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Search results 2701 to 2800 out of 2847 for Fgfr2

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0.016s

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Type Details Score
Publication
10541313 | -
First Author: Graeff RW
Year: 1999
Journal: Pediatr Res
Title: KGF and FGF-10 stimulate liquid secretion in human fetal lung.
Volume: 46
Issue: 5
Pages: 523-9
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Publication
9740653 | J:50000
First Author: Park WY
Year: 1998
Journal: Dev Biol
Title: FGF-10 is a chemotactic factor for distal epithelial buds during lung development.
Volume: 201
Issue: 2
Pages: 125-34
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Publication
17292422 | -
First Author: Pereira CT
Year: 2007
Journal: J Surg Res
Title: Liposomal gene transfer of keratinocyte growth factor improves wound healing by altering growth factor and collagen expression.
Volume: 139
Issue: 2
Pages: 222-8
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Publication
11973338 | -
First Author: Ruehl M
Year: 2002
Journal: J Biol Chem
Title: The epithelial mitogen keratinocyte growth factor binds to collagens via the consensus sequence glycine-proline-hydroxyproline.
Volume: 277
Issue: 30
Pages: 26872-8
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Publication
10702276 | -
First Author: Mongiat M
Year: 2000
Journal: J Biol Chem
Title: The protein core of the proteoglycan perlecan binds specifically to fibroblast growth factor-7.
Volume: 275
Issue: 10
Pages: 7095-100
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Publication
9287324 | J:42892
First Author: Emoto H
Year: 1997
Journal: J Biol Chem
Title: Structure and expression of human fibroblast growth factor-10.
Volume: 272
Issue: 37
Pages: 23191-4
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Publication
11923311 | J:113981
First Author: Bagai S
Year: 2002
Journal: J Biol Chem
Title: Fibroblast growth factor-10 is a mitogen for urothelial cells.
Volume: 277
Issue: 26
Pages: 23828-37
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Publication
9916808 | J:51966
First Author: Sekine K
Year: 1999
Journal: Nat Genet
Title: Fgf10 is essential for limb and lung formation.
Volume: 21
Issue: 1
Pages: 138-41
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Publication
9927546 | -
First Author: Jimenez PA
Year: 1999
Journal: J Surg Res
Title: Keratinocyte growth factor-2 accelerates wound healing in incisional wounds.
Volume: 81
Issue: 2
Pages: 238-42
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Protein Domain
IPR028252 | FGF10
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 10 (FGF10), also known as keratinocyte growth factor 2. This protein plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. FGF10 exhibits mitogenic activity for keratinizing epidermal cells, but essentially no activity for fibroblasts, which is similar to the biological activity of FGF7 []. Studies suggest FGF10 is required for embryonic epidermal morphogenesis including brain development, lung morphogenesis, and initiation of limb bud formation [, , ]. FGF10 is also implicated as a primary factor in the process of wound healing [, ]. FGF10 interacts with FGFR1, but has a higher affinity FGFR2 [, ].
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Protein Domain
IPR028242 | FGF6
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 6 (FGF6). This protein plays an important role in the regulation of cell proliferation, cell differentiation, angiogenesis and myogenesis, and is required for normal muscle regeneration [, , ]. It may also regulate bone metabolism, as shown by its activity on both osteoblasts and osteoclasts []. FGF6 has a high affinity for FGFR1, FGFR2 and FGFR4 [].
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Protein Domain
IPR028240 | FGF5
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 5 (FGF5). This protein plays an important role in the regulation of cell proliferation and cell differentiation. It is required for normal regulation of the hair growth cycle, as it functions as an inhibitor of hair elongation by promoting progression from anagen, the growth phase of the hair follicle, into catagen, the apoptosis-induced regression phase [, ]. FGF5 has a high affinity for FGFR1 and FGFR2 [].
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Protein Domain
IPR028247 | FGF7
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 7 (FGF7), also known as keratinocyte growth factor (KGF). This protein plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation. It is a potent epithelial cell-specific growth factor, whose mitogenic activity is predominantly exhibited in keratinocytes, but not in fibroblasts and endothelial cells []. Studies of mouse and rat have implicated FGF7 in morphogenesis of epithelium, wound repair, hair development and early lung organogenesis [, , , ]. FGF7 has a high affinity for FGFR2 and has also been shown to interact with various collagens []and heparan sulfate proteoglycan 2 (perlecan) [].
