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PDGFRbeta was activated around the injury site after experimental traumatic brain injury (TBI), and primarily expressed in astrocytes, microglia, OPC and leukocytes in the boundary of the lesion site, suggesting PDGFRbeta was involved in glial scar formation. Then the PDGFR inhibitor (AG1296) was administered following TBI. Reactive astrocytes were significantly inhibited in AG1296-treated mice.
Increasing the adipogenic capacity of Pdgfrbeta(+) precursors through Pparg overexpression results in healthy visceral white adipose tissue expansion in obesity and adiponectin-dependent improvements in glucose homeostasis.
PDGFRalpha/PDGFRbeta signaling balance determines progenitor commitment to beige (PDGFRalpha) or white (PDGFRbeta) adipogenesis.
The data of this study revealed an acute accumulation of PDGFRbeta+ BBB-related cells in degenerating brain areas, which can be long lasting, suggesting an active role for PDGFRbeta-signaling in blood vessel and post-injury tissue recovery.
Ltbp4 regulates Pdgfrb expression via TGFbeta (show TGFB1 Proteins)-dependent modulation of Nrf2 (show NFE2L2 Proteins) transcription factor function.
The results provide functional evidence that elevated PDGFRbeta signaling causes tissue wasting or overgrowth reminiscent of human genetic syndromes and that the STAT1 (show STAT1 Proteins) pathway is a crucial modulator of this phenotypic spectrum.
Identify PDGFRbeta as a driver in activating Akt (show AKT1 Proteins)/mTORC1 nexus for high glucose-mediated expression of collagen I (alpha2) in proximal tubular epithelial cells, which contributes to tubulointerstitial fibrosis in diabetic nephropathy.
Data show that three platelet-derived growth factor receptor beta (PDGFRB) mutants (R561C, P660T and N666K) were able to transform NIH3T3 and Ba/F3 cells to different extents.
data therefore collectively suggest that upon TGFbeta (show TGFB1 Proteins) stimulation, SP1 (show SP1 Proteins) recruits SMAD2 (show SMAD2 Proteins) to the promoter of Pdgfrb to up-regulate its expression and thus Pdgfrb is a direct downstream target of the TGFbeta (show TGFB1 Proteins)/SMAD2 (show SMAD2 Proteins) signaling
PdgfrbetaF7/F7 mice between 4-6 and 36-48 weeks of age developed a region-dependent loss in pericyte coverage (22-46, 24-44 and 4-31%) and cell numbers (36-49, 34-64 and 11-36%), reduction in capillary length (20-39, 13-46 and 1-30%), and an increase in extravascular fibrinogen-derived deposits (3.4-5.2, 2.8-4.1 and 0-3.6-fold) demonstrating BBB breakdown in the cortex, hippocampus and thalamus, respectively.
Study investigated the more detailed mechanism for this cis (show CISH Proteins)-interaction of Necl-5 (show PVR Proteins) with the PDGF (show PDGFA Proteins) receptor beta. Necl-5 (show PVR Proteins) contains three Ig-like domains and the PDGF (show PDGFA Proteins) receptor beta contains five Ig-like domains at their extracellular regions; showed that the third Ig-like domain of Necl-5 (show PVR Proteins) cis (show CISH Proteins)-interacted with the fifth Ig-like domain of the PDGF (show PDGFA Proteins) receptor beta.
Melatonin reinforces the anticancer activity of sorafenib by downregulation of PDGFR-beta/STAT3 (show STAT3 Proteins) signaling pathway and melatonin receptor (MT)-mediated STAT3 (show STAT3 Proteins).
High GLI2 or PDGFRB expression is associated with unfavorable survival in GC patients. GLI2 can induce PDGFRB expression in GC cells via directly binding to its promoter. In addition, the GLI2-PDGFRB axis might be an important signaling pathway modulating CSC properties of GC cells.
The cell surface PDGFRB is a major link between high glucose and its effectors Hif1a (show HIF1A Proteins) and TGFB (show TGFB1 Proteins) for induction of diabetic mesangial cell hypertrophy.
describes three unique PDGFRB fusions in childhood B- or T-ALL. All three PDGFRB fusion partners have previously been reported to be implicated in hematopoiesis and immune responses
These findings indicated that miR (show MLXIP Proteins)-518b may function as a tumor suppressor by targeting PDGFRB in the occurrence and development of GBM.
Data show that an equilibrium mixture of two unusual end-insertion G-quadruplexes forms in a native promoter sequence and appears to be the molecular recognition for platelet derived growth factor receptor beta (PDGFR-beta) downregulation.
Case Report: heterozygous PDGFRB mutation in a family presenting with multicentric autosomal dominant infantile myofibromatosis.
anlotinib inhibits the activation of VEGFR2 (show KDR Proteins), PDGFRbeta and FGFR1 (show FGFR1 Proteins) as well their common downstream ERK (show EPHB2 Proteins) signaling
PDGFRB is not a major causative gene of primary familial brain calcification in Chinese population.
This gene encodes a cell surface tyrosine kinase receptor for members of the platelet-derived growth factor family. These growth factors are mitogens for cells of mesenchymal origin. The identity of the growth factor bound to a receptor monomer determines whether the functional receptor is a homodimer or a heterodimer, composed of both platelet-derived growth factor receptor alpha and beta polypeptides. This gene is flanked on chromosome 5 by the genes for granulocyte-macrophage colony-stimulating factor and macrophage-colony stimulating factor receptor\; all three genes may be implicated in the 5-q syndrome. A translocation between chromosomes 5 and 12, that fuses this gene to that of the translocation, ETV6, leukemia gene, results in chronic myeloproliferative disorder with eosinophilia.
CD140 antigen-like family member B
, PDGF beta chain
, beta platelet-derived growth factor receptor
, beta-type platelet-derived growth factor receptor
, platelet-derived growth factor receptor 1
, platelet-derived growth factor receptor beta
, platelet-derived growth factor receptor beta variant 1
, Platelet-derived growth factor receptor, beta
, protein tyrosin kinase