Academic literature on the topic 'FGF2 Signaling'

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Journal articles on the topic "FGF2 Signaling"

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Bellosta, Paola, Akiyo Iwahori, Alexander N. Plotnikov, Anna V. Eliseenkova, Claudio Basilico, and Moosa Mohammadi. "Identification of Receptor and Heparin Binding Sites in Fibroblast Growth Factor 4 by Structure-Based Mutagenesis." Molecular and Cellular Biology 21, no. 17 (2001): 5946–57. http://dx.doi.org/10.1128/mcb.21.17.5946-5957.2001.

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ABSTRACT Fibroblast growth factors (FGFs) comprise a large family of multifunctional, heparin-binding polypeptides that show diverse patterns of interaction with a family of receptors (FGFR1 to -4) that are subject to alternative splicing. FGFR binding specificity is an essential mechanism in the regulation of FGF signaling and is achieved through primary sequence differences among FGFs and FGFRs and through usage of two alternative exons, IIIc and IIIb, for the second half of immunoglobulin-like domain 3 (D3) in FGFRs. While FGF4 binds and activates the IIIc splice forms of FGFR1 to -3 at com
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Britto, Jonathan A., Robert D. Evans, Richard D. Hayward та Barry M. Jones. "Toward Pathogenesis of Apert Cleft Palate: FGF, FGFR, and TGFβ Genes Are Differentially Expressed in Sequential Stages of Human Palatal Shelf Fusion". Cleft Palate-Craniofacial Journal 39, № 3 (2002): 332–40. http://dx.doi.org/10.1597/1545-1569_2002_039_0332_tpoacp_2.0.co_2.

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Objective: Critical cellular events at the palatal medial edge epithelium (MEE) occur in unperturbed mammalian palatogenesis, the molecular control of which involves a number of growth factors including transforming growth factor β3 (TGFβ3). Apert syndrome is a monogenic human disorder in which cleft palate has been significantly correlated to the fibroblast growth factor receptor (FGFR) 2-Ser252Trp mutation. We report the relative expression of these genes in human palatogenesis. Methods: The expression of the IgIIIa/b and IgIIIa/c transcript isoforms of FGFR2 and the proteins FGFR1, FGFR2, a
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Kwabi-Addo, B., M. Ozen, and M. Ittmann. "The role of fibroblast growth factors and their receptors in prostate cancer." Endocrine-Related Cancer 11, no. 4 (2004): 709–24. http://dx.doi.org/10.1677/erc.1.00535.

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Prostate cancer is the most common malignancy in men in the USA and the second leading cause of cancer deaths. Fibroblast growth factors (FGFs), including FGF1 (acidic FGF), FGF2 (basic FGF), FGF6 and FGF8 are all expressed at increased levels in prostate cancer as paracrine and/or autocrine growth factors for the prostate cancer cells. In addition, increased mobilization of FGFs from the extracellular matrix in cancer tissues can increase the availability of FGFs to cancer cells. Prostate cancer epithelial cells express all four types of FGF receptors (FGFR-1 to -4) at variable frequencies. E
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Price, Christopher A. "Mechanisms of fibroblast growth factor signaling in the ovarian follicle." Journal of Endocrinology 228, no. 2 (2015): R31—R43. http://dx.doi.org/10.1530/joe-15-0414.

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Fibroblast growth factors (FGFs) have been shown to alter growth and differentiation of reproductive tissues in a variety of species. Within the female reproductive tract, the effects of FGFs have been focused on the ovary, and the most studied one is FGF2, which stimulates granulosa cell proliferation and decreases differentiation (decreased steroidogenesis). Other FGFs have also been implicated in ovarian function, and this review summarizes the effects of members of two subfamilies on ovarian function; the FGF7 subfamily that also contains FGF10, and the FGF8 subfamily that also contains FG
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Yeh, Brian K., Anna V. Eliseenkova, Alexander N. Plotnikov, et al. "Structural Basis for Activation of Fibroblast Growth Factor Signaling by Sucrose Octasulfate." Molecular and Cellular Biology 22, no. 20 (2002): 7184–92. http://dx.doi.org/10.1128/mcb.22.20.7184-7192.2002.

