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Search results 1201 to 1300 out of 2229 for Fgfr3

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Type Details Score
Publication
First Author: Rivers LE
Year: 2008
Journal: Nat Neurosci
Title: PDGFRA/NG2 glia generate myelinating oligodendrocytes and piriform projection neurons in adult mice.
Volume: 11
Issue: 12
Pages: 1392-401
Publication  
First Author: Anttonen T
Year: 2012
Journal: Sci Rep
Title: Cdc42-dependent structural development of auditory supporting cells is required for wound healing at adulthood.
Volume: 2
Pages: 978
Publication
First Author: Kirjavainen A
Year: 2015
Journal: Biol Open
Title: The Rho GTPase Cdc42 regulates hair cell planar polarity and cellular patterning in the developing cochlea.
Volume: 4
Issue: 4
Pages: 516-26
Publication
First Author: Cilvik SN
Year: 2013
Journal: PLoS One
Title: Fibroblast growth factor receptor 1 signaling in adult cardiomyocytes increases contractility and results in a hypertrophic cardiomyopathy.
Volume: 8
Issue: 12
Pages: e82979
Genotype
Symbol: Tg(Myh6-rtTA)8585Jam/? Tg(tetO-Fgfr3*R248C/Fgfr1)#Dor/?
Background: involves: 129 * C57BL/6 * FVB/N * FVB/NTac
Zygosity: cx
Has Mutant Allele: true
Genotype
Symbol: Gt(ROSA)26Sor/Gt(ROSA)26Sor<+> Tg(Fgfr3-icre/ERT2)4-2Wdr/?
Background: involves: 129S6/SvEvTac * C57BL/6 * CBA
Zygosity: cn
Has Mutant Allele: true
Publication
First Author: Tsai SJ
Year: 2002
Journal: Endocrinology
Title: Fibroblast growth factor-9 is an endometrial stromal growth factor.
Volume: 143
Issue: 7
Pages: 2715-21
Publication
First Author: Giri D
Year: 1999
Journal: J Cell Physiol
Title: FGF9 is an autocrine and paracrine prostatic growth factor expressed by prostatic stromal cells.
Volume: 180
Issue: 1
Pages: 53-60
Publication
First Author: Kim Y
Year: 2006
Journal: PLoS Biol
Title: Fgf9 and Wnt4 act as antagonistic signals to regulate mammalian sex determination.
Volume: 4
Issue: 6
Pages: e187
Publication
First Author: Colvin JS
Year: 2001
Journal: Cell
Title: Male-to-female sex reversal in mice lacking fibroblast growth factor 9.
Volume: 104
Issue: 6
Pages: 875-89
Protein Domain
Type: Family
Description: Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].This entry represents fibroblast growth factor 9 (FGF9), also known as glia-activating factor and heparin-binding growth factor 9. This protein plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. It is involved in cyclic proliferation of uterine endometrial stroma []and can act as both a paracrine mitogen for epithelial cells and an autocrine mitogen for stromal cells []. FGF9 has also been shown to play a vital role in male development, as it is needed to carry out important masculinising developmental functions, such testicular embryogenesis [, ]. FGF9 Interacts with FGFR1, FGFR2, FGFR3 and FGFR4, but has highest affinity for FGFR3 [, ].
Publication
First Author: Yoneda K
Year: 1999
Journal: Mamm Genome
Title: Localization of a locus responsible for the bovine chondrodysplastic dwarfism (bcd) on chromosome 6.
Volume: 10
Issue: 6
Pages: 597-600
Publication
First Author: Ahmad I
Year: 2012
Journal: Dis Model Mech
Title: Exploring molecular genetics of bladder cancer: lessons learned from mouse models.
Volume: 5
Issue: 3
Pages: 323-32
Publication
First Author: Yang J
Year: 2015
Journal: Cell Cycle
Title: Binding of FGF2 to FGFR2 in an autocrine mode in trophectoderm cells is indispensable for mouse blastocyst formation through PKC-p38 pathway.
Volume: 14
Issue: 20
Pages: 3318-30
Publication  
First Author: Chakraborty D
Year: 2020
Journal: Sci Transl Med
Title: Fibroblast growth factor receptor 3 activates a network of profibrotic signaling pathways to promote fibrosis in systemic sclerosis.
Volume: 12
Issue: 563
Publication
First Author: Ng JQ
Year: 2023
Journal: Nat Commun
Title: Loss of Grem1-lineage chondrogenic progenitor cells causes osteoarthritis.
Volume: 14
Issue: 1
Pages: 6909
Publication
First Author: Chellaiah A
Year: 1999
Journal: J Biol Chem
Title: Mapping ligand binding domains in chimeric fibroblast growth factor receptor molecules. Multiple regions determine ligand binding specificity.
