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MAP kinase-interacting serine/threonine-protein kinase 1 was identified as a direct target of miR-483-5p, which was confirmed by luciferase reporter assay and Western blotting.
In GBM cells, ATO-activated translation initiation cellular events via the MNK1-eIF4E signaling axis.
MNK1 is involved in regulating both IRES- and cap-dependent viral mRNA translation. [review]
High expression of MNK1 is frequent in HCC tissues, which promotes tumor proliferation and invasion, and is correlated with a poor overall survival.
High MNK1 expression in epithelial ovarian cancer tissues indicates poor clinical outcomes
these data show that NDRG1 is regulated by the oncogenic MAP kinase-interacting kinase pathway, a target for cancer therapy
MKNK1 polymorphism was associated with treatment response in metastatic colorectal cancer.
Elevated levels of p-Mnk1, p-eIF4E and p-p70S6K proteins are associated with tumor recurrence and poor prognosis in astrocytomas. Overexpression of p-eIF4E and co-expression of p-Mnk1, p-eIF4E and p-p70S6K proteins could be used as novel independent poor prognostic biomarkers for patients with astrocytomas.
MNK-1 controls chemokine secretion and proliferation in human airway smooth muscle cells.
MNK1 encodes a Ser/Thr protein kinase that interacts with extracellular signal-regulated kinase 1 and p38 mitogen-activated protein kinase, a pathway that is involved in Blood Pressure regulation through norepinephrine and angiotensin II.
Data show that galeterone (gal) and VNPT55 inhibit migration and invasion of prostate cancer cells, possibly by down-regulating protein expression via antagonizing the Mnk1/2-eIF4E axis.
data suggest a physiological role for MNK1a-Ser(353) phosphorylation in regulation of the MNK1a kinase, which correlates with increased eIF4E phosphorylation in vitro and in vivo.
Data suggest MNK1/MNK2 stimulate mRNA translation but only of mRNA containing both 5-prime-terminal cap and hairpin duplex; this stimulation involves up-regulation of phosphorylation/mRNA un-winding activity of eIF4E (via decreased binding to eIF4G).
Simultaneous targeting of androgen receptor and MNK1 by novel retinamides inhibits growth of human prostate cancer cell lines.
MNK1 and MNK2 inhibition ablates eIF4E1 phosphorylation and concurrently enhances eIF4E3 expression in diffuse large B-cell lymphoma.
Data show that interferon-gamma regulated the metabolism and mRNA translation of macrophages by targeting the kinases mTORC1 and MNK1/2, both of which converge on the selective regulator of translation initiation eukaryotic initiation factor-4E (eIF4E).
Data suggest that a combined pharmacologic inhibition of mTORC1 and Mnk1/2 kinases offers a therapeutic opportunity in blast crisis-chronic myeloid leukemia (BC-CML).
Authors show that MNK regulates SRPK via mTOR and AKT.
ERK1/2 signal induced MNK catalytic activity enabled enterovirus type 1 internal ribosomal entry site-mediated translation/host cell cytotoxicity through negative regulation of the Ser/Arg (SR)-rich protein kinase (SRPK).
These data indicate multiple myeloma cells exploit the MNK/eIF-4E pathway for selective mRNA translation without enhancing global translation and risking ER stress.
MNK1 participates in mediating high-fat diet-induced insulin resistance. Our findings reveal distinct roles for the MNKs in a novel area of disease biology
Mnk1 is a novel pancreatic acinar cell-specific stress response kinase that regulates digestive enzyme abundance and eIF4E phosphorylation.
Long-term potentiation (LTP) consolidation in the dentate gyrus of live rodents requires sustained (hours) BDNF-TrkB signaling and from TrkB to MAP-kinase-interacting kinase.
Data suggest that Mnk1 and Mnk2 regulate cell migration/wound healing, expression of vimentin, stability of vimentin protein, and binding of eIF4E (eukaryotic translation initiation factor 4E) and Cyfip1 (cytoplasmic FMR1 interacting protein 1).
Mnk1/2 has a minimal role in T cell development and activation but may regulate non-T cell lineages to control Th1 and Th17 differentiation in vivo.
oncogenic role for Mnk1/2 in tumor development
Mnk1 phosphorylation by caspase-activated Pak2/gamma-PAK inhibits phosphorylation and interaction of eIF4G with Mnk
Mnk2 and Mnk1 are essential for constitutive and inducible phosphorylation of eukaryotic initiation factor 4E but not for cell growth or development
Mnk activation by oxidative stress leading to enhanced eIF4E phosphorylation may play a role in promoting stress-induced hyperproliferative diseases, such as smooth muscle cell proliferation and hypertrophy in cardiovascular disease.
The roles of features in the catalytic domains and C termini in determining the regulatory properties and basal activities of Mnk1 AND Mnk2 are reported.
Roles of mitogen-activated protein kinase signal-integrating kinases 1 and 2 in oxidant-mediated eIF4E phosphorylation.
mTOR inhibition increases eIF4E phosphorylation through a PI3K-dependent and Mnk-mediated mechanism.
MNK1 and MNK2 are kinases involved in anti-apoptotic signaling in response to serum withdrawal
Pharmacological inhibition of Mnk kinases or siRNA-mediated knockdown of Mnk1 and Mnk2 results in partial reversal of the suppressive effects of IFNalpha on normal and leukemic hematopoietic progenitors.
This gene encodes a Ser/Thr protein kinase that interacts with, and is activated by ERK1 and p38 mitogen-activated protein kinases, and thus may play a role in the response to environmental stress and cytokines. This kinase may also regulate transcription by phosphorylating eIF4E via interaction with the C-terminal region of eIF4G. Alternatively spliced transcript variants have been noted for this gene.
MAP kinase signal-integrating kinase 1
, MAP kinase-interacting serine/threonine-protein kinase 1
, MAPK signal-integrating kinase 1
, MAP kinase interacting serine/threonine kinase 1
, MAP kinase-interacting kinase 1