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ABSTRACT Sucrose octasulfate (SOS) is believed to stimulate fibroblast growth factor (FGF) signaling by binding and stabilizing FGFs. In this report, we show that SOS induces FGF-dependent dimerization of FGF receptors (FGFRs). The crystal structure of the dimeric FGF2-FGFR1-SOS complex at 2.6-Å resolution reveals a symmetric assemblage of two 1:1:1 FGF2-FGFR1-SOS ternary complexes. Within each ternary complex SOS binds to FGF and FGFR and thereby increases FGF-FGFR affinity. SOS also interacts with the adjoining FGFR and thereby promotes protein-protein interactions that stabilize dimerizati
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Karajannis, Matthias A., Loïc Vincent, Fan Zhang, et al. "Fibroblast Growth Factor Receptor-1 Expression and Signaling in Acute Myeloid Leukemia." Blood 104, no. 11 (2004): 4477. http://dx.doi.org/10.1182/blood.v104.11.4477.4477.

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Abstract Fibroblast growth factor receptors (FGFRs) are tyrosine kinase receptors affecting cell proliferation, motility and survival. Fibroblast growth factor 2 (FGF2, basic FGF) represents the prototype FGFR ligand. Expression of FGFRs has been demonstrated in a subset of acute myeloid leukemias (AMLs) and FGF2 is overexpressed in the bone marrow of AML patients. The role of FGF/FGFR signaling in AML however is controversial, and downstream signaling cascades activated by FGFR1 are not known. Therefore, we hypothesized that subsets of primary acute leukemic cells may express functional FGFR1
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Naimy, Hicham, Jo Ann Buczek-Thomas, Matthew A. Nugent, Nancy Leymarie, and Joseph Zaia. "Highly Sulfated Nonreducing End-derived Heparan Sulfate Domains Bind Fibroblast Growth Factor-2 with High Affinity and Are Enriched in Biologically Active Fractions." Journal of Biological Chemistry 286, no. 22 (2011): 19311–19. http://dx.doi.org/10.1074/jbc.m110.204693.

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Human fibroblast growth factor-2 (FGF2) regulates cellular processes including proliferation, adhesion, motility, and angiogenesis. FGF2 exerts its biological function by binding and dimerizing its receptor (FGFR), which activates signal transduction cascades. Effective binding of FGF2 to its receptor requires the presence of heparan sulfate (HS), a linear polysaccharide with N-sulfated domains (NS) localized at the cell surface and extracellular matrix. HS acts as a platform facilitating the formation of a functional FGF-FGFR-HS ternary complex. Crystal structures of the signaling ternary com
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Bei, M., and R. Maas. "FGFs and BMP4 induce both Msx1-independent and Msx1-dependent signaling pathways in early tooth development." Development 125, no. 21 (1998): 4325–33. http://dx.doi.org/10.1242/dev.125.21.4325.

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During early tooth development, multiple signaling molecules are expressed in the dental lamina epithelium and induce the dental mesenchyme. One signal, BMP4, has been shown to induce morphologic changes in dental mesenchyme and mesenchymal gene expression via Msx1, but BMP4 cannot substitute for all the inductive functions of the dental epithelium. To investigate the role of FGFs during early tooth development, we examined the expression of epithelial and mesenchymal Fgfs in wild-type and Msx1 mutant tooth germs and tested the ability of FGFs to induce Fgf3 and Bmp4 expression in wild-type an
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Kumar, Karthiga Santhana, Cyrill Brunner, Matthias Schuster, et al. "MODL-14. SMALL MOLECULE TARGETING OF ONCOGENIC FGF2-FGFR SIGNALING IN BRAIN TUMORS." Neuro-Oncology 22, Supplement_3 (2020): iii413—iii414. http://dx.doi.org/10.1093/neuonc/noaa222.588.

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Abstract FGF2, the ligand of FGF receptors (FGFRs), is expressed in the developing and adult brain. FGF2-FGFR1 signaling causes the induction and maintenance of cancer stem cells through ERK-dependent up-regulation of ZEB1 and Olig2 in glioblastoma. In SHH medulloblastoma, Olig2 triggers tumor initiation from GCPs, maintains quiescent stem-like cells during the disease and contributes to tumor outgrowth at recurrence. We found that FGF2-FGFR signaling causes increased growth and tissue invasion through the FGFR adaptor protein FRS2 in SHH and group-3 medulloblastoma 1. Thus, targeting of FGFR-
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Dettmer, Rabea, Karsten Cirksena, Julia Münchhoff, et al. "FGF2 Inhibits Early Pancreatic Lineage Specification during Differentiation of Human Embryonic Stem Cells." Cells 9, no. 9 (2020): 1927. http://dx.doi.org/10.3390/cells9091927.

