Daniel Lietha

2.7k total citations
31 papers, 2.1k citations indexed

About

Daniel Lietha is a scholar working on Molecular Biology, Immunology and Allergy and Cell Biology. According to data from OpenAlex, Daniel Lietha has authored 31 papers receiving a total of 2.1k indexed citations (citations by other indexed papers that have themselves been cited), including 21 papers in Molecular Biology, 19 papers in Immunology and Allergy and 17 papers in Cell Biology. Recurrent topics in Daniel Lietha's work include Cell Adhesion Molecules Research (19 papers), Cellular Mechanics and Interactions (12 papers) and Protein Kinase Regulation and GTPase Signaling (8 papers). Daniel Lietha is often cited by papers focused on Cell Adhesion Molecules Research (19 papers), Cellular Mechanics and Interactions (12 papers) and Protein Kinase Regulation and GTPase Signaling (8 papers). Daniel Lietha collaborates with scholars based in Spain, United States and Germany. Daniel Lietha's co-authors include Michael J. Eck, Michael D. Schaller, Xinming Cai, Derek F. Ceccarelli, Margaret C. Frame, Yiqun Li, Bryan Serrels, Hitesh Patel, Johanne Le Coq and Christiane Garbay and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Daniel Lietha

31 papers receiving 2.0k citations

Author Peers

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

Author Last Decade Papers Cites
Daniel Lietha 1.2k 909 834 327 210 31 2.1k
Sean Uryu 1.1k 0.9× 767 0.8× 908 1.1× 342 1.0× 292 1.4× 26 1.9k
Chungho Kim 1.4k 1.2× 1.0k 1.1× 1.6k 1.9× 246 0.8× 241 1.1× 53 3.0k
Jill K. Slack‐Davis 1.1k 0.9× 767 0.8× 661 0.8× 580 1.8× 358 1.7× 29 2.1k
Ian Pass 2.1k 1.7× 827 0.9× 402 0.5× 409 1.3× 458 2.2× 25 2.9k
Russell Bainer 988 0.8× 523 0.6× 168 0.2× 412 1.3× 212 1.0× 20 1.7k
Cheryl A. Borgman 1.0k 0.8× 768 0.8× 1.1k 1.3× 312 1.0× 294 1.4× 14 1.9k
Rebecca A. Worthylake 1.1k 0.9× 910 1.0× 527 0.6× 468 1.4× 109 0.5× 20 2.1k
Valerie J. Fincham 1.7k 1.4× 1.4k 1.5× 1.1k 1.3× 380 1.2× 253 1.2× 30 2.7k
Xiao Lei Chen 1.2k 1.0× 935 1.0× 1.1k 1.3× 467 1.4× 360 1.7× 32 2.3k
Emma T. Bowden 1.1k 0.9× 619 0.7× 330 0.4× 407 1.2× 319 1.5× 25 1.8k

