Richard J. Payne

10.4k total citations
254 papers, 7.9k citations indexed

About

Richard J. Payne is a scholar working on Molecular Biology, Organic Chemistry and Oncology. According to data from OpenAlex, Richard J. Payne has authored 254 papers receiving a total of 7.9k indexed citations (citations by other indexed papers that have themselves been cited), including 191 papers in Molecular Biology, 85 papers in Organic Chemistry and 37 papers in Oncology. Recurrent topics in Richard J. Payne's work include Chemical Synthesis and Analysis (87 papers), Glycosylation and Glycoproteins Research (49 papers) and Carbohydrate Chemistry and Synthesis (46 papers). Richard J. Payne is often cited by papers focused on Chemical Synthesis and Analysis (87 papers), Glycosylation and Glycoproteins Research (49 papers) and Carbohydrate Chemistry and Synthesis (46 papers). Richard J. Payne collaborates with scholars based in Australia, United States and United Kingdom. Richard J. Payne's co-authors include Lara R. Malins, Chi‐Huey Wong, Robert E. Thompson, Brendan L. Wilkinson, Sameer S. Kulkarni, Jessica Sayers, Leo Corcilius, Nicholas J. Mitchell, Emma E. Watson and Martin J. Stone and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Richard J. Payne

242 papers receiving 7.8k 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. Payne Australia 50 5.6k 3.3k 1.1k 782 689 254 7.9k
Norbert Sewald Germany 49 5.1k 0.9× 3.1k 1.0× 733 0.7× 815 1.0× 479 0.7× 483 9.8k
Avadhesha Surolia India 58 7.6k 1.4× 3.3k 1.0× 472 0.4× 2.4k 3.1× 718 1.0× 366 11.0k
Ursula Pieper United States 38 7.3k 1.3× 1.1k 0.3× 678 0.6× 649 0.8× 477 0.7× 81 10.8k
Carlo Pedone Italy 56 8.8k 1.6× 3.8k 1.1× 1.0k 1.0× 439 0.6× 503 0.7× 401 11.9k
Hiroaki Suga Japan 63 11.6k 2.1× 2.3k 0.7× 1.3k 1.2× 303 0.4× 2.0k 2.8× 349 13.2k
Anthony C. Willis Australia 48 3.1k 0.6× 5.0k 1.5× 975 0.9× 2.3k 3.0× 409 0.6× 371 10.9k
Mirosław Cygler Canada 59 10.2k 1.8× 1.4k 0.4× 717 0.7× 706 0.9× 442 0.6× 246 13.8k
K. Ravi Acharya United Kingdom 58 7.1k 1.3× 1.1k 0.3× 1.0k 0.9× 1.9k 2.4× 341 0.5× 272 12.0k
Stephan A. Sieber Germany 50 4.9k 0.9× 2.6k 0.8× 978 0.9× 176 0.2× 357 0.5× 236 7.8k
Lewis K. Pannell United States 55 4.6k 0.8× 2.1k 0.6× 567 0.5× 666 0.9× 179 0.3× 208 9.4k

Countries citing papers authored by Richard J. Payne

Since Specialization
Citations

This map shows the geographic impact of Richard J. Payne'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. Payne 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. Payne more than expected).

