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Search results 1401 to 1483 out of 1483 for Pdgfa

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Type Details Score
Protein
Organism: Mus musculus/domesticus
Length: 670  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 663  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 173  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 373  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 373  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 400  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 323  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 437  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 663  
Fragment?: false
Publication
First Author: Suriano AR
Year: 2005
Journal: Mol Cell Biol
Title: GCF2/LRRFIP1 represses tumor necrosis factor alpha expression.
Volume: 25
Issue: 20
Pages: 9073-81
Publication
First Author: Dai P
Year: 2009
Journal: J Immunol
Title: Modulation of TLR signaling by multiple MyD88-interacting partners including leucine-rich repeat Fli-I-interacting proteins.
Volume: 182
Issue: 6
Pages: 3450-60
Publication
First Author: Liu J
Year: 2005
Journal: Proc Natl Acad Sci U S A
Title: Identification of the Wnt signaling activator leucine-rich repeat in Flightless interaction protein 2 by a genome-wide functional analysis.
Volume: 102
Issue: 6
Pages: 1927-32
Protein Domain
Type: Family
Description: Leucine-rich repeat flightless-interacting protein 1 (LRRFIP1) is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'-AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA []. It may control smooth muscle cell proliferation following artery injury through PDGFA repression and may also bind double-stranded RNA. It interacts with the leucine-rich repeat domain of human flightless-I (FliI) protein [].Leucine-rich repeat flightless-interacting protein 2 (LRRFIP2) may function as activator of the canonical Wnt signaling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin []. It positively regulates Toll-like receptor (TLR) signalling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding [].
Publication
First Author: Saba L
Year: 2006
Journal: Mamm Genome
Title: Candidate genes and their regulatory elements: alcohol preference and tolerance.
Volume: 17
Issue: 6
Pages: 669-88
Genotype
Symbol: Pdgfa/Pdgfa Pdgfra/Pdgfra<+>
Background: involves: 129S1/Sv * 129S4/SvJaeSor * 129X1/SvJ * C57BL/6
Zygosity: cx
Has Mutant Allele: true
Publication
First Author: Ozawa T
Year: 2014
Journal: Cancer Cell
Title: Most human non-GCIMP glioblastoma subtypes evolve from a common proneural-like precursor glioma.
Volume: 26
Issue: 2
Pages: 288-300
Publication
First Author: Philip B
Year: 2018
Journal: Cell Rep
Title: Mutant IDH1 Promotes Glioma Formation In Vivo.
Volume: 23
Issue: 5
Pages: 1553-1564
Publication
First Author: Hoeman CM
Year: 2019
Journal: Nat Commun
Title: ACVR1 R206H cooperates with H3.1K27M in promoting diffuse intrinsic pontine glioma pathogenesis.
Volume: 10
Issue: 1
Pages: 1023
Publication
First Author: Smith JC
Year: 2007
Journal: J Proteome Res
Title: A differential phosphoproteomic analysis of retinoic acid-treated P19 cells.
Volume: 6
Issue: 8
Pages: 3174-86
Publication  
First Author: Baguma-Nibasheka M
Year: 2021
Journal: Cells
Title: Regulation of Transplanted Cell Homing by FGF1 and PDGFB after Doxorubicin Myocardial Injury.
Volume: 10
Issue: 11
Publication
First Author: Tomita Y
Year: 2022
Journal: Glia
Title: A novel mouse model of diffuse midline glioma initiated in neonatal oligodendrocyte progenitor cells highlights cell-of-origin dependent effects of H3K27M.
Volume: 70
Issue: 9
Pages: 1681-1698
Publication
First Author: Habets GG
Year: 1992
Journal: Cytogenet Cell Genet
Title: Sublocalization of an invasion-inducing locus and other genes on human chromosome 7.
Volume: 60
Issue: 3-4
Pages: 200-5
Publication
First Author: Muratoglu SC
Year: 2011
Journal: PLoS One
Title: Macrophage LRP1 suppresses neo-intima formation during vascular remodeling by modulating the TGF-β signaling pathway.
Volume: 6
Issue: 12
Pages: e28846
Publication
First Author: Yie TA
Year: 2023
Journal: Am J Respir Cell Mol Biol
Title: Hedgehog and Platelet-derived Growth Factor Signaling Intersect during Postnatal Lung Development.
