Stephen J. Eyles

2.6k total citations
45 papers, 2.0k citations indexed

About

Stephen J. Eyles is a scholar working on Molecular Biology, Spectroscopy and Materials Chemistry. According to data from OpenAlex, Stephen J. Eyles has authored 45 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 32 papers in Molecular Biology, 21 papers in Spectroscopy and 7 papers in Materials Chemistry. Recurrent topics in Stephen J. Eyles's work include Mass Spectrometry Techniques and Applications (20 papers), Protein Structure and Dynamics (16 papers) and Metabolomics and Mass Spectrometry Studies (5 papers). Stephen J. Eyles is often cited by papers focused on Mass Spectrometry Techniques and Applications (20 papers), Protein Structure and Dynamics (16 papers) and Metabolomics and Mass Spectrometry Studies (5 papers). Stephen J. Eyles collaborates with scholars based in United States, United Kingdom and China. Stephen J. Eyles's co-authors include Igor A. Kaltashov, Lila M. Gierasch, Sheena E. Radford, Carol V. Robinson, Christopher M. Dobson, A. T. Hagler, Kannan Gunasekaran, Rinat R. Abzalimov, Mark Mayhew and Michael L. Gross and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Stephen J. Eyles

45 papers receiving 2.0k citations

Peers

Stephen J. Eyles
Anton Iliuk United States
Atanas V. Koulov United States
Andrea M. Hounslow United Kingdom
Franz Hagn Germany
Alan M. Sandercock United Kingdom
Ann H. Kwan Australia
Stephen J. Eyles
Citations per year, relative to Stephen J. Eyles Stephen J. Eyles (= 1×) peers Marco Gaspari

Countries citing papers authored by Stephen J. Eyles

Since Specialization
Citations

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

Fields of papers citing papers by Stephen J. Eyles

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Stephen J. Eyles

This figure shows the co-authorship network connecting the top 25 collaborators of Stephen J. Eyles. A scholar is included among the top collaborators of Stephen J. Eyles 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 Stephen J. Eyles. Stephen J. Eyles 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.
Tran, Thomas, Aruni P. K. K. Karunanayake Mudiyanselage, Stephen J. Eyles, & Lynmarie K. Thompson. (2023). Bacterial chemoreceptor signaling complexes control kinase activity by stabilizing the catalytic domain of CheA. Proceedings of the National Academy of Sciences. 120(32). e2218467120–e2218467120. 5 indexed citations
2.
Graham, Jill B., et al.. (2023). TTC17 is an endoplasmic reticulum resident TPR-containing adaptor protein. Journal of Biological Chemistry. 299(12). 105450–105450. 2 indexed citations
3.
Li, Danning, Hongxia Xu, Qin Su, et al.. (2023). Renewal of oligodendrocyte lineage reverses dysmyelination and CNS neurodegeneration through corrected N-acetylaspartate metabolism. Progress in Neurobiology. 226. 102460–102460. 6 indexed citations
4.
Gonzalez-Hernandez, Alberto J., et al.. (2023). Dissecting the molecular basis for the modulation of neurotransmitter GPCR signaling by GINIP. Structure. 32(1). 47–59.e7. 7 indexed citations
5.
Ke, Haiping, Stephen J. Eyles, Malaiyalam Mariappan, et al.. (2023). ER chaperones use a protein folding and quality control glyco-code. Molecular Cell. 83(24). 4524–4537.e5. 11 indexed citations
6.
Du, Jiale, Yanfeng Li, Kirandeep K. Deol, et al.. (2022). A cryptic K48 ubiquitin chain binding site on UCH37 is required for its role in proteasomal degradation. eLife. 11. 18 indexed citations
7.
Duan, Qiaohong, Ming‐Che Liu, Daniel Kita, et al.. (2020). FERONIA controls pectin- and nitric oxide-mediated male–female interaction. Nature. 579(7800). 561–566. 154 indexed citations
8.
Fernandez, Katharine, Katie Spielbauer, Aaron E. Rusheen, et al.. (2020). Lovastatin protects against cisplatin-induced hearing loss in mice. Hearing Research. 389. 107905–107905. 46 indexed citations
9.
Li, Xuni, Stephen J. Eyles, & Lynmarie K. Thompson. (2019). Hydrogen exchange of chemoreceptors in functional complexes suggests protein stabilization mediates long-range allosteric coupling. Journal of Biological Chemistry. 294(44). 16062–16079. 13 indexed citations
10.
Bobst, Cedric E., et al.. (2019). Sterilization of epidermal growth factor with supercritical carbon dioxide and peracetic acid; analysis of changes at the amino acid and protein level. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1868(2). 140334–140334. 9 indexed citations
11.
Guerra, Damian D., et al.. (2018). Direct Measurement of S-Nitrosothiols with an Orbitrap Fusion Mass Spectrometer: S-Nitrosoglutathione Reductase as a Model Protein. Methods in molecular biology. 1747. 143–160. 1 indexed citations
12.
He, Tao, Anne Gershenson, Stephen J. Eyles, et al.. (2015). Fluorinated Aromatic Amino Acids Distinguish Cation-π Interactions from Membrane Insertion. Journal of Biological Chemistry. 290(31). 19334–19342. 23 indexed citations
13.
Chen, Yuanhan, et al.. (2008). Auto-hydroxylation of FIH-1: an Fe(ii), α-ketoglutarate-dependent human hypoxia sensor. Chemical Communications. 4768–4768. 31 indexed citations
14.
Greene, Lesley H., Daizo Hamada, Stephen J. Eyles, & Keith Brew. (2003). Conserved signature proposed for folding in the lipocalin superfamily. FEBS Letters. 553(1-2). 39–44. 23 indexed citations
15.
Kaltashov, Igor A. & Stephen J. Eyles. (2002). Studies of biomolecular conformations and conformational dynamics by mass spectrometry. Mass Spectrometry Reviews. 21(1). 37–71. 234 indexed citations
16.
Gunasekaran, Kannan, Stephen J. Eyles, A. T. Hagler, & Lila M. Gierasch. (2001). Keeping it in the family: folding studies of related proteins. Current Opinion in Structural Biology. 11(1). 83–93. 100 indexed citations
17.
Eyles, Stephen J. & Lila M. Gierasch. (2000). Multiple roles of prolyl residues in structure and folding 1 1Edited by C. Robert Matthews. Journal of Molecular Biology. 301(3). 737–747. 78 indexed citations
18.
Eyles, Stephen J., et al.. (1999). Unfolding dynamics of aβ-sheet protein studied by mass spectrometry. Journal of Mass Spectrometry. 34(12). 1289–1295. 41 indexed citations
19.
Eyles, Stephen J., Sheena E. Radford, Carol V. Robinson, & Christopher M. Dobson. (1994). Kinetic Consequences of the Removal of a Disulfide Bridge on the Folding of Hen Lysozyme. Biochemistry. 33(44). 13038–13048. 81 indexed citations
20.
Cooper, Alan, Stephen J. Eyles, Sheena E. Radford, & Christopher M. Dobson. (1992). Thermodynamic consequences of the removal of a disulphide bridge from hen lysozyme. Journal of Molecular Biology. 225(4). 939–943. 81 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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