Relevant bibliographies by topics / FGF4

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'FGF4'

Author: Grafiati
Published: 4 June 2021
Last updated: 27 April 2022

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Journal articles on the topic "FGF4"

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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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Kiefer, P., G. Peters, and C. Dickson. "Retention of fibroblast growth factor 3 in the Golgi complex may regulate its export from cells." Molecular and Cellular Biology 13, no. 9 (1993): 5781–93. http://dx.doi.org/10.1128/mcb.13.9.5781.

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The fibroblast growth factors (FGFs) fall into two distinct groups with respect to their mode of release from cells. Whereas FGF1 and FGF2 lack conventional signal peptides, the remaining members have typical features of secreted proteins. However, the behavior of mouse FGF3 is anomalous, since, despite entering the secretory pathway and undergoing primary glycosylation, its release from transfected COS-1 cells is very inefficient compared with that of FGF4 and FGF5. To investigate the unusual properties of FGF3, we analyzed the processing, secretion, and intracellular localization of a series
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Kiefer, P., G. Peters, and C. Dickson. "Retention of fibroblast growth factor 3 in the Golgi complex may regulate its export from cells." Molecular and Cellular Biology 13, no. 9 (1993): 5781–93. http://dx.doi.org/10.1128/mcb.13.9.5781-5793.1993.

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The fibroblast growth factors (FGFs) fall into two distinct groups with respect to their mode of release from cells. Whereas FGF1 and FGF2 lack conventional signal peptides, the remaining members have typical features of secreted proteins. However, the behavior of mouse FGF3 is anomalous, since, despite entering the secretory pathway and undergoing primary glycosylation, its release from transfected COS-1 cells is very inefficient compared with that of FGF4 and FGF5. To investigate the unusual properties of FGF3, we analyzed the processing, secretion, and intracellular localization of a series
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Dichmann, Darwin S., Claude Rescan, Ulrik Frandsen, and Palle Serup. "Unspecific Labeling of Pancreatic Islets by Antisera Against Fibroblast Growth Factors and Their Receptors." Journal of Histochemistry & Cytochemistry 51, no. 3 (2003): 397–400. http://dx.doi.org/10.1177/002215540305100314.

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Six distinct fibroblast growth factors (FGF5) have been detected in pancreatic islets by immunohistochemistry (IHC) using commercially available antisera. We show here that these antisera are useful for Western blotting but that only two are suited for IHC. By Western blotting, these antisera detect recombinant FGFs. Detection can be eliminated by preabsorption with immunizing peptide but not with irrelevant peptide. By IHC we find specific labeling of islets with anti-FGF1 and anti-FGF2 antisera. Labeling can be abolished by preabsorption with the immunizing peptides. In contrast, prominent s
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Jiang, Zhongliang, and Christopher A. Price. "Differential actions of fibroblast growth factors on intracellular pathways and target gene expression in bovine ovarian granulosa cells." REPRODUCTION 144, no. 5 (2012): 625–32. http://dx.doi.org/10.1530/rep-12-0199.

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Several fibroblast growth factors (FGFs), including FGF1, FGF4 and FGF10, alter ovarian granulosa cell function. These ligands exhibit different patterns of receptor activation, and their mechanisms of action on granulosa cells remain unknown. The objective of this study was to identify the major pathways and target genes activated by FGF1, FGF4 and FGF10 in primary oestrogenic granulosa cells cultured under serum-free conditions. FGF1 and FGF4 increased levels of mRNA encoding Sprouty family members,SPRY2andSPRY4, and the orphan nuclear receptorsNR4A1andNR4A3. Both FGF1 and FGF4 decreased lev
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KREUGER, Johan, Per JEMTH, Emil SANDERS-LINDBERG, et al. "Fibroblast growth factors share binding sites in heparan sulphate." Biochemical Journal 389, no. 1 (2005): 145–50. http://dx.doi.org/10.1042/bj20042129.

