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

DEK oncogene

DEK, protein DEK
This gene encodes a protein with one SAP domain. This protein binds to cruciform and superhelical DNA and induces positive supercoils into closed circular DNA, and is also involved in splice site selection during mRNA processing. Chromosomal aberrations involving this region, increased expression of this gene, and the presence of antibodies against this protein are all associated with various diseases. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2008] (from NCBI)
Top mentioned proteins: CAN, HAD, POLYMERASE, p53, Histone
Papers on DEK
Significance of DEK overexpression for the prognostic evaluation of non-small cell lung carcinoma.
Gao et al., Dandong, China. In Oncol Rep, Jan 2016
In the present study, we explored the role of DEK expression for the prognostic evaluation of non-small cell lung carcinoma (NSCLC).
IRAK1 is a novel DEK transcriptional target and is essential for head and neck cancer cell survival.
Wells et al., Cincinnati, United States. In Oncotarget, Jan 2016
The chromatin-binding DEK protein was recently reported to promote the growth of HPV+ and HPV- head and neck squamous cell carcinomas (HNSCCs).
The DEK Oncoprotein Is a Critical Component of the EKLF/KLF1 Enhancer in Erythroid Cells.
Bieker et al., New York City, United States. In Mol Cell Biol, Nov 2015
Using biochemical affinity purification, we have identified the DEK oncoprotein as a critical factor that interacts with an essential upstream enhancer element of the EKLF promoter and exerts a positive effect on EKLF levels.
DEK: A novel early screening and prognostic marker for breast cancer.
Wu et al., Harbin, China. In Mol Med Report, Nov 2015
The present study aimed to investigate the expression status and clinical implications of DEK in breast cancer, in order to contribute to developments in breast cancer management.
The DEK oncoprotein and its emerging roles in gene regulation.
Gullberg et al., Lund, Sweden. In Leukemia, Aug 2015
The DEK oncogene is highly expressed in cells from most human tissues and overexpressed in a large and growing number of cancers.
Oncogene- and drug resistance-associated alternative exon usage in acute myeloid leukemia (AML).
Mortreux et al., Lyon, France. In Oncotarget, Jun 2015
We performed exon-array analysis and exon-specific PCR (ESPCR) to identify specific landscapes of exon expression that are associated with DEK and WT1 oncogene expression and the resistance of AML cells to AraC, doxorubicin or azacitidine.
Dissecting the Potential Interplay of DEK Functions in Inflammation and Cancer.
Privette Vinnedge et al., Cincinnati, United States. In J Oncol, 2014
Here, we discuss the association of the unique DEK protein with these processes.
NUP214-RAC1 and RAC1-COL12A1 Fusion in Complex Variant Translocations Involving Chromosomes 6, 7 and 9 in an Acute Myeloid Leukemia Case with DEK-NUP214.
Emi et al., Japan. In Cytogenet Genome Res, 2014
DEK-NUP214 gene fusion in acute myeloid leukemia (AML) is associated with poor prognosis.
MicroRNA-592 targets DEK oncogene and suppresses cell growth in the hepatocellular carcinoma cell line HepG2.
Su et al., Changchun, China. In Int J Clin Exp Pathol, 2014
A tumor oncogene, DEK, was identified as a direct target of miR-592.
Prostate cancer. Ubiquitylome analysis identifies dysregulation of effector substrates in SPOP-mutant prostate cancer.
Garraway et al., Cambridge, United States. In Science, 2014
Of these, DEK and TRIM24 emerged as effector substrates consistently up-regulated by SPOP mutants.
Nucleoporins and nucleocytoplasmic transport in hematologic malignancies.
Yaseen et al., Saint Louis, United States. In Semin Cancer Biol, 2014
DEK-NUP214 is the most common NUP214 fusion in AML; it tends to occur in younger patients and is usually associated with FLT3 internal tandem duplications.
Histone H3 dynamics in plant cell cycle and development.
Gutierrez et al., Madrid, Spain. In Cytogenet Genome Res, 2013
We also include a discussion on the histone H3 chaperones that actively participate in H3 deposition, in particular CAF-1, HIRA and ASF1, and on the putative plant homologs of human ATRX and DEK chaperones.
Concise review: role of DEK in stem/progenitor cell biology.
Markovitz et al., Indianapolis, United States. In Stem Cells, 2013
DEK, a non-histone nuclear phosphoprotein initially identified as a putative proto-oncogene, has recently been linked to regulate hematopoiesis.
DEK regulates hematopoietic stem engraftment and progenitor cell proliferation.
Markovitz et al., Indianapolis, United States. In Stem Cells Dev, 2012
DEK has potent effects on HSCs, HPCs, and hematopoiesis, information of biological and potential clinical interest.
Silencing of the DEK gene induces apoptosis and senescence in CaSki cervical carcinoma cells via the up-regulation of NF-κB p65.
Zhang et al., Shenyang, China. In Biosci Rep, 2012
DEK knockdown results in a significant growth repression of CaSki cells by inducing cell apoptosis and senescence via upregulation of p65.
C/EBPα and DEK coordinately regulate myeloid differentiation.
Marto et al., Boston, United States. In Blood, 2012
C/EBPalpha and DEK coordinately activate myeloid gene expression.
DEK overexpression is correlated with the clinical features of breast cancer.
Lin et al., Yanji, China. In Pathol Int, 2012
DEK overexpression appears to be associated with breast cancer progression
Maintenance of muscle stem-cell quiescence by microRNA-489.
Rando et al., Stanford, United States. In Nature, 2012
Further analysis revealed that miR-489 functions as a regulator of satellite-cell quiescence, as it post-transcriptionally suppresses the oncogene Dek, the protein product of which localizes to the more differentiated daughter cell during asymmetric division of satellite cells and promotes the transient proliferative expansion of myogenic progenitors.
Oncoprotein DEK as a tissue and urinary biomarker for bladder cancer.
Trama et al., United States. In Bmc Cancer, 2010
DEK protein is expressed in bladder tumor tissue and voided urine of bladder cancer patients.
Intron removal requires proofreading of U2AF/3' splice site recognition by DEK.
Valcárcel et al., Barcelona, Spain. In Science, 2006
DEK enforces 3' splice site discrimination by U2AF; DEK phosphorylated at serines 19 and 32 associates with U2AF35, facilitates the U2AF35-AG interaction and prevents binding of U2AF65 to pyrimidine tracts not followed by AG
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