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Protein Domain
IPR028223 | FGF2
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 [, ].
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Publication
16502419 | J:108218
First Author: Connerney J
Year: 2006
Journal: Dev Dyn
Title: Twist1 dimer selection regulates cranial suture patterning and fusion.
Volume: 235
Issue: 5
Pages: 1345-57
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Publication
9640329 | J:174265
First Author: Robinson ML
Year: 1998
Journal: Dev Biol
Title: Disregulation of ocular morphogenesis by lens-specific expression of FGF-3/int-2 in transgenic mice.
Volume: 198
Issue: 1
Pages: 13-31
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Publication
19515808 | J:150719
First Author: Gattineni J
Year: 2009
Journal: Am J Physiol Renal Physiol
Title: FGF23 decreases renal NaPi-2a and NaPi-2c expression and induces hypophosphatemia in vivo predominantly via FGF receptor 1.
Volume: 297
Issue: 2
Pages: F282-91
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Publication
11287183 | J:69279
First Author: Mailleux AA
Year: 2001
Journal: Mech Dev
Title: Evidence that SPROUTY2 functions as an inhibitor of mouse embryonic lung growth and morphogenesis.
Volume: 102
Issue: 1-2
Pages: 81-94
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Publication
10196476 | J:54853
First Author: Zhang Y
Year: 1999
Journal: Gene
Title: Genomic organization of the human fibroblast growth factor receptor 2 (FGFR2) gene and comparative analysis of the human FGFR gene family.
Volume: 230
Issue: 1
Pages: 69-79
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Protein Coding Gene
MGI:97583 | Pik3r1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:98354 | Sos1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:98397 | Src
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1206581 | Pik3ca
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1321161 | Ppp2cb
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
P26450
Organism: Mus musculus/domesticus
Length: 724  
Fragment?: false
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Protein
P05480
Organism: Mus musculus/domesticus
Length: 535  
Fragment?: false
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Protein
Q62245
Organism: Mus musculus/domesticus
Length: 1319  
Fragment?: false
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Protein
P62715
Organism: Mus musculus/domesticus
Length: 309  
Fragment?: false
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Protein
P42337
Organism: Mus musculus/domesticus
Length: 1068  
Fragment?: false
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Publication
10713090 | J:61068
First Author: Reilly JF
Year: 2000
Journal: J Biol Chem
Title: Association of fibroblast growth factor receptor 1 with the adaptor protein Grb14. Characterization of a new receptor binding partner.
Volume: 275
Issue: 11
Pages: 7771-8
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Publication
10629055 | -
First Author: Ong SH
Year: 2000
Journal: Mol Cell Biol
Title: FRS2 proteins recruit intracellular signaling pathways by binding to diverse targets on fibroblast growth factor and nerve growth factor receptors.
Volume: 20
Issue: 3
Pages: 979-89
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Publication
7537362 | -
First Author: Karlsson T
Year: 1995
Journal: Oncogene
Title: Molecular interactions of the Src homology 2 domain protein Shb with phosphotyrosine residues, tyrosine kinase receptors and Src homology 3 domain proteins.
Volume: 10
Issue: 8
Pages: 1475-83
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Publication
11030354 | -
First Author: Schlessinger J
Year: 2000
Journal: Mol Cell
Title: Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization.
Volume: 6
Issue: 3
Pages: 743-50
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Publication
16207751 | J:102949
First Author: Li C
Year: 2005
Journal: Development
Title: FGFR1 function at the earliest stages of mouse limb development plays an indispensable role in subsequent autopod morphogenesis.
Volume: 132
Issue: 21
Pages: 4755-64
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Publication
2162671 | -
First Author: Itoh N
Year: 1990
Journal: Biochem Biophys Res Commun
Title: The complete amino acid sequence of the shorter form of human basic fibroblast growth factor receptor deduced from its cDNA.
