John S. Allingham

2.2k total citations
46 papers, 1.6k citations indexed

About

John S. Allingham is a scholar working on Molecular Biology, Cell Biology and Organic Chemistry. According to data from OpenAlex, John S. Allingham has authored 46 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 27 papers in Molecular Biology, 21 papers in Cell Biology and 7 papers in Organic Chemistry. Recurrent topics in John S. Allingham's work include Microtubule and mitosis dynamics (13 papers), Cellular Mechanics and Interactions (9 papers) and Cellular transport and secretion (6 papers). John S. Allingham is often cited by papers focused on Microtubule and mitosis dynamics (13 papers), Cellular Mechanics and Interactions (9 papers) and Cellular transport and secretion (6 papers). John S. Allingham collaborates with scholars based in Canada, United States and China. John S. Allingham's co-authors include Ivan Rayment, Robert Smith, Vadim A. Klenchin, Robert L. Campbell, Peter L. Davies, Gerard Marriott, Junichi Tanaka, David B. Haniford, Feng-Hsu Lin and Tianjun Sun and has published in prestigious journals such as Science, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

John S. Allingham

45 papers receiving 1.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
John S. Allingham Canada 22 841 501 266 200 162 46 1.6k
Perttu Permi Finland 35 2.0k 2.4× 585 1.2× 188 0.7× 146 0.7× 288 1.8× 147 3.6k
Nobuhisa Watanabe Japan 29 1.4k 1.7× 137 0.3× 375 1.4× 134 0.7× 156 1.0× 128 2.5k
Jorge Alegre‐Cebollada Spain 25 1.1k 1.4× 412 0.8× 127 0.5× 270 1.4× 233 1.4× 54 2.1k
J. Seetharaman United States 29 2.0k 2.3× 220 0.4× 238 0.9× 65 0.3× 71 0.4× 80 3.0k
Martin Kollmar Germany 27 1.6k 1.9× 588 1.2× 211 0.8× 299 1.5× 31 0.2× 62 2.4k
Steven M. Pascal United States 19 2.6k 3.0× 331 0.7× 94 0.4× 128 0.6× 61 0.4× 44 3.2k
Toshiro Oda Japan 18 718 0.9× 699 1.4× 96 0.4× 362 1.8× 40 0.2× 51 1.6k
S.J. Harrop Australia 27 2.0k 2.4× 292 0.6× 389 1.5× 77 0.4× 79 0.5× 57 3.0k
Amy H. Andreotti United States 29 2.0k 2.4× 201 0.4× 305 1.1× 52 0.3× 60 0.4× 73 3.4k
Tadashi Satoh Japan 27 1.3k 1.6× 464 0.9× 175 0.7× 163 0.8× 72 0.4× 112 2.1k

Countries citing papers authored by John S. Allingham

Since Specialization
Citations

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

Fields of papers citing papers by John S. Allingham

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by John S. Allingham. 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 John S. Allingham. The network helps show where John S. Allingham may publish in the future.