Volume: 68
Issue: 5
Pages: 523-536
Protein Domain
Type: Domain
Description: Platelet-derived growth factor (PDGF) [, ]is a potent mitogen for cells ofmesenchymal origin, including smooth muscle cells and glial cells. In both mouse and human, the PDGF signalling network consists of four ligands, PDGFA-D, and two receptors, PDGFRalpha and PDGFRbeta. All PDGFs function as secreted, disulphide-linkedhomodimers, but only PDGFA and B can form functional heterodimers. PDGFRs also function as homo- and heterodimers. All known PDGFs have characteristic `PDGF domains',which include eight conserved cysteines that are involved in inter- and intramolecular bonds.Alternate splicing of the A chain transcript can give rise to two differentforms that differ only in their C-terminal extremity. The transforming proteinof Woolly monkey sarcoma virus (WMSV) (Simian sarcoma virus), encoded by the v-sis oncogene, is derived from the B chain of PDGF.PDGFs are mitogenic during early developmental stages, driving the proliferation of undifferentiated mesenchyme and some progenitor populations. During later maturation stages, PDGF signalling has been implicated in tissue remodelling and cellular differentiation, and in inductive events involved in patterning and morphogenesis. In addition to drivingmesenchymal proliferation, PDGFs have been shown to direct the migration, differentiation and function of a variety of specialised mesenchymal and migratory cell types, both during development and in theadult animal [].PDGF is structurally related to a number of other growth factors which also form disulphide-linked homo- or heterodimers.This domain consists of the N-terminal regions of PGDF A and B.
Protein Domain
Type: Family
Description: Platelet-derived growth factor (PDGF) [, ]is a potent mitogen for cells of mesenchymal origin, including smooth muscle cells and glial cells. In both mouse and human, the PDGF signalling network consists of four ligands, PDGFA-D, and two receptors, PDGFRalpha and PDGFRbeta. All PDGFs function as secreted, disulphide-linked homodimers, but only PDGFA and B can form functional heterodimers. PDGFRs also function as homo- and heterodimers. All known PDGFs have characteristic `PDGF domains', which include eight conserved cysteines that are involved in inter- and intramolecular bonds. Alternate splicing of the A chain transcript can give rise to two different forms that differ only in their C-terminal extremity. The transforming protein of Woolly monkey sarcoma virus (WMSV) (Simian sarcoma virus), encoded by the v-sis oncogene, is derived from the B chain of PDGF.PDGFs are mitogenic during early developmental stages, driving the proliferation of undifferentiated mesenchyme and some progenitor populations. During later maturation stages, PDGF signalling has been implicated in tissue remodelling and cellular differentiation, and in inductive events involved in patterning and morphogenesis. In addition to driving mesenchymal proliferation, PDGFs have been shown to direct the migration, differentiation and function of a variety of specialised mesenchymal and migratory cell types, both during development and in the adult animal [].PDGF is structurally related to a number of other growth factors which also form disulphide-linked homo- or heterodimers.This entry represents the beta subunit of PGDF.
Protein
Organism: Mus musculus/domesticus
Length: 241  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 241  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 169  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 219  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 241  
Fragment?: false
Publication
First Author: Hannink M
Year: 1989
Journal: Biochim Biophys Acta
Title: Structure and function of platelet-derived growth factor (PDGF) and related proteins.
Volume: 989
Issue: 1
Pages: 1-10
Publication
First Author: Heldin CH
Year: 1992
Journal: EMBO J
Title: Structural and functional studies on platelet-derived growth factor.
Volume: 11
Issue: 12
Pages: 4251-9
Publication
First Author: Hoch RV
Year: 2003
Journal: Development
Title: Roles of PDGF in animal development.
