James E. Pease

6.3k total citations
105 papers, 4.8k citations indexed

About

James E. Pease is a scholar working on Immunology, Oncology and Molecular Biology. According to data from OpenAlex, James E. Pease has authored 105 papers receiving a total of 4.8k indexed citations (citations by other indexed papers that have themselves been cited), including 73 papers in Immunology, 63 papers in Oncology and 27 papers in Molecular Biology. Recurrent topics in James E. Pease's work include Chemokine receptors and signaling (60 papers), T-cell and B-cell Immunology (27 papers) and Immune Cell Function and Interaction (21 papers). James E. Pease is often cited by papers focused on Chemokine receptors and signaling (60 papers), T-cell and B-cell Immunology (27 papers) and Immune Cell Function and Interaction (21 papers). James E. Pease collaborates with scholars based in United Kingdom, United States and Japan. James E. Pease's co-authors include Ian Sabroe, Richard Horuk, Timothy J. Williams, Philip M. Murphy, Timothy J. Williams, Georgina Xanthou, Roberto Solari, Emma L. Wise, Adam J. Byrne and Paul Ponath and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and The Journal of Experimental Medicine.

In The Last Decade

James E. Pease

103 papers receiving 4.7k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
James E. Pease United Kingdom 44 2.8k 1.8k 1.2k 924 430 105 4.8k
Dolores J. Schendel Germany 42 4.4k 1.6× 2.2k 1.2× 1.2k 1.0× 440 0.5× 514 1.2× 174 6.5k
T Hirano Japan 36 2.9k 1.0× 1.9k 1.1× 1.4k 1.1× 491 0.5× 522 1.2× 117 6.1k
Jean‐François Gauchat Canada 39 3.4k 1.2× 833 0.5× 1.1k 0.9× 834 0.9× 368 0.9× 95 5.4k
Fernando Bazán France 20 3.9k 1.4× 1.4k 0.8× 1.5k 1.2× 958 1.0× 193 0.4× 68 6.7k
Marinus C. Lamers Germany 28 3.8k 1.4× 794 0.4× 1.3k 1.0× 763 0.8× 693 1.6× 60 6.1k
Kuldeep Neote Canada 28 2.5k 0.9× 1.9k 1.0× 1.1k 0.9× 789 0.9× 179 0.4× 42 4.4k
Robert J. B. Nibbs United Kingdom 45 4.6k 1.7× 4.0k 2.2× 1.8k 1.4× 494 0.5× 230 0.5× 99 7.4k
M P Beckmann United States 33 3.8k 1.4× 1.7k 0.9× 1.9k 1.5× 515 0.6× 640 1.5× 44 6.9k
Thierry Velu Belgium 39 2.7k 1.0× 1.6k 0.9× 1.9k 1.5× 310 0.3× 345 0.8× 125 5.7k
Dagmar Scheel‐Toellner United Kingdom 35 2.5k 0.9× 1.0k 0.6× 1.9k 1.5× 424 0.5× 292 0.7× 63 5.4k

Countries citing papers authored by James E. Pease

Since Specialization
Citations

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

Fields of papers citing papers by James E. Pease

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by James E. Pease. 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 James E. Pease. The network helps show where James E. Pease may publish in the future.

