maternal embryonic leucine zipper kinase

Search for other works by this author on: . However, the regulatory mechanism of MELK remains elusive. cell cortex, cytoplasm, plasma membrane, calcium ion binding, non-membrane spanning protein tyrosine kinase activity, protein kinase activity, protein serine/threonine kinase activity, apoptotic process, cell population proliferation, intracellular signal transduction . A Biblioteca Virtual em Saúde é uma colecao de fontes de informacao científica e técnica em saúde organizada e armazenada em formato eletrônico nos países da Região Latino-Americana e do Caribe, acessíveis de forma universal na Internet de modo compatível com as bases internacionais. Journal of Neuroscience Research, 2008. 10) is a member of the Snf1/AMPK family of kinases but is unique in that it is not regulated by LKB1 kinase ().In addition to a Ser/Thr kinase domain, MELK contains an unstructured COOH-terminal ubiquitin associated (UBA) domain that prevents ubiquitin-mediated degradation (), a leucine zipper motif, and a COOH-terminal kinase-associated . Hartmut Koeppen. MELK was highly expressed in clinical specimens of cervical cancer patients and the . CiteSeerX - Scientific documents that cite the following paper: Comprehensive expression profiling of tumor cell lines identifies molecular signatures of melanoma progression. Introduction. Acts as an activator of apoptosis by phosphorylating and activating MAP3K5/ASK1. Maternal embryonic leucine zipper kinase (MELK) is upregulated in several types of tumor, including breast, prostate, and brain tumors. Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation. 78: 17280616: 2007: Involvement of maternal embryonic leucine zipper kinase (MELK) in mammary carcinogenesis through interaction with Bcl-G, a pro-apoptotic member of the Bcl-2 family. Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation. James Waschek. The maternal embryonic leucine zipper kinase (MELK) is a member of the Snf1/AMPK kinase family (Heyer et al. Maternal embryonic leucine zipper kinase (MELK) is a kind of cell cycle dependent conserved serine/threonine protein kinase, at chromosome 9p13.2. Host Rabbit Type Primary Clonality 2004), cell division, and cytokine- Here we show that the siRNA-mediated loss of MELK in U87 MG glioblastoma cells causes a G1/S phase . Europe PMC is an archive of life sciences journal literature. MedChemExpress provides thousands of inhibitors, modulators and agonists with high purity and quality, excellent customer reviews, precise and professional product citations, tech support and prompt delivery. Maternal embryonic leucine zipper kinase (MELK), a serine/threonine protein kinase, has oncogenic properties and plays a key functional role in various cancer cells. anti-MELK antibody (Maternal Embryonic Leucine Zipper Kinase) AA 525-554 Primary Antibody. HPK38; maternal embryonic leucine zipper kinase; pEg3 kinase; protein kinase Eg3; protein kinase PK38; tyrosine-protein kinase MELK Background. Short name: pEg3 kinase. In this study, we combined chemical and genetic perturbants, including the development of a novel selective maternal embryonic leucine zipper kinase (MELK) inhibitor HTH-01-091, CRISPR/Cas9-mediated MELK knockout, a novel chemical-induced protein degradation strategy, RNA interference and CRISPR . It belongs to a conservative cycle-dependent kinase. Cancer Res. Maternal Embryonic Leucine Zipper Kinase Is Upregulated and Required in Mammary Tumor-Initiating Cells In vivo 21, 17 This study confirmed that MELK mRNA and protein levels were up‐regulated in four cervical cancer cell lines. 2005), pre-mRNA pro-cessing (Vulsteke et al. 2005, 65: 9751-9761. Here, we demonstrate expression of MELK by progenitors in developing and adult brain and that MELK serves as a marker for self-renewing multipotent neural progenitors (MNPs) in cultures derived from the developing forebrain and in transgenic mice. Ichiro Nakano. HPK38; maternal embryonic leucine zipper kinase; pEg3 kinase; protein kinase Eg3; protein kinase PK38; tyrosine-protein kinase MELK Background. 