Edwin A. Yates

7.2k total citations
168 papers, 4.7k citations indexed

About

Edwin A. Yates is a scholar working on Molecular Biology, Cell Biology and Organic Chemistry. According to data from OpenAlex, Edwin A. Yates has authored 168 papers receiving a total of 4.7k indexed citations (citations by other indexed papers that have themselves been cited), including 112 papers in Molecular Biology, 95 papers in Cell Biology and 37 papers in Organic Chemistry. Recurrent topics in Edwin A. Yates's work include Proteoglycans and glycosaminoglycans research (92 papers), Glycosylation and Glycoproteins Research (67 papers) and Carbohydrate Chemistry and Synthesis (34 papers). Edwin A. Yates is often cited by papers focused on Proteoglycans and glycosaminoglycans research (92 papers), Glycosylation and Glycoproteins Research (67 papers) and Carbohydrate Chemistry and Synthesis (34 papers). Edwin A. Yates collaborates with scholars based in United Kingdom, Italy and Brazil. Edwin A. Yates's co-authors include Jeremy E. Turnbull, Timothy R. Rudd, Mark A. Skidmore, Marcelo A. Lima, Marco Guerrini, John Knox, Scott E. Guimond, David G. Fernig, Giangiacomo Torri and Helena B. Nader and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Edwin A. Yates

167 papers receiving 4.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Edwin A. Yates United Kingdom 35 2.8k 1.9k 607 574 379 168 4.7k
Toshihiko Toida Japan 45 3.8k 1.4× 3.4k 1.8× 1.2k 2.0× 627 1.1× 297 0.8× 216 7.1k
Barbara Mulloy United Kingdom 56 4.3k 1.6× 3.6k 1.9× 1.1k 1.8× 731 1.3× 521 1.4× 163 9.8k
Lars C. Pedersen United States 54 5.1k 1.8× 1.2k 0.7× 1.0k 1.7× 266 0.5× 1.0k 2.7× 175 7.7k
Christian Slomianny France 51 3.5k 1.3× 681 0.4× 506 0.8× 273 0.5× 478 1.3× 151 7.4k
Janko Kos Slovenia 57 4.3k 1.5× 920 0.5× 796 1.3× 663 1.2× 311 0.8× 314 10.9k
Zhenqing Zhang China 35 2.0k 0.7× 1.4k 0.7× 708 1.2× 617 1.1× 111 0.3× 195 4.2k
Andrew A. Gooley Australia 39 4.4k 1.6× 559 0.3× 468 0.8× 436 0.8× 388 1.0× 111 6.7k
Peter G. Parsons Australia 51 4.4k 1.6× 1.2k 0.6× 635 1.0× 331 0.6× 434 1.1× 268 9.0k
G. Ya. Wiederschain United States 18 3.5k 1.3× 602 0.3× 1.3k 2.1× 362 0.6× 270 0.7× 46 5.6k
Wei‐Chiang Shen United States 43 4.5k 1.6× 651 0.4× 351 0.6× 791 1.4× 535 1.4× 131 6.8k

Countries citing papers authored by Edwin A. Yates

Since Specialization
Citations

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

Fields of papers citing papers by Edwin A. Yates

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Edwin A. Yates. 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 Edwin A. Yates. The network helps show where Edwin A. Yates may publish in the future.

