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Search results 2401 to 2500 out of 2616 for Fgfr1

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Type Details Score
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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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
32103583 | J:289968
     
First Author: Bae JH
Year: 2020
Journal: J Cachexia Sarcopenia Muscle
Title: Satellite cell-specific ablation of Cdon impairs integrin activation, FGF signalling, and muscle regeneration.
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Publication
26818521 | J:231463
First Author: Haque K
Year: 2016
Journal: J Neurosci
Title: MEKK4 Signaling Regulates Sensory Cell Development and Function in the Mouse Inner Ear.
Volume: 36
Issue: 4
Pages: 1347-61
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Publication
28674667 | J:247584
 
First Author: Collette JC
Year: 2017
Journal: PeerJ
Title: -Glial and stem cell expression of murine Fibroblast Growth Factor Receptor 1 in the embryonic and perinatal nervous system.
Volume: 5
Pages: e3519
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Publication
28439461 | J:247583
 
First Author: Choubey L
Year: 2017
Journal: PeerJ
Title: Quantitative assessment of fibroblast growth factor receptor 1 expression in neurons and glia.
Volume: 5
Pages: e3173
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Publication
36153352 | J:334765
First Author: Hurley MM
Year: 2022
Journal: Sci Rep
Title: FGF receptor inhibitor BGJ398 partially rescues osteoarthritis-like phenotype in older high molecular weight FGF2 transgenic mice via multiple mechanisms.
Volume: 12
Issue: 1
Pages: 15968
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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
Q8BLW1
Organism: Mus musculus/domesticus
Length: 728  
Fragment?: false
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Protein
Q76LY2
Organism: Mus musculus/domesticus
Length: 37  
Fragment?: true
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Protein
A0A1W2P6Z1
Organism: Mus musculus/domesticus
Length: 168  
Fragment?: true
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Protein
A0A0G2JDZ8
Organism: Mus musculus/domesticus
Length: 272  
Fragment?: true
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Protein
A0A0G2JFT2
Organism: Mus musculus/domesticus
Length: 175  
Fragment?: true
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Protein
A2AK24
Organism: Mus musculus/domesticus
Length: 117  
Fragment?: false
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Protein
A0A0G2JDZ3
Organism: Mus musculus/domesticus
Length: 161  
Fragment?: true
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Protein
A0A0G2JDY6
Organism: Mus musculus/domesticus
Length: 354  
Fragment?: true
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Protein
A0A0G2JFI0
Organism: Mus musculus/domesticus
Length: 169  
Fragment?: true
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Protein
Q6QRP1
Organism: Mus musculus/domesticus
Length: 178  
Fragment?: false
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Protein
J3QNK9
Organism: Mus musculus/domesticus
Length: 154  
Fragment?: true
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Protein
D6RJ38
Organism: Mus musculus/domesticus
Length: 78  
Fragment?: false
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Protein
Q8BUK9
Organism: Mus musculus/domesticus
Length: 114  
Fragment?: true
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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 Domain
IPR043204 | Basigin-like
Type: Family
Description: Neuroplastin and basigin are members of the immunoglobulin (Ig) superfamily. They have two Ig domains that project into the extracellular space. They are also present as isoforms containing an additional N-terminal Ig domain. They contain a glutamate (E) at exactly the same position in the transmembrane domain, which may be important for molecular interactions within the membrane region [].Basigin is present on the surface of tumour cells and stimulate nearby fibroblasts to synthesise matrix metalloproteases (MMPs), which play an important role in tumour invasiveness and metastasis []. Basigin has also been repeatedly implicated in the proper function of the blood brain barrier [, ]. In addition, the protein is essential for fertility in both males and females[]. In males, it is required for the completion of spermatogenesis, while in females, it is needed for maintaining normal reproductive functions. Basigins are highly glycosylated membrane proteins, the degree of glycosylation varying with tissue type. The extracellular region of basigin contains two randomly arranged Ig domains: an Ig-like C2-type domain and an Ig-like V-domain [].Neuroplastin is a probable homophilic and heterophilic cell adhesion molecule involved in long term potentiation at hippocampal excitatory synapses through activation of p38MAPK []. It may also regulate neurite outgrowth by activating the FGFR1 signaling pathway []. It may play a role in synaptic plasticity [].Contactins are cell adhesion molecules that belong to the immunoglobulin superfamily and are involved in neural development []. Contactin-2 (CNTN2/axonin-1/TAG-1/TAX-1) is highly expressed at the axon growth cone and plays an important role in regulating axon guidance and path finding, as well as in neuron migration. Contactin-6 (CNTN6/NB-3) binds Notch and and promotes oligodendrogliogenesis from progenitor cells and differentiation of oligodendrocyte precursor cells.Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays a role in axon guidance, self-avoidance and synaptic formation []. DSCAM is one of the largest Immunoglobulin (Ig) superfamily CAMs [], and contributes to defects in the central nervous system in Down syndrome patients [].This entry represents a family of neuronal cell adhesion molecules that belong to the immunoglobulin superfamily and are involved in neural development.