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Growth factors are important regulators during organ development. For many vertebrates (but not humans) it is known how they contribute to the formation and expansion of PDX1-positive cells during pancreas organogenesis. Here, the effects of the fibroblast growth factors FGF2, FGF7, FGF10, and epidermal growth factor (EGF) on pancreas development in humans were assessed by using human pluripotent stem cells (hPSCs). During this, FGF2 was identified as a potent anti-pancreatic factor whereas FGF7, FGF10, and EGF increased the cell mass while retaining PDX1-positivity. FGF2 increased the express
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Dissertations / Theses on the topic "FGF2 Signaling"

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BENNETT, MICHAEL R. "PERTURBATIONS IN OLIGODENDROCYTE PROGENITOR GROWTH AND DIFFERENTIATION: NEUROFIBROMIN AND FGF2 SIGNALING." University of Cincinnati / OhioLINK, 2004. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1100015367.

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Bennett, Michael R. "Perturbations in oligodendrocyte progenitor growth and differentiation neurofibromin and FGF2 signaling /." Cincinnati, Ohio : University of Cincinnati, 2004. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=ucin1100015367.

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Dolivo, David. "Fibroblast activation and pro-fibrotic phenotypes: modulation by FGF2 and MAPK signaling." Digital WPI, 2018. https://digitalcommons.wpi.edu/etd-dissertations/477.

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Fibrotic diseases are a leading cause of morbidity and mortality in the developed world. Despite this, the lack of therapies for fibrotic pathological disease states is severe. A large part of the reason for this lack of viable therapies is due to an incomplete understanding of the early processes driving tissue fibrosis, as well as the dismal results of pharmacologic monotherapies at the clinical trial stage in humans thus far. Therefore, better understanding of the upstream mechanisms driving tissue fibrosis is imperative. One of the common mechanisms underlying all fibroses is the presence
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Payne, Laura Beth. "Differential Impact of VEGF and FGF2 Signaling Mechanisms on Flt1 Pre-mRNA Splicing." Diss., Virginia Tech, 2016. http://hdl.handle.net/10919/81133.

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The human proteome is exponentially derived from a limited number of genes via alternative splicing, where one gene gives rise to multiple proteins. Alternatively spliced gene products, although crucial for normal physiology, are also linked to an increasing number of pathologies. Consequently, a growing focus is currently being placed on elucidating the extrinsic cues and ensuing signaling mechanisms which direct changes in gene splicing to yield functionally distinct proteins. Of note is the dysregulation of the vascular endothelial growth factor (VEGF) receptor, Flt1 and its soluble splice
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Olson, Nels Eric. "FGF2 is weakly mitogenic for intimal smooth muscle cells : role of FGF receptor expression, cytoplasmic signaling and cell cycle regulation /." Thesis, Connect to this title online; UW restricted, 2000. http://hdl.handle.net/1773/6335.

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Kinkl, Norbert. "Mechanisms of action of fibroblast growth factor 2 (FGF2) in rat retinal cells : photoreceptor survival and intracellular signaling." Université Louis Pasteur (Strasbourg) (1971-2008), 2001. http://www.theses.fr/2001STR13166.

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La dégénérescence des photorécepteurs est à l'origine de nombreuses pathologies rétiniennes aboutissant à une malvoyance voire à la cécité. Les facteurs neurotrophiques représentent une approche thérapeutique potentielle. Au cours de cette thèse nous nous sommes intéressés aux mécanismes d'actions in vitro d'un facteur neurotrophique exprimé dans la rétine, le FGF2. Afin d'étudier les effets directs du FGF2 sur la survie des photorécepteurs, nous avons mis au point un nouveau modèle de culture pure en photorécepteurs à partir de rétine jeune de rat. La pureté en photorécepteurs des cultures es
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Kolanczyk, Maria Elzbieta. "Signaling mechanisms and developmental function of fibroblast growth factor receptors in zebrafish." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2009. http://nbn-resolving.de/urn:nbn:de:bsz:14-ds-1242722157657-12154.

