Irit Lax
About
Irit Lax is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Oncology.
According to data from OpenAlex, Irit Lax has authored 80 papers receiving a total of 11.6k indexed citations (citations by other indexed papers that have themselves been cited), including 64 papers in Molecular Biology, 30 papers in Radiology, Nuclear Medicine and Imaging and 21 papers in Oncology. Recurrent topics in Irit Lax's work include Monoclonal and Polyclonal Antibodies Research (30 papers), Fibroblast Growth Factor Research (24 papers) and Glycosylation and Glycoproteins Research (17 papers). Irit Lax is often cited by papers focused on Monoclonal and Polyclonal Antibodies Research (30 papers), Fibroblast Growth Factor Research (24 papers) and Glycosylation and Glycoproteins Research (17 papers). Irit Lax collaborates with scholars based in United States, Israel and Japan. Irit Lax's co-authors include Joseph Schlessinger, Veraragavan P. Eswarakumar, Yaron R. Hadari, Mark A. Lemmon, Towia A. Libermann, Haruhiko Kouhara, Richard Kris, Taly R. Spivak-Kroizman, Noriko Gotoh and A. Ullrich and has published in prestigious journals such as Nature, Cell and Proceedings of the National Academy of Sciences.
In The Last Decade
Irit Lax
79 papers receiving 11.2k citations
Hit Papers
Peers — A (Enhanced Table)
Peers by citation overlap · career bar shows stage (early→late) cites · hero ref
| Name | h | Career | Trend | Papers | Cites | |||||
|---|---|---|---|---|---|---|---|---|---|---|
| Irit Lax United States | 51 | 8.5k | 2.8k | 2.3k | 1.8k | 1.2k | 80 | 11.6k | ||
| Andrius Kazlauskas United States | 60 | 9.8k 1.2× | 2.4k 0.8× | 2.2k 1.0× | 1.9k 1.1× | 2.3k 1.9× | 188 | 15.1k | ||
| Gregory D. Plowman United States | 59 | 8.6k 1.0× | 5.0k 1.8× | 2.2k 1.0× | 2.2k 1.2× | 1.6k 1.3× | 98 | 13.8k | ||
| Albert J. Wong United States | 54 | 6.3k 0.7× | 3.8k 1.3× | 1.3k 0.6× | 1.2k 0.7× | 1.3k 1.1× | 94 | 10.5k | ||
| Paul Polakis United States | 64 | 17.8k 2.1× | 4.9k 1.8× | 3.1k 1.3× | 1.4k 0.8× | 1.3k 1.0× | 118 | 21.9k | ||
| S A Aaronson United States | 46 | 5.8k 0.7× | 3.1k 1.1× | 1.1k 0.5× | 1.3k 0.7× | 1.1k 0.9× | 98 | 9.6k | ||
| Ben Margolis United States | 67 | 11.8k 1.4× | 2.3k 0.8× | 5.2k 2.3× | 1.1k 0.6× | 1.4k 1.1× | 116 | 15.9k | ||
| Wilson H. Burgess United States | 53 | 7.5k 0.9× | 1.3k 0.5× | 2.6k 1.2× | 632 0.4× | 1.4k 1.1× | 106 | 11.3k | ||
| Martin L. Breitman Canada | 44 | 11.0k 1.3× | 3.0k 1.1× | 2.1k 0.9× | 530 0.3× | 1.4k 1.1× | 95 | 13.8k | ||
| Jorge Filmus Canada | 54 | 7.8k 0.9× | 2.7k 1.0× | 3.5k 1.5× | 723 0.4× | 1.2k 1.0× | 103 | 11.8k | ||
| Michael D. Schaller United States | 57 | 10.2k 1.2× | 3.0k 1.1× | 7.7k 3.4× | 1.7k 0.9× | 2.1k 1.7× | 106 | 18.4k |
Countries citing papers authored by Irit Lax
Since
Specialization
Citations
This map shows the geographic impact of Irit Lax'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 Irit Lax with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Irit Lax more than expected).
Fields of papers citing papers by Irit Lax
Since
Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences
This network shows the impact of papers produced by Irit Lax. 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 Irit Lax. The network helps show where Irit Lax may publish in the future.
Co-authorship network of co-authors of Irit Lax
This figure shows the co-authorship network connecting the top 25 collaborators of Irit Lax. A scholar is included among the top collaborators of Irit Lax 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 Irit Lax. Irit Lax is excluded from the visualization to improve readability, since they are connected to all nodes in the network.
All Works
1.
Krimmer, S.G., Yoshihisa Suzuki, Jyotidarsini Mohanty, et al.. (2023). Cryo-EM analyses of KIT and oncogenic mutants reveal structural oncogenic plasticity and a target for therapeutic intervention. Proceedings of the National Academy of Sciences. 120(13). e2300054120–e2300054120.
2.
Li, Tongqing, Steven E. Stayrook, Yuko Tsutsui, et al.. (2021). Structural basis for ligand reception by anaplastic lymphoma kinase. Nature. 600(7887). 148–152.