Co-authorship network of co-authors of John S. Allingham

This figure shows the co-authorship network connecting the top 25 collaborators of John S. Allingham. A scholar is included among the top collaborators of John S. Allingham 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 John S. Allingham. John S. Allingham 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.
Eves, Robert, Tyler D. R. Vance, Adam P. Sage, et al.. (2025). Aeromonas hydrophila RTX adhesin has three ligand-binding domains that give the bacterium the potential to adhere to and aggregate a wide variety of cell types. mBio. 16(5). e0315824–e0315824. 1 indexed citations
2.
Jiang, Yun, Rebecca L. Grange, Murugan Subaramanian, et al.. (2024). Toward a Template for Synthetic Actin-Targeting Macrolide Analogues That Inhibit Cancer Cell Invasiveness. Journal of Medicinal Chemistry. 67(7). 5315–5332.
3.
Allingham, John S., et al.. (2023). New insights into the mechanochemical coupling mechanism of kinesin–microtubule complexes from their high-resolution structures. Biochemical Society Transactions. 51(4). 1505–1520. 7 indexed citations
4.
Asenjo, Ana B., et al.. (2022). Kinesin-8-specific loop-2 controls the dual activities of the motor domain according to tubulin protofilament shape. Nature Communications. 13(1). 4198–4198. 13 indexed citations
5.
Subramaniam, Rajagopal, et al.. (2020). Ste2 receptor-mediated chemotropism of Fusarium graminearum contributes to its pathogenicity against wheat. Scientific Reports. 10(1). 10770–10770. 23 indexed citations
6.
Loewen, Peter C., Jacek Switala, James P. Wells, et al.. (2018). Structure and function of a lignostilbene-α,β-dioxygenase orthologue from Pseudomonas brassicacearum. BMC Biochemistry. 19(1). 8–8. 15 indexed citations
7.
Paydar, Mohammadjavad, et al.. (2018). Ternary complex of Kif2A-bound tandem tubulin heterodimers represents a kinesin-13-mediated microtubule depolymerization reaction intermediate. Nature Communications. 9(1). 2628–2628. 46 indexed citations
8.
Guo, Shuaiqi, Corey A. Stevens, Tyler D. R. Vance, et al.. (2017). Structure of a 1.5-MDa adhesin that binds its Antarctic bacterium to diatoms and ice. Science Advances. 3(8). e1701440–e1701440. 73 indexed citations
9.
Sun, Tianjun, Feng-Hsu Lin, Robert L. Campbell, John S. Allingham, & Peter L. Davies. (2014). An Antifreeze Protein Folds with an Interior Network of More Than 400 Semi-Clathrate Waters. Science. 343(6172). 795–798. 148 indexed citations
10.
Guo, Shuaiqi, et al.. (2013). Role of Ca2+ in folding the tandem β‐sandwich extender domains of a bacterial ice‐binding adhesin. FEBS Journal. 280(22). 5919–5932. 23 indexed citations
11.
Duan, Da, et al.. (2013). Kar3Vik1 Mechanochemistry Is Inhibited by Mutation or Deletion of the C Terminus of the Vik1 Subunit. Journal of Biological Chemistry. 288(52). 36957–36970. 3 indexed citations
12.
Everingham, Stephanie, et al.. (2012). FES Kinase Promotes Mast Cell Recruitment to Mammary Tumors via the Stem Cell Factor/KIT Receptor Signaling Axis. Molecular Cancer Research. 10(7). 881–891. 12 indexed citations
13.
Allingham, John S., et al.. (2012). Crystal structure of the Candida albicans Kar3 kinesin motor domain fused to maltose-binding protein. Biochemical and Biophysical Research Communications. 428(4). 427–432. 4 indexed citations
14.
Duan, Da, et al.. (2012). Neck Rotation and Neck Mimic Docking in the Noncatalytic Kar3-associated Protein Vik1. Journal of Biological Chemistry. 287(48). 40292–40301. 11 indexed citations
15.
Duan, Da, et al.. (2011). Crystal structure of the Kar3‐like kinesin motor domain from the filamentous fungus Ashbya gossypii. Proteins Structure Function and Bioinformatics. 80(4). 1016–1027. 7 indexed citations
16.
Wen, Kuo‐Kuang, et al.. (2011). Functional Adaptation between Yeast Actin and Its Cognate Myosin Motors. Journal of Biological Chemistry. 286(35). 30384–30392. 6 indexed citations
17.
Allingham, John S., Christopher O. Miles, & Ivan Rayment. (2007). A Structural Basis for Regulation of Actin Polymerization by Pectenotoxins. Journal of Molecular Biology. 371(4). 959–970. 56 indexed citations
18.
Allingham, John S., et al.. (2007). Vik1 Modulates Microtubule-Kar3 Interactions through a Motor Domain that Lacks an Active Site. Cell. 128(6). 1161–1172. 68 indexed citations
19.
Allingham, John S., Robert Smith, & Ivan Rayment. (2005). The structural basis of blebbistatin inhibition and specificity for myosin II. Nature Structural & Molecular Biology. 12(4). 378–379. 252 indexed citations
20.
Santagata, Sandro, Eva Besmer, Anna Villa, et al.. (1999). The RAG1/RAG2 Complex Constitutes a 3′ Flap Endonuclease. Molecular Cell. 4(6). 935–947. 65 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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