Elisabeth Schaffner‐Reckinger

731 total citations
30 papers, 566 citations indexed

About

Elisabeth Schaffner‐Reckinger is a scholar working on Immunology and Allergy, Molecular Biology and Cell Biology. According to data from OpenAlex, Elisabeth Schaffner‐Reckinger has authored 30 papers receiving a total of 566 indexed citations (citations by other indexed papers that have themselves been cited), including 21 papers in Immunology and Allergy, 12 papers in Molecular Biology and 11 papers in Cell Biology. Recurrent topics in Elisabeth Schaffner‐Reckinger's work include Cell Adhesion Molecules Research (21 papers), Platelet Disorders and Treatments (9 papers) and Cellular Mechanics and Interactions (9 papers). Elisabeth Schaffner‐Reckinger is often cited by papers focused on Cell Adhesion Molecules Research (21 papers), Platelet Disorders and Treatments (9 papers) and Cellular Mechanics and Interactions (9 papers). Elisabeth Schaffner‐Reckinger collaborates with scholars based in Luxembourg, United Kingdom and France. Elisabeth Schaffner‐Reckinger's co-authors include Nelly Kieffer, Sébastien Plançon, Chantal Melchior, Willem H. Ouwehand, Ping Chen, Michèle Moes, Marie‐Christine Morel‐Kopp, Nicholas A. Watkins, Graham A. Smith and Evelyne Friederich and has published in prestigious journals such as Journal of Biological Chemistry, Blood and PLoS ONE.

In The Last Decade

Elisabeth Schaffner‐Reckinger

26 papers receiving 556 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Elisabeth Schaffner‐Reckinger Luxembourg 15 287 194 188 155 70 30 566
M N Blackburn United States 11 136 0.5× 248 1.3× 283 1.5× 182 1.2× 110 1.6× 13 737
W.C. Kouns Switzerland 14 427 1.5× 178 0.9× 445 2.4× 51 0.3× 68 1.0× 17 718
Bernadette Swart Australia 8 86 0.3× 141 0.7× 156 0.8× 40 0.3× 127 1.8× 14 389
Trish K. Lankford United States 12 172 0.6× 266 1.4× 37 0.2× 125 0.8× 73 1.0× 18 592
Grant E. Blouse United States 15 65 0.2× 226 1.2× 189 1.0× 77 0.5× 44 0.6× 29 522
Thomas Schürpf United States 10 189 0.7× 230 1.2× 37 0.2× 87 0.6× 145 2.1× 13 502
Mary Rose Burnham United States 9 399 1.4× 501 2.6× 39 0.2× 340 2.2× 115 1.6× 12 849
Durwin Tsay United States 7 216 0.8× 309 1.6× 37 0.2× 169 1.1× 267 3.8× 7 571
François Bourre France 10 135 0.5× 261 1.3× 100 0.5× 23 0.1× 23 0.3× 15 471
Pranshu Sahgal Finland 11 216 0.8× 334 1.7× 18 0.1× 231 1.5× 71 1.0× 15 622

Countries citing papers authored by Elisabeth Schaffner‐Reckinger

Since Specialization
Citations

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

Fields of papers citing papers by Elisabeth Schaffner‐Reckinger

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Elisabeth Schaffner‐Reckinger. 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 Elisabeth Schaffner‐Reckinger. The network helps show where Elisabeth Schaffner‐Reckinger may publish in the future.

