M. Otero, et al.. (2014). Insights into substrate binding and catalysis in bacterial type I dehydroquinase. Biochemical Journal. 462(3). 415–424. 8 indexed citations

18.

Johnson, Christopher, Paul Thompson, Jun-Yong Huang, et al.. (2010). The transcription repressor NmrA is subject to proteolysis by three Aspergillus nidulans proteases. Protein Science. 19(7). 1405–1419. 17 indexed citations

19.

Lamb, Heather K., Jingshan Ren, Alison Park, et al.. (2004). Modulation of the ligand binding properties of the transcription repressor NmrA by GATA‐containing DNA and site‐directed mutagenesis. Protein Science. 13(12). 3127–3138. 45 indexed citations

20.

Lamb, Heather K., Kris Leslie, Margaret Nutley, et al.. (2003). The Negative Transcriptional Regulator NmrA Discriminates between Oxidized and Reduced Dinucleotides. Journal of Biological Chemistry. 278(34). 32107–32114. 63 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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