Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
Study found that DYRK2 regulates liver metastases of colorectal cancer cells through the activation of EMT (show ITK Proteins), and that patients with low DYRK2-expressing colorectal cancer liver metastases had worse outcomes than those with high DYRK2-expressing metastases.
our results delineate a novel mechanism of cancer stem cell regulation by the DYRK2-AR-KLF4 (show KLF4 Proteins) axis. Restoration of the expression and function of DYRK2 is a potential therapeutic strategy against breast cancer stem cells.
lower DYRK2 levels were correlated with tumor sites, advanced clinical stages, and shorter survival in the advanced clinical stages. DYRK2 is a novel prognostic biomarker of human colorectal cancer.
Diminished DYRK2 expression sensitizes hormone receptor (show NR4A1 Proteins)-positive breast cancer to everolimus by preventing mTOR (show FRAP1 Proteins) degradation.
Findings indicate direct interaction of dual-specificity tyrosine phosphorylation-regulated kinase 2 (DYRK2) with ring finger protein (C3HC4 type) 8 (RNF8) in regulating response to DNA damage.
the downregulated expression of DYRK2 in HCC (show FAM126A Proteins) tumor tissues could promote the proliferation of hepatocellular carcinoma (HCC (show FAM126A Proteins)) cells. In addition, reducing DYRK2 expression was associated with poor prognosis and Oxaliplatin resistance in HCC (show FAM126A Proteins).
Silencing of DYRK2 increases cell proliferation but reverses CAM (show CALM1 Proteins)-DR in Non-Hodgkin's Lymphoma
DYRK2 may regulate EMT (show ITK Proteins) through Snail (show SNAI1 Proteins) 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 facilitates its subsequent ubiquitination by UBR5.
These results suggest that the phosphorylation of Dpysl2 (show DPYSL2 Proteins) and Dpysl3 (show DPYSL3 Proteins) by Cdk5 (show CDK5 Proteins) and DYRK2 is required for the proper positioning of Rohon-Beard neurons and neural crest cells during neurulation in zebrafish embryos.
DYRK2 regulates tumor progression through modulation of c-Jun (show JUN Proteins) and c-Myc (show MYC Proteins)
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