Volume: 130
Issue: 20
Pages: 4769-84
Protein Domain
Type: Domain
Description: Platelet-derived growth factor (PDGF) [, , ]is a potent mitogen for cells of mesenchymal origin, including smooth muscle cells and glial cells. In both mouse and human, the PDGF signalling network consists of four ligands, PDGFA-D, and two receptors, PDGFRalpha and PDGFRbeta. All PDGFs function as secreted, disulphide-linkedhomodimers, but only PDGFA and B can form functional heterodimers. PDGFRs also function as homo- and heterodimers. All known PDGFs have characteristic 'PDGF domains', which include eight conserved cysteines that are involved in inter- and intramolecular bonds. Alternate splicing of the A chain transcript can give rise to two different forms that differ only in their C-terminal extremity. The transforming protein of Woolly monkey sarcoma virus (WMSV) (Simian sarcoma virus), encoded by the v-sis oncogene, is derived from the B chain of PDGF.PDGFs are mitogenic during early developmental stages, driving the proliferation of undifferentiated mesenchyme and some progenitor populations. During later maturation stages, PDGF signalling has been implicated in tissue remodelling and cellular differentiation, and in inductive events involved in patterning and morphogenesis. In addition to driving mesenchymal proliferation, PDGFs have been shown to direct the migration, differentiation and function of a variety of specialised mesenchymal and migratory cell types, both during development and in the adult animal [].Other growth factors in this family include vascular endothelial growth factors B and C (VEGF-B, VEGF-C) [, ]which are active in angiogenesis and endothelial cell growth, and placenta growth factor (PlGF) which is also active in angiogenesis []. VEGF is a potent mitogen in embryonic and somatic angiogenesis with a unique specificity for vascular endothelial cells. VEGF forms homodimers and exists in 4 different isoforms. Overall, the VEGF monomer resembles that of PDGF, but its N-terminal segment is helical rather than extended.PDGF is structurally related to a number of other growth factors which also form disulphide-linked homo- or heterodimers. A cysteine knot motif is a common feature of this domain [, , ].
Publication
First Author: Girolamo F
Year: 2019
Journal: PLoS One
Title: Defining the role of NG2-expressing cells in experimental models of multiple sclerosis. A biofunctional analysis of the neurovascular unit in wild type and NG2 null mice.
Volume: 14
Issue: 3
Pages: e0213508
Protein
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 196  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
Publication
First Author: Oefner C
Year: 1992
Journal: EMBO J
Title: Crystal structure of human platelet-derived growth factor BB.
Volume: 11
Issue: 11
Pages: 3921-6
Protein Domain
Type: Conserved_site
Description: Platelet-derived growth factor (PDGF) [, , ]is a potent mitogen for cells of mesenchymal origin, including smooth muscle cells and glial cells. In both mouse and human, the PDGF signalling network consists of four ligands, PDGFA-D, and two receptors, PDGFRalpha and PDGFRbeta. All PDGFs function as secreted, disulphide-linkedhomodimers, but only PDGFA and B can form functional heterodimers. PDGFRs also function as homo- and heterodimers. All known PDGFs have characteristic 'PDGF domains', which include eight conserved cysteines that are involved in inter- and intramolecular bonds. Alternate splicing of the A chain transcript can give rise to two different forms that differ only in their C-terminal extremity. The transforming protein of Woolly monkey sarcoma virus (WMSV) (Simian sarcoma virus), encoded by the v-sis oncogene, is derived from the B chain of PDGF.PDGFs are mitogenic during early developmental stages, driving the proliferation of undifferentiated mesenchyme and some progenitor populations. During later maturation stages, PDGF signalling has been implicated in tissue remodelling and cellular differentiation, and in inductive events involved in patterning and morphogenesis. In addition to driving mesenchymal proliferation, PDGFs have been shown to direct the migration, differentiation and function of a variety of specialised mesenchymal and migratory cell types, both during development and in the adult animal [].Other growth factors in this family include vascular endothelial growth factors B and C (VEGF-B, VEGF-C) [, ]which are active in angiogenesis and endothelial cell growth, and placenta growth factor (PlGF) which is also active in angiogenesis []. VEGF is a potent mitogen in embryonic and somatic angiogenesis with a unique specificity for vascular endothelial cells. VEGF forms homodimers and exists in 4 different isoforms. Overall, the VEGF monomer resembles that of PDGF, but its N-terminal segment is helical rather than extended.PDGF is structurally related to a number of other growth factors which also form disulphide-linked homo- or heterodimers. A cysteine knot motif is a common feature of this domain [, , ].This entry represents a conserved site found in PDGF and VEGF families, amongst others, that includes four of the eight cysteines conserved in the sequences of these proteins. In PDGF, these cysteines are known to be involved in intra and inter-chain disulphide bonds [].
Protein
Organism: Mus musculus/domesticus
Length: 158  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 214  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 358  
Fragment?: false
Publication
First Author: Olofsson B
Year: 1996
Journal: Proc Natl Acad Sci U S A
Title: Vascular endothelial growth factor B, a novel growth factor for endothelial cells.