Volume: 274
Issue: 49
Pages: 34785-94
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein
Organism: Mus musculus/domesticus
Length: 251  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 207  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 264  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 202  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 508  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 207  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 155  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 424  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1302  
Fragment?: false
Publication
First Author: Young KM
Year: 2010
Journal: Glia
Title: An Fgfr3-iCreER(T2) transgenic mouse line for studies of neural stem cells and astrocytes.
Volume: 58
Issue: 8
Pages: 943-53
Publication
First Author: Zawadzka M
Year: 2010
Journal: Cell Stem Cell
Title: CNS-resident glial progenitor/stem cells produce Schwann cells as well as oligodendrocytes during repair of CNS demyelination.
Volume: 6
Issue: 6
Pages: 578-90
Publication
First Author: Ellis K
Year: 2019
Journal: Dev Biol
Title: GSK3 regulates hair cell fate in the developing mammalian cochlea.
Volume: 453
Issue: 2
Pages: 191-205
Publication    
First Author: Sun S
Year: 2021
Journal: Elife
Title: Dual expression of Atoh1 and Ikzf2 promotes transformation of adult cochlear supporting cells into outer hair cells.
Volume: 10
Publication  
First Author: Maass JC
Year: 2015
Journal: Front Cell Neurosci
Title: Changes in the regulation of the Notch signaling pathway are temporally correlated with regenerative failure in the mouse cochlea.
Volume: 9
Pages: 110
Publication
First Author: Kolla L
Year: 2020
Journal: Nat Commun
Title: Characterization of the development of the mouse cochlear epithelium at the single cell level.
Volume: 11
Issue: 1
Pages: 2389
Publication
First Author: Kubota M
Year: 2021
Journal: Cell Rep
Title: Greater epithelial ridge cells are the principal organoid-forming progenitors of the mouse cochlea.
Volume: 34
Issue: 3
Pages: 108646
Publication
First Author: Kubota M
Year: 2021
Journal: STAR Protoc
Title: Murine cochlear cell sorting and cell-type-specific organoid culture.
Volume: 2
Issue: 3
Pages: 100645
Publication  
First Author: Lukashkina VA
Year: 2024
Journal: J Neurosci
Title: Optogenetics Reveals Roles for Supporting Cells in Force Transmission to and From Outer Hair Cells in the Mouse Cochlea.
Volume: 44
Issue: 4
Protein
Organism: Mus musculus/domesticus
Length: 724  
Fragment?: false
Publication
First Author: Geering B
Year: 2007
Journal: Biochem Soc Trans
Title: Regulation of class IA PI3Ks: is there a role for monomeric PI3K subunits?
Volume: 35
Issue: Pt 2
Pages: 199-203
Publication
First Author: Jimenez C
Year: 2002
Journal: J Biol Chem
Title: The p85 regulatory subunit controls sequential activation of phosphoinositide 3-kinase by Tyr kinases and Ras.
Volume: 277
Issue: 44
Pages: 41556-62
Publication
First Author: Kawai M
Year: 2013
Journal: J Biol Chem
Title: FGF23 suppresses chondrocyte proliferation in the presence of soluble α-Klotho both in vitro and in vivo.
Volume: 288
Issue: 4
Pages: 2414-27
Publication
First Author: Touchberry CD
Year: 2013
Journal: Am J Physiol Endocrinol Metab
Title: FGF23 is a novel regulator of intracellular calcium and cardiac contractility in addition to cardiac hypertrophy.
Volume: 304
Issue: 8
Pages: E863-73
Publication
First Author: Xiao L
Year: 2004
Journal: J Biol Chem
Title: Stat1 controls postnatal bone formation by regulating fibroblast growth factor signaling in osteoblasts.
Volume: 279
Issue: 26
Pages: 27743-52
Publication  
First Author: Zhao H
Year: 2006
Journal: Mol Vis
Title: Fibroblast growth factor receptor 1 (Fgfr1) is not essential for lens fiber differentiation in mice.
Volume: 12
Pages: 15-25
Publication
First Author: Eswarakumar VP
Year: 2004
Journal: Proc Natl Acad Sci U S A
Title: A gain-of-function mutation of Fgfr2c demonstrates the roles of this receptor variant in osteogenesis.
Volume: 101
Issue: 34
Pages: 12555-60
Publication
First Author: Karolak MR
Year: 2015
Journal: Hum Mol Genet
Title: FGFR1 signaling in hypertrophic chondrocytes is attenuated by the Ras-GAP neurofibromin during endochondral bone formation.
Volume: 24
Issue: 9
Pages: 2552-64
Publication
First Author: Liu Z
Year: 2002
Journal: Genes Dev
Title: Coordination of chondrogenesis and osteogenesis by fibroblast growth factor 18.