3.
Lee, Sangwon, Jungyuen Choi, Jyotidarsini Mohanty, et al.. (2018). Structures of β-klotho reveal a ‘zip code’-like mechanism for endocrine FGF signalling. Nature. 553(7689). 501–505.
4.
Opatowsky, Yarden, Irit Lax, Francisco Tomé, et al.. (2014). Structure, domain organization, and different conformational states of stem cell factor-induced intact KIT dimers. Proceedings of the National Academy of Sciences. 111(5). 1772–1777.
5.
Bae, Jae Hyun, Titus J. Boggon, Francisco Tomé, et al.. (2010). Asymmetric receptor contact is required for tyrosine autophosphorylation of fibroblast growth factor receptor in living cells. Proceedings of the National Academy of Sciences. 107(7). 2866–2871.
6.
Margulies, David H., Yarden Opatowsky, Steven Fletcher, et al.. (2009). Surface Binding Inhibitors of the SCF–KIT Protein–Protein Interaction. ChemBioChem. 10(12). 1955–1958.
7.
Eswarakumar, Veraragavan P., Irit Lax, & Joseph Schlessinger. (2005). Cellular signaling by fibroblast growth factor receptors. Cytokine & Growth Factor Reviews. 16(2). 139–149.
8.
Gotoh, Noriko, Shaked Laks, Misako Nakashima, Irit Lax, & Joseph Schlessinger. (2004). FRS2 family docking proteins with overlapping roles in activation of MAP kinase have distinct spatial‐temporal patterns of expression of their transcripts. FEBS Letters. 564(1-2). 14–18.
9.
Lamothe, Betty, Masashi Yamada, Ute Schaeper, et al.. (2004). The Docking Protein Gab1 Is an Essential Component of an Indirect Mechanism for Fibroblast Growth Factor Stimulation of the Phosphatidylinositol 3-Kinase/Akt Antiapoptotic Pathway. Molecular and Cellular Biology. 24(13). 5657–5666.
10.
Mattoon, Dawn, Peter S. Klein, Mark A. Lemmon, Irit Lax, & Joseph Schlessinger. (2004). The tethered configuration of the EGF receptor extracellular domain exerts only a limited control of receptor function. Proceedings of the National Academy of Sciences. 101(4). 923–928.
11.
Lax, Irit, Andy Kin On Wong, Betty Lamothe, et al.. (2002). The Docking Protein FRS2α Controls a MAP Kinase-Mediated Negative Feedback Mechanism for Signaling by FGF Receptors. Molecular Cell. 10(4). 709–719.
12.
Ong, S.H., Graeme R. Guy, Yaron R. Hadari, et al.. (2000). FRS2 Proteins Recruit Intracellular Signaling Pathways by Binding to Diverse Targets on Fibroblast Growth Factor and Nerve Growth Factor Receptors. Molecular and Cellular Biology. 20(3). 979–989.
13.
Hadari, Yaron R., Haruhiko Kouhara, Irit Lax, & Joseph Schlessinger. (1998). Binding of Shp2 Tyrosine Phosphatase to FRS2 Is Essential for Fibroblast Growth Factor-Induced PC12 Cell Differentiation. Molecular and Cellular Biology. 18(7). 3966–3973.
14.
Abe, Yoshito, Masafumi Odaka, Fuyuhiko Inagaki, et al.. (1998). Disulfide Bond Structure of Human Epidermal Growth Factor Receptor. Journal of Biological Chemistry. 273(18). 11150–11157.
15.
Moreno, Herman, Marcela S. Nadal, Elena Leznik, et al.. (1998). Nerve growth factor acutely reduces chemical transmission by means of postsynaptic TrkA-like receptors in squid giant synapse. Proceedings of the National Academy of Sciences. 95(25). 14997–15002.
16.
Schlessinger, Joseph, Irit Lax, & Mark A. Lemmon. (1995). Regulation of growth factor activation by proteoglycans: What is the role of the low affinity receptors?. Cell. 83(3). 357–360.
17.
Spivak-Kroizman, Taly R., Daniela Rotin, Dalia Pinchasi, et al.. (1992). Heterodimerization of c-erbB2 with different epidermal growth factor receptor mutants elicits stimulatory or inhibitory responses.. Journal of Biological Chemistry. 267(12). 8056–8063.
18.
Dull, Thomas J., et al.. (1989). HER2 cytoplasmic domain generates normal mitogenic and transforming signals in a chimeric receptor.. The EMBO Journal. 8(1). 167–173.
19.
Lax, Irit, Ann Johnson, R. Howk, et al.. (1988). Chicken Epidermal Growth Factor (EGF) Receptor: cDNA Cloning, Expression in Mouse Cells, and Differential Binding of EGF and Transforming Growth Factor Alpha. Molecular and Cellular Biology. 8(5). 1970–1978.
20.
Schlessinger, Joseph, Alain B. Schreiber, Andrea Levi, et al.. (1983). Regulation of Cell Proliferation by Epidermal Growth Factor. 14(2). 93–111.
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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