Richard J. Pleass

3.7k total citations
79 papers, 2.7k citations indexed

About

Richard J. Pleass is a scholar working on Immunology, Radiology, Nuclear Medicine and Imaging and Molecular Biology. According to data from OpenAlex, Richard J. Pleass has authored 79 papers receiving a total of 2.7k indexed citations (citations by other indexed papers that have themselves been cited), including 37 papers in Immunology, 35 papers in Radiology, Nuclear Medicine and Imaging and 30 papers in Molecular Biology. Recurrent topics in Richard J. Pleass's work include Monoclonal and Polyclonal Antibodies Research (35 papers), Glycosylation and Glycoproteins Research (20 papers) and Malaria Research and Control (17 papers). Richard J. Pleass is often cited by papers focused on Monoclonal and Polyclonal Antibodies Research (35 papers), Glycosylation and Glycoproteins Research (20 papers) and Malaria Research and Control (17 papers). Richard J. Pleass collaborates with scholars based in United Kingdom, United States and Norway. Richard J. Pleass's co-authors include Jenny M. Woof, Daniel M. Czajkowsky, Zhifeng Shao, Jun Hu, Anthony A. Holder, Richard S. McIntosh, Annemarie C. Lellouch, Taj S. Mattu, Antony C. Willis and Mark R. Wormald and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Nano Letters.

In The Last Decade

Richard J. Pleass

79 papers receiving 2.7k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Richard J. Pleass United Kingdom 28 1.2k 1.1k 908 622 324 79 2.7k
George L. Spitalny United States 26 1.2k 1.0× 676 0.6× 359 0.4× 368 0.6× 214 0.7× 49 2.8k
Leonard Moise United States 33 1.1k 1.0× 1.5k 1.4× 774 0.9× 165 0.3× 453 1.4× 99 2.7k
Morten A. Nielsen Denmark 36 1.8k 1.6× 890 0.8× 291 0.3× 3.0k 4.8× 231 0.7× 89 4.2k
Doris Scheidegger Switzerland 13 3.1k 2.7× 1.3k 1.1× 885 1.0× 158 0.3× 197 0.6× 16 4.6k
Michael D.P. Boyle United States 28 567 0.5× 699 0.6× 344 0.4× 984 1.6× 721 2.2× 103 2.4k
Gunilla B. Karlsson Hedestam Sweden 37 2.1k 1.8× 1.2k 1.0× 602 0.7× 253 0.4× 1.1k 3.3× 113 4.0k
Hedvig Perlmann Sweden 37 2.1k 1.8× 834 0.7× 644 0.7× 2.1k 3.4× 151 0.5× 98 4.1k
R. Hamers Belgium 30 920 0.8× 2.0k 1.7× 1.7k 1.9× 1.0k 1.7× 175 0.5× 103 3.9k
C. R. Jenkin Australia 21 1.2k 1.0× 1.5k 1.4× 1.2k 1.3× 231 0.4× 261 0.8× 46 3.7k
David Snary United Kingdom 33 1.1k 1.0× 1.3k 1.2× 509 0.6× 650 1.0× 69 0.2× 77 3.1k

Countries citing papers authored by Richard J. Pleass

Since Specialization
Citations

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

Fields of papers citing papers by Richard J. Pleass

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Richard J. Pleass. 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 Richard J. Pleass. The network helps show where Richard J. Pleass may publish in the future.

