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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Maternal embryonic leucine zipper kinase

MELK, maternal embryonic leucine zipper kinase, MPK38
Top mentioned proteins: CAN, AMPK, V1a, p53, HNF-3
Papers on MELK
The p53-p21-DREAM-CDE/CHR pathway regulates G2/M cell cycle genes.
Engeland et al., Leipzig, Germany. In Nucleic Acids Res, Feb 2016
The target gene list was verified by detailed analysis of p53-dependent repression of the cell cycle genes B-MYB (MYBL2), BUB1, CCNA2, CCNB1, CHEK2, MELK, POLD1, RAD18 and RAD54L.
A genome landscape of SRSF3-regulated splicing events and gene expression in human osteosarcoma U2OS cells.
Zheng et al., Frederick, United States. In Nucleic Acids Res, Jan 2016
By global profiling of the SRSF3-regulated splicing events in human osteosarcoma U2OS cells, we found that SRSF3 regulates the expression of 60 genes including ERRFI1, ANXA1 and TGFB2, and 182 splicing events in 164 genes, including EP300, PUS3, CLINT1, PKP4, KIF23, CHK1, SMC2, CKLF, MAP4, MBNL1, MELK, DDX5, PABPC1, MAP4K4, Sp1 and SRSF1, which are primarily associated with cell proliferation or cell cycle.
Maternal embryonic leucine zipper kinase serves as a poor prognosis marker and therapeutic target in gastric cancer.
Ji et al., Beijing, China. In Oncotarget, Jan 2016
UNASSIGNED: Maternal embryonic leucine zipper kinase (MELK) is upregulated in a variety of human tumors, and is considered an attractive molecular target for cancer treatment.
Co-expression of mitosis-regulating genes contributes to malignant progression and prognosis in oligodendrogliomas.
Jiang et al., Beijing, China. In Oncotarget, Dec 2015
To identify critical gene(s) associated with tumor grades and TCGA subtypes, we analyzed 34 normal brain tissue (NBT), 146 WHO grade II and 130 grade III ODs by microarray and RNA sequencing, and identified a co-expression network of six genes (AURKA, NDC80, CENPK, KIAA0101, TIMELESS and MELK) that was associated with tumor grades and TCGA subtypes as well as Ki-67 expression.
Coordinate Activation of Redox-dependent ASK1/TGF-β Signaling by a Multi-protein Complex (MPK38, ASK1, SMADs, ZPR9, and TRX) Improves Glucose and Lipid Metabolism in Mice.
Ha et al., Ch'ŏngju, South Korea. In Antioxid Redox Signal, Oct 2015
RESULTS: We provide evidence that the ASK1 and TGF-β signaling pathways are interconnected by a multi-protein complex harboring murine protein serine-threonine kinase 38 (MPK38), ASK1, Sma- and Mad-related proteins (SMADs), zinc-finger-like protein 9 (ZPR9), and thioredoxin (TRX) and demonstrate that activation of either ASK1 or TGF-β activity is sufficient to activate both the redox-dependent ASK1 and TGF-β signaling pathways.
PAR-4 and anillin regulate myosin to coordinate spindle and furrow position during asymmetric division.
Michaux et al., Rennes, France. In J Cell Biol, Oct 2015
We find that PAR-4/LKB1 impinges on myosin via two pathways, an anillin-dependent pathway that also responds to the cullin CUL-5 and an anillin-independent pathway involving the kinase PIG-1/MELK.
Emerging targets for glioblastoma stem cell therapy.
Bijangi-Vishehsaraei et al., Indianapolis, United States. In J Biomed Res, Oct 2015
Several signaling pathways including mTOR, AKT, maternal embryonic leucine zipper kinase (MELK), NOTCH1 and Wnt/β-catenin as well as expression of cancer stem cell markers CD133, CD44, Oct4, Sox2, Nanog, and ALDH1A1 maintain GSC properties.
Integration of copy number and transcriptomics provides risk stratification in prostate cancer: A discovery and validation cohort study.
CamCaP Study Group et al., Cambridge, United Kingdom. In Ebiomedicine, Sep 2015
We confirm alterations in six genes previously associated with prostate cancer (MAP3K7, MELK, RCBTB2, ELAC2, TPD52, ZBTB4), and also identify 94 genes not previously linked to prostate cancer progression that would not have been detected using either transcript or copy number data alone.