Volume: 16
Issue: 7
Pages: 859-69
Publication
First Author: Karuppaiah K
Year: 2016
Journal: Development
Title: FGF signaling in the osteoprogenitor lineage non-autonomously regulates postnatal chondrocyte proliferation and skeletal growth.
Volume: 143
Issue: 10
Pages: 1811-22
Publication
First Author: McGowan SE
Year: 2015
Journal: Am J Physiol Lung Cell Mol Physiol
Title: Fibroblast growth factor signaling in myofibroblasts differs from lipofibroblasts during alveolar septation in mice.
Volume: 309
Issue: 5
Pages: L463-74
Publication
First Author: Azim K
Year: 2012
Journal: Glia
Title: Intraventricular injection of FGF-2 promotes generation of oligodendrocyte-lineage cells in the postnatal and adult forebrain.
Volume: 60
Issue: 12
Pages: 1977-90
Publication      
First Author: Ng JQ
Year: 2023
Journal: bioRxiv
Title: Loss of Grem1 -articular cartilage progenitor cells causes osteoarthritis.
Publication
First Author: Li Z
Year: 2001
Journal: Blood
Title: The myeloma-associated oncogene fibroblast growth factor receptor 3 is transforming in hematopoietic cells.
Volume: 97
Issue: 8
Pages: 2413-9
Publication
First Author: Mathieu M
Year: 1995
Journal: J Biol Chem
Title: Fibroblast growth factor (FGF) 3 from Xenopus laevis (XFGF3) binds with high affinity to FGF receptor 2.
Volume: 270
Issue: 12
Pages: 6779-87
Publication
First Author: McEwen DG
Year: 1998
Journal: J Biol Chem
Title: Regulation of the fibroblast growth factor receptor 3 promoter and intron I enhancer by Sp1 family transcription factors.
Volume: 273
Issue: 9
Pages: 5349-57
Publication
First Author: Bloom MW
Year: 2006
Journal: Anat Rec A Discov Mol Cell Evol Biol
Title: Aspects of achondroplasia in the skulls of dwarf transgenic mice: a cephalometric study.
Volume: 288
Issue: 3
Pages: 316-22
Publication
First Author: Kelleher FC
Year: 2013
Journal: Carcinogenesis
Title: Fibroblast growth factor receptors, developmental corruption and malignant disease.
Volume: 34
Issue: 10
Pages: 2198-205
Publication
First Author: Saucedo L
Year: 2018
Journal: Reproduction
Title: Involvement of fibroblast growth factor 2 (FGF2) and its receptors in the regulation of mouse sperm physiology.
Volume: 156
Issue: 2
Pages: 163-172
Publication
First Author: Miao K
Year: 2019
Journal: J Biol Chem
Title: Optimizing CRISPR/Cas9 technology for precise correction of the Fgfr3-G374R mutation in achondroplasia in mice.
Volume: 294
Issue: 4
Pages: 1142-1151
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 593  
Fragment?: false
Publication
First Author: Walters BJ
Year: 2017
Journal: Cell Rep
Title: In Vivo Interplay between p27Kip1, GATA3, ATOH1, and POU4F3 Converts Non-sensory Cells to Hair Cells in Adult Mice.
Volume: 19
Issue: 2
Pages: 307-320
Publication
First Author: Leng L
Year: 2018
Journal: Neuron
Title: Menin Deficiency Leads to Depressive-like Behaviors in Mice by Modulating Astrocyte-Mediated Neuroinflammation.
Volume: 100
Issue: 3
Pages: 551-563.e7
Publication  
First Author: Laos M
Year: 2017
Journal: Sci Rep
Title: Indispensable role of Mdm2/p53 interaction during the embryonic and postnatal inner ear development.
Volume: 7
Pages: 42216
Publication
First Author: Xiong W
Year: 2019
Journal: J Neurosci
Title: Astrocytic Epoxyeicosatrienoic Acid Signaling in the Medial Prefrontal Cortex Modulates Depressive-like Behaviors.
Volume: 39
Issue: 23
Pages: 4606-4623
Publication  
First Author: Goto H
Year: 2018
Journal: Development
Title: Loss of Mob1a/b in mice results in chondrodysplasia due to YAP1/TAZ-TEAD-dependent repression of SOX9.
Volume: 145
Issue: 6
Publication
First Author: Yamashita T
Year: 2018
Journal: PLoS Genet
Title: High-resolution transcriptional dissection of in vivo Atoh1-mediated hair cell conversion in mature cochleae identifies Isl1 as a co-reprogramming factor.
Volume: 14
Issue: 7
Pages: e1007552
Publication
First Author: Chrysostomou E
Year: 2020
Journal: J Neurosci
Title: The Notch Ligand Jagged1 Is Required for the Formation, Maintenance, and Survival of Hensen's Cells in the Mouse Cochlea.