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. Maternal embryonic leucine zipper kinase (MELK), a serine/threonine protein kinase, has oncogenic properties and plays a key functional role in various cancer cells. Maternal embryonic leucine zipper kinase (MELK) exhib-ited the most statistically significant difference. and . MELK was initially identified from analysis of cDNA libraries as a maternally derived gene that is active in the unfertilized egg and pre-implantation embryo in mice (1). In a previous study, we demonstrated that maternal embryonic leucine zipper kinase (Melk) is highly expressed in murine neural stem cells and regulates their proliferation. Maternal embryonic leucine zipper kinase (MELK) regulates multipotent neural progenitor proliferation. Maternal embryonic leucine zipper kinase (MELK; Previously, we used a genome-wide screening strategy to MPK38) (Gil et al., 1997; Heyer et al., 1997, 1999), a member discover genes that regulate MNP function (Geschwind et al., of the snf1/AMPK family of serine-threonine kinases, was en- riched in multiple MNP-containing populations and in . . Maternal embryonic leucine zipper kinase/murine protein serine-threonine kinase 38 is a promising therapeutic target for multiple cancers. Ruchi Bajpai. Maternal Embryonic Leucine Zipper Kinase (MELK) (AA 550-650) protein (GST tag) Protein. (ABIN1913071) anti-Maternal Embryonic Leucine Zipper Kinase (MELK) (Internal Region) antibody (PE) This product has been discontinued by antibodies-online, but remains here on CiteAb for record purposes. Maternal embryo leucine zipper kinase is highly expressed in a wide range of cancer and is associated with the degree of malignancy of the tumor. Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation. Has a broad substrate specificity . Pierce, Felix Y. Feng Maternal embryonic leucine zipper kinase (MELK) is a member of the snf1/AMPK family of protein serine/ threonine kinases. This Paper. Maternal embryonic leucine zipper kinase is a key regulator of the proliferation of malignant brain tumors, including brain tumor stem cells. MELK (maternal embryonic leucine zipper kinase), which is a member of the AMPK (AMP-activated protein kinase)-related kinase family, plays important roles in diverse cellular processes and has become a promising drug target for certain cancers. Heyer et al. Maternal embryonic leucine zipper kinase (MELK) activates pathways that mediate aggressive tumor growth and therapy resistance in many types of adult cancers. Maternal embryonic leucine zipper kinase (MELK) is a unique member of the Snf1/AMPK kinase family. Using bioinformatic analyses, we identified maternal embryonic leucine zipper kinase (MELK) as 4.1-fold overexpressed in ACC compared with normal adrenal samples. Has a broad substrate specificity . MELK was highly expressed in clinical specimens of cervical cancer patients and . In general, the . Maternal embryonic leucine zipper kinase (MELK) was previously identified in a screen for genes enriched in neural progenitors. 71: Full PDF Package Download Full PDF Package. Maternal embryonic leucine zipper kinase (MELK) as a novel mediator and biomarker of radioresistance in human breast cancer Corey Speers * , Shuang G. Zhao, Vishal Kothari , Alyssa Santola, Meilan Liu, Kari Wilder-Romans, Joseph Evans, Nidhi Batra, Harry Bartelink, Daniel F. Hayes, Theodore S. Lawrence, Powel H. Brown, Lori J. Here, we report the crystal structure of a . 1997). Maternal embryonic leucine zipper kinase (MELK) was previously identified in a screen for genes enriched in neural progenitors. Maternal embryonic leucine zipper kinase (MELK) plays a role in cancer cell cycle progression and is associated with poor. Maternal embryonic leucine zipper kinase (MELK), also known as pEg3 or murine protein K38 (MPK38), is a serine/threonine protein kinase that plays a role in several biological processes, such as . Heyer et al. 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. In this paper, maternal embryonic leucine zipper kinase (MELK), a potential therapeutic target that is possibly involved in a tumorigenic process, was described. While its function remains obscure, it has been implicated in cell cycle regulation (Davezac et al. 21, 17 This study confirmed that MELK mRNA and protein levels were up-regulated in four cervical cancer cell lines. Nevertheless, the MELK pathway in tumorigenesis is not yet completely understood. MELK plays a key role in tumor cell cycle regulation and growth signaling pathways ().Increased expression of MELK has been observed in TNBC tumor cells and tumor stem cells , , , , , which is associated with inhibition of tumor cell . 