Relevant bibliographies by topics / H3K4 methyltransferase

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'H3K4 methyltransferase'

Author: Grafiati
Published: 4 June 2021
Last updated: 18 February 2022

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Journal articles on the topic "H3K4 methyltransferase"

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Umezawa, Ryohei, Masanobu Yamada, Kazuhiko Horiguchi, et al. "Aberrant Histone Modifications at the Thyrotropin-Releasing Hormone Gene in Resistance to Thyroid Hormone: Analysis of F455S Mutant Thyroid Hormone Receptor." Endocrinology 150, no. 7 (2009): 3425–32. http://dx.doi.org/10.1210/en.2008-1738.

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We reported a novel mutation of thyroid hormone receptor (TR)-β, F455S, in a patient with pituitary resistance to thyroid hormone (RTH), who showed impaired release of nuclear receptor corepressor and abnormal histone deacetylation. In the present study, we further analyzed the histone modifications and the dynamics of TR and RNA polymerase II on the TRH gene. The lysine residues 9 (H3K9) and 14 (K14) of the histone H3 were acetylated in the absence of thyroid hormone (TH), and addition of TH caused a temporary deacetylation of both residues. Although H3K4 was di- and trimethylated in the abse
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Gregory, Gregory D., Christopher R. Vakoc, Tanya Rozovskaia, et al. "Mammalian ASH1L Is a Histone Methyltransferase That Occupies the Transcribed Region of Active Genes." Molecular and Cellular Biology 27, no. 24 (2007): 8466–79. http://dx.doi.org/10.1128/mcb.00993-07.

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ABSTRACT Histone lysine methylation regulates genomic functions, including gene transcription. Previous reports found various degrees of methylation at H3K4, H3K9, and H4K20 within the transcribed region of active mammalian genes. To identify the enzymes responsible for placing these modifications, we examined ASH1L, the mammalian homolog of the Drosophila melanogaster Trithorax group (TrxG) protein Ash1. Drosophila Ash1 has been reported to methylate H3K4, H3K9, and H4K20 at its target sites. Here we demonstrate that mammalian ASH1L associates with the transcribed region of all active genes e
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Yang, Liu, Mingli Jin, and Kwang Won Jeong. "Histone H3K4 Methyltransferases as Targets for Drug-Resistant Cancers." Biology 10, no. 7 (2021): 581. http://dx.doi.org/10.3390/biology10070581.

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The KMT2 (MLL) family of proteins, including the major histone H3K4 methyltransferase found in mammals, exists as large complexes with common subunit proteins and exhibits enzymatic activity. SMYD, another H3K4 methyltransferase, and SET7/9 proteins catalyze the methylation of several non-histone targets, in addition to histone H3K4 residues. Despite these structural and functional commonalities, H3K4 methyltransferase proteins have specificity for their target genes and play a role in the development of various cancers as well as in drug resistance. In this review, we examine the overall role
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Napieralski, Rudolf, Ernst Wagner, Harry Gebhard, et al. "Alternation of histone and DNA methylation in human atherosclerotic carotid plaques." Thrombosis and Haemostasis 114, no. 08 (2015): 390–402. http://dx.doi.org/10.1160/th14-10-0852.

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SummaryLittle is known about epigenetics and its possible role in atherosclerosis. We here analysed histone and DNA methylation and the expression of corresponding methyltransferases in early and advanced human atherosclerotic carotid lesions in comparison to healthy carotid arteries. Western Blotting was performed on carotid plaques from our biobank with early (n=60) or advanced (n=60) stages of atherosclerosis and healthy carotid arteries (n=12) to analyse di-methylation patterns of histone H3 at positions K4, K9 and K27. In atherosclerotic lesions, di-methylation of H3K4 was unaltered and t
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Kwon, Minjung, Kihyun Park, Kwangbeom Hyun, et al. "H2B ubiquitylation enhances H3K4 methylation activities of human KMT2 family complexes." Nucleic Acids Research 48, no. 10 (2020): 5442–56. http://dx.doi.org/10.1093/nar/gkaa317.

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Abstract In mammalian cells, distinct H3K4 methylation states are created by deposition of methyl groups by multiple complexes of histone lysine methyltransferase 2 (KMT2) family proteins. For comprehensive analyses that directly compare the catalytic properties of all six human KMT2 complexes, we employed a biochemically defined system reconstituted with recombinant KMT2 core complexes (KMT2CoreCs) containing minimal components required for nucleosomal H3K4 methylation activity. We found that each KMT2CoreC generates distinct states and different levels of H3K4 methylation, and except for MLL
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Wang, Pengbo, Marcel Dreger, Elena Madrazo, et al. "WDR5 modulates cell motility and morphology and controls nuclear changes induced by a 3D environment." Proceedings of the National Academy of Sciences 115, no. 34 (2018): 8581–86. http://dx.doi.org/10.1073/pnas.1719405115.