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HS (heparan sulphate) proteoglycans bind secreted signalling proteins, including FGFs (fibroblast growth factors) through their HS side chains. Such chains contain a wealth of differentially sulphated saccharide epitopes. Whereas specific HS structures are commonly believed to modulate FGF-binding and activity, selective binding of defined HS epitopes to FGFs has generally not been demonstrated. In the present paper, we have identified a series of sulphated HS octasaccharide epitopes, derived from authentic HS or from biosynthetic libraries that bind with graded affinities to FGF4, FGF7 and FG
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Han, Peng, Hilda Guerrero-Netro, Anthony Estienne, Binyun Cao, and Christopher A. Price. "Regulation and action of early growth response 1 in bovine granulosa cells." Reproduction 154, no. 4 (2017): 547–57. http://dx.doi.org/10.1530/rep-17-0243.

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Fibroblast growth factors (FGF) modify cell proliferation and differentiation through receptor tyrosine kinases, which stimulate the expression of transcription factors including members of the early growth response (EGR) family. In ovarian granulosa cells, most FGFs activate typical response genes, although the role of EGR proteins has not been described. In the present study, we determined the regulation of EGR mRNA by FGFs and explored the role of EGR1 in the regulation of FGF-response genes. Addition of FGF1, FGF2, FGF4 or FGF8b increased EGR1 and EGR3 mRNA levels, whereas FGF18 increased
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Li, L., Q. Tang, H. J. E. Kwon, Z. Wu, E. J. Kim, and H. S. Jung. "An Explanation for How FGFs Predict Species-Specific Tooth Cusp Patterns." Journal of Dental Research 97, no. 7 (2018): 828–34. http://dx.doi.org/10.1177/0022034518759625.

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Species-specific cusp patterns result from the iterative formation of enamel knots, the epithelial signaling centers, at the future cusp positions. The expressions of fibroblast growth factors (FGFs), especially Fgf4, in the secondary enamel knots in the areas of the future cusp tips are generally used to manifest the appearance of species-specific tooth shapes. However, the mechanism underlying the predictive role of FGFs in species-specific cusp patterns remains obscure. Here, we demonstrated that gerbils, which have a lophodont pattern, exhibit a striped expression pattern of Fgf4, whereas
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Li, Yong, Changye Sun, Edwin A. Yates, Chao Jiang, Mark C. Wilkinson, and David G. Fernig. "Heparin binding preference and structures in the fibroblast growth factor family parallel their evolutionary diversification." Open Biology 6, no. 3 (2016): 150275. http://dx.doi.org/10.1098/rsob.150275.

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The interaction of a large number of extracellular proteins with heparan sulfate (HS) regulates their transport and effector functions, but the degree of molecular specificity underlying protein–polysaccharide binding is still debated. The 15 paracrine fibroblast growth factors (FGFs) are one of the paradigms for this interaction. Here, we measure the binding preferences of six FGFs (FGF3, FGF4, FGF6, FGF10, FGF17, FGF20) for a library of modified heparins, representing structures in HS, and model glycosaminoglycans, using differential scanning fluorimetry. This is complemented by the identifi
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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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Dissertations / Theses on the topic "FGF4"

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Souttou, Boussad. "Regulation autocrine de la progression tumorale des cellules epitheliales mammaires humaines hbl100 par le fgf2 et le fgf4." Paris 6, 1994. http://www.theses.fr/1994PA066443.

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Les fgfs (fibroblast growth factors) sont des polypeptides mitogeniques pour un large spectre de cellules. Ils jouent un role important pendant le developpement embryonnaire, la reparation tissulaire, l'angiogenese et le developpement tumoral. Dans le but d'etudier le role des fgfs dans l'apparition et la progression des tumeurs mammaires humaines, nous avons utilise la lignee de cellules epitheliales de sein hbl100, qui est immortelle mais pas tumorale. Nous avons demontre que cette lignee synthetise les trois formes (18 kda, 22 kda et 24 kda) du fgf2 (fgf basique). Ces polypeptides ont ete d
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Romain, Guillaume. "Dérégulation de l’axe endocrine FGF15/FGF4 lors d’infection du système entérohépatique." Mémoire, Université de Sherbrooke, 2014. http://hdl.handle.net/11143/5389.