Volume: 40
Issue: 49
Pages: 9401-9413
Publication
First Author: Liu Z
Year: 2012
Journal: J Neurosci
Title: Regulation of p27Kip1 by Sox2 maintains quiescence of inner pillar cells in the murine auditory sensory epithelium.
Volume: 32
Issue: 31
Pages: 10530-40
Publication
First Author: Shimoyama Y
Year: 1991
Journal: Jpn J Cancer Res
Title: Characterization of high-molecular-mass forms of basic fibroblast growth factor produced by hepatocellular carcinoma cells: possible involvement of basic fibroblast growth factor in hepatocarcinogenesis.
Volume: 82
Issue: 11
Pages: 1263-70
Publication
First Author: Reich-Slotky R
Year: 1995
Journal: J Biol Chem
Title: Chimeric molecules between keratinocyte growth factor and basic fibroblast growth factor define domains that confer receptor binding specificities.
Volume: 270
Issue: 50
Pages: 29813-8
Publication
First Author: Shen B
Year: 1998
Journal: Biochem Biophys Res Commun
Title: Intracellular association of FGF-2 with the ribosomal protein L6/TAXREB107.
Volume: 252
Issue: 2
Pages: 524-8
Publication
First Author: Soulet F
Year: 2001
Journal: Biochem Biophys Res Commun
Title: Fibroblast growth factor-2 interacts with free ribosomal protein S19.
Volume: 289
Issue: 2
Pages: 591-6
Publication  
First Author: Riazuddin S
Year: 2011
Journal: BMC Med Genet
Title: Variable expressivity of FGF3 mutations associated with deafness and LAMM syndrome.
Volume: 12
Pages: 21
Publication
First Author: Yan G
Year: 1993
Journal: Mol Cell Biol
Title: Exon switching and activation of stromal and embryonic fibroblast growth factor (FGF)-FGF receptor genes in prostate epithelial cells accompany stromal independence and malignancy.
Volume: 13
Issue: 8
Pages: 4513-22
Publication
First Author: Crossley PH
Year: 1995
Journal: Development
Title: The mouse Fgf8 gene encodes a family of polypeptides and is expressed in regions that direct outgrowth and patterning in the developing embryo.
Volume: 121
Issue: 2
Pages: 439-51
Publication
First Author: Liu SB
Year: 2012
Journal: Toxicology
Title: The role of androgen-induced growth factor (FGF8) on genital tubercle development in a hypospadiac male rat model of prenatal exposure to di-n-butyl phthalate.
Volume: 293
Issue: 1-3
Pages: 53-8
Publication
First Author: Mattila MM
Year: 2001
Journal: Oncogene
Title: FGF-8b increases angiogenic capacity and tumor growth of androgen-regulated S115 breast cancer cells.
Volume: 20
Issue: 22
Pages: 2791-804
Publication
First Author: Yoshiura K
Year: 1997
Journal: Am J Med Genet
Title: Genomic structure, sequence, and mapping of human FGF8 with no evidence for its role in craniosynostosis/limb defect syndromes.
Volume: 72
Issue: 3
Pages: 354-62
Protein Domain
Type: Family
Description: Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].This entry represents fibroblast growth factor 8 (FGF8), also known as androgen-induced growth factor. It plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. FGF8 is also required for normal brain, eye, ear and limb development during embryogenesis, and is required for normal development of the gonadotropin-releasing hormone (GnRH) neuronal system [, , , , ]. Fibroblast growth factor 8 also supports androgen and anchorage independent growth of mammary tumor cells []. FGF8 has an affinity for the all the growth factor receptors, but has the highest affinity with FGFR3 and FGFR4 [, ].This entry also includes the orthologous Fibroblast growth factor 8b from zebrafish.
Protein Domain
Type: Family
Description: Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].This entry represents fibroblast growth factor 3 (FGF3), also known as heparin-binding growth factor 3 and INT-2 proto-oncogene protein. The protein plays an important role in the regulation of embryonic development, cell proliferation and differentiation, and is required for normal ear development [, ]. FGF3 has a high affinity for FGFR3 and FGFR2, but a low affinity for FGFR1 [].
Protein Domain
Type: Family
Description: Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuousgrowth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].This entry represents fibroblast growth factor 2 (FGF2), also known as heparin-binding growth factor 2 and basic fibroblast growth factor. The protein plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration and is a potent mitogen in vitro [, ]. FGF2 has a high affinity for FGFR1, FGFR2 and FGFR4, but a very low affinity with FGFR3 [, , , ]. FGF2 has also been shown to interact with casein kinase II subunit alpha []and some ribosomal proteins [, ].