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DYRK2 belongs to a family of protein kinases whose members are presumed to be involved in cellular growth and/or development. Additionally we are shipping DYRK2 Antibodies (94) and DYRK2 Proteins (5) and many more products for this protein.
Silencing of DYRK2 increases cell proliferation but reverses CAM (show CALM1 ELISA Kits)-DR in Non-Hodgkin's Lymphoma
DYRK2 may regulate EMT (show ITK ELISA Kits) through Snail (show SNAI1 ELISA Kits) degradation in ovarian SA and might be a predictive marker for a favorable prognosis in the treatment of this cancer.
Downregulation of DYRK2 is associated with recurrence in early stage breast cancer.
DYRK2-dependent phosphorylation of pregnane X receptor (show NR1I2 ELISA Kits) facilitates its subsequent ubiquitination by UBR5 (show UBR5 ELISA Kits).
DYRK2 controls the epithelial-mesenchymal transition in breast cancer by degrading Snail (show SNAI1 ELISA Kits).
DYRK2-mediated phosphorylation of p53 (show TP53 ELISA Kits) at Ser46 is impaired under hypoxic conditions, suggesting a molecular mechanism underlying chemotherapy resistance in solid tumors.
Data indicate that Dyrk2 phosphorylates TERT (show TERT ELISA Kits) protein, which is then associated with the EDD (show UBR5 ELISA Kits)-DDB1 (show DDB1 ELISA Kits)-VprBP E3 ligase complex for subsequent ubiquitin-mediated TERT (show TERT ELISA Kits) protein degradation.
DYRK2 regulates tumor progression through modulation of c-Jun (show JUN ELISA Kits) and c-Myc (show MYC ELISA Kits)
The findings indicate that ATM (show ATM ELISA Kits) controls stability and pro-apoptotic function of DYRK2 in response to DNA damage.
These findings indicate that DYRK2 regulates p53 (show TP53 ELISA Kits) to induce apoptosis in response to DNA damage.
These results suggest that the phosphorylation of Dpysl2 (show DPYSL2 ELISA Kits) and Dpysl3 (show DPYSL3 ELISA Kits) by Cdk5 (show CDK5 ELISA Kits) and DYRK2 is required for the proper positioning of Rohon-Beard neurons and neural crest cells during neurulation in zebrafish embryos.
DYRK2 belongs to a family of protein kinases whose members are presumed to be involved in cellular growth and/or development. The family is defined by structural similarity of their kinase domains and their capability to autophosphorylate on tyrosine residues. DYRK2 has demonstrated tyrosine autophosphorylation and catalyzed phosphorylation of histones H3 and H2B in vitro. Two isoforms of DYRK2 have been isolated. The predominant isoform, isoform 1, lacks a 5' terminal insert.
dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 2
, dual specificity tyrosine-phosphorylation-regulated kinase 2