Volume: 169
Issue: 2
Pages: 680-5
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Publication
17360555 | -
First Author: Riley BM
Year: 2007
Journal: Proc Natl Acad Sci U S A
Title: Impaired FGF signaling contributes to cleft lip and palate.
Volume: 104
Issue: 11
Pages: 4512-7
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Publication
21331089 | -
First Author: Dixon MJ
Year: 2011
Journal: Nat Rev Genet
Title: Cleft lip and palate: understanding genetic and environmental influences.
Volume: 12
Issue: 3
Pages: 167-78
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Protein Domain
IPR028174 | FGF_rcpt_1
Type: Domain
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 [].The FGFRs consist of an extracellular ligand-binding domain composed of three immunoglobulin-like domains (D1-D3), a single transmembrane helix domain, and an intracellular domain with tyrosine kinase activity []. The three immunoglobin(Ig)-like domains, D1, D2, and D3, present a stretch of acidic amino acids (known as the acid box) between D1 and D2. This acid box can participate in the regulation of FGF binding to the FGFR. Immunoglobulin-like domains D2 and D3 are sufficient for FGF binding. FGFR family members differ from one another in their ligandaffinities and tissue distribution [, ]. Most FGFs can bind to several different FGFR subtypes. Indeed, FGF1 is sometimes referred to as the universal ligand, as it is capable of activating all of the different FGFRs []. However, there are some exceptions. For example, FGF7 only interacts with FGFR2 []and FGF18 was recently shown to only activate FGFR3 []. Fibroblast growth factor receptor 1 (FGFR1) binds both acidic and basic fibroblast growth factors and is involved in limb induction []. FGFR1 has been shown to be associated with Pfeiffer syndrome [], and cleft lip and/or palate [, ]. Fibroblast growth factor receptor 1 has been shown to interact with growth factor receptor-bound protein 14 (GRB14) [], Src homology 2 domain containing adaptor protein B (SHB) [], fibroblast growth factor receptor substrate 2 (FRS2)[]and fibroblast growth factor 1 (FGF1) [, ].This entry represents the catalytic domain of FGFR1.
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Protein Domain
IPR016248 | FGF_rcpt_fam
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 [].The FGFRs consist of an extracellular ligand-binding domain composed of three immunoglobulin-like domains (D1-D3), a single transmembrane helix domain, and an intracellular domain with tyrosine kinase activity []. The three immunoglobin(Ig)-like domains, D1, D2, and D3, present a stretch of acidic amino acids (known as the acid box) between D1 and D2. This acid box can participate in the regulation of FGF binding to the FGFR. Immunoglobulin-like domains D2 and D3 are sufficient for FGF binding. FGFR family members differ from one another in their ligand affinities and tissue distribution [, ]. Most FGFs can bind to several different FGFR subtypes. Indeed, FGF1 is sometimes referred to as the universal ligand, as it is capable of activating all of the different FGFRs []. However, there are some exceptions. For example, FGF7 only interacts with FGFR2 []and FGF18 was recently shown to only activate FGFR3 []. This entry represents the fibroblast growth factor receptor family.
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Protein
D3YWT1
Organism: Mus musculus/domesticus
Length: 331  
Fragment?: false
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Protein
D3Z3N4
Organism: Mus musculus/domesticus
Length: 346  
Fragment?: false
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Publication
16829530 | -
First Author: Duchesne L
Year: 2006
Journal: J Biol Chem
Title: N-glycosylation of fibroblast growth factor receptor 1 regulates ligand and heparan sulfate co-receptor binding.
Volume: 281
Issue: 37
Pages: 27178-89
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Publication
9212826 | -
First Author: Hughes SE
Year: 1997
Journal: J Histochem Cytochem
Title: Differential expression of the fibroblast growth factor receptor (FGFR) multigene family in normal human adult tissues.
Volume: 45
Issue: 7
Pages: 1005-19
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Publication
18216218 | -
First Author: Cotton LM
Year: 2008
Journal: Endocr Rev
Title: Cellular signaling by fibroblast growth factors (FGFs) and their receptors (FGFRs) in male reproduction.