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Protein
P70377
Organism: Mus musculus/domesticus
Length: 245  
Fragment?: false
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Protein
P36363
Organism: Mus musculus/domesticus
Length: 194  
Fragment?: false
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Protein
E9Q2N2
Organism: Mus musculus/domesticus
Length: 91  
Fragment?: false
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Protein
Q544I6
Organism: Mus musculus/domesticus
Length: 194  
Fragment?: false
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Protein
Q80ZL6
Organism: Mus musculus/domesticus
Length: 244  
Fragment?: false
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Protein
Q3TPG0
Organism: Mus musculus/domesticus
Length: 104  
Fragment?: false
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Protein
A0A140LIL5
Organism: Mus musculus/domesticus
Length: 161  
Fragment?: true
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Protein
Q3TYJ7
Organism: Mus musculus/domesticus
Length: 200  
Fragment?: true
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Protein
E1APJ6
Organism: Mus musculus/domesticus
Length: 208  
Fragment?: false
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Protein
Q3V279
Organism: Mus musculus/domesticus
Length: 215  
Fragment?: false
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Protein
B1AU20
Organism: Mus musculus/domesticus
Length: 187  
Fragment?: false
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Protein
E9Q864
Organism: Mus musculus/domesticus
Length: 30  
Fragment?: true
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Protein
A0A7U3JW48
Organism: Mus musculus/domesticus
Length: 260  
Fragment?: false
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Protein
D3Z208
Organism: Mus musculus/domesticus
Length: 140  
Fragment?: false
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Protein
A0A7U3JW69
Organism: Mus musculus/domesticus
Length: 245  
Fragment?: false
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Protein
D3Z207
Organism: Mus musculus/domesticus
Length: 233  
Fragment?: false
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Protein
A0A7U3L5J2
Organism: Mus musculus/domesticus
Length: 208  
Fragment?: false
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Protein
Q8C386
Organism: Mus musculus/domesticus
Length: 194  
Fragment?: false
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Protein
G3DRA7
Organism: Mus musculus/domesticus
Length: 191  
Fragment?: true
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Protein
A0A7U3JW74
Organism: Mus musculus/domesticus
Length: 203  
Fragment?: false
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Publication
24220145 | J:227323
First Author: Pfefferle AD
Year: 2013
Journal: Genome Biol
Title: Transcriptomic classification of genetically engineered mouse models of breast cancer identifies human subtype counterparts.
Volume: 14
Issue: 11
Pages: R125
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Publication
2361961 | J:10584
First Author: Miyauchi T
Year: 1990
Journal: J Biochem
Title: Basigin, a new, broadly distributed member of the immunoglobulin superfamily, has strong homology with both the immunoglobulin V domain and the beta-chain of major histocompatibility complex class II antigen.
Volume: 107
Issue: 2
Pages: 316-23
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Publication
19945391 | J:155397
First Author: Fuerst PG
Year: 2009
Journal: Neuron
Title: DSCAM and DSCAML1 function in self-avoidance in multiple cell types in the developing mouse retina.
Volume: 64
Issue: 4
Pages: 484-97
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Protein
Q8BSM5
Organism: Mus musculus/domesticus
Length: 595  
Fragment?: false
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Protein
Q9Z1S8
Organism: Mus musculus/domesticus
Length: 665  
Fragment?: false
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Protein
Q505A4
Organism: Mus musculus/domesticus
Length: 695  
Fragment?: false
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Protein
Q3ZB57
Organism: Mus musculus/domesticus
Length: 666  
Fragment?: false
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Protein
B1AYB9
Organism: Mus musculus/domesticus
Length: 556  
Fragment?: false
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Protein
B9EIZ0
Organism: Mus musculus/domesticus
Length: 596  
Fragment?: false
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Protein
Q8BLD3
Organism: Mus musculus/domesticus
Length: 655  
Fragment?: true
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Protein
A0A1B0GS41
Organism: Mus musculus/domesticus
Length: 725  