Fields of papers citing papers by Richard J. Payne

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

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

This figure shows the co-authorship network connecting the top 25 collaborators of Richard J. Payne. A scholar is included among the top collaborators of Richard J. Payne 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. Payne. Richard J. Payne 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.
Li, Xiang, Wanting Jiao, Yannasittha Jiramongkol, et al.. (2024). Integrating Phenotypic and Chemoproteomic Approaches to Identify Covalent Targets of Dietary Electrophiles in Platelets. ACS Central Science. 10(2). 344–357. 3 indexed citations
3.
Franck, Charlotte, Joel P. Mackay, Emma Sierecki, et al.. (2024). Expressed Protein Ligation in Flow. Journal of the American Chemical Society. 146(31). 22027–22035. 7 indexed citations
4.
Patel, Karishma, Yannasittha Jiramongkol, Alexander Norman, et al.. (2024). The enzymatic oxygen sensor cysteamine dioxygenase binds its protein substrates through their N-termini. Journal of Biological Chemistry. 300(9). 107653–107653. 2 indexed citations
5.
Ullrich, Sven, Anupriya Aggarwal, Mark Larance, et al.. (2024). Exploiting Hydrophobic Amino Acid Scanning to Develop Cyclic Peptide Inhibitors of the SARS‐CoV‐2 Main Protease with Antiviral Activity. Chemistry - A European Journal. 30(44). e202401606–e202401606. 2 indexed citations
6.
Bartolec, Tara K., Xabier Vázquez-Campos, Alexander Norman, et al.. (2023). Cross-linking mass spectrometry discovers, evaluates, and corroborates structures and protein–protein interactions in the human cell. Proceedings of the National Academy of Sciences. 120(17). e2219418120–e2219418120. 39 indexed citations
7.
Payne, Richard J., et al.. (2023). Second generation synthesis of the anti-infective natural product gallinamide A. Tetrahedron. 139. 133445–133445. 4 indexed citations
8.
Kulkarni, Sameer S., Mihai V. Popescu, Robert S. Paton, et al.. (2023). Electrochemical Modification of Polypeptides at Selenocysteine. Angewandte Chemie. 135(50). 1 indexed citations
9.
Kulkarni, Sameer S., Emma E. Watson, Susanne Huhmann, et al.. (2022). Expressed Protein Selenoester Ligation. Angewandte Chemie. 134(20). e202200163–e202200163. 2 indexed citations
10.
Kulkarni, Sameer S., Emma E. Watson, Susanne Huhmann, et al.. (2022). Expressed Protein Selenoester Ligation. Angewandte Chemie International Edition. 61(20). e202200163–e202200163. 22 indexed citations
11.
Payne, Richard J., et al.. (2020). Revealing the functional roles of tyrosine sulfation using synthetic sulfopeptides and sulfoproteins. Current Opinion in Chemical Biology. 58. 72–85. 34 indexed citations
12.
Clayton, Daniel, Sameer S. Kulkarni, Jessica Sayers, et al.. (2020). Chemical synthesis of a haemathrin sulfoprotein library reveals enhanced thrombin inhibition following tyrosine sulfation. RSC Chemical Biology. 1(5). 379–384. 5 indexed citations
13.
Patel, Karishma, Louise J. Walport, J.L. Walshe, et al.. (2020). Cyclic peptides can engage a single binding pocket through highly divergent modes. Proceedings of the National Academy of Sciences. 117(43). 26728–26738. 32 indexed citations
14.
Watson, Emma E., Jorge Ripoll‐Rozada, Ashley Lee, et al.. (2019). Rapid assembly and profiling of an anticoagulant sulfoprotein library. Proceedings of the National Academy of Sciences. 116(28). 13873–13878. 24 indexed citations
15.
Conibear, Anne C., Emma E. Watson, Richard J. Payne, & Christian F. W. Becker. (2018). Native chemical ligation in protein synthesis and semi-synthesis. Chemical Society Reviews. 47(24). 9046–9068. 246 indexed citations
16.
Wang, Xiaoyi, Julie Sanchez, Martin J. Stone, & Richard J. Payne. (2017). Sulfation of the Human Cytomegalovirus Protein UL22A Enhances Binding to the Chemokine RANTES. Angewandte Chemie International Edition. 56(29). 8490–8494. 28 indexed citations
17.
Tran, Anh, Emma E. Watson, Venugopal Pujari, et al.. (2017). Sansanmycin natural product analogues as potent and selective anti-mycobacterials that inhibit lipid I biosynthesis. Nature Communications. 8(1). 14414–14414. 40 indexed citations
18.
Kiermaier, Eva, Christine Moussion, Christopher T. Veldkamp, et al.. (2015). Polysialylation controls dendritic cell trafficking by regulating chemokine recognition. Science. 351(6269). 186–190. 128 indexed citations
19.
Malins, Lara R. & Richard J. Payne. (2014). Modern Extensions of Native Chemical Ligation for Chemical Protein Synthesis. Topics in current chemistry. 362. 27–87. 18 indexed citations
20.
Thompson, Robert E., Katrina A. Jolliffe, & Richard J. Payne. (2011). Total Synthesis of Microcin B17 via a Fragment Condensation Approach. Organic Letters. 13(4). 680–683. 26 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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