Genome Wide Methylome Alterations in Lung Cancer.
Spivack et al., New York City, United States. In Plos One, 2014
Of the canonical changes noted, promoter (PR) DM loci with reciprocal changes in expression in adenocarcinomas included HBEGF, AGER, PTPRM, DPT, CST1, MELK; DM GB loci with concordant changes in expression included FOXM1, FERMT1, SLC7A5, and FAP genes.
MELK-T1, a small-molecule inhibitor of protein kinase MELK, decreases DNA-damage tolerance in proliferating cancer cells.
Bollen et al., Beerse, Belgium. In Biosci Rep, 2014
Maternal embryonic leucine zipper kinase (MELK), a serine/threonine protein kinase, has oncogenic properties and is overexpressed in many cancer cells.
Maternal embryonic leucine zipper kinase: key kinase for stem cell phenotype in glioma and other cancers.
Nakano et al., Los Angeles, United States. In Mol Cancer Ther, 2014
Maternal embryonic leucine zipper kinase (MELK) is a member of the snf1/AMPK family of protein serine/threonine kinases that has recently gained significant attention in the stem cell and cancer biology field.
The regulation and function of the NUAK family.
Zhao et al., Taipei, Taiwan. In J Mol Endocrinol, 2013
Twelve AMPK-related kinases (ARKs; BRSK1, BRSK2, NUAK1, NUAK2, QIK, QSK, SIK, MARK1, MARK2, MARK3, MARK4, and MELK) have been identified recently.
Maternal embryonic leucine zipper kinase (MELK): a novel regulator in cell cycle control, embryonic development, and cancer.
Zhang et al., China. In Int J Mol Sci, 2012
Maternal embryonic leucine zipper kinase (MELK) functions as a modulator of intracellular signaling and affects various cellular and biological processes, including cell cycle, cell proliferation, apoptosis, spliceosome assembly, gene expression, embryonic development, hematopoiesis, and oncogenesis.
Murine protein serine-threonine kinase 38 activates p53 function through Ser15 phosphorylation.
Ha et al., Ch'ŏngju, South Korea. In J Biol Chem, 2012
MPK38 may act as a novel regulator for promoting p53 activity through direct phosphorylation of p53 at Ser(15).
PDK1 protein phosphorylation at Thr354 by murine protein serine-threonine kinase 38 contributes to negative regulation of PDK1 protein activity.
Ha et al., Ch'ŏngju, South Korea. In J Biol Chem, 2012
an important role for MPK38-mediated phosphorylation of PDK1 in the negative regulation of PDK1 activity.
Resistance of colorectal cancer cells to radiation and 5-FU is associated with MELK expression.
Ku et al., Seoul, South Korea. In Biochem Biophys Res Commun, 2011
MELK could be associated with increased resistance of colorectal cancer cells against radiation and 5-FU.
Siomycin A targets brain tumor stem cells partially through a MELK-mediated pathway.
Kornblum et al., Columbus, United States. In Neuro Oncol, 2011
High MELK is associated with brain tumor.
A functional analysis of MELK in cell division reveals a transition in the mode of cytokinesis during Xenopus development.
Tassan et al., Rennes, France. In J Cell Sci, 2011
Overexpression of xMELK leads to failure of cytokinesis and impairs accumulation RhoA- a pivotal regulator of cytokinesis.
Glioma-initiating cells and molecular pathology: implications for therapy.
Wakabayashi et al., Nagoya, Japan. In Brain Tumor Pathol, 2011
Here, we review some of the signaling mechanisms involved in GIC biology, such as phosphatase and tensin homolog (PTEN), sonic hedgehog, Notch, and WNT signaling pathways, maternal embryonic leucine-zipper kinase (MELK), BMI1, and Janus kinase signal transducer and activator of transcription (JAK-STAT) signaling.
The regulation and function of mammalian AMPK-related kinases.
Carling et al., London, United Kingdom. In Acta Physiol (oxf), 2009
Recently, 12 AMPK-related kinases (BRSK1, BRSK2, NUAK1, NUAK2, QIK, QSK, SIK, MARK1, MARK2, MARK3, MARK4 and MELK) were identified that are closely related by sequence homology to the catalytic domain of AMPK.
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