Jonathan Backer

31.1k total citations · 6 hit papers
147 papers, 17.4k citations indexed

About

Jonathan Backer is a scholar working on Molecular Biology, Cell Biology and Surgery. According to data from OpenAlex, Jonathan Backer has authored 147 papers receiving a total of 17.4k indexed citations (citations by other indexed papers that have themselves been cited), including 120 papers in Molecular Biology, 62 papers in Cell Biology and 27 papers in Surgery. Recurrent topics in Jonathan Backer's work include Protein Kinase Regulation and GTPase Signaling (56 papers), Cellular transport and secretion (42 papers) and PI3K/AKT/mTOR signaling in cancer (28 papers). Jonathan Backer is often cited by papers focused on Protein Kinase Regulation and GTPase Signaling (56 papers), Cellular transport and secretion (42 papers) and PI3K/AKT/mTOR signaling in cancer (28 papers). Jonathan Backer collaborates with scholars based in United States, Germany and United Kingdom. Jonathan Backer's co-authors include Morris F. White, C. Ronald Kahn, Xiao‐Jian Sun, Martin G. Myers, Peter A. Wilden, James T. Murray, Paul Rothenberg, Ying Yan, Montserrat Miralpeix and E. Y. Skolnik and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Jonathan Backer

147 papers receiving 17.1k citations

Hit Papers

Structure of the insulin receptor substrate IRS-1 defines... 1991 2026 2002 2014 1991 1992 1993 2005 1999 400 800 1.2k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Jonathan Backer United States 71 12.6k 4.8k 2.4k 2.1k 2.0k 147 17.4k
John Bergeron Canada 69 10.0k 0.8× 6.5k 1.3× 1.8k 0.8× 1.4k 0.7× 1.5k 0.8× 184 14.8k
Timothy E. McGraw United States 55 8.0k 0.6× 3.9k 0.8× 2.4k 1.0× 967 0.5× 2.2k 1.1× 106 12.2k
Tamás Balla United States 74 15.3k 1.2× 8.6k 1.8× 1.6k 0.7× 1.6k 0.8× 2.3k 1.2× 225 21.6k
Toshiaki Katada Japan 69 13.1k 1.0× 3.7k 0.8× 1.5k 0.6× 678 0.3× 1.7k 0.9× 300 18.1k
Clive A. Slaughter United States 70 15.1k 1.2× 4.3k 0.9× 1.1k 0.5× 1.6k 0.8× 2.2k 1.1× 182 20.5k
Vesa M. Olkkonen Finland 60 6.3k 0.5× 4.0k 0.8× 2.8k 1.1× 1.7k 0.8× 1.6k 0.8× 235 11.2k
Enrique Rozengurt United Kingdom 99 22.2k 1.8× 5.2k 1.1× 3.3k 1.3× 1.3k 0.6× 2.5k 1.2× 504 32.9k
Phillip T. Hawkins United Kingdom 66 12.8k 1.0× 4.5k 0.9× 1.3k 0.5× 785 0.4× 1.6k 0.8× 181 18.7k
Wouter H. Moolenaar Netherlands 84 18.7k 1.5× 5.6k 1.2× 1.3k 0.6× 683 0.3× 2.8k 1.4× 198 23.4k
Sara C. Kozma United States 54 12.0k 1.0× 1.7k 0.3× 1.5k 0.6× 1.5k 0.7× 2.2k 1.1× 97 16.5k