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Fibroblast Growth Factor 19 (FGF19 chez l’humain ; FGF15 chez la souris) est un régulateur central du métabolisme hépatique. Cette molécule a un impact important au niveau de la différentiation neurologique et de l’oreille interne au stade foetal. À l’âge adulte, le patron d’expression est restreint au système gastro-intestinal. Contrairement aux autres membres de la superfamille des FGFs, FGF19/15 agit de manière endocrine car il n’est pas retenu par la matrice extracellulaire et peut rejoindre la circulation sanguine. L’expression de FGF19/15 est induite par les acides biliaires au niv
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Low, Keri Lynn. "FGF4 and Wnt5a/PCP signaling promote limb outgrowth by polarizing limb mesenchyme /." Diss., CLICK HERE for online access, 2006. http://contentdm.lib.byu.edu/ETD/image/etd1612.pdf.

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Chauveau, Sabine. "Etude des embryons doubles mutants Nanog-/- ; Gata6-/- durant la spécification de la masse cellulaire interne. Mise en évidence d'une nouvelle hétérogénéité." Thesis, Clermont-Ferrand 1, 2016. http://www.theses.fr/2016CLF1MM29/document.

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Lors de la formation du blastocyste, l'embryon de souris est constitué d'un épithélium externe, le trophectoderme (TE), et d'une masse cellulaire interne (MCI). L’épiblaste (EPI) et l’endoderme primitif (EPr) se spécifient au sein de la MCI sous un patron de « sel et poivre » caractérisé par l’expression complémentaire de NANOG, marqueur de l’EPI et de GATA6, marqueur de l’EPr. Nanog est nécessaire pour l’acquisition d’une identité EPI et Gata6 induit le devenir en EPr. La voie FGF/MAPK joue un rôle critique dans l’acquisition de l’identité EPr et la perturbation de son activité impacte direct
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Allen, John C. "FGF4 Induced Wnt5a Gradient in the Limb Bud Mediates Mesenchymal Cell Directed Migration and Division." BYU ScholarsArchive, 2013. https://scholarsarchive.byu.edu/etd/4309.

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The AER has a vital role in directing embryonic limb development. Several models have been developed that attempt to explain how the AER directs limb development, but none of them are fully supported by existing data. I provide evidence that FGFs secreted from the AER induce a gradient of Wnt5a. I also demonstrate that limb mesenchyme grows toward increasing concentrations of Wnt5a. We hypothesize that the changing shape of the AER is critical for patterning the limb along the proximal to distal axis. To better understand the pathway through which Wnt5a elicits its effects, we have performed v
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Knobloch, Thomas J. "Analysis of the human fibroblast growth factor 4 (FGF4) gene regulatory elements and characterization of the human glasgow rearranged sequence (GRS) gene /." The Ohio State University, 1999. http://rave.ohiolink.edu/etdc/view?acc_num=osu1488187049540656.

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Guillonneau, Xavier. "Regulation de l'activite des fgf1 et fgf2 dans la retine normale et pathologique : identification d'un recepteur soluble aux fgf -." Paris 5, 1997. http://www.theses.fr/1997PA05W078.

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Belgacem, Mohamed Rabie. "FGF/FGFR un couple en pleine évolution : étude de l'évolution de la spécificité/affinité des couples FGFs/FGFRs chez les chordés." Paris 6, 2011. http://www.theses.fr/2011PA066444.

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Les FGFs (fibroblast growth factor) sont de petits peptides de faible poids moléculaire généralement secrétés et présents chez tous les métazoaires. Les FGFs réalisent leur fonction en se liant à leurs récepteurs FGFRs. La liaison au récepteur peut activer trois voies de signalisation intracellulaires majeures : PLCgamma/PKC, PI3K/Akt et Ras/MAPK. Les travaux de ma thèse ont consisté en une étude comparative à la fois évolutive et fonctionnelle de la spécificité/affinité des couples FGFs/FGFRs chez les chordés. En utilisant différentes approches bioinformatiques nous avons pu éclaircir plusieu
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Dadone-Montaudié, Bérengère. "La voie de signalisation FGF/FGFR : nouvelle cible thérapeutique dans les liposarcomes." Electronic Thesis or Diss., Université Côte d'Azur, 2020. http://www.theses.fr/2020COAZ6024.

