Ruth Lupu
About
Ruth Lupu is a scholar working on Molecular Biology, Cancer Research and Oncology.
According to data from OpenAlex, Ruth Lupu has authored 143 papers receiving a total of 9.7k indexed citations (citations by other indexed papers that have themselves been cited), including 95 papers in Molecular Biology, 65 papers in Cancer Research and 61 papers in Oncology. Recurrent topics in Ruth Lupu's work include Cancer, Lipids, and Metabolism (55 papers), HER2/EGFR in Cancer Research (43 papers) and Cancer, Hypoxia, and Metabolism (27 papers). Ruth Lupu is often cited by papers focused on Cancer, Lipids, and Metabolism (55 papers), HER2/EGFR in Cancer Research (43 papers) and Cancer, Hypoxia, and Metabolism (27 papers). Ruth Lupu collaborates with scholars based in United States, Spain and Argentina. Ruth Lupu's co-authors include Javier A. Menéndez, Rámón Colomer, Luciano Vellón, Inderjit Mehmi, Marc E. Lippman, A E Hornby, Santiago Ropero, Valerie M. Weaver, Fei Wang and Per Briand and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of Clinical Investigation.
In The Last Decade
Ruth Lupu
142 papers receiving 9.6k 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 | |||||
|---|---|---|---|---|---|---|---|---|---|---|
| Ruth Lupu United States | 54 | 6.2k | 4.3k | 2.8k | 917 | 831 | 143 | 9.7k | ||
| Juan Carlos Lacal Spain | 54 | 5.7k 0.9× | 1.8k 0.4× | 1.8k 0.7× | 785 0.9× | 501 0.6× | 162 | 8.4k | ||
| Georgia Hatzivassiliou United States | 23 | 6.0k 1.0× | 4.0k 0.9× | 1.1k 0.4× | 275 0.3× | 358 0.4× | 34 | 8.6k | ||
| Gail E. Sonenshein United States | 62 | 6.7k 1.1× | 3.3k 0.8× | 2.8k 1.0× | 338 0.4× | 1.0k 1.2× | 155 | 10.9k | ||
| Takao Yamori Japan | 57 | 7.7k 1.2× | 1.3k 0.3× | 2.4k 0.9× | 312 0.3× | 536 0.6× | 241 | 11.7k | ||
| Dean G. Tang United States | 66 | 8.6k 1.4× | 4.5k 1.0× | 5.3k 1.9× | 284 0.3× | 883 1.1× | 172 | 14.4k | ||
| Raymond E. Meyn United States | 49 | 4.5k 0.7× | 1.6k 0.4× | 2.5k 0.9× | 695 0.8× | 640 0.8× | 135 | 7.0k | ||
| Ubaldo Martinez‐Outschoorn United States | 63 | 10.1k 1.6× | 8.3k 1.9× | 3.8k 1.4× | 276 0.3× | 369 0.4× | 147 | 14.8k | ||
| Nicholas Mitsiades United States | 66 | 10.1k 1.6× | 2.4k 0.6× | 4.5k 1.6× | 823 0.9× | 653 0.8× | 172 | 15.3k | ||
| Keping Xie United States | 71 | 11.0k 1.8× | 5.4k 1.2× | 5.5k 2.0× | 284 0.3× | 1.1k 1.3× | 210 | 17.2k | ||
| Heather R. Christofk United States | 35 | 6.0k 1.0× | 4.0k 0.9× | 1.1k 0.4× | 181 0.2× | 478 0.6× | 72 | 8.5k |
Countries citing papers authored by Ruth Lupu
Since
Specialization
Citations
This map shows the geographic impact of Ruth Lupu'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 Ruth Lupu with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Ruth Lupu more than expected).
Fields of papers citing papers by Ruth Lupu
Since
Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences
This network shows the impact of papers produced by Ruth Lupu. 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 Ruth Lupu. The network helps show where Ruth Lupu may publish in the future.
Co-authorship network of co-authors of Ruth Lupu
This figure shows the co-authorship network connecting the top 25 collaborators of Ruth Lupu. A scholar is included among the top collaborators of Ruth Lupu 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 Ruth Lupu. Ruth Lupu is excluded from the visualization to improve readability, since they are connected to all nodes in the network.
All Works
1.
Verdura, Sara, Eva Martinez‐Balibrea, Joaquim Bosch‐Barrera, et al.. (2025). Mitochondrial priming and response to BH3 mimetics in “one-two punch” senogenic-senolytic strategies. Cell Death Discovery. 11(1). 91–91.
2.
Cuyàs, Elisabet, Salvador Fernández‐Arroyo, Sara Verdura, et al.. (2022). Metabolomic and Mitochondrial Fingerprinting of the Epithelial-to-Mesenchymal Transition (EMT) in Non-Tumorigenic and Tumorigenic Human Breast Cells. Cancers. 14(24). 6214–6214.
3.