Co-authorship network of co-authors of James E. Pease

This figure shows the co-authorship network connecting the top 25 collaborators of James E. Pease. A scholar is included among the top collaborators of James E. Pease 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 James E. Pease. James E. Pease 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.
2.
Pease, James E., et al.. (2023). What defines a chemokine? – The curious case of CXCL17. Cytokine. 168. 156224–156224. 9 indexed citations
3.
Mincham, Kyle T., Robert J. Snelgrove, Tomoko Tsuchiya, et al.. (2023). CXCL17 binds efficaciously to glycosaminoglycans with the potential to modulate chemokine signaling. Frontiers in Immunology. 14. 1254697–1254697. 10 indexed citations
4.
Puttur, Franz, Laura Denney, Lisa G. Gregory, et al.. (2019). Pulmonary environmental cues drive group 2 innate lymphoid cell dynamics in mice and humans. Science Immunology. 4(36). 97 indexed citations
5.
Fox, James M., Fahima Kausar, Michael P. Osborne, et al.. (2018). CXCL4/Platelet Factor 4 is an agonist of CCR1 and drives human monocyte migration. Scientific Reports. 8(1). 9466–9466. 65 indexed citations
6.
Blazek, Katrina, Hayley L. Eames, Miriam Weiss, et al.. (2015). IFN-λ resolves inflammation via suppression of neutrophil infiltration and IL-1β production. The Journal of Experimental Medicine. 212(6). 845–853. 173 indexed citations
7.
Solari, Roberto, James E. Pease, & Malcolm Begg. (2014). “Chemokine receptors as therapeutic targets: Why aren’t there more drugs?”. European Journal of Pharmacology. 746. 363–367. 70 indexed citations
8.
Nedjai, Belinda, Hubert Li, Ilana L. Stroke, et al.. (2011). Small molecule chemokine mimetics suggest a molecular basis for the observation that CXCL10 and CXCL11 are allosteric ligands of CXCR3. British Journal of Pharmacology. 166(3). 912–923. 35 indexed citations
9.
Horowitz, Amir, Maryam Mehrabi, Emma L. Wise, et al.. (2011). A distinct subset of human NK cells expressing HLA‐DR expand in response to IL‐2 and can aid immune responses to BCG. European Journal of Immunology. 41(7). 1924–1933. 81 indexed citations
10.
Collington, Sarah J., Jenny Hallgren, James E. Pease, et al.. (2010). The Role of the CCL2/CCR2 Axis in Mouse Mast Cell Migration In Vitro and In Vivo. The Journal of Immunology. 184(11). 6114–6123. 88 indexed citations
11.
Meiser, Andrea, Anja Müeller, Emma L. Wise, et al.. (2008). The Chemokine Receptor CXCR3 Is Degraded following Internalization and Is Replenished at the Cell Surface by De Novo Synthesis of Receptor. The Journal of Immunology. 180(10). 6713–6724. 106 indexed citations
12.
Qin, Shulin, Yongjun Sui, Adam C. Soloff, et al.. (2008). Chemokine and Cytokine Mediated Loss of Regulatory T Cells in Lymph Nodes during Pathogenic Simian Immunodeficiency Virus Infection. The Journal of Immunology. 180(8). 5530–5536. 36 indexed citations
13.
Wise, Emma L., et al.. (2007). Small Molecule Receptor Agonists and Antagonists of CCR3 Provide Insight into Mechanisms of Chemokine Receptor Activation. Journal of Biological Chemistry. 282(38). 27935–27943. 46 indexed citations
14.
Fox, James M., Pilar Najarro, Geoffrey L. Smith, et al.. (2006). Structure/Function Relationships of CCR8 Agonists and Antagonists. Journal of Biological Chemistry. 281(48). 36652–36661. 26 indexed citations
15.
Fonseca, da, et al.. (2004). Site-directed Mutagenesis of CC Chemokine Receptor 1 Reveals the Mechanism of Action of UCB 35625, a Small Molecule Chemokine Receptor Antagonist. Journal of Biological Chemistry. 280(6). 4808–4816. 58 indexed citations
16.
Najarro, Pilar, Han Joo Lee, James M. Fox, James E. Pease, & Geoffrey L. Smith. (2003). Yaba-like disease virus protein 7L is a cell-surface receptor for chemokine CCL1. Journal of General Virology. 84(12). 3325–3336. 11 indexed citations
17.
Stubbs, Victoria, et al.. (2003). Variations in Eosinophil Chemokine Responses: An Investigation of CCR1 and CCR3 Function, Expression in Atopy, and Identification of a Functional CCR1 Promoter. The Journal of Immunology. 170(12). 6190–6201. 32 indexed citations
18.
Pease, James E., et al.. (2002). Alanine scanning mutagenesis of CCR3 reveals that the three intracellular loops are essential for functional receptor expression. European Journal of Immunology. 32(4). 1052–1058. 31 indexed citations
19.
Pease, James E. & Ian Sabroe. (2002). The Role of Interleukin-8 and its Receptors in Inflammatory Lung Disease. PubMed. 1(1). 19–25. 171 indexed citations
20.
Pease, James E., Juan Wang, Paul Ponath, & Philip M. Murphy. (1998). The N-terminal Extracellular Segments of the Chemokine Receptors CCR1 and CCR3 Are Determinants for MIP-1α and Eotaxin Binding, Respectively, but a Second Domain Is Essential for Efficient Receptor Activation. Journal of Biological Chemistry. 273(32). 19972–19976. 93 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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