Martin J. Stone

5.5k total citations
106 papers, 4.2k citations indexed

About

Martin J. Stone is a scholar working on Molecular Biology, Immunology and Oncology. According to data from OpenAlex, Martin J. Stone has authored 106 papers receiving a total of 4.2k indexed citations (citations by other indexed papers that have themselves been cited), including 71 papers in Molecular Biology, 33 papers in Immunology and 31 papers in Oncology. Recurrent topics in Martin J. Stone's work include Chemokine receptors and signaling (31 papers), Glycosylation and Glycoproteins Research (22 papers) and Protein Structure and Dynamics (17 papers). Martin J. Stone is often cited by papers focused on Chemokine receptors and signaling (31 papers), Glycosylation and Glycoproteins Research (22 papers) and Protein Structure and Dynamics (17 papers). Martin J. Stone collaborates with scholars based in United States, Australia and United Kingdom. Martin J. Stone's co-authors include Dudley H. Williams, Lukáš Žı́dek, Richard J. Payne, Peter E. Wright, Justin P. Ludeman, Julie Sanchez, Shirley K. Rahman, Miloš V. Novotný, Cheng Huang and Jiqing Ye and has published in prestigious journals such as Chemical Reviews, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Martin J. Stone

99 papers receiving 4.1k citations

Peers

Martin J. Stone
Craig J. Morton Australia
Torleif Härd Sweden
Jacek Otlewski Poland
Amy H. Andreotti United States
W.F. Anderson United States
Bruce A. Johnson United States
Alexander S. Arseniev Russia
Daisuke Kohda Japan
Jim Warwicker United Kingdom
Stanley C. Gill United States
Craig J. Morton Australia
Martin J. Stone
Citations per year, relative to Martin J. Stone Martin J. Stone (= 1×) peers Craig J. Morton

Countries citing papers authored by Martin J. Stone

Since Specialization
Citations

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

Fields of papers citing papers by Martin J. Stone

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Martin J. Stone

This figure shows the co-authorship network connecting the top 25 collaborators of Martin J. Stone. A scholar is included among the top collaborators of Martin J. Stone 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 Martin J. Stone. Martin J. Stone 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.
Huang, Cheng, Simon R. Foster, Anup D. Shah, et al.. (2020). Phosphoproteomic characterization of the signaling network resulting from activation of the chemokine receptor CCR2. Journal of Biological Chemistry. 295(19). 6518–6531. 14 indexed citations
2.
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
3.
Wang, Xiaoyi, et al.. (2017). Sulfation of the Human Cytomegalovirus Protein UL22A Enhances Binding to the Chemokine RANTES. Angewandte Chemie. 129(29). 8610–8614. 5 indexed citations
4.
Sanchez, Julie, Herman D. Lim, Jessica L. Bridgford, et al.. (2017). Key determinants of selective binding and activation by the monocyte chemoattractant proteins at the chemokine receptor CCR2. Science Signaling. 10(480). 43 indexed citations
5.
Stone, Martin J.. (2014). Caesar prophesies the future: Sallust "Catiline" 51.35-6: an exercise in historiography. 231–249.
6.
Millard, Christopher J., Justin P. Ludeman, Meritxell Canals, et al.. (2014). Structural Basis of Receptor Sulfotyrosine Recognition by a CC Chemokine: The N-Terminal Region of CCR3 Bound to CCL11/Eotaxin-1. Structure. 22(11). 1571–1581. 63 indexed citations
7.
Zhu, John, et al.. (2009). Regulation of Chemokine Recognition by Site-Specific Tyrosine Sulfation of Receptor Peptides. Chemistry & Biology. 16(2). 153–161. 62 indexed citations
8.
Cortajarena, Aitziber L., et al.. (2008). Comparison of the backbone dynamics of a natural and a consensus designed 3-TPR domain. Journal of Biomolecular NMR. 41(3). 169–178. 6 indexed citations
9.
10.
Edmonds, Katherine A., et al.. (2004). Thermodynamic consequences of disrupting a water‐mediated hydrogen bond network in a protein:pheromone complex. Protein Science. 14(1). 249–256. 37 indexed citations
11.
Stone, Martin J., et al.. (2004). High level expression, activation, and antagonism of CC chemokine receptors CCR2 and CCR3 in Chinese hamster ovary cells. Cytokine. 27(1). 38–46. 19 indexed citations
12.
Pichumani, Kumar, et al.. (2003). Covariation of backbone motion throughout a small protein domain. Nature Structural & Molecular Biology. 10(11). 962–965. 34 indexed citations
13.
Stone, Martin J., et al.. (2003). Soluble mimics of a chemokine receptor: Chemokine binding by receptor elements juxtaposed on a soluble scaffold. Protein Science. 12(11). 2482–2491. 15 indexed citations
14.
Stone, Martin J., et al.. (2002). Backbone dynamics of the CC‐chemokine eotaxin‐2 and comparison among the eotaxin group chemokines. Proteins Structure Function and Bioinformatics. 50(2). 184–191. 7 indexed citations
15.
16.
Huang, Mingdong, Rashid Syed, E.A. Stura, et al.. (1998). The mechanism of an inhibitory antibody on TF-initiated blood coagulation revealed by the crystal structures of human tissue factor, Fab 5G9 and TF·5G9 complex 1 1Edited by D. C. Rees. Journal of Molecular Biology. 275(5). 873–894. 102 indexed citations
17.
Jennings, Patricia A., Martin J. Stone, & Peter E. Wright. (1995). Overexpression of myoglobin and assignment of its amide, C? and C? resonances. Journal of Biomolecular NMR. 6(3). 271–6. 56 indexed citations
18.
Ruf, Wolfram, John R. Schullek, Martin J. Stone, & Thomas S. Edgington. (1994). Mutational Mapping of Functional Residues in Tissue Factor: Identification of Factor VII Recognition Determinants in Both Structural Modules of the Predicted Cytokine Receptor Homology Domain. Biochemistry. 33(6). 1565–1572. 64 indexed citations
19.
Nedderman, Angus N. R., Martin J. Stone, Dudley H. Williams, Paul Kong Thoo Lin, & D. M. Brown. (1993). Molecular Basis for Methoxyamine-initiated Mutagenesis: 1H Nuclear Magnetic Resonance Studies of Oligonucleotide Duplexes Containing Base-modified Cytosine Residues. Journal of Molecular Biology. 230(3). 1068–1076. 34 indexed citations
20.
Williams, Dudley H., et al.. (1990). Molecular recognition by secondary metabolites. Biochemical Pharmacology. 40(1). 27–34. 10 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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