Co-authorship network of co-authors of Elisabeth Schaffner‐Reckinger

This figure shows the co-authorship network connecting the top 25 collaborators of Elisabeth Schaffner‐Reckinger. A scholar is included among the top collaborators of Elisabeth Schaffner‐Reckinger 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 Elisabeth Schaffner‐Reckinger. Elisabeth Schaffner‐Reckinger 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.
Schaffner‐Reckinger, Elisabeth, et al.. (2025). The impact of RAS on cell differentiation in health and disease. Biochemical Journal. 482(22). 1737–1756.
2.
Schaffner‐Reckinger, Elisabeth, et al.. (2025). Drugging Ras trafficking—are there new roads to travel?. Open Repository and Bibliography (University of Luxembourg). 2(1). 1 indexed citations
3.
Schaffner‐Reckinger, Elisabeth, Ganesh babu Manoharan, Vladimir Vukić, et al.. (2024). An Improved PDE6D Inhibitor Combines with Sildenafil To Inhibit KRAS Mutant Cancer Cell Growth. Journal of Medicinal Chemistry. 67(11). 8569–8584. 8 indexed citations
4.
Schaffner‐Reckinger, Elisabeth, et al.. (2023). Eliminating oncogenic RAS: back to the future at the drawing board. Biochemical Society Transactions. 51(1). 447–456. 15 indexed citations
5.
Chippalkatti, Rohan, et al.. (2023). Abstract 3493: Drug targeting of KRAS accumulation on the cilium inhibits its stemness driving activity. Cancer Research. 83(7_Supplement). 3493–3493.
6.
Machado, Raquel A. C., et al.. (2021). L-plastin Ser5 phosphorylation is modulated by the PI3K/SGK pathway and promotes breast cancer cell invasiveness. Cell Communication and Signaling. 19(1). 22–22. 9 indexed citations
7.
Schaffner‐Reckinger, Elisabeth & Raquel A. C. Machado. (2020). The actin-bundling protein L-plastin—A double-edged sword: Beneficial for the immune response, maleficent in cancer. International review of cell and molecular biology. 355. 109–154. 8 indexed citations
8.
Schaffner‐Reckinger, Elisabeth, et al.. (2017). The PET and LIM1-2 domains of testin contribute to intramolecular and homodimeric interactions. PLoS ONE. 12(5). e0177879–e0177879. 5 indexed citations
9.
Halavatyi, Aliaksandr, Sandrine Medves, Marleen Van Troys, et al.. (2015). Delineating the Tes Interaction Site in Zyxin and Studying Cellular Effects of Its Disruption. PLoS ONE. 10(10). e0140511–e0140511. 5 indexed citations
10.
Lee, Wen‐Hwa, Elisabeth Schaffner‐Reckinger, Demokritos Tsoukatos, et al.. (2015). Inhibition of αIIbβ3 Ligand Binding by an αIIb Peptide that Clasps the Hybrid Domain to the βI Domain of β3. PLoS ONE. 10(9). e0134952–e0134952. 1 indexed citations
11.
Tanoury, Ziad Al, Elisabeth Schaffner‐Reckinger, Aliaksandr Halavatyi, et al.. (2010). Quantitative Kinetic Study of the Actin-Bundling Protein L-Plastin and of Its Impact on Actin Turn-Over. PLoS ONE. 5(2). e9210–e9210. 38 indexed citations
12.
Schaffner‐Reckinger, Elisabeth, Najet Debili, Julien Bellis, et al.. (2009). Overexpression of the partially activated αIIbβ3D723H integrin salt bridge mutant downregulates RhoA activity and induces microtubule‐dependent proplatelet–like extensions in Chinese hamster ovary cells. Journal of Thrombosis and Haemostasis. 7(7). 1207–1217. 19 indexed citations
13.
Janji, Bassam, Laurent Vallar, Ziad Al Tanoury, et al.. (2009). The actin filament cross‐linker L‐plastin confers resistance to TNF‐α in MCF‐7 breast cancer cells in a phosphorylation‐dependent manner. Journal of Cellular and Molecular Medicine. 14(6a). 1264–1275. 33 indexed citations
14.
Rodius, Sophie, Olivier Chaloin, Michèle Moes, et al.. (2008). The Talin Rod IBS2 α-Helix Interacts with the β3 Integrin Cytoplasmic Tail Membrane-proximal Helix by Establishing Charge Complementary Salt Bridges. Journal of Biological Chemistry. 283(35). 24212–24223. 48 indexed citations
15.
16.
Schaffner‐Reckinger, Elisabeth, et al.. (2005). A New Functional Role of the Fibrinogen RGD Motif as the Molecular Switch That Selectively Triggers Integrin αIIbβ3-dependent RhoA Activation during Cell Spreading. Journal of Biological Chemistry. 280(39). 33610–33619. 44 indexed citations
17.
Schaffner‐Reckinger, Elisabeth, et al.. (2005). RGD, the Rho’d to cell spreading. European Journal of Cell Biology. 85(3-4). 249–254. 23 indexed citations
18.
Watkins, Nicholas A., Elisabeth Schaffner‐Reckinger, David L. Allen, et al.. (2002). HPA-1a phenotype–genotype discrepancy reveals a naturally occurring Arg93Gln substitution in the platelet β3 integrin that disrupts the HPA-1a epitope. Blood. 99(5). 1833–1839. 30 indexed citations
19.
Watkins, Nicholas A., Elisabeth Schaffner‐Reckinger, Deonie Allen, et al.. (2000). A naturally occurring Arg -> Gln substitution at position 93 of platelet beta 3 integrin abolishes anti-HPA-1a binding.. Blood. 96.
20.
Schaffner‐Reckinger, Elisabeth, et al.. (1998). Distinct Involvement of β3 Integrin Cytoplasmic Domain Tyrosine Residues 747 and 759 in Integrin-mediated Cytoskeletal Assembly and Phosphotyrosine Signaling. Journal of Biological Chemistry. 273(20). 12623–12632. 67 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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