Ivan Gout

15.4k total citations · 7 hit papers
157 papers, 12.8k citations indexed

About

Ivan Gout is a scholar working on Molecular Biology, Neurology and Cell Biology. According to data from OpenAlex, Ivan Gout has authored 157 papers receiving a total of 12.8k indexed citations (citations by other indexed papers that have themselves been cited), including 138 papers in Molecular Biology, 32 papers in Neurology and 28 papers in Cell Biology. Recurrent topics in Ivan Gout's work include Protein Kinase Regulation and GTPase Signaling (33 papers), Neurological diseases and metabolism (32 papers) and PI3K/AKT/mTOR signaling in cancer (32 papers). Ivan Gout is often cited by papers focused on Protein Kinase Regulation and GTPase Signaling (33 papers), Neurological diseases and metabolism (32 papers) and PI3K/AKT/mTOR signaling in cancer (32 papers). Ivan Gout collaborates with scholars based in United Kingdom, Ukraine and United States. Ivan Gout's co-authors include Michael Fry, Ritu Dhand, George Panayotou, Michael D. Waterfield, Michael D. Waterfield, Julian Downward, Pablo Rodriguez‐Viciana, Patricia H. Warne, Bart Vanhaesebroeck and I. Hiles and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Ivan Gout

154 papers receiving 12.6k citations

Hit Papers

Phosphatidylinositol-3-OH... 1991 2026 2002 2014 1994 2004 1991 1992 1998 500 1000 1.5k

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
Ivan Gout 9.7k 2.8k 2.3k 1.7k 978 157 12.8k
George Panayotou 7.9k 0.8× 2.1k 0.8× 1.6k 0.7× 1.5k 0.9× 657 0.7× 155 11.1k
Stevan R. Hubbard 9.6k 1.0× 3.7k 1.3× 1.4k 0.6× 2.5k 1.5× 921 0.9× 89 14.4k
Edward Y. Skolnik 7.5k 0.8× 2.1k 0.8× 1.6k 0.7× 1.6k 0.9× 585 0.6× 84 11.2k
Andrius Kazlauskas 9.8k 1.0× 2.2k 0.8× 2.3k 1.0× 2.4k 1.4× 1.9k 1.9× 188 15.1k
Nicholas F. Totty 7.9k 0.8× 2.6k 0.9× 1.8k 0.7× 1.9k 1.2× 676 0.7× 66 11.3k
Ben Margolis 11.8k 1.2× 5.2k 1.9× 1.4k 0.6× 2.3k 1.4× 1.1k 1.1× 116 15.9k
Xosé R. Bustelo 7.0k 0.7× 1.9k 0.7× 2.8k 1.2× 2.0k 1.2× 687 0.7× 172 11.1k
J. Justin Hsuan 8.0k 0.8× 3.1k 1.1× 1.7k 0.7× 1.6k 1.0× 403 0.4× 97 11.9k
Lars Rönnstrand 5.9k 0.6× 1.2k 0.4× 2.0k 0.8× 2.0k 1.2× 506 0.5× 173 10.2k
Daniel D. Billadeau 7.5k 0.8× 3.2k 1.2× 4.5k 1.9× 2.9k 1.7× 465 0.5× 215 14.4k

Countries citing papers authored by Ivan Gout

Since Specialization
Citations

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

Fields of papers citing papers by Ivan Gout

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Ivan Gout. 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 Ivan Gout. The network helps show where Ivan Gout may publish in the future.