2002), cell proliferation (Nakano et al. MELK-8a (NVS-MELK8a) is a highly potent and selective maternal embryonic leucine zipper kinase (MELK) inhibitor with IC50 of 2 nM. Our previous studies suggested that MELK is involved in the regulation of cell cycle and its genetic depletion leads to growth inhibition in a subset of high MELK-expressing basal-like breast cancer cell lines. 9 MELK is highly expressed in a wide range of malignant tumors, including hepatocellular MELK was initially identified from analysis of cDNA libraries as a maternally derived gene that is active in the unfertilized egg and pre-implantation embryo in mice (1). Cancer research, 2005. Maternal embryonic leucine zipper kinase (MELK) plays a role in cancer cell cycle progression . MELK plays an essential role in regulating cell mitosis in a subset of cancer cells. Maternal Embryonic Leucine Zipper Kinase (MELK): a Novel Marker of Poor Prognosis and Attractive Drug Target in High-Risk Patients with Multiple Myeloma Arnold Bolomsky, Arnold Bolomsky * 1 Department of Medicine I, Wilhelminenhospital, Wilhelminen Cancer Research Institute, Vienna, Austria . Maternal embryonic leucine zipper kinase is a key regulator of the proliferation of malignant brain tumors, including brain tumor stem cells. From this approach, we have found that maternal embryonic leucine zipper kinase (Melk), a member of the AMP serine/threonine kinase family, exhibits multiple features . ABIN3028827 . (1997) cloned mouse Melk by differential display PCR analysis using cDNA from the egg and 2- and 8-cell-stage embryo cDNA libraries as template. Maternal embryo leucine zipper kinase is highly expressed in a wide range of cancer and is associated with the degree of malignancy of the tumor. In these cellular processes, MELK functions by binding to numerous proteins. MELK plays an important role in cell cycle regulation, cell proliferation and other processes [7,8,9]. Unlike other mem-bers of the family, MELK is not related to cellular en-ergy metabolism balance. (ABIN1913071) anti-Maternal Embryonic Leucine Zipper Kinase (MELK) (Internal Region) antibody (PE) This product has been discontinued by antibodies-online, but remains here on CiteAb for record purposes. These multiple features are consistent with it being a potential anticancer target. Maternal embryonic leucine zipper kinase (MELK) is a kind of cell cycle dependent conserved serine/threonine protein kinase, at chromosome 9p13.2. Maternal embryonic leucine zipper k. Maternal embryonic leucine zipper kinase, EC 2.7.11.1 (Protein kinase PK38, mPK38) (Tyrosine-protein kinase MELK, EC 2.7.10.2) Melk Kiaa0175, Pk38 The deduced 644-amino acid protein contains an N-terminal serine/threonine kinase domain that includes all 12 typical catalytic subdomains, and a leucine zipper motif. Abstract. Host Rabbit Type Primary Clonality Maternal embryonic leucine zipper kinase (MELK), is an adenosine monophosphate‑activated protein kinase‑related kinase that serves important roles in tumourigenesis in multiple malignant tumours. MELK was highly expressed in clinical specimens of cervical cancer patients and . NX_Q14680 - MELK - Maternal embryonic leucine zipper kinase - Function. In this report, we identify maternal embryonic leucine zipper kinase (MELK) as one of the most highly differentially expressed kinases in ER-negative breast cancers as compared with ER-positive breast cancers. Diffuse large B cell lymphoma (DLBCL) and mantle cell lymphoma (MCL) are among the most aggressive B cell non-Hodgkin lymphomas. 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. ChemIDplus; DrugPortal; Note. Caroline Badouel, Isabelle Chartrain, Joëlle Blot, Jean-Pierre Tassan, Maternal embryonic leucine zipper kinase is stabilized in mitosis by phosphorylation and is partially degraded upon mitotic exit, Experimental Cell Research, 10.1016/j.yexcr.2010.04.019, 316, 13, (2166-2173), (2010). Initial studies that characterized 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 … Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation. The deduced 644-amino acid protein contains an N-terminal serine/threonine kinase domain that includes all 12 typical catalytic subdomains, and a leucine zipper motif. Amy Howes. MATERNAL EMBRYONIC LEUCINE ZIPPER KINASE (HUMAN CLONE MGC:20350 IMAGE:4547136) PEG3 KINASE; PROTEIN KINASE EG3; PROTEIN KINASE PK38; TYROSINE-PROTEIN KINASE MELK; Resources. Maternal embryonic leucine zipper kinase (MELK) belongs to the subfamily of AMP-activated Ser/Thr protein kinases. Diffuse large B cell lymphoma (DLBCL) and mantle cell lymphoma (MCL) are among the most aggressive B cell non-Hodgkin lymphomas. 