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An alternative targeting strategy of MK5/PRAK (termed MK5/PRAK-Deltaex6) increased neither tumor incidence in the one step skin carcinogenesis model, nor Ras-induced transformation in primary cells.
MK5 positively regulates Rag transcription via phosphorylation of Foxo1 (show FOXO1 Proteins) in developing B cells.
observations have demonstrated that PRAK is not required for either the rottlerin-mediated anti-chlamydial activity or rottlerin inhibition of sphingolipid trafficking, suggesting rottlerin may achieve its inhibitory role by targeting other host factors
Results suggest that PRAK may function as a tumor suppressor in multiple types of cancers.
the regulation of neuronal morphogenesis is proposed as the first physiological function of the ERK3 (show RYK Proteins)/MK5 signaling module
It was shown that the tumor-suppressing and tumor-promoting functions of the p38 (show CRK Proteins)-PRAK pathway are temporally and spatially separated during cancer development in vivo, relying on the stimulus, and the tissue type and the stage of cancer development.
Rheb (show RHEB Proteins) inactivation by PRAK-mediated phosphorylation is essential for energy-depletion-induced suppression of mTORC1
MK5 co-immunoprecipitated ERK3 (show RYK Proteins), but not ERK4 (show MAPK4 Proteins) or p38 alpha (show MAPK14 Proteins), in control and hypertrophying hearts (MK5).
Both binding and activation of p38 mitogen-activated protein kinase (show MAPK14 Proteins) (MAPK (show MAPK1 Proteins)) play essential roles in regulation of the nucleocytoplasmic distribution of MAPK-activated protein kinase 5 by cellular stress.
Data suggest that the differences between the phenotypes of MK5- and MK2 (show KCNA2 Proteins)-deficient mice result from clearly different functional properties of both enzymes.
PRAK might be a potential therapeutic target of Alzheimer's disease involved in receptor for advanced glycation end products-mediated cell signaling induced by Abeta (show APP Proteins)
Plasma MAPKAPK5 protein was found to positively associate with the 10-year change in paired associates learning assessment in asymptomatic older twins.
Data highlight that DJ-1 (show PARK7 Proteins) is the downstream interacting target for PRAK, and in response to oxidative stress PRAK may exert a cytoprotective effect by facilitating DJ-1 (show PARK7 Proteins) to sequester Daxx (show DAXX Proteins) in the nucleus, thus preventing cell death.
Data indicate that the structurally most flexible regions during molecular dynamics (MD) simulations of the native mitogen-activated protein kinase (show MAPK1 Proteins)-activated protein kinase (show CDK7 Proteins) MK5 model were the loop regions.
Studies with specific phosphoantibodies indicate that MK5 phosphorylates Hsp40/DnaJB1 (show DNAJB1 Proteins) in vivo at Ser (show SIGLEC1 Proteins)-149 or/and Ser (show SIGLEC1 Proteins)-151 and Ser (show SIGLEC1 Proteins)-171 in the C-terminal domain of Hsp40/DnaJB1 (show DNAJB1 Proteins).
study shows Tip60 (show KAT5 Proteins) plays an essential role in oncogenic ras-induced senescence; revealed a cascade of posttranslational modifications involving p38 (show CRK Proteins), Tip60 (show KAT5 Proteins) and PRAK, 3 proteins essential for ras-induced senescence; these modifications are critical for prosenescent function of Tip60 (show KAT5 Proteins) and PRAK
these results firstly demonstrate that MK5 is degraded in response to doxorubicin and negatively regulates doxorubicin-induced apoptosis, providing novel insights into the molecular mechanism of doxorubicin resistance in hepatoma cells.
IGF2BP1 promotes the velocity and directionality of tumor-derived cell migration by determining the cytoplasmic fate of two novel target mRNAs: MAPK4 and PTEN
Activation loop phosphorylation of ERK3/ERK4 (show MAPK4 Proteins) by group I p21 (show CDKN1A Proteins)-activated kinases (PAKs) defines a novel PAK-ERK3 (show MAPK4 Proteins)/4-MAPK-activated protein kinase 5 signaling pathway.
The protein encoded by this gene is a tumor suppressor and member of the serine/threonine kinase family. In response to cellular stress and proinflammatory cytokines, this kinase is activated through its phosphorylation by MAP kinases including MAPK1/ERK, MAPK14/p38-alpha, and MAPK11/p38-beta. The encoded protein is found in the nucleus but translocates to the cytoplasm upon phosphorylation and activation. This kinase phosphorylates heat shock protein HSP27 at its physiologically relevant sites. Two alternately spliced transcript variants of this gene encoding distinct isoforms have been reported.
mitogen-activated protein kinase-activated protein kinase 5
, MAP kinase-activated protein kinase 5
, MAP kinase-activated protein kinase 5-like
, MAPK-activated protein kinase 5
, MAPKAP kinase 5
, p38-regulated/activated protein kinase