Co-authorship network of co-authors of Ivan Gout

This figure shows the co-authorship network connecting the top 25 collaborators of Ivan Gout. A scholar is included among the top collaborators of Ivan Gout 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 Ivan Gout. Ivan Gout 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.
Lin, Chao‐Chieh, Yi-Tzu Lin, Denise Dunn, et al.. (2025). Coenzyme A protects against ferroptosis via CoAlation of mitochondrial thioredoxin reductase. Journal of Clinical Investigation. 135(19).
2.
Bdzhola, Volodymyr G., Olivier E. Pardo, Michael J. Seckl, et al.. (2024). Investigating the Regulation of Ribosomal Protein S6 Kinase 1 by CoAlation. International Journal of Molecular Sciences. 25(16). 8747–8747. 2 indexed citations
3.
Brett, C., et al.. (2024). Immunofluorescent detection of protein CoAlation in mammalian cells under oxidative stress. Biology Open. 13(10). 1 indexed citations
4.
Tossounian, Maria‐Armineh, Darío A. Estrı́n, Madia Trujillo, et al.. (2023). A Unique Mode of Coenzyme A Binding to the Nucleotide Binding Pocket of Human Metastasis Suppressor NME1. International Journal of Molecular Sciences. 24(11). 9359–9359. 9 indexed citations
5.
Khalil, Mahmoud, Heba Ismail, Ganna Panasyuk, et al.. (2023). Asymmetric Dimethylation of Ribosomal S6 Kinase 2 Regulates Its Cellular Localisation and Pro-Survival Function. International Journal of Molecular Sciences. 24(10). 8806–8806. 2 indexed citations
6.
Filonenko, Valeriy, et al.. (2023). Changes of the Protein CoAlation Pattern in Response to Oxidative Stress and Capacitation in Human Spermatozoa. International Journal of Molecular Sciences. 24(15). 12526–12526. 6 indexed citations
7.
Tossounian, Maria‐Armineh, Sayoni Das, Darío A. Estrı́n, et al.. (2022). Profiling the Site of Protein CoAlation and Coenzyme A Stabilization Interactions. Antioxidants. 11(7). 1362–1362. 14 indexed citations
8.
Peak‐Chew, Sew‐Yeu, Amy Switzer, Lynn Burchell, et al.. (2021). Redox Regulation of the Quorum-sensing Transcription Factor AgrA by Coenzyme A. Antioxidants. 10(6). 841–841. 15 indexed citations
9.
Ahmed, Ahmed A., Chaojie Luo, Christopher Thrasivoulou, et al.. (2018). Three‐dimensional cancer cell culture in high‐yield multiscale scaffolds by shear spinning. Biotechnology Progress. 35(2). e2750–e2750. 5 indexed citations
10.
Gout, Ivan, et al.. (2012). Development of Monoclonal Antibodies Specific to Ribosomal Protein S6 Kinase 2. Hybridoma. 31(4). 289–294. 6 indexed citations
11.
Gryshkova, Vitalina, et al.. (2011). Generation of Monoclonal Antibodies Against Tumor-Associated Antigen MX35/sodium-Dependent Phosphate Transporter NaPi2b. Hybridoma. 30(1). 37–42. 7 indexed citations
12.
Kiyamova, Ramziya, Vitalina Gryshkova, Beatrice W.T. Yin, et al.. (2008). Development of Monoclonal Antibodies Specific for the Human Sodium-dependent Phosphate Co-transporter NaPi2b. Hybridoma. 27(4). 277–284. 18 indexed citations
13.
Filonenko, Valeriy, et al.. (2006). Generation and Characterization of Monoclonal Antibodies Against FABP4. Hybridoma. 25(2). 86–90. 8 indexed citations
14.
Pardo, Olivier E., Claudia Wellbrock, Muriel Aubert, et al.. (2006). FGF‐2 protects small cell lung cancer cells from apoptosis through a complex involving PKCε, B‐Raf and S6K2. The EMBO Journal. 25(13). 3078–3088. 144 indexed citations
15.
Panasyuk, Ganna, et al.. (2005). Generation and Characterization of Monoclonal Antibodies to Protein Kinase 2 (CK2) β Subunit. Hybridoma. 24(4). 206–210. 3 indexed citations
16.
Gout, Ivan, Kenta Hara, Yosuke Tsujishita, et al.. (1998). Molecular Cloning and Characterization of a Novel p70 S6 Kinase, p70 S6 Kinase β Containing a Proline-rich Region. Journal of Biological Chemistry. 273(46). 30061–30064. 124 indexed citations
17.
Banin, Sharon, O Truong, David R. Katz, et al.. (1996). Wiskott–Aldrich syndrome protein (WASp) is a binding partner for c-Src family protein-tyrosine kinases. Current Biology. 6(8). 981–988. 126 indexed citations
18.
Zvelebil, Marketa, Lindsay K. MacDougall, Sally J. Leevers, et al.. (1996). Structural and functional diversity of phosphoinositide 3-kinases. Philosophical Transactions of the Royal Society B Biological Sciences. 351(1336). 217–223. 86 indexed citations
19.
Panayotou, George, G Gish, Peter End, et al.. (1993). Interactions Between SH2 Domains and Tyrosine-Phosphorylated Platelet-Derived Growth Factor β-receptor Sequences: Analysis of Kinetic Parameters by a Novel Biosensor-Based Approach. Molecular and Cellular Biology. 13(6). 3567–3576. 31 indexed citations
20.
Booker, Grant W., Alexander L. Breeze, A. Kristina Downing, et al.. (1992). Structure of an SH2 domain of the p85α subunit of phosphatidylinositol-3-OH kinase. Nature. 358(6388). 684–687. 136 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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