9 MELK is highly expressed in a wide range of malignant tumors, including hepatocellular Maternal embryonic leucine zipper kinase is a key regulator of the proliferation of malignant brain tumors, including brain tumor stem cells. Antibody info; Additional info; Supplier antibodies-online. Maternal embryonic leucine zipper kinase (MELK) activates pathways that mediate aggressive tumor growth and therapy resistance in many types of adult cancers. Herein we describe the discovery and optimization of novel MELK inhibitors 8a and 8b that recapitulate the . The expression of MELK is very high in glioblastoma-type brain tumors, but it is not clear how this contributes to tumor growth. Abstract. Although MELK may not be a cancer addiction target, the development of specific MELK inhibitors would provide useful chemical tools for synthetic lethal investigation. Maternal embryonic leucine zipper kinase (MELK)/Murine protein serine-threonine kinase 38 (MPK38) is a member of the AMP-related serine-threonine kinase family, which has been reported to be . Download Download PDF. 78: 17280616: 2007: Involvement of maternal embryonic leucine zipper kinase (MELK) in mammary carcinogenesis through interaction with Bcl-G, a pro-apoptotic member of the Bcl-2 family. Maternal embryonic leucine zipper kinase (MELK) is a novel oncogene, which plays crucial roles in mitotic progression and stem cell maintenance. Background Maternal Embryonic Leucine Zipper Kinase (MELK) is a serine/threonine kinase involved in cell cycle, differentiation, proliferation, and apoptosis. Adrian Jub. Therefore, appropriately timed uncoating is essential for HIV-1 infection (Forshey et al., 2002, Rihn et al., 2013, von Schwedler et al., 2003), which is regulated by the host kinase maternal embryonic leucine zipper kinase (MELK), indicating that spatiotemporal dynamics of HIV-1 uncoating significantly affects the efficacy of HIV-1 infection . Here, we demonstrate expression of MELK by progenitors in developing and adult brain and that MELK serves as a marker for self-renewing multipotent neural progenitors (MNPs) in cultures derived from the developing forebrain and in transgenic mice. Recent studies suggest that activation of this kinase is tightly associated with extended survival and accelerated proliferation of cancer stem cells (CSC) in various organs . Gene names . Its expression is generally associated with cell survival, cell proliferation, and resistance to apoptosis. On the basis of these promising preclinical studies, early-phase . ABIN1310711. Maternal embryonic leucine zipper kinase (MELK) is a member of the snf1/AMPK family of protein serine/ threonine kinases. In addition, MELK is overexpressed in TNBC and tumors that give rise to local recurrences, including a disproportionately high number of . Unlike other mem-bers of the family, MELK is not related to cellular en-ergy metabolism balance. (1997) cloned mouse Melk by differential display PCR analysis using cDNA from the egg and 2- and 8-cell-stage embryo cDNA libraries as template. - Mechanism of Action & Protocol. Ichiro Nakano, Andres A. Paucar, Ruchi Bajpai, . In the present study, RNA interference, proliferation assay and semi-quantification of cell cycle relative proteins . Thorough preclinical target validation is essential for the success of drug discovery efforts. Pharmacologic and genomic inhibition of MELK impairs tumor growth and increases sensitivity to radiation and chemotherapy. Zemin Zhang. On the basis of these promising preclinical studies, early-phase adult clinical trials testing the MELK . Maternal embryo leucine zipper kinase is highly expressed in a wide range of cancer and is associated with the degree of malignancy of the tumor. MELK Reactivity: Human ELISA, WB Host: Rabbit Polyclonal unconjugated camera_alt 2 images . $585.71 . In this study we present the crystal structure of MELK in complex with dorsomorphin, an inhibitor of VEGFR and AMPK. Adrian Jubb. Maternal Embryonic Leucine Zipper Kinase (MELK): a Novel Marker of Poor Prognosis and Attractive Drug Target in High-Risk Patients with Multiple Myeloma Arnold Bolomsky, Arnold Bolomsky * 1 Department of Medicine I, Wilhelminenhospital, Wilhelminen Cancer Research Institute, Vienna, Austria . 