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The expression level of DYRK2 was positively correlated with glioma pathological grade.
Results provide evidence that DYRK2 suppresses the proliferation of breast cancer cells and invasion through CDK14 expression.
Study found that DYRK2 regulates liver metastases of colorectal cancer cells through the activation of EMT, 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 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-positive breast cancer to everolimus by preventing mTOR 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 tumor tissues could promote the proliferation of hepatocellular carcinoma (HCC) cells. In addition, reducing DYRK2 expression was associated with poor prognosis and Oxaliplatin resistance in HCC.
Silencing of DYRK2 increases cell proliferation but reverses CAM-DR in Non-Hodgkin's Lymphoma
DYRK2 may regulate EMT through Snail 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.
DYRK2 controls the epithelial-mesenchymal transition in breast cancer by degrading Snail.
DYRK2-mediated phosphorylation of p53 at Ser46 is impaired under hypoxic conditions, suggesting a molecular mechanism underlying chemotherapy resistance in solid tumors.
Data indicate that Dyrk2 phosphorylates TERT protein, which is then associated with the EDD-DDB1-VprBP E3 ligase complex for subsequent ubiquitin-mediated TERT protein degradation.
DYRK2 regulates tumor progression through modulation of c-Jun and c-Myc
The findings indicate that ATM controls stability and pro-apoptotic function of DYRK2 in response to DNA damage.
These findings indicate that DYRK2 regulates p53 to induce apoptosis in response to DNA damage.
A protein kinase, DYRK2, has unexpected role as a scaffold for an E3 ubiquitin ligase complex.
disease control rate of the DYRK2-positive non-small cell lung cancer patients was significantly different from the DYRK2-negative group
data indicate that DYRK2 is expressed in the developing muscle progenitor cells in somites and that it positively regulates fast-twitch muscle differentiation, at least at the early stages
These results suggest that the phosphorylation of Dpysl2 and Dpysl3 by Cdk5 and DYRK2 is required for the proper positioning of Rohon-Beard neurons and neural crest cells during neurulation in zebrafish embryos.
Dyrk2 regulates osteoclast fusion in a cell heterotypic manner.
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