Volume: 93
Issue: 6
Pages: 2576-81
Protein
Organism: Mus musculus/domesticus
Length: 207  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 415  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 123  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 208  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 118  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 368  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 392  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 81  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 137  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 64  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 162  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 170  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 158  
Fragment?: false
Publication
First Author: Joukov V
Year: 1996
Journal: EMBO J
Title: A novel vascular endothelial growth factor, VEGF-C, is a ligand for the Flt4 (VEGFR-3) and KDR (VEGFR-2) receptor tyrosine kinases.
Volume: 15
Issue: 2
Pages: 290-98
Publication
First Author: Maglione D
Year: 1993
Journal: Oncogene
Title: Two alternative mRNAs coding for the angiogenic factor, placenta growth factor (PlGF), are transcribed from a single gene of chromosome 14.
Volume: 8
Issue: 4
Pages: 925-31
Publication
First Author: Muller YA
Year: 1997
Journal: Proc Natl Acad Sci U S A
Title: Vascular endothelial growth factor: crystal structure and functional mapping of the kinase domain receptor binding site.
Volume: 94
Issue: 14
Pages: 7192-7
Publication
First Author: Westermark B
Year: 1993
Journal: Acta Oncol
Title: Platelet-derived growth factor. Structure, function and implications in normal and malignant cell growth.
Volume: 32
Issue: 2
Pages: 101-5
Publication
First Author: Shibuya M
Year: 2001
Journal: Cell Struct Funct
Title: Structure and function of VEGF/VEGF-receptor system involved in angiogenesis.
Volume: 26
Issue: 1
Pages: 25-35
Protein
Organism: Mus musculus/domesticus
Length: 345  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 370  
Fragment?: false
Publication
First Author: Zhou H
Year: 2008
Journal: J Proteome Res
Title: Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis.
Volume: 7
Issue: 9
Pages: 3957-67
Publication
First Author: Sweet SM
Year: 2009
Journal: Mol Cell Proteomics
Title: Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry.
Volume: 8
Issue: 5
Pages: 904-12
Publication        
First Author: Mouse Genome Database and National Center for Biotechnology Information Editorial Staff Collaboration
Year: 2001
Title: LocusLink Collaboration
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: MGC Data curation in Mouse Genome Informatics
Publication
First Author: Friedel RH
Year: 2007
Journal: Brief Funct Genomic Proteomic
Title: EUCOMM--the European conditional mouse mutagenesis program.
Volume: 6
Issue: 3
Pages: 180-5
Publication
First Author: Park J
Year: 2013
Journal: Mol Cell
Title: SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways.
Volume: 50
Issue: 6
Pages: 919-30
Publication      
First Author: Velocigene
Year: 2008
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by Velocigene (Regeneron Pharmaceuticals)
Publication        
First Author: Haiming Tang, Dustin Ebert, Matthias Blum, Robert Finn, Paul Thomas
Year: 2023
Title: TreeGrafter-generated GO annotations
Publication      
First Author: International Mouse Strain Resource
Year: 2014
Journal: Database Download
Title: MGI download of germline transmission data for alleles from IMSR strain data
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Journal: Database Download
Title: Integrating Computational Gene Models into the Mouse Genome Informatics (MGI) Database
Publication      
First Author: Shanghai Model Organisms Center
Year: 2017
Journal: MGI Direct Data Submission
Title: Information obtained from the Shanghai Model Organisms Center (SMOC), Shanghai, China
Publication
First Author: Villén J
Year: 2007
Journal: Proc Natl Acad Sci U S A
Title: Large-scale phosphorylation analysis of mouse liver.
Volume: 104
Issue: 5
Pages: 1488-93
Publication      
First Author: Wellcome Trust Sanger Institute
Year: 2009
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by the Wellcome Trust Sanger Institute
Publication
First Author: Magdaleno S
Year: 2006
Journal: PLoS Biol
Title: BGEM: an in situ hybridization database of gene expression in the embryonic and adult mouse nervous system.
Volume: 4
Issue: 4
Pages: e86
Publication        
First Author: GOA curators
Year: 2016
Title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Publication
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7
Publication
First Author: Huttlin EL
Year: 2010
Journal: Cell
Title: A tissue-specific atlas of mouse protein phosphorylation and expression.
Volume: 143
Issue: 7
Pages: 1174-89