Volume: 29
Issue: 2
Pages: 193-216
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Protein Coding Gene
MGI:1321159 | Ppp2ca
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1346858 | Mapk1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1926334 | Ppp2r1a
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1346859 | Mapk3
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q76MZ3
Organism: Mus musculus/domesticus
Length: 589  
Fragment?: false
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Protein
P63085
Organism: Mus musculus/domesticus
Length: 358  
Fragment?: false
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Protein
Q63844
Organism: Mus musculus/domesticus
Length: 380  
Fragment?: false
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Protein
P63330
Organism: Mus musculus/domesticus
Length: 309  
Fragment?: false
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Protein
Q60631-1
 
Organism: Mus musculus/domesticus
Length:  
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Protein
Q925A1
Organism: Mus musculus/domesticus
Length: 109  
Fragment?: false
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Protein
Q541T2
Organism: Mus musculus/domesticus
Length: 154  
Fragment?: false
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Protein
Q925A2
Organism: Mus musculus/domesticus
Length: 112  
Fragment?: false
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Protein
Q3TH23
Organism: Mus musculus/domesticus
Length: 512  
Fragment?: false
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Protein
A0A7U3L698
Organism: Mus musculus/domesticus
Length: 264  
Fragment?: false
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Protein
Q7TPG9
Organism: Mus musculus/domesticus
Length: 105  
Fragment?: true
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Protein
A0A7U3L4H7
Organism: Mus musculus/domesticus
Length: 208  
Fragment?: false
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Protein
Q8C399
Organism: Mus musculus/domesticus
Length: 195  
Fragment?: true
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Protein
Q925A3
Organism: Mus musculus/domesticus
Length: 153  
Fragment?: false
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Publication
12145206 | -
First Author: Skjerpen CS
Year: 2002
Journal: EMBO J
Title: Binding of FGF-1 variants to protein kinase CK2 correlates with mitogenicity.
Volume: 21
Issue: 15
Pages: 4058-69
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Publication
10574949 | -
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
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Publication
15781473 | J:99916
First Author: Davidson D
Year: 2005
Journal: J Biol Chem
Title: Fibroblast growth factor (FGF) 18 signals through FGF receptor 3 to promote chondrogenesis.
Volume: 280
Issue: 21
Pages: 20509-15
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Publication
8663044 | -
First Author: Ornitz DM
Year: 1996
Journal: J Biol Chem
Title: Receptor specificity of the fibroblast growth factor family.
Volume: 271
Issue: 25
Pages: 15292-7
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Protein
Q3US41
Organism: Mus musculus/domesticus
Length: 680  
Fragment?: false
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Protein
Q8K0G8
Organism: Mus musculus/domesticus
Length: 717  
Fragment?: false
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Protein
Q544I6
Organism: Mus musculus/domesticus
Length: 194  
Fragment?: false
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Protein
A0A7U3JW48
Organism: Mus musculus/domesticus
Length: 260  
Fragment?: false
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Protein
D3Z139
Organism: Mus musculus/domesticus
Length: 592  
Fragment?: true
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Protein
Z4YJI3
Organism: Mus musculus/domesticus
Length: 659  
Fragment?: false
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Protein
F8WGU3
Organism: Mus musculus/domesticus
Length: 681  
Fragment?: false
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Protein
Q8C386
Organism: Mus musculus/domesticus
Length: 194  
Fragment?: false
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Publication
16597617 | J:153201
First Author: Zhang X
Year: 2006
Journal: J Biol Chem
Title: Receptor specificity of the fibroblast growth factor family. The complete mammalian FGF family.
Volume: 281
Issue: 23
Pages: 15694-700
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Publication
2549857 | -
 
First Author: Burgess WH
Year: 1989
Journal: Annu Rev Biochem
Title: The heparin-binding (fibroblast) growth factor family of proteins.
Volume: 58
Pages: 575-606
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Publication
7583099 | -
First Author: Wilkie AO
Year: 1995
Journal: Curr Biol
Title: Functions of fibroblast growth factors and their receptors.
Volume: 5
Issue: 5
Pages: 500-7
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Publication
3072709 | -
First Author: Thomas KA
Year: 1988
Journal: Trends Biochem Sci
Title: Transforming potential of fibroblast growth factor genes.
