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Search results 1001 to 1100 out of 1271 for Fgfr4

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0.017s

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Hits by Strain

Type Details Score
Protein
P32883
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: false
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Protein
P08556
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: false
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Protein
P35235
Organism: Mus musculus/domesticus
Length: 593  
Fragment?: false
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Publication
9742123 | J:50034
First Author: Hu MC
Year: 1998
Journal: Mol Cell Biol
Title: FGF-18, a novel member of the fibroblast growth factor family, stimulates hepatic and intestinal proliferation.
Volume: 18
Issue: 10
Pages: 6063-74
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Publication
15896984 | -
First Author: Moore EE
Year: 2005
Journal: Osteoarthritis Cartilage
Title: Fibroblast growth factor-18 stimulates chondrogenesis and cartilage repair in a rat model of injury-induced osteoarthritis.
Volume: 13
Issue: 7
Pages: 623-31
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Publication
11741978 | J:75070
First Author: Shimoaka T
Year: 2002
Journal: J Biol Chem
Title: Regulation of osteoblast, chondrocyte, and osteoclast functions by fibroblast growth factor (FGF)-18 in comparison with FGF-2 and FGF-10.
Volume: 277
Issue: 9
Pages: 7493-500
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Protein Domain
IPR002209 | Fibroblast_GF_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 [].
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Protein Domain
IPR028289 | FGF18
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 18 (FGF18), also referred to ZFGF5. FGF18 is required for normal ossification and bone development and stimulates hepatic and intestinal proliferation [, , , ].
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Protein Domain
IPR028253 | FGF11
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 11 (FGF11), also known as fibroblast growth factor homologous factor 3. It currently has no known function, but it is thought to be involved in nervous system development and function [].
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Publication
35588797 | J:327423
First Author: Zhang X
Year: 2022
Journal: Gastroenterology
Title: Induction of Fibroblast Growth Factor Receptor 4 by Helicobacter pylori via Signal Transducer and Activator of Transcription 3 With a Feedforward Activation Loop Involving Steroid Receptor Coactivator Signaling in Gastric Cancer.
Volume: 163
Issue: 3
Pages: 620-636.e9
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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
15806171 | J:100761
First Author: Beer HD
Year: 2005
Journal: Oncogene
Title: The fibroblast growth factor binding protein is a novel interaction partner of FGF-7, FGF-10 and FGF-22 and regulates FGF activity: implications for epithelial repair.
Volume: 24
Issue: 34
Pages: 5269-77
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Protein
P61329
Organism: Mus musculus/domesticus
Length: 243  
Fragment?: false
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Protein
P15656
Organism: Mus musculus/domesticus
Length: 264  
Fragment?: false
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Protein
Q9ESS2
Organism: Mus musculus/domesticus
Length: 162  
Fragment?: false
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Protein
P70379
Organism: Mus musculus/domesticus
Length: 247  
Fragment?: false
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Protein
P70378
Organism: Mus musculus/domesticus
Length: 225  
Fragment?: false
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Protein
P05524
Organism: Mus musculus/domesticus
Length: 245  
Fragment?: false
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Protein
D6RCX9
Organism: Mus musculus/domesticus
Length: 78  
Fragment?: false
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Protein
B1AU23
Organism: Mus musculus/domesticus
Length: 69  
Fragment?: true
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Protein
Q6NXW2
Organism: Mus musculus/domesticus
Length: 197  
Fragment?: false
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Protein
B7ZMS7
Organism: Mus musculus/domesticus
Length: 205  
Fragment?: false
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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
Q3U1V5
Organism: Mus musculus/domesticus
Length: 251  
Fragment?: false
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Protein
Q0VG15
Organism: Mus musculus/domesticus
Length: 245  
Fragment?: false
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Protein
A0A7U3L6F4
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
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Protein
Q3UFZ2
Organism: Mus musculus/domesticus
Length: 115  
Fragment?: false
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Protein
A0A7U3JW51
Organism: Mus musculus/domesticus
Length: 207  
Fragment?: false
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Protein
D3YWD4
Organism: Mus musculus/domesticus
Length: 156  
Fragment?: true
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Protein
A0A1X7SB63
Organism: Mus musculus/domesticus
Length: 221  
Fragment?: true
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Protein
D3YU10
Organism: Mus musculus/domesticus
Length: 157  
Fragment?: false
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Protein
Q71UP6
Organism: Mus musculus/domesticus
Length: 64  
Fragment?: true
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Protein
Q8C471
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: false
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Protein
A0A7U3JW73
Organism: Mus musculus/domesticus
Length: 276  
Fragment?: false
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Protein
A0A7U3JW52
Organism: Mus musculus/domesticus
Length: 162  
Fragment?: false
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Protein
Q0VF19
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: false
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Protein
A0A140LIV6
Organism: Mus musculus/domesticus
Length: 52  
Fragment?: true
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Protein
D3Z6H1
Organism: Mus musculus/domesticus
Length: 60  
Fragment?: false
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Protein
O35340
Organism: Mus musculus/domesticus
Length: 78  
Fragment?: true