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Les sarcomes, tumeurs conjonctives malignes, constituent un groupe hétérogène de tumeurs en fonction de la ligne de différenciation. Les liposarcomes (LPS), de différenciation adipocytaire, représentent une classe de sarcomes de tissus mous fréquente chez l’adulte. Parmi les LPS, on distingue deux types histologiques majoritaires : les tumeurs lipomateuses atypiques (TLA) ou liposarcomes bien différenciés (LBD) et les liposarcomes dédifférenciés (LDD). Alors que les TLA/LBD sont de malignité intermédiaire c’est-à-dire d’agressivité essentiellement locale, les LDD ont un potentiel métastatique
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Vetter, Katja. "Die Funktion von FGF2 und FGF8 während der Entwicklung des Nervensystems in der Maus." [S.l.] : [s.n.], 2000. http://deposit.ddb.de/cgi-bin/dokserv?idn=960644989.

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Books on the topic "FGF4"

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Kuro-o, Makoto, ed. Endocrine FGFs and Klothos. Springer US, 2012. http://dx.doi.org/10.1007/978-1-4614-0887-1.

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Thompson, Stuart David. Fibroblast growth factor 2 and its receptor, FGFR 1 in the normal thyroid and multinodular goitre. University of Birmingham, 2000.

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Martens, David James. Separate proliferation kinetics of FGF-responsive and EGF-responsive neural stem cells within the embryonic forebrain germinal zone. National Library of Canada, 1999.

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Kuro-o, Makoto. Endocrine FGFs and Klothos. Springer, 2012.

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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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Endocrine Fgfs and Klothos Advances in Experimental Medicine and Biology. Springer, 2012.

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Field Guide to Visual and Ophthalmic Optics (SPIE Vol. FG04). SPIE Publications, 2004.

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Han, In Suk. Basic FGF and FGF receptor involvement in testicular cell-cell interactions and expression of FSH receptor and SGP-2 fusion proteins. 1993.

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Simons, Michael. Fibroblast Growth Factors: Biology and Clinical Application - Fgf Biology and Therapeutics. World Scientific Publishing Co Pte Ltd, 2016.

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Horsford, David Jonathan. Chx10 is necessary for mammalian neuroretinal cell identity in a pathway with FGF and Mitf. 2003.

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Book chapters on the topic "FGF4"

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Katoh, Masaru, Giorgio Berton, Anna Baruzzi, et al. "FGF4." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100444.

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Ngo-Muller, Valerie, Shaoguang Li, Scott A. Schaller, et al. "FGF4 and Skeletal Morphogenesis." In The Skeleton. Humana Press, 2004. http://dx.doi.org/10.1007/978-1-59259-736-9_9.

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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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Salajegheh, Ali. "Fibroblast Growth Factors (Acidic: FGF-1; Basic: FGF-2) and Its Receptors (FGFR)." In Angiogenesis in Health, Disease and Malignancy. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-28140-7_18.

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Katoh, Masaru, Giorgio Berton, Anna Baruzzi, et al. "FGD4." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100425.

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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. "FGF14." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100432.

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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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Conference papers on the topic "FGF4"

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Patel, Nisha S., and Alisa Morss Clyne. "A Computational Model of Fibroblast Growth Factor-2 Binding to Isolated and Intact Cell Surface Receptors: Effects of Fibroblast Growth Factor-2 Concentration, Flow and Delivery Mode." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80798.

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Fibroblast growth factor-2 (FGF2) plays an important role in both healthy vascular cell functions and pathogenesis in cancer, atherosclerosis and reduced perfusion in diabetes (1–4). FGF2 therapy and targeted drug delivery have great potential in the treatment of such diseases, but have had little clinical success. FGF2 binding kinetics to heparan sulfate proteoglycan (HSPG) and fibroblast growth factor receptors (FGFR) have been largely studied under static conditions (5), however FGF2 binding to endothelial cells occurs physiologically under fluid flow conditions. Understanding complex FGF2
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Yongbin, Chen, Zhang Liyan, and Guo Guozhen. "Effect of EMP on mice polydactylia and related genes expression (Gli3, Shh and Fgf4) during the development of mice limbs." In 2006 4th Asia-Pacific Conference on Environmental Electromagnetics. IEEE, 2006. http://dx.doi.org/10.1109/ceem.2006.257966.