Volume: 13
Issue: 9
Pages: 327-8
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Publication
11276432 | J:67832
First Author: Ornitz DM
Year: 2001
Journal: Genome Biol
Title: Fibroblast growth factors.
Volume: 2
Issue: 3
Pages: REVIEWS3005
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Publication
10830168 | -
First Author: Plotnikov AN
Year: 2000
Journal: Cell
Title: Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity.
Volume: 101
Issue: 4
Pages: 413-24
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Publication
8652550 | -
First Author: Blaber M
Year: 1996
Journal: Biochemistry
Title: X-ray crystal structure of human acidic fibroblast growth factor.
Volume: 35
Issue: 7
Pages: 2086-94
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Publication
1705486 | -
First Author: Vlodavsky I
Year: 1990
Journal: Cancer Metastasis Rev
Title: Extracellular matrix-resident growth factors and enzymes: possible involvement in tumor metastasis and angiogenesis.
Volume: 9
Issue: 3
Pages: 203-26
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Publication
8760337 | -
First Author: Green PJ
Year: 1996
Journal: Bioessays
Title: Promiscuity of fibroblast growth factor receptors.
Volume: 18
Issue: 8
Pages: 639-46
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Publication
23000357 | -
First Author: Yardley N
Year: 2012
Journal: Dev Biol
Title: FGF signaling transforms non-neural ectoderm into neural crest.
Volume: 372
Issue: 2
Pages: 166-77
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Publication
15689573 | -
First Author: Böttcher RT
Year: 2005
Journal: Endocr Rev
Title: Fibroblast growth factor signaling during early vertebrate development.
Volume: 26
Issue: 1
Pages: 63-77
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Publication
10441498 | J:56785
First Author: Koga C
Year: 1999
Journal: Biochem Biophys Res Commun
Title: Characterization of a novel member of the FGF family, XFGF-20, in Xenopus laevis.
Volume: 261
Issue: 3
Pages: 756-65
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Publication
23108135 | -
First Author: Nakamizo S
Year: 2013
Journal: Skin Pharmacol Physiol
Title: Topical treatment with basic fibroblast growth factor promotes wound healing and barrier recovery induced by skin abrasion.
Volume: 26
Issue: 1
Pages: 22-9
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Publication
23016864 | -
First Author: Kumar SB
Year: 2013
Journal: Curr Pharm Des
Title: Fibroblast growth factor receptor inhibitors.
Volume: 19
Issue: 4
Pages: 687-701
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Publication
1649700 | -
First Author: Amaya E
Year: 1991
Journal: Cell
Title: Expression of a dominant negative mutant of the FGF receptor disrupts mesoderm formation in Xenopus embryos.
Volume: 66
Issue: 2
Pages: 257-70
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Publication
11746231 | -
First Author: Borland CZ
Year: 2001
Journal: Bioessays
Title: Fibroblast growth factor signaling in Caenorhabditis elegans.
Volume: 23
Issue: 12
Pages: 1120-30
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Publication
14745970 | -
First Author: Coumoul X
Year: 2003
Journal: Birth Defects Res C Embryo Today
Title: Roles of FGF receptors in mammalian development and congenital diseases.
Volume: 69
Issue: 4
Pages: 286-304
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Publication
8978613 | -
First Author: Sutherland D
Year: 1996
Journal: Cell
Title: branchless encodes a Drosophila FGF homolog that controls tracheal cell migration and the pattern of branching.
Volume: 87
Issue: 6
Pages: 1091-101
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Protein Coding Gene
MGI:1925544 | Rps27a
Type: protein_coding_gene
Organism: mouse, laboratory
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•
Protein Coding Gene
MGI:98887 | Uba52
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:98888 | Ubb
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:98889 | Ubc
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein
P62984
Organism: Mus musculus/domesticus
Length: 128  
Fragment?: false
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•
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•
Protein
P0CG50
Organism: Mus musculus/domesticus
Length: 734  
Fragment?: false
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•
•
•
Protein
P62983
Organism: Mus musculus/domesticus
Length: 156  
Fragment?: false
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•
•
•
•
Protein
P0CG49
Organism: Mus musculus/domesticus
Length: 305  
Fragment?: false
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•
•
•




MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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