Co-authorship network of co-authors of Richard J. Pleass

This figure shows the co-authorship network connecting the top 25 collaborators of Richard J. Pleass. A scholar is included among the top collaborators of Richard J. Pleass 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 Richard J. Pleass. Richard J. Pleass 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.
Pleass, Richard J.. (2021). The therapeutic potential of sialylated Fc domains of human IgG. mAbs. 13(1). 1953220–1953220. 11 indexed citations
2.
Blundell, Patricia A., et al.. (2020). Choice of Host Cell Line Is Essential for the Functional Glycosylation of the Fc Region of Human IgG1 Inhibitors of Influenza B Viruses. The Journal of Immunology. 204(4). 1022–1034. 20 indexed citations
3.
4.
Lloyd, Katy A., Jiabin Wang, Britta C. Urban, Daniel M. Czajkowsky, & Richard J. Pleass. (2017). Glycan-independent binding and internalization of human IgM to FCMR, its cognate cellular receptor. Scientific Reports. 7(1). 42989–42989. 16 indexed citations
5.
Foss, Stian, Algirdas Grevys, Kine Marita Knudsen Sand, et al.. (2015). Enhanced FcRn-dependent transepithelial delivery of IgG by Fc-engineering and polymerization. Journal of Controlled Release. 223. 42–52. 23 indexed citations
6.
Islahudin, Farida, Ian R. Mellor, Hans E. M. Christensen, et al.. (2014). The antimalarial drug quinine interferes with serotonin biosynthesis and action. Scientific Reports. 4(1). 3618–3618. 14 indexed citations
7.
Hitchen, Paul G., Maria Panico, Howard R. Morris, et al.. (2012). Glycoproteomic characterization of recombinant mouse α-dystroglycan. Glycobiology. 22(5). 662–675. 50 indexed citations
8.
Alcocer, Marcos, et al.. (2011). Native-State Stability Determines the Extent of Degradation Relative to Secretion of Protein Variants from Pichia pastoris. PLoS ONE. 6(7). e22692–e22692. 43 indexed citations
9.
Mekhaiel, David, Daniel M. Czajkowsky, Jan Terje Andersen, et al.. (2011). Polymeric human Fc-fusion proteins with modified effector functions. Scientific Reports. 1(1). 124–124. 58 indexed citations
10.
Czajkowsky, Daniel M., Ali Salanti, Sisse B. Ditlev, et al.. (2010). IgM, FcμRs, and Malarial Immune Evasion. The Journal of Immunology. 184(9). 4597–4603. 26 indexed citations
11.
Pleass, Richard J. & Jerzy M. Behnke. (2009). B-cells get the T-cells but antibodies get the worms. Trends in Parasitology. 25(10). 443–446. 4 indexed citations
12.
Pleass, Richard J.. (2009). Do Escherichia coli express Fc-receptors for immunoglobulin?. Molecular Immunology. 46(11-12). 2439–2440. 1 indexed citations
13.
Ghumra, Ashfaq, Jean‐Philippe Semblat, Richard S. McIntosh, et al.. (2008). Identification of Residues in the Cμ4 Domain of Polymeric IgM Essential for Interaction with Plasmodium falciparum Erythrocyte Membrane Protein 1 (PfEMP1). The Journal of Immunology. 181(3). 1988–2000. 53 indexed citations
14.
Jackson, Joseph A., Richard J. Pleass, Jo Cable, Janette E. Bradley, & R. C. Tinsley. (2006). Heterogenous interspecific interactions in a host–parasite system. International Journal for Parasitology. 36(13). 1341–1349. 41 indexed citations
15.
Lewis, Melanie J., Richard J. Pleass, Margaret R. Batten, Julie D. Atkin, & Jenny M. Woof. (2005). Structural Requirements for the Interaction of Human IgA with the Human Polymeric Ig Receptor. The Journal of Immunology. 175(10). 6694–6701. 36 indexed citations
16.
Morton, H. Craig, Richard J. Pleass, Anne K. Storset, et al.. (2004). Cloning and characterization of an immunoglobulin A Fc receptor from cattle. Immunology. 111(2). 204–211. 18 indexed citations
17.
McGuinness, David, et al.. (2003). Pattern recognition molecules and innate immunity to parasites. Trends in Parasitology. 19(7). 312–319. 64 indexed citations
18.
Pleass, Richard J. & Jenny M. Woof. (2001). Fc receptors and immunity to parasites. Trends in Parasitology. 17(11). 545–551. 51 indexed citations
19.
Krugmann, Sonja, Richard J. Pleass, Julie D. Atkin, & Jenny M. Woof. (1997). Structural requirements for assembly of dimeric IgA probed by site-directed mutagenesis of J chain and a cysteine residue of the α-chain CH2 domain. The Journal of Immunology. 159(1). 244–249. 43 indexed citations
20.
Pleass, Richard J., James I. Dunlop, & Jenny M. Woof. (1997). Multiple transcripts of human IgA Fc receptor CD89 in neutrophils, eosinophils and the monocyte-like cell line THP-1. Biochemical Society Transactions. 25(2). 327S–327S. 5 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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