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Bahnassy, Abeer A., Abdel-Rahman N. zekri, Salem E. Salem, Hala Aziz, Abeer E. Moustafa, and Rabab M. Gaafar. "Abstract 2384: Assessment of PITX2, BMP4, FGF4, ERalpha, ERbeta promoter methylation in the circulating tumor cells (CTCs) can predict metastasis and survival in primary invasive duct carcinoma (PIDC) patients." 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.am2012-2384.

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Li, Yuan, Long Wu, Yanlei Cheng, et al. "Abstract 4882: Expression atlas of FGF and FGFR genes in pan-cancer uncovered predictive biomarkers for FGFR inhibition response in clinical trials." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-4882.

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Li, Yuan, Long Wu, Yanlei Cheng, et al. "Abstract 4882: Expression atlas of FGF and FGFR genes in pan-cancer uncovered predictive biomarkers for FGFR inhibition response in clinical trials." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-4882.

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Bell, Katherine, Dana Gaffney, Gabriela Martinez-Cardona, Jayaprakash Karkera, and Suso Platero. "Abstract 4326: Co-amplification of FGF receptors and ligands in FGFR inhibitor-sensitive cell lines." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-4326.

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Meric-Bernstam, Funda, Lipika Goyal, Ben Tran, et al. "Abstract CT238: TAS-120 in patients with advanced solid tumors bearing FGF/FGFR aberrations: A Phase I study." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-ct238.

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Meric-Bernstam, Funda, Lipika Goyal, Ben Tran, et al. "Abstract CT238: TAS-120 in patients with advanced solid tumors bearing FGF/FGFR aberrations: A Phase I study." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-ct238.

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Zaid, Tarrik, Melissa S. Thompson, Kwong-kwok Wong, et al. "Abstract 3132: Proliferative effects of FGF1 on ovarian cancer cells correlate with FGFR4 over expression and are mediated by MAPK/ERK signaling." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-3132.

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Mao, Pingping, Ofir Cohen, Kailey Kowalski, et al. "Abstract 314: Acquired FGF and FGFR alterations confer resistance to estrogen receptor (ER) targeted therapy in metastatic ER+ breast cancer." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-314.

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Reports on the topic "FGF4"

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Kern, Francis G. Novel Inhibitors of FGF Signal transduction in Breast Cancer: Targeting the FGFR Adapter Protein SNT-1. Defense Technical Information Center, 2004. http://dx.doi.org/10.21236/ada426436.

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Estes, Norman R., and Francis G. Kern. Inactivation of FGF Receptors by Targeting Ribozymes Against FGFR mRNAs and Their Effect on FGF Dependent In Vitro and In Vivo Breast Cancer Growth Phenotypes. Defense Technical Information Center, 2003. http://dx.doi.org/10.21236/ada416690.

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Donoghue, Daniel J. FGFR4 Downregulation of Cell Adhesion in Prostate Cancer. Defense Technical Information Center, 2008. http://dx.doi.org/10.21236/ada510472.

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Donoghue, Daniel J., April N. Meyer, and Kristine A. Drafahl. FGFR4 Downregulation of Cell Adhesion in Prostate Cancer. Defense Technical Information Center, 2007. http://dx.doi.org/10.21236/ada468675.

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Donoghue, Daniel J. FGFR4 Downregulation of Cell Adhesion in Prostate Cancer. Defense Technical Information Center, 2008. http://dx.doi.org/10.21236/ada593283.

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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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8

MacAuthur, Craig A. Role of FGF-8 in Breast Cancer. Defense Technical Information Center, 1999. http://dx.doi.org/10.21236/ada374037.

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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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You might also be interested in the extended bibliographies on the topic 'FGF4' for particular source types:
Journal articles Dissertations / Theses
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