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Fibroblast growth factor (Fgf) signaling plays multiple inductive roles during development of vertebrates (Itoh 2007). Some Fgfs, such as Fgf8, are locally secreted and signal over a long range to provide positional information in the target tissue (Scholpp and Brand 2004). Fgf ligands signal in a receptor-dependent manner via tyrosine kinase receptors, four of which have been so far identified. Fgf8 signaling was shown to depend both on receptor activation as well as endocytosis. The specificity of Fgf ligands and receptors as well as the function of receptors in the control of the Fgf signal
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Goetz, Rebekka [Verfasser], and Annette [Akademischer Betreuer] Neubüser. "FGF signaling in mouse olfactory placode development = Der FGF Signalweg und seine Rolle während der Entwicklung des olfaktorischen Systems der Maus." Freiburg : Universität, 2012. http://d-nb.info/1123472912/34.

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Bobbs, Alexander Sebastian. "FGF Signaling During Gastrulation and Cardiogenesis." Diss., The University of Arizona, 2012. http://hdl.handle.net/10150/265335.

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An early event in animal development is the formation of the three primary germ layers that define the body plan. During gastrulation, cells migrate through the primitive streak of the embryo and undergo changes in morphology and gene expression, thus creating the mesodermal and endodermal cell layers. Gastrulation requires expression of Fibroblast Growth Factor (FGF), Wnt, and Platelet-Derived Growth Factor (PDGF). Embryos treated with FGF inhibitors fail to gastrulate, as cell migration is completely halted. During gastrulation, 44 microRNAs are expressed in the primitive streak of G. gallus
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Stewart, Courtney Elizabeth. "Astrocyte Development and Function is FGF8 Signaling Dependent." Kent State University / OhioLINK, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=kent1556290142104336.

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Books on the topic "FGF2 Signaling"

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Fibroblast Growth Factor Receptor (FGFR) Signaling Pathway in Tumor. MDPI, 2020. http://dx.doi.org/10.3390/books978-3-03936-785-6.

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Book chapters on the topic "FGF2 Signaling"

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Katoh, Masaru, Giorgio Berton, Anna Baruzzi, et al. "FGF2." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100437.

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Driguez, Pierre-Alexandre. "Synthesis of Natural and Nonnatural Heparin Fragments: Optimizations and Applications toward Modulation of FGF2-Mediated FGFR Signaling." In Modern Synthetic Methods in Carbohydrate Chemistry. Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527658947.ch7.

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Mohammadi, Moosa, and Andrew Beenken. "FGF-FGFR Signaling in Cancer." In Cancer Therapeutic Targets. Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4419-0717-2_19.

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Mohammadi, Moosa, and Andrew Beenken. "FGF-FGFR Signaling in Cancer." In Cancer Therapeutic Targets. Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4614-6613-0_19-4.

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Marie, Pierre J. "FGF/FGFR Signaling in Skeletal Dysplasias." In Bone and Development. Springer London, 2010. http://dx.doi.org/10.1007/978-1-84882-822-3_6.

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Katoh, Masaru, Giorgio Berton, Anna Baruzzi, et al. "FGF1." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100427.

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Katoh, Masaru, Giorgio Berton, Anna Baruzzi, et al. "FGF12." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100430.

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Katoh, Masaru, Giorgio Berton, Anna Baruzzi, et al. "FGF20." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100438.

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Katoh, Masaru, Giorgio Berton, Anna Baruzzi, et al. "FGF21." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100440.

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Katoh, Masaru, Giorgio Berton, Anna Baruzzi, et al. "FGF22." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100441.

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Conference papers on the topic "FGF2 Signaling"

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Izikki, M., C. Guignabert, E. Fadel, et al. "Role for Dysregulated Endothelium-Derived FGF2 Signaling in Progression of Pulmonary Hypertension." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a1820.

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Coleman, Stacey, Hemant Kocher, and Richard Grose. "Abstract B65: Investigating the role of nuclear FGF2 signaling in pancreatic cancer." In Abstracts: AACR Special Conference on Pancreatic Cancer: Progress and Challenges; June 18-21, 2012; Lake Tahoe, NV. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.panca2012-b65.