Countries citing papers authored by Jonathan Backer

Since Specialization
Citations

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

Fields of papers citing papers by Jonathan Backer

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Jonathan Backer

This figure shows the co-authorship network connecting the top 25 collaborators of Jonathan Backer. A scholar is included among the top collaborators of Jonathan Backer 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 Jonathan Backer. Jonathan Backer 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.
Jakubik, Charles T., et al.. (2022). PIP3abundance overcomes PI3K signaling selectivity in invadopodia. FEBS Letters. 596(4). 417–426. 1 indexed citations
2.
Jakubik, Charles T., et al.. (2019). PI3Kβ is selectively required for growth factor-stimulated macropinocytosis. Journal of Cell Science. 132(16). 22 indexed citations
3.
Erami, Zahra, Bassem D. Khalil, Yanhua Yao, et al.. (2017). Rac1-stimulated macropinocytosis enhances Gβγ activation of PI3Kβ. Biochemical Journal. 474(23). 3903–3914. 18 indexed citations
4.
Khalil, Bassem D., Yanyan Cao, Widian F. Abi Saab, et al.. (2016). GPCR Signaling Mediates Tumor Metastasis via PI3Kβ. Cancer Research. 76(10). 2944–2953. 45 indexed citations
5.
LoPiccolo, Jaclyn, Seung Joong Kim, Yi Shi, et al.. (2015). Assembly and Molecular Architecture of the Phosphoinositide 3-Kinase p85α Homodimer. Journal of Biological Chemistry. 290(51). 30390–30405. 20 indexed citations
6.
Salamon, Rachel S. & Jonathan Backer. (2013). Phosphatidylinositol‐3,4,5‐trisphosphate: Tool of choice for class I PI 3‐kinases. BioEssays. 35(7). 602–611. 31 indexed citations
7.
Смирнова, Т. А., Rory Flinn, Jeffrey Wyckoff, et al.. (2011). Phosphoinositide 3-kinase signaling is critical for ErbB3-driven breast cancer cell motility and metastasis. Oncogene. 31(6). 706–715. 53 indexed citations
8.
Flinn, Rory, Antonia Patsialou, Jeffrey Wyckoff, et al.. (2009). Differential Enhancement of Breast Cancer Cell Motility and Metastasis by Helical and Kinase Domain Mutations of Class IA Phosphoinositide 3-Kinase. Cancer Research. 69(23). 8868–8876. 70 indexed citations
9.
Juhász, Gábor, Jahda H. Hill, Ying Yan, et al.. (2008). The class III PI(3)K Vps34 promotes autophagy and endocytosis but not TOR signaling in Drosophila. The Journal of Cell Biology. 181(4). 655–666. 251 indexed citations
10.
Cao, Canhong, Jonathan Backer, Jocelyn Laporte, Edward J. Bedrick, & Angela Wandinger‐Ness. (2008). Sequential Actions of Myotubularin Lipid Phosphatases Regulate Endosomal PI(3)P and Growth Factor Receptor Trafficking. Molecular Biology of the Cell. 19(8). 3334–3346. 105 indexed citations
11.
Sidani, Mazen, Deborah Wessels, Ghassan Mouneimne, et al.. (2007). Cofilin determines the migration behavior and turning frequency of metastatic cancer cells. The Journal of Cell Biology. 179(4). 777–791. 161 indexed citations
12.
Fu, Zheng, Eliah Aronoff‐Spencer, Haiyan Wu, Gary J. Gerfen, & Jonathan Backer. (2004). The iSH2 domain of PI 3-kinase is a rigid tether for p110 and not a conformational switch. Archives of Biochemistry and Biophysics. 432(2). 244–251. 20 indexed citations
13.
Summers, Scott A., et al.. (1999). Protein Kinase A-Dependent and -Independent Signaling Pathways Contribute to Cyclic AMP-Stimulated Proliferation. Molecular and Cellular Biology. 19(9). 5882–5891. 158 indexed citations
14.
Chen, Daxin, et al.. (1997). Specific Activation of p85-p110 Phosphatidylinositol 3′-Kinase Stimulates DNA Synthesis by ras- and p70 S6 Kinase-Dependent Pathways. Molecular and Cellular Biology. 17(1). 248–255. 66 indexed citations
15.
Chen, Daxin, et al.. (1995). Insulin Receptor Substrate 1 Rescues Insulin Action in CHO Cells Expressing Mutant Insulin Receptors That Lack a Juxtamembrane NPXY Motif. Molecular and Cellular Biology. 15(9). 4711–4717. 24 indexed citations
16.
Chuang, Lee‐Ming, Martin G. Myers, Jonathan Backer, et al.. (1993). Insulin-Stimulated Oocyte Maturation Requires Insulin Receptor Substrate 1 and Interaction with the SH2 Domains of Phosphatidylinositol 3-Kinase. Molecular and Cellular Biology. 13(11). 6653–6660. 14 indexed citations
17.
Wilden, Peter A., et al.. (1992). The role of insulin receptor kinase domain autophosphorylation in receptor-mediated activities. Analysis with insulin and anti-receptor antibodies.. Journal of Biological Chemistry. 267(19). 13719–13727. 92 indexed citations
18.
Backer, Jonathan & George L. King. (1991). Regulation of receptor-mediated endocytosis by phorbol esters. Biochemical Pharmacology. 41(9). 1267–1277. 36 indexed citations
19.
Sun, Xiao‐Jian, Paul Rothenberg, C. Ronald Kahn, et al.. (1991). Structure of the insulin receptor substrate IRS-1 defines a unique signal transduction protein. Nature. 352(6330). 73–77. 1321 indexed citations breakdown →
20.
Wilden, Peter A., et al.. (1990). The insulin receptor with phenylalanine replacing tyrosine-1146 provides evidence for separate signals regulating cellular metabolism and growth.. Proceedings of the National Academy of Sciences. 87(9). 3358–3362. 99 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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