Fragment?: false
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Protein
Q3ZB56
Organism: Mus musculus/domesticus
Length: 666  
Fragment?: false
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Protein
Q9D003
Organism: Mus musculus/domesticus
Length: 422  
Fragment?: false
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Protein
Q3ZB59
Organism: Mus musculus/domesticus
Length: 665  
Fragment?: false
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Publication
9426258 | J:45496
First Author: Yamakawa K
Year: 1998
Journal: Hum Mol Genet
Title: DSCAM: a novel member of the immunoglobulin superfamily maps in a Down syndrome region and is involved in the development of the nervous system.
Volume: 7
Issue: 2
Pages: 227-37
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Publication
21270903 | -
First Author: Zhu K
Year: 2011
Journal: Neurosci Bull
Title: Down syndrome cell adhesion molecule and its functions in neural development.
Volume: 27
Issue: 1
Pages: 45-52
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Publication
11992541 | -
First Author: Kanekura T
Year: 2002
Journal: Int J Cancer
Title: Basigin (CD147) is expressed on melanoma cells and induces tumor cell invasion by stimulating production of matrix metalloproteinases by fibroblasts.
Volume: 99
Issue: 4
Pages: 520-8
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Publication
2357963 | -
First Author: Seulberger H
Year: 1990
Journal: EMBO J
Title: The inducible blood--brain barrier specific molecule HT7 is a novel immunoglobulin-like cell surface glycoprotein.
Volume: 9
Issue: 7
Pages: 2151-8
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Publication
1383894 | -
First Author: Seulberger H
Year: 1992
Journal: Neurosci Lett
Title: HT7, Neurothelin, Basigin, gp42 and OX-47--many names for one developmentally regulated immuno-globulin-like surface glycoprotein on blood-brain barrier endothelium, epithelial tissue barriers and neurons.
Volume: 140
Issue: 1
Pages: 93-7
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Publication
9559645 | J:46952
First Author: Kuno N
Year: 1998
Journal: FEBS Lett
Title: Female sterility in mice lacking the basigin gene, which encodes a transmembrane glycoprotein belonging to the immunoglobulin superfamily.
Volume: 425
Issue: 2
Pages: 191-4
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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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Protein
Q9JJN1
Organism: Mus musculus/domesticus
Length: 210  
Fragment?: false
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Protein
A0A0A0MQN8
Organism: Mus musculus/domesticus
Length: 122  
Fragment?: false
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Protein
A0A7U3L6A3
Organism: Mus musculus/domesticus
Length: 210  
Fragment?: false
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Protein
O35622
Organism: Mus musculus/domesticus
Length: 218  
Fragment?: false
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Protein
P97300
Organism: Mus musculus/domesticus
Length: 397  
Fragment?: false
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Protein
Z4YLB7
Organism: Mus musculus/domesticus
Length: 277  
Fragment?: false
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Protein
H3BKA7
Organism: Mus musculus/domesticus
Length: 193  
Fragment?: false
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Protein
Q3TJ05
Organism: Mus musculus/domesticus
Length: 386  
Fragment?: false
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Protein
H3BIX4
Organism: Mus musculus/domesticus
Length: 221  
Fragment?: true
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Protein
Q790L8
Organism: Mus musculus/domesticus
Length: 218  
Fragment?: false
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Publication
10858549 | J:63008
First Author: Nishimura T
Year: 2000
Journal: Biochim Biophys Acta
Title: Identification of a novel FGF, FGF-21, preferentially expressed in the liver.
Volume: 1492
Issue: 1
Pages: 203-6
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Publication
15902306 | J:99202
First Author: Kharitonenkov A
Year: 2005
Journal: J Clin Invest
Title: FGF-21 as a novel metabolic regulator.
Volume: 115
Issue: 6
Pages: 1627-35
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Protein
A0A1W2P7R6
Organism: Mus musculus/domesticus
Length: 81  
Fragment?: true
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Publication
18687777 | -
First Author: Coskun T
Year: 2008
Journal: Endocrinology
Title: Fibroblast growth factor 21 corrects obesity in mice.
Volume: 149
Issue: 12
Pages: 6018-27
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Publication
25300137 | -
 
First Author: Mohebiany AN
Year: 2014
Journal: Adv Neurobiol
Title: New insights into the roles of the contactin cell adhesion molecules in neural development.
Volume: 8
Pages: 165-94
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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
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Protein Coding Gene
MGI:98888 | Ubb
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:98889 | Ubc
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
P62984
Organism: Mus musculus/domesticus
Length: 128  
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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