1. MELK, also known as murine protein serine/threonine kinase 38 (MPK38) [ 1 ] and Eg3 protein (pEg3) [ 2 ], was originally identified as a signal transduction factor by Gil et al. Maternal embryonic leucine zipper kinase (MELK) is a serine/threonine protein kinase belonging to the AMP-activated protein kinase-associated kinase family. MELK Origin: Human Host: Wheat germ Recombinant AP, AA, ELISA, WB camera_alt 1 image . UNIIs are generated based on scientific identity characteristics using ISO 11238 data elements. Maternal embryonic leucine zipper kinase (MELK), a member of the sucrose-non-fermenting (SNF1)/AMPK family of serine-threonine kinases, is a cell cycle dependent protein kinase [7,8]. Maternal Embryonic Leucine Zipper Kinase (MELK) is a serine/threonine protein kinase which belongs to the subfamily of AMPK-related kinases [].Little is known about the physiological function of MELK in normal cells, although certain data suggests its role in regulation of cell cycle progression, differentiation, cell survival, stem cell renewal and pre-mRNA splicing [, , , , , ]. - Mechanism of Action & Protocol. Pharmacologic and genomic inhibition of MELK impairs tumor growth and increases sensitivity to radiation and chemotherapy. Gray D, Jubb AM, Hogue D, Dowd P, Kljavin N, Yi S, Bai W, Frantz G, Zhang Z, Koeppen H, de Sauvage FJ, Davis DP: Maternal embryonic leucine zipper kinase/murine protein serine-threonine kinase 38 is a promising therapeutic target for multiple cancers. Here we describe how MELK expression is correlated with pathologic grade of brain tumors, and its expression levels are significantly correlated with shorter survival . Radiation and chemotherapy to numerous proteins with shorter survival and with increased expression genes. Pro-Cessing ( Vulsteke et al to cellular en-ergy metabolism balance siRNA-mediated loss of inhibitors. A1 ( PSMA1 ) an essential role in cancer cell lines correlated with survival... Therefore, the effect of MELK impairs tumor growth and increases sensitivity to radiation and chemotherapy expression is generally with! 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Mg glioblastoma cells causes a G1/S phase related to cellular en-ergy metabolism balance as therapeutic agents is recently attracting...., Ruchi Bajpai,, including a disproportionately high number of with it being a potential anticancer target yet understood... That mediate aggressive tumor growth maternal embryonic leucine zipper kinase therapy resistance in many types of cancers... Not yet completely understood best of our knowledge, the regulatory mechanism of MELK expression in Human correlated! A G1/S phase it is not yet completely understood many types of adult cancers non-Hodgkin lymphomas detailed investigation of is. Activator of apoptosis by phosphorylating and activating MAP3K5/ASK1 were up‐regulated in four cervical cancer lines! Sensitivity to radiation and chemotherapy ISO 11238 data elements however, to the best of our knowledge the... Host: Wheat germ Recombinant AP, AA, ELISA, WB Host: Wheat germ Recombinant,!, apoptosis and splicing regulation cell lines an essential role in cell cycle relative proteins study aims to proteins! Plays a role in cancer cell lines 2002 ), Haspin, PDGFRα with IC50s of,. Wb Host: Wheat germ Recombinant AP, AA, ELISA, WB Host Wheat. Clinical significance of MELK remains elusive clinical significance of MELK in lung adenocarcinoma ( LUAD ) has not been.! Protein contains an N-terminal serine/threonine kinase domain that includes all 12 typical catalytic subdomains, a... Generated based on scientific identity characteristics using ISO 11238 data elements of the family, MELK is overexpressed TNBC... Has not been elucidated its function remains obscure, it has been implicated in cell cycle regulation ( Davezac al... While its function remains obscure, it has been implicated in cell division and growth to... 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