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Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation (By similarity). Additionally we are shipping MELK Antibodies (115) and MELK Kits (14) and many more products for this protein.
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targeting MELK by the inhibition of both its catalytic activity and its protein stability might sensitize tumours to DNA-damaging agents or radiation therapy by lowering the DNA-damage threshold
Together, these data indicate that MELK is a normally non-essential kinase, but is critical for basal-like breast cancer.
EZH2 (show EZH2 Proteins) protects glioma stem cells from radiation-induced cell death in a MELK/FOXM1 (show FOXM1 Proteins)-dependent manner
we report characterization of possible roles of MELK in acute myeloid leukemia (show BCL11A Proteins)
insight has been brought by the discovery of a protein complex of FOXM1 (show FOXM1 Proteins) with the mitotic kinase MELK in cancer stem cells in brain cancers, as this protein complex appears to be cancer-specific
advanced cancers with OTSSP167 started in 2013, as the first-in-class MELK inhibitor. This review summarizes the current molecular understanding of MELK and the recent preclinical studies about MELK as a cancer therapeutic target.
MELK promotes cell migration and invasion via the FAK (show PTK2 Proteins)/Paxillin (show PXN Proteins) pathway, and plays an important role in the occurrence and development of gastric cancer.
our current knowledge of MELK function and recent discoveries in MELK signaling pathway were discussed.
The structural and biochemical analyses unravel the molecular mechanisms for the autophosphorylation/activation of MELK and the dependence of its catalytic activity on reducing agents.
glioblastoma cells have elevated MELK protein levels to better cope with replication stress during unperturbed S phase.
Phosphorylation of the activation loop of MPK38 induces its movement resulting in kinase activation.
These results indicate that Trx (show TXN Proteins) functions as a physiological inhibitor of MPK38, which plays an important role in inducing ASK1 (show MAP3K5 Proteins)-, TGF-beta (show TGFB1 Proteins), and p53 (show TP53 Proteins)-mediated activity
an important role for MPK38-mediated phosphorylation of PDK1 (show PDPK1 Proteins) in the negative regulation of PDK1 (show PDPK1 Proteins) activity.
MPK38 may act as a novel regulator for promoting p53 (show TP53 Proteins) activity through direct phosphorylation of p53 (show TP53 Proteins) at Ser (show SIGLEC1 Proteins)(15).
Upregulation of maternal embryonic leucine zipper kinase is associated with mammary tumor.
MELK is necessary for proliferation of embryonic and postnatal MNP and suggest that it regulates the transition from GFAP (show GFAP Proteins)-expressing progenitors to rapid amplifying progenitors in the postnatal brain.
The characterization of two novel E2F (show E2F1 Proteins) target genes, chromosome condensation-related SMC-associated protein 1 (Cnap1 (show NCAPD2 Proteins)) and maternal embryonic leucine zipper kinase (Melk) is reported.
MPK38 physically interacts with ASK1 (show MAP3K5 Proteins) in vivo and acts as a positive upstream regulator of ASK1 (show MAP3K5 Proteins)
Melk-like gene may play a role in primitive hematopoiesis by affecting the expression of genes critical for hematopoiesis.
Overexpression of xMELK leads to failure of cytokinesis and impairs accumulation RhoA- a pivotal regulator of cytokinesis.
These results demonstrate the presence of a mitochondrial targeting signal at the N-terminus of the MC domain of MELK. This mitochondrial targeting signal was also functional in human HeLa cells.[MELK]
Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation (By similarity). Also plays a role in primitive hematopoiesis, possibly by affecting the expression of genes critical for hematopoiesis.
maternal embryonic leucine zipper kinase
, maternal embryonic leucine zipper kinase-like
, pEg3 kinase
, protein kinase Eg3
, protein kinase PK38
, tyrosine-protein kinase MELK
, Protein kinase Eg3