ReviewCancer metastasis reviews2026
The dual fate of DYRK2 in cancer: balancing the light and dark side of tumorigenesis.
Review in Cancer metastasis reviews, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed.
- Nuclear factor of activated T cells as a driver of tumor progression and a target for precision therapy.Animal models and experimental medicine · 2026Review
- Molecular Targeting of EGFR, BRAF, and HER2 Signaling in Colorectal Cancer: Contemporary Advances with Panitumumab, Encorafenib, and Tucatinib.Journal of clinical medicine · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Dual-specificity tyrosine-phosphorylation-regulated kinase 2 (DYRK2) is emerging as a pivotal player in cancer biology due to its pleiotropic cellular roles, functioning either as a tumor suppressor or an oncogene in a tissue- and genotype-dependent manner. DYRK2 regulates critical processes including cell cycle progression, DNA damage response, and stress signaling. As a tumor suppressor, DYRK2 facilitates the degradation of oncogenic proteins (e.g., c-Myc, SNAIL, TERT) and enhances apoptosis via p53 activation. Loss of DYRK2 has been associated with poor prognosis and chemoresistance in cancers such as colorectal, breast, and liver. Conversely, DYRK2 overexpression in certain tumors, including triple-negative breast cancer and ovarian carcinoma, supports oncogenic roles by enhancing proteasome function, promoting epithelial-mesenchymal transition, and contributing to therapy resistance. This functional dichotomy is modulated by post-translational modifications, microenvironmental stress, epigenetic regulation, subcellular localization, and interaction with protein complexes, underscoring the complexity of DYRK2 regulation. Therapeutically, DYRK2 represents a promising but context-sensitive target, with inhibitors showing efficacy in preclinical models of proteasome-addicted cancers, although precise biomarkers and cancer subtype stratification remain critical. Future directions include refining in vivo models and delineating the role of DYRK2 in cancer stem cell dynamics and immune modulation, emphasizing that understanding its context-dependent activity is essential to exploit its full therapeutic potential in oncology.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.