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


Top mentioned proteins: Histone, demethylase, CAN, Jumonji, V1a
Papers using JMJD2D antibodies
Mutations in the p53 Tumor Suppressor Gene: Important Milestones at the Various Steps of Tumorigenesis.
Futscher Bernard W., In PLoS ONE, 2010
... Similarly, endogenous JMJD2D in HCT116 cells (American Type Culture Collection CCL-247) was immunoprecipitated with anti-JMJD2D antibodies (Aviva Systems Biology ARP35946) ...
Papers on JMJD2D
An Iridium(III) Complex Inhibits JMJD2 Activities and Acts as a Potential Epigenetic Modulator.
Leung et al., Aomen, Macao. In J Med Chem, Sep 2015
Moreover, 1 suppressed the trimethylation of the p21 promoter on H3K9me3 and interrupted the JMJD2D-H3K9me3 interactions in human cells, suggesting that it could act as an epigenetic modulator.
The emerging role of lysine demethylases in DNA damage response: dissecting the recruitment mode of KDM4D/JMJD2D to DNA damage sites.
Ayoub et al., Haifa, Israel. In Cell Cycle, 2014
KDM4D is a lysine demethylase that removes tri- and di- methylated residues from H3K9 and is involved in transcriptional regulation and carcinogenesis.
Molecular basis for substrate recognition by lysine methyltransferases and demethylases.
Trievel et al., Ann Arbor, United States. In Biochim Biophys Acta, 2014
This review explores recent progress in elucidating the molecular basis of these specificities, highlighting structural and functional studies of the methyltransferases SUV4-20H1 (KMT5B), SUV4-20H2 (KMT5C), and ATXR5, and the demethylases UTX (KDM6A), JMJD3 (KDM6B), and JMJD2D (KDM4D).
Cell-type-specific Jumonji histone demethylase gene expression in the healthy rat CNS: detection by a novel flow cytometry method.
Watters et al., Madison, United States. In Asn Neuro, 2013
While JMJD2D was neuron-restricted, PHF8 and JMJD1C were expressed in all three cell types although the expression was highest in neurons.
Pro-growth role of the JMJD2C histone demethylase in HCT-116 colon cancer cells and identification of curcuminoids as JMJD2 inhibitors.
Janknecht et al., Oklahoma City, United States. In Am J Transl Res, 2013
We demonstrate that the histone demethylases JMJD2A, JMJD2B and JMJD2C are overexpressed in colon cancer cell lines, whereas another related protein, JMJD2D, is not.
KDM4/JMJD2 histone demethylases: epigenetic regulators in cancer cells.
Janknecht et al., Oklahoma City, United States. In Cancer Res, 2013
This protein family consists of three ~130-kDa proteins (KDM4A-C) and KDM4D/JMJD2D, which is half the size, lacks the double PHD and Tudor domains that are epigenome readers and present in the other KDM4 proteins, and has a different substrate specificity.
Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases.
Trievel et al., Ann Arbor, United States. In Structure, 2013
JMJD2 lysine demethylases (KDMs) participate in diverse genomic processes.
Poly (ADP-ribose) glycohydrolase regulates retinoic acid receptor-mediated gene expression.
Coin et al., Strasbourg, France. In Mol Cell, 2013
In the absence of PARG, we found that the H3K9 demethylase KDM4D/JMJD2D became PARsylated.
Purification and assay protocols for obtaining highly active Jumonji C demethylases.
Trievel et al., Ann Arbor, United States. In Anal Biochem, 2012
Jumonji C (JmjC) lysine demethylases (KDMs) are Fe(II)-dependent hydroxylases that catalyze the oxidative demethylation of methyllysine residues in histones and nonhistone proteins.
Enabling lead discovery for histone lysine demethylases by high-throughput RapidFire mass spectrometry.
Argyrou et al., Stevenage, United Kingdom. In J Biomol Screen, 2012
A high-throughput RapidFire mass spectrometry assay is described for the JMJD2 family of Fe(2+), O(2), and α-ketoglutarate-dependent histone lysine demethylases.
Regulation of tumor suppressor p53 and HCT116 cell physiology by histone demethylase JMJD2D/KDM4D.
Janknecht et al., Oklahoma City, United States. In Plos One, 2011
Results demonstrate that JMJD2D can stimulate cell proliferation and survival, suggesting that its inhibition may be helpful in the fight against cancer
Histone H1 variant-specific lysine methylation by G9a/KMT1C and Glp1/KMT1D.
Schneider et al., Freiburg, Germany. In Epigenetics Chromatin, 2009
We found that the histone lysine methyltransferases G9a/KMT1C and Glp1/KMT1D methylate H1.2 in vitro and in vivo, and we mapped this novel site to lysine 187 (H1.2K187) in the C-terminus of H1.
Activation of androgen receptor by histone demethylases JMJD2A and JMJD2D.
Janknecht et al., Rochester, United States. In Biochem Biophys Res Commun, 2007
identified two related histone demethylases, JMJD2A and JMJD2D
Comparative integromics on JMJD2A, JMJD2B and JMJD2C: preferential expression of JMJD2C in undifferentiated ES cells.
Katoh et al., Japan. In Int J Mol Med, 2007
In 2004, we identified and characterized JMJD2A/JHDM3A, JMJD2B, JMJD2C, JMJD2D, JMJD2E and JMJD2F.
Diversity within the JMJD2 histone demethylase family.
Janknecht et al., Rochester, United States. In Biochem Biophys Res Commun, 2007
JMJD2D is the most structurally divergent JMJD2 protein as it lacks the PHD and Tudor domains present in JMJD2A-C.
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