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PURA product is a sequence-specific, single-stranded DNA-binding protein. Additionally we are shipping PURA Antibodies (43) and many more products for this protein.
Showing 5 out of 6 products:
This study underlines the importance of Puralpha in the proliferation of neuronal precursor cells during postnatal brain development and suggest a role for Puralpha in the regulation of the expression and cellular distribution of dendritic and axonal proteins.
Data suggest that Puralpha has a role in nucleotide excision repair and the repair of UVC-induced DNA damage.
Overexpression of Purbeta (show PURB Proteins), but not Puralpha, significantly downregulated GnRH1 (show GNRH1 Proteins) mRNA Levels in transiently transfected GT1 (show MYL4 Proteins)-7 cells, suggesting that Purbeta (show PURB Proteins) acts as a repressor of GnRH1 (show GNRH1 Proteins) gene transcription.
Identification of mrna/protein (mRNA) complexes and their association with rough endoplasmic reticulum equipped with a kinesin motor
Pura is essential for postnatal brain development and developmentally coupled cellular proliferation as revealed by genetic inactivation.
we also determined a region in Pur alpha which is required for the association with the purine rich element binding protein by using deletion mutants of Pur alpha
Puralpha has been shown to colocalize with cyclin A (show CCNA2 Proteins)/Cdk2 (show CDK2 Proteins) and to coimmunoprecipitate with cyclin A (show CCNA2 Proteins) during S-phase and we show that this interaction is mediated by a specific affinity of Puralpha for Cdk2 (show CDK2 Proteins).
analysis of of DNA binding and localized strand separation by Pur alpha and comparison with Pur beta (show PURB Proteins)
Pur alpha and Pur beta (show PURB Proteins) repress smooth muscle alpha-actin (show ACTA2 Proteins) gene transcription by means of DNA strand-selective cis (show CISH Proteins)-element binding and cell type-dependent protein-protein interactions
E2F-1 (show E2F1 Proteins) and Puralpha interplay appears to be involved in the regulation of Puralpha expression and the cell cycle.
The results of this study emphasizes the importance of stress granules in ALS (show IGFALS Proteins) pathogenesis and identifies Pur-alpha as a novel regulator of cytoplasmic stress granules dynamics.
These findings provide definitive evidence for the role of PURA in causing a variable syndrome of neurodevelopmental delay, learning disability, neonatal hypotonia, feeding difficulties, abnormal movements and epilepsy in humans
Mutations in PURA cause profound neonatal hypotonia, seizures, and encephalopathy in 5q31.3 microdeletion syndrome.
Data show that protein PURalpha is specifically involved in the transcriptional activation of the secondary promoter and may exert its function by forming a complex with E2F-1 and RNA polymerase II.
Suggest dynamic interplay between transcriptional activators Pur-alpha/Pur-beta (show PURB Proteins) and repressors in regulating SMalphaA (show ACTA2 Proteins) gene output during myofibroblast differentiation.
This study showed that Pur-alpha showed inadequate expression in monocytes, and the translation of Pur-alpha mRNA was repressed by cell-expressed microRNA.
The study identifies three functionally distinct PURA promoters and show that these are utilized differentially in human cell types and that they respond differently to cytomegalovirus infection.
The ability of Puralpha to activate the CD11c (show ITGAX Proteins) gene promoter increases in differentiating U937 monocytic cells.
acts together with hnRNP-K (show HNRNPK Proteins) to repress the transcriptional activity of the CD43 (show SPN Proteins) gene promoter during lymphocyte activation
results show that PUR proteins are capable of binding to alpha-MHC (show MYH6 Proteins) mRNA and attenuate its translational efficiency; also show robust expression of PUR proteins in failing hearts where alpha-MHC (show MYH6 Proteins) mRNA levels are suppressed
repressor of gata2 gene expression in the nervous system
This gene product is a sequence-specific, single-stranded DNA-binding protein. It binds preferentially to the single strand of the purine-rich element termed PUR, which is present at origins of replication and in gene flanking regions in a variety of eukaryotes from yeasts through humans. Thus, it is implicated in the control of both DNA replication and transcription. Deletion of this gene has been associated with myelodysplastic syndrome and acute myelogenous leukemia.
purine-rich element binding protein A
, Pur alpha
, purine-rich single-stranded DNA-binding protein alpha
, transcriptional activator protein Pur-alpha