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Fortier, S. M., L. R. K. Penke та M. Peters-Golden. "FGF2 and PGE2 Utilize Distinct Signaling Pathways to Accelerate the Degradation of αSma mRNA in Human Lung Myofibroblasts". У American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a5536.

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Wesley, Umadevi V., Cedric S. Wesley, and Robert J. Dempsey. "Abstract 4979: Co-operative role for Notch and fibroblast growth factor FGF2 signaling pathways in maintaining malignant phenotype of neuroblastoma: Potential targets for neuroblastoma growth inhibition." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4979.

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Turcatel, G., G. Carraro, D. Tefft, R. Costa, and D. Warburton. "Mir-99a Coordinates FGFs and mTor Signaling Pathways during Lung Development." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a2486.

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Dadone-Montaudié, Bérengère, Audrey Laroche-Clary, Aline Mongis, et al. "Abstract 5185: Analysis of the role of FGFR signaling in liposarcomas: Dual targeting of FGFR and MDM2 is synergistic." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-5185.

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Banu, Arshiya, Carolina Zandueta, Fernando Lecanda, and Agamemnon E. Grigoriadis. "Abstract 416: Regulation of osteosarcoma cell metastasis by FGFR and mTOR signaling." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-416.

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Guzy, R., S. Dorry, A. Meliton, D. Ornitz, and G. M. Mutlu. "Alveolar Epithelial Fgfr2 Signaling Is Required for Recovery from Bleomycin-Induced Injury." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a1241.

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Sharif, Ghada M., Marcel O. Schmidt, Casey Shuptrine, Weiner M. Louis, Anna T. Riegel, and Anton Wellstein. "Abstract A15: SMC2 role in regulating tumor angiogenesis via FGF signaling." In Abstracts: AACR Special Conference on Tumor Metastasis; November 30-December 3, 2015; Austin, TX. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.tummet15-a15.

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Li, Fang, Joseph Growney, Linda Battalagine, et al. "Abstract B65: Antitumor activity of imatinib in GIST is attenuated by FGFR signaling." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Oct 19-23, 2013; Boston, MA. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1535-7163.targ-13-b65.

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Reports on the topic "FGF2 Signaling"

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Swift, Matthew R. FGF Activation and Signaling in Breast Cancer. Defense Technical Information Center, 2005. http://dx.doi.org/10.21236/ada442267.

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Swift, Matthew R. FGF Activation and Signaling in Breast Cancer. Defense Technical Information Center, 2004. http://dx.doi.org/10.21236/ada432081.

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Swift, Matthew R. FGF Activation and Signaling in Breast Cancer. Defense Technical Information Center, 2003. http://dx.doi.org/10.21236/ada423280.

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Mann, David M. Regulation of Breast Tumor Angiogenesis by Interactive FGFR-Notch Signaling. Defense Technical Information Center, 2000. http://dx.doi.org/10.21236/ada394159.

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Mann, David M. Regulation of Breast Tumor Angiogenesis by Interactive FGFR-Notch Signaling. Defense Technical Information Center, 1999. http://dx.doi.org/10.21236/ada377825.

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Ozen, Mustafa. Disruption of Fibroblast Growth Factor Receptor (FGFR) Signaling as an Approach to Prostate Cancer Therapy. Defense Technical Information Center, 2005. http://dx.doi.org/10.21236/ada443202.

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Ozen, Mustafa. Disruption of Fibroblast Growth Factor Receptor (FGFR) Signaling as an Approach to Prostate Cancer Therapy. Defense Technical Information Center, 2006. http://dx.doi.org/10.21236/ada455329.

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Ozen, Mustafa. Disruption of Fibroblast Growth Factor Receptor (FGFR) Signaling as an Approach to Prostate Cancer Therapy. Defense Technical Information Center, 2004. http://dx.doi.org/10.21236/ada427152.

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Ray, Ranjan. The Regulation of the Angiogenic Factor FGF-Binding Protein (FGF-BP) by the APC/beta-Catenin Signaling Pathway in the Progression of Breast Cancer. Defense Technical Information Center, 2002. http://dx.doi.org/10.21236/ada406733.

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Stylianou, Dora C. The Regulation of the Angiogenic Factor FGF Binding Protein (FGF-BP) by the APC/Beta-Catenin Signaling Pathway in the Progression of Breast Cancer. Defense Technical Information Center, 2004. http://dx.doi.org/10.21236/ada425854.

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