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Protein
A0A7U3L698
Organism: Mus musculus/domesticus
Length: 264  
Fragment?: false
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Protein
O54837
Organism: Mus musculus/domesticus
Length: 70  
Fragment?: true
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Protein
A0A7U3JW80
Organism: Mus musculus/domesticus
Length: 202  
Fragment?: false
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Protein
Q7TPG9
Organism: Mus musculus/domesticus
Length: 105  
Fragment?: true
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Protein
A0A338P752
Organism: Mus musculus/domesticus
Length: 115  
Fragment?: false
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Protein
Q0VBJ8
Organism: Mus musculus/domesticus
Length: 251  
Fragment?: false
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Protein
Q5SQB3
Organism: Mus musculus/domesticus
Length: 98  
Fragment?: false
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Protein
A0A338P764
Organism: Mus musculus/domesticus
Length: 171  
Fragment?: true
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Protein
D3Z192
Organism: Mus musculus/domesticus
Length: 49  
Fragment?: true
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Protein
C6EQH1
Organism: Mus musculus/domesticus
Length: 115  
Fragment?: false
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Protein
A0A7U3L4H2
Organism: Mus musculus/domesticus
Length: 225  
Fragment?: false
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Protein
A0A7U3JW65
Organism: Mus musculus/domesticus
Length: 243  
Fragment?: false
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Protein
A0A067XG51
Organism: Mus musculus/domesticus
Length: 97  
Fragment?: true
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Protein
D3Z6E2
Organism: Mus musculus/domesticus
Length: 78  
Fragment?: true
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Protein
Q6ZWS1
Organism: Mus musculus/domesticus
Length: 155  
Fragment?: false
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Protein
O89096
Organism: Mus musculus/domesticus
Length: 252  
Fragment?: false
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Protein
Q925A3
Organism: Mus musculus/domesticus
Length: 153  
Fragment?: false
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Protein
A0A494BBG9
Organism: Mus musculus/domesticus
Length: 104  
Fragment?: false
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Protein
Q059W0
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
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Protein
A0A0R4J063
Organism: Mus musculus/domesticus
Length: 247  
Fragment?: false
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Protein
Q0VER9
Organism: Mus musculus/domesticus
Length: 126  
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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Protein Domain
IPR028303 | FGF15/FGF19
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 [].Fibroblast growth factor 15 (FGF15) plays a key role in enterohepatic signaling, regulation of liver bile acid biosynthesis, gallbladder motility and metabolic homeostasis [, , ]. Mouse FGF15 has been shown to be stimulated when bile acids bind to farnesoid X receptor (FXR) [], and is therefore thought to a factor in chronic bile acid diarrhoea and in certain metabolic disorders [].FGF15 has been experimentally characterised in mouse, but has not been found in other species. However, there is an orthologous human protein, FGF19, and together they share about 50% amino acid identity and display similar endocrine functions, so are often referred to as FGF15/19 [, ]. FGF15 and FGF19 differ from other FGFs due to subtle changes in their tertiary structure, they have low heparin binding affinity enabling them to diffuse away from their site of secretion and signal to distantcells. FGF signaling through the FGF receptors is also different, as they require klotho protein cofactors rather than heparin sulfate proteoglycan [].Fibroblast growth factor 19 (FGF19) plays a key role in enterohepatic signaling, regulation of liver bile acid biosynthesis, gallbladder motility and metabolic homeostasis [, , ]. Human FGF19 expression has been shown to be stimulated approximately 300-fold by physiological concentrations of bile acids including chenodeoxycholic acid, glycochenodeoxycholic acid and obeticholic acid in explants of ileal mucosa []. The protein is thought to be a factor in chronic bile acid diarrhoea and in certain metabolic disorders [, ]. FGF19 has been experimentally characterised in humans and other species, but has not been found in mouse. However there is an orthologous mouse protein, FGF15, and together they share about 50% amino acid identity and display similar endocrine functions, so are often referred to as FGF15/19 [, ]. FGF15 and FGF19 differ from other FGFs due to subtle changes in their tertiary structure. They have low heparin binding affinity, enabling them to diffuse away from their site of secretion and signal to distant cells. FGF signaling through the FGF receptors is also different, as they require klotho protein cofactors rather than heparin sulfate proteoglycan []. Unlike other members of the family that can bind several FGF receptors, FGF19 is specific for FGFR4 [].
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Publication
11062477 | J:65463
First Author: ADHR Consortium.
Year: 2000
Journal: Nat Genet
Title: Autosomal dominant hypophosphataemic rickets is associated with mutations in FGF23.
Volume: 26
Issue: 3
Pages: 345-8
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Publication
9514906 | J:46389
First Author: Hoshikawa M
Year: 1998
Journal: Biochem Biophys Res Commun
Title: Structure and expression of a novel fibroblast growth factor, FGF-17, preferentially expressed in the embryonic brain.
Volume: 244
Issue: 1
Pages: 187-91
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Publication
11342227 | J:67825
First Author: Nakatake Y
Year: 2001
Journal: Biochim Biophys Acta
Title: Identification of a novel fibroblast growth factor, FGF-22, preferentially expressed in the inner root sheath of the hair follicle.
Volume: 1517
Issue: 3
Pages: 460-3
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Publication
20145243 | -
First Author: Fernández IS
Year: 2010
Journal: J Biol Chem
Title: Gentisic acid, a compound associated with plant defense and a metabolite of aspirin, heads a new class of in vivo fibroblast growth factor inhibitors.
Volume: 285
Issue: 15
Pages: 11714-29
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Publication
10510314 | -
 