Countries citing papers authored by Daniel Lietha

Since Specialization
Citations

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

Fields of papers citing papers by Daniel Lietha

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Daniel Lietha

This figure shows the co-authorship network connecting the top 25 collaborators of Daniel Lietha. A scholar is included among the top collaborators of Daniel Lietha 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 Daniel Lietha. Daniel Lietha 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.
Matesanz, Ruth, et al.. (2025). Phospho-regulated tethering of focal adhesion kinase to vinculin links force transduction to focal adhesion signaling. Cell Communication and Signaling. 23(1). 190–190. 2 indexed citations
2.
Bauer, Magnus S., Lukas F. Milles, Thomas Nicolaus, et al.. (2022). A tethered ligand assay to probe SARS-CoV-2:ACE2 interactions. Proceedings of the National Academy of Sciences. 119(14). e2114397119–e2114397119. 39 indexed citations
3.
Nozal, Vanesa, Loreto Martínez‐González, Paula Santana, et al.. (2022). TDP-43 Modulation by Tau-Tubulin Kinase 1 Inhibitors: A New Avenue for Future Amyotrophic Lateral Sclerosis Therapy. Journal of Medicinal Chemistry. 65(2). 1585–1607. 28 indexed citations
4.
Takahashi, Kohta, Kristiina Kanerva, Leonardo Almeida‐Souza, et al.. (2021). ORP2 couples LDL‐cholesterol transport to FAK activation by endosomal cholesterol/PI(4,5)P 2 exchange. The EMBO Journal. 40(14). e106871–e106871. 37 indexed citations
5.
Acebrón, Iván, Ricardo D. Righetto, Christina Schoenherr, et al.. (2020). Structural basis of Focal Adhesion Kinase activation on lipid membranes. The EMBO Journal. 39(19). e104743–e104743. 52 indexed citations
6.
Dawson, John C., Bryan Serrels, Adam Byron, et al.. (2019). A Synergistic Anticancer FAK and HDAC Inhibitor Combination Discovered by a Novel Chemical–Genetic High-Content Phenotypic Screen. Molecular Cancer Therapeutics. 19(2). 637–649. 19 indexed citations
7.
Yen‐Pon, Expédite, Bo Li, John C. Dawson, et al.. (2018). Structure-Based Design, Synthesis, and Characterization of the First Irreversible Inhibitor of Focal Adhesion Kinase. ACS Chemical Biology. 13(8). 2067–2073. 28 indexed citations
8.
Dao, Pascal, Daniel Lietha, Mélanie Ethève‐Quelquejeu, Christiane Garbay, & Huixiong Chen. (2017). Synthesis of novel 1,2,4-triazine scaffold as FAK inhibitors with antitumor activity. Bioorganic & Medicinal Chemistry Letters. 27(8). 1727–1730. 43 indexed citations
10.
Zhou, Jing, Agnieszka K. Bronowska, Johanne Le Coq, Daniel Lietha, & Frauke Gräter. (2015). Allosteric Regulation of Focal Adhesion Kinase by PIP2 and ATP. Biophysical Journal. 108(3). 698–705. 36 indexed citations
11.
Fawal, Mohamad-Ali, Clara M. Santiveri, Joshua Yang, et al.. (2015). Alternative Activation Mechanisms of Protein Kinase B Trigger Distinct Downstream Signaling Responses. Journal of Biological Chemistry. 290(41). 24975–24985. 14 indexed citations
12.
Dao, Pascal, Rafika Jarray, Nikaïa Smith, et al.. (2014). Inhibition of both focal adhesion kinase and fibroblast growth factor receptor 2 pathways induces anti-tumor and anti-angiogenic activities. Cancer Letters. 348(1-2). 88–99. 21 indexed citations
13.
Dao, Pascal, Rafika Jarray, Johanne Le Coq, et al.. (2013). Synthesis of novel diarylamino-1,3,5-triazine derivatives as FAK inhibitors with anti-angiogenic activity. Bioorganic & Medicinal Chemistry Letters. 23(16). 4552–4556. 57 indexed citations
14.
Chang, Fumin, Christopher A. Lemmon, Daniel Lietha, Michael J. Eck, & Lewis H. Romer. (2011). Tyrosine Phosphorylation of Rac1: A Role in Regulation of Cell Spreading. PLoS ONE. 6(12). e28587–e28587. 50 indexed citations
15.
Frame, Margaret C., Hitesh Patel, Bryan Serrels, Daniel Lietha, & Michael J. Eck. (2010). The FERM domain: organizing the structure and function of FAK. Nature Reviews Molecular Cell Biology. 11(11). 802–814. 290 indexed citations
16.
Lietha, Daniel & Michael J. Eck. (2008). Crystal Structures of the FAK Kinase in Complex with TAE226 and Related Bis-Anilino Pyrimidine Inhibitors Reveal a Helical DFG Conformation. PLoS ONE. 3(11). e3800–e3800. 91 indexed citations
17.
Lietha, Daniel, Xinming Cai, Derek F. Ceccarelli, et al.. (2007). Structural Basis for the Autoinhibition of Focal Adhesion Kinase. Cell. 129(6). 1177–1187. 371 indexed citations
18.
Lyon, Malcolm, Jon A. Deakin, Daniel Lietha, Ermanno Gherardi, & John T. Gallagher. (2004). The Interactions of Hepatocyte Growth Factor/Scatter Factor and Its NK1 and NK2 Variants with Glycosaminoglycans Using a Modified Gel Mobility Shift Assay. Journal of Biological Chemistry. 279(42). 43560–43567. 49 indexed citations
19.
Watanabe, Keiichi, Dimitri Y. Chirgadze, Daniel Lietha, et al.. (2002). A New Crystal Form of the NK1 Splice Variant of HGF/SF Demonstrates Extensive Hinge Movement and Suggests That the NK1 Dimer Originates by Domain Swapping. Journal of Molecular Biology. 319(2). 283–288. 17 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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