Schroeder, Barbara, Ingrid Espinoza, Zeng Hu, et al.. (2021). Fatty acid synthase (FASN) regulates the mitochondrial priming of cancer cells. Cell Death and Disease. 12(11). 977–977.
4.
Menéndez, Javier A., Adriana Papadimitropoulou, Elisabet Cuyàs, et al.. (2021). Fatty Acid Synthase Confers Tamoxifen Resistance to ER+/HER2+ Breast Cancer. Cancers. 13(5). 1132–1132.
5.
Cuyàs, Elisabet, Sara Verdura, Begoña Martı́n-Castillo, et al.. (2020). Tumor Cell-Intrinsic Immunometabolism and Precision Nutrition in Cancer Immunotherapy. Cancers. 12(7). 1757–1757.
6.
Menéndez, Javier A., Inderjit Mehmi, Adriana Papadimitropoulou, et al.. (2020). Fatty Acid Synthase Is a Key Enabler for Endocrine Resistance in Heregulin-Overexpressing Luminal B-Like Breast Cancer. International Journal of Molecular Sciences. 21(20). 7661–7661.
7.
Menéndez, Javier A., Barbara Schroeder, Luciano Vellón, et al.. (2015). Blockade of a Key Region in the Extracellular Domain Inhibits HER2 Dimerization and Signaling. JNCI Journal of the National Cancer Institute. 107(6). djv090–djv090.
8.
Vázquez‐Martín, Alejandro, Bruna Corominas-Faja, Sílvia Cufí, et al.. (2013). The mitochondrial H+-ATP synthase and the lipogenic switch. Cell Cycle. 12(2). 207–218.
9.
Li, Binghui, et al.. (2007). Inhibition of fatty acid synthase induces reactive oxygen species (ROS) to inhibit HER2 overexpressing breast cancer cell growth. Cancer Research. 67. 4462–4462.
10.
Menéndez, Javier A., Gershon Y. Locker, & Ruth Lupu. (2005). Regulation of Fatty Acid Synthase (FAS) gene expression by Peroxisome Proliferator-activated receptor-gamma (PPARγ) is dependent of Her-2/neu (erbB-2) signaling in breast cancer cells. Cancer Research. 65. 877–877.
11.
Menéndez, Javier A., et al.. (2005). In support of Fatty Acid Synthase (FAS) as a metabolic oncogene in breast cancer: Extracellular acidosis acts in an epigenetic fashion activating Fatty Acid Synthase (FAS) gene expression in non-cancerous human breast epithelial MCF10A and breast cancer MCF-7 cells. Cancer Research. 65. 655–655.
12.
Menéndez, Javier A., Luciano Vellón, & Ruth Lupu. (2005). Antitumoral actions of the anti-obesity drug orlistat (Xenical™) in breast cancer cells: blockade of cell cycle progression, promotion of apoptotic cell death and PEA3-mediated transcriptional repression of Her2/neu (erbB-2) oncogene. Annals of Oncology. 16(8). 1253–1267.
13.
Puricelli, Lydia, Letícia Labriola, Mariana Salatino, et al.. (2002). Heregulin inhibits proliferation via ERKs and phosphatidyl‐inositol 3‐kinase activation but regulates urokinase plasminogen activator independently of these pathways in metastatic mammary tumor cells. International Journal of Cancer. 100(6). 642–653.
14.
Balañá, María Eugenia, Ruth Lupu, Letícia Labriola, Eduardo H. Charreau, & Patricia V. Elizalde. (1999). Interactions between progestins and heregulin (HRG) signaling pathways: HRG acts as mediator of progestins proliferative effects in mouse mammary adenocarcinomas. Oncogene. 18(46). 6370–6379.
15.
Tang, Careen K., et al.. (1996). Involvement of heregulin-beta2 in the acquisition of the hormone-independent phenotype of breast cancer cells.. PubMed. 56(14). 3350–8.
16.
Ávila, Matías A., et al.. (1995). Hyperactive autocrine loop mediated by a NDF-related factor in neoplastic hamster embryo fibroblasts expressing an activated cph oncogene.. PubMed. 10(5). 963–71.
17.
Bacus, S S, Andrei V. Gudkov, C R Zelnick, et al.. (1993). Neu differentiation factor (heregulin) induces expression of intercellular adhesion molecule 1: implications for mammary tumors.. PubMed. 53(21). 5251–61.
18.
Noguchi, Masayuki, Masaaki Murakami, William P. Bennett, et al.. (1993). Biological consequences of overexpression of a transfected c-erbB-2 gene in immortalized human bronchial epithelial cells.. PubMed. 53(9). 2035–43.
19.
Pérez, Caridad N., et al.. (1993). Characterization and cloning of the gp30 ligand for the erbB-2 receptor, from human breast cancer cells. 34. 97.
20.
Bacus, S S, Eliezer Huberman, D Chin, et al.. (1992). A ligand for the erbB-2 oncogene product (gp30) induces differentiation of human breast cancer cells.. PubMed. 3(7). 401–11.
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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