First Author: Mizukoshi E
Year: 1999
Journal: Biochem J
Title: Fibroblast growth factor-1 interacts with the glucose-regulated protein GRP75/mortalin.
Volume: 343 Pt 2
Pages: 461-6
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Publication
9806903 | -
 
First Author: Kolpakova E
Year: 1998
Journal: Biochem J
Title: Cloning of an intracellular protein that binds selectively to mitogenic acidic fibroblast growth factor.
Volume: 336 ( Pt 1)
Pages: 213-22
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Publication
1721615 | -
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
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Publication
8530375 | -
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
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Publication
9826564 | J:51038
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
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Publication
11716516 | -
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
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Publication
21306635 | -
 
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
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Publication
9477322 | J:47321
First Author: Kim HJ
Year: 1998
Journal: Development
Title: FGF-, BMP- and Shh-mediated signalling pathways in the regulation of cranial suture morphogenesis and calvarial bone development.
Volume: 125
Issue: 7
Pages: 1241-51
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Publication
8001146 | -
First Author: Laufer E
Year: 1994
Journal: Cell
Title: Sonic hedgehog and Fgf-4 act through a signaling cascade and feedback loop to integrate growth and patterning of the developing limb bud.
Volume: 79
Issue: 6
Pages: 993-1003
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Publication
7923352 | J:20551
First Author: Hébert JM
Year: 1994
Journal: Cell
Title: FGF5 as a regulator of the hair growth cycle: evidence from targeted and spontaneous mutations.
Volume: 78
Issue: 6
Pages: 1017-25
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Publication
12713572 | J:83352
First Author: Cho YM
Year: 2003
Journal: J Invest Dermatol
Title: Hair-cycle-dependent expression of parathyroid hormone-related protein and its type I receptor: evidence for regulation at the anagen to catagen transition.
Volume: 120
Issue: 5
Pages: 715-27
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Publication
2915979 | J:29167
First Author: Rubin JS
Year: 1989
Journal: Proc Natl Acad Sci U S A
Title: Purification and characterization of a newly identified growth factor specific for epithelial cells.
Volume: 86
Issue: 3
Pages: 802-6
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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
12072406 | -
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
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Publication
10362017 | -
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
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Publication
16700629 | J:110252
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
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Publication
11290325 | J:68379
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
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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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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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