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Inhibition of DAPK1 by deleting a catalytic domain or a death domain of DAPK1 rescues the Excitatory pyramidal neurons in the entorhinal cortical layer II region synaptic loss
in Alzheimer's disease (AD) brains, elevated DAPK1 levels showed co-relation with the increase of APP (show APP Proteins) phosphorylation. Combined together, these results suggest that DAPK1 promotes the phosphorylation and amyloidogenic processing of APP (show APP Proteins), and that may serve a potential therapeutic target for AD.
This study demonstrate that phosphorylation of Tau at Serine 262 by the kinase domain of DAPK1 mediates spine damage and the subsequent neuronal death in ischemic stroke.
DAPK1-p53 (show TP53 Proteins) interaction is a preferred target for therapeutic intervention of stroke.
Suggest that DAPK1 is a novel regulator of tau protein abundance, and that DAPK1 upregulation might contribute to tau-related pathologies in Alzheimer disease.
the DAPK1-p53 (show TP53 Proteins) interaction is a signaling point of convergence of necrotic and apoptotic pathways
a new function of DAPK in suppressing TNF (show TNF Proteins)-induced STAT3 (show STAT3 Proteins) activation, was identified.
TSC2 binds to the death domain of DAPK. This interaction is required for TSC2 to reduce DAPK protein levels and half-life. DAPK is regulated by the lysosome pathway. Lysosome inhibition blocks TSC2-mediated degradation of DAPK.
Results identify DAPK as a molecule required for full production of IL-1beta (show IL1B Proteins) and functional assembly of the NLRP3 (show NLRP3 Proteins) inflammasome.
Study reports that cerebral ischemia recruits death-associated protein kinase 1 (DAPK1) into the NMDA receptor NR2B (show GRIN2B Proteins) protein complex in the cortex of adult mice.
The current study supports a relevant role for p15 (show CDKN2B Proteins), p16, and DAPK hypermethylation in the genesis of the plasma cell neoplasm. DAPK hypermethylation also might be an important step in the progression from MGUS to MM.
DAPK1 methylation is associated with the risk of gastrointestinal cancer.
downregulation of HOXC9 (show HOXC9 Proteins) releases its transcriptional inhibition of DAPK1, resulting in the activation of the DAPK1-Beclin1 (show BECN1 Proteins) pathway, which induces autophagy in glioblastoma cells
findings evidence a positive correlation between SIRT1 (show SIRT1 Proteins) and BCL6 (show BCL6 Proteins) expression increase in follicular lymphomas (FL) . SIRT1 (show SIRT1 Proteins) methylation decreases in FL and diffuse large-B cell lymphomas (DLBCL)and this parallels the increase of KLF4 (show KLF4 Proteins), DAPK1 and SPG20 (show SPG20 Proteins) methylation
results suggest that DAPK1 is an important prognostic marker and therapeutic target for bladder cancer and have identified possible therapeutic agents for future testing in bladder cancer models with low DAPK1 expression
Study provides evidence that DAPK1 is a negative-feedback regulator of the RIG-I (show DDX58 Proteins) pathway. RIG-I (show DDX58 Proteins)-mediated antiviral signaling activates DAPK1 kinase activity and DAPK1 inactivates RIG-I (show DDX58 Proteins) RNA sensing by direct phosphorylation of RIG-I (show DDX58 Proteins).
Meta-analysis suggested that aberrant methylation of DAPK promoter was associated with head and neck squamous cell carcinoma.
our study characterized DAPK1 as a novel transcriptional target of BRMS1 (show BRMS1 Proteins). Transcriptional activation of DAPK1 might be another important mechanism accounting for the metastasis suppressive activity of BRMS1 (show BRMS1 Proteins).
The result suggests that DAPK promoter methylation is significantly increased in bladder cancer patients compared to normal controls. DAPK promoter methylation could serve as a biomarker for bladder cancer detection and management.
Death-associated protein kinase 1 is a positive mediator of gamma-interferon induced programmed cell death. DAPK1 encodes a structurally unique 160-kD calmodulin dependent serine-threonine kinase that carries 8 ankyrin repeats and 2 putative P-loop consensus sites. It is a tumor suppressor candidate.
death-associated protein kinase 1
, death-associated protein kinase 1-like
, DAP kinase 1