Co-authorship network of co-authors of Edwin A. Yates

This figure shows the co-authorship network connecting the top 25 collaborators of Edwin A. Yates. A scholar is included among the top collaborators of Edwin A. Yates 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 Edwin A. Yates. Edwin A. Yates 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.
Barsukov, Igor, et al.. (2025). Detection of β-d-glucuronidase activity in environmental samples using 4-fluorophenyl β-d-glucuronide and 19F NMR. Analytical Methods. 17(9). 2015–2020. 1 indexed citations
2.
Elli, Stefano, et al.. (2024). Differential Solvent DEEP-STD NMR and MD Simulations Enable the Determinants of the Molecular Recognition of Heparin Oligosaccharides by Antithrombin to Be Disentangled. International Journal of Molecular Sciences. 25(9). 4669–4669. 1 indexed citations
4.
Maciej-Hulme, Marissa L., Scott E. Guimond, Jeremy E. Turnbull, et al.. (2023). High sensitivity (zeptomole) detection of BODIPY-labelled heparan sulfate (HS) disaccharides by ion-paired RP-HPLC and LIF detection enables analysis of HS from mosquito midguts. Analytical Methods. 15(11). 1461–1469. 3 indexed citations
5.
Lindsay, Susan L., Jiangshan Zhan, Miriam Scheld, et al.. (2023). Low sulfated heparan sulfate mimetic differentially affects repair in immune‐mediated and toxin‐induced experimental models of demyelination. Glia. 71(7). 1683–1698. 2 indexed citations
6.
Lindsay, Susan L., Edwin A. Yates, Bryan E. Thacker, et al.. (2023). Validation of Recombinant Heparan Sulphate Reagents for CNS Repair. Biology. 12(3). 407–407. 1 indexed citations
7.
Li, Yong, Sarah H. Hewitt, Edwin A. Yates, et al.. (2021). Anion binding to a cationic europium( iii ) probe enables the first real-time assay of heparan sulfotransferase activity. Organic & Biomolecular Chemistry. 20(3). 596–605. 8 indexed citations
8.
Fullwood, Nigel J., et al.. (2020). Aggregation Kinetics and Filament Structure of a Tau Fragment Are Influenced by the Sulfation Pattern of the Cofactor Heparin. Biochemistry. 59(41). 4003–4014. 18 indexed citations
9.
McGrath, Michael A., Thomas D. Otto, Richard Burchmore, et al.. (2018). Low sulfated heparins target multiple proteins for central nervous system repair. Glia. 67(4). 668–687. 19 indexed citations
10.
Byrne, Dominic P., Yong Li, Igor Barsukov, et al.. (2018). New tools for carbohydrate sulfation analysis: heparan sulfate 2- O -sulfotransferase (HS2ST) is a target for small-molecule protein kinase inhibitors. Biochemical Journal. 475(15). 2417–2433. 17 indexed citations
11.
Skidmore, Mark A., et al.. (2017). A semi-synthetic glycosaminoglycan analogue inhibits and reverses Plasmodium falciparum cytoadherence. PLoS ONE. 12(10). e0186276–e0186276. 11 indexed citations
12.
Li, Yong, Changye Sun, Edwin A. Yates, et al.. (2016). Heparin binding preference and structures in the fibroblast growth factor family parallel their evolutionary diversification. Open Biology. 6(3). 150275–150275. 52 indexed citations
13.
Solari, Valeria, Lucia Borriello, Gianluca Turcatel, et al.. (2014). MYCN-Dependent Expression of Sulfatase-2 Regulates Neuroblastoma Cell Survival. Cancer Research. 74(21). 5999–6009. 9 indexed citations
14.
Rudd, Timothy R. & Edwin A. Yates. (2010). Conformational degeneracy restricts the effective information content of heparan sulfate. Molecular BioSystems. 6(5). 902–908. 17 indexed citations
15.
Skidmore, Mark A., et al.. (2010). Disaccharide compositional analysis of heparan sulfate and heparin polysaccharides using UV or high-sensitivity fluorescence (BODIPY) detection. Nature Protocols. 5(12). 1983–1992. 46 indexed citations
16.
Patey, Susannah J., Elizabeth A. Edwards, Edwin A. Yates, & Jeremy E. Turnbull. (2008). Engineered Heparins: Novel β-Secretase Inhibitors as Potential Alzheimer’s Disease Therapeutics. Neurodegenerative Diseases. 5(3-4). 197–199. 28 indexed citations
17.
Patel, Vaishali, Simona Zisman‐Rozen, Ifat Sher, et al.. (2008). Specific Heparan Sulfate Structures Modulate FGF10-mediated Submandibular Gland Epithelial Morphogenesis and Differentiation. Journal of Biological Chemistry. 283(14). 9308–9317. 87 indexed citations
18.
Patey, Susannah J., Elizabeth A. Edwards, Edwin A. Yates, & Jeremy E. Turnbull. (2006). Heparin Derivatives as Inhibitors of BACE-1, the Alzheimer's β-Secretase, with Reduced Activity against Factor Xa and Other Proteases. Journal of Medicinal Chemistry. 49(20). 6129–6132. 57 indexed citations
19.
Yates, Edwin A., Susannah J. Patey, & Jeremy E. Turnbull. (2005). Novel heparan sulphate analogues: inhibition of β-secretase cleavage of amyloid precursor protein. Biochemical Society Transactions. 33(5). 1116–1116. 12 indexed citations
20.
Yates, Edwin A., Bodo Philipp, Catherine M. Buckley, et al.. (2002). N -Acylhomoserine Lactones Undergo Lactonolysis in a pH-, Temperature-, and Acyl Chain Length-Dependent Manner during Growth of Yersinia pseudotuberculosis and Pseudomonas aeruginosa. Infection and Immunity. 70(10). 5635–5646. 491 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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