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Cell migration through extracellular matrices requires nuclear deformation, which depends on nuclear stiffness. In turn, chromatin structure contributes to nuclear stiffness, but the mechanosensing pathways regulating chromatin during cell migration remain unclear. Here, we demonstrate that WD repeat domain 5 (WDR5), an essential component of H3K4 methyltransferase complexes, regulates cell polarity, nuclear deformability, and migration of lymphocytes in vitro and in vivo, independent of transcriptional activity, suggesting nongenomic functions for WDR5. Similarly, depletion of RbBP5 (another
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Zhang, Zhiren, Yanhui Zhai, Xiaoling Ma, et al. "Down-Regulation of H3K4me3 by MM-102 Facilitates Epigenetic Reprogramming of Porcine Somatic Cell Nuclear Transfer Embryos." Cellular Physiology and Biochemistry 45, no. 4 (2018): 1529–40. http://dx.doi.org/10.1159/000487579.

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Background/Aims: Aberrantly high levels of H3K4me3, caused by incomplete epigenetic reprogramming, likely cause a low efficiency of somatic cell nuclear transfer (SCNT). Smal molecule inhibitors aimed at epigenetic modification can be used to improve porcine SCNT embryo development. In this study, we examined the effects of MM-102, an H3K4 histone methyltransferase inhibitor, on porcine SCNT preimplantation embryos to investigate the mechanism by which H3K4 methylation regulated global epigenetic reprograming during SCNT. Methods: MM-102 was added to the SCNT embryos culture system and the glo
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Li, Xingguo, Shaohua Wang, Ying Li, Yi Qiu, and Suming Huang. "Chromatin Boundaries Require the Functional Cooperation Between hSET1 and NURF Complexes." Blood 116, no. 21 (2010): 646. http://dx.doi.org/10.1182/blood.v116.21.646.646.

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Abstract Abstract 646 Chromatin modification and remodeling activities play a central role in organizing nuclear functions in eukaryotic genome. Chromatin domains with characteristic epigenetic marks are organized by chromatin insulator. The chicken b-globin insulator, 5′HS4, is an excellent model system to study how insulator maintains gene function and prevents the encroachment of repressive heterochromatin. We showed previously that USF1/2 bound 5′HS4 insulator mediates chromatin barrier activity by recruiting and organizing active histone modifications in the chicken b-globin locus. Howeve
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Klonou, Alexia, Sarantis Chlamydas, and Christina Piperi. "Structure, Activity and Function of the MLL2 (KMT2B) Protein Lysine Methyltransferase." Life 11, no. 8 (2021): 823. http://dx.doi.org/10.3390/life11080823.

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The Mixed Lineage Leukemia 2 (MLL2) protein, also known as KMT2B, belongs to the family of mammalian histone H3 lysine 4 (H3K4) methyltransferases. It is a large protein of 2715 amino acids, widely expressed in adult human tissues and a paralog of the MLL1 protein. MLL2 contains a characteristic C-terminal SET domain responsible for methyltransferase activity and forms a protein complex with WRAD (WDR5, RbBP5, ASH2L and DPY30), host cell factors 1/2 (HCF 1/2) and Menin. The MLL2 complex is responsible for H3K4 trimethylation (H3K4me3) on specific gene promoters and nearby cis-regulatory sites,
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Cao, Fang, Elizabeth C. Townsend, Hacer Karatas, et al. "Targeting MLL1 H3K4 Methyltransferase Activity in Mixed-Lineage Leukemia." Molecular Cell 53, no. 2 (2014): 247–61. http://dx.doi.org/10.1016/j.molcel.2013.12.001.

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Dissertations / Theses on the topic "H3K4 methyltransferase"

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Ciotta, Giovanni. "Tagging methods as a tool to investigate histone H3 methylation dynamics in mouse embryonic stem cells." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2011. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-70526.

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Covalent modification of histones is an important factor in the regulation of the chromatin structure implicated in DNA replication, repair, recombination, and transcription, as well as in RNA processing. In recent years, histone methylation has emerged as one of the key modifications regulating chromatin function. However, the mechanisms involved are complex and not well understood. Histone 3 lysine 4 (H3K4) methylation is deposited by a family of histone H3K4 methyltransferases (HMTs) that share a conserved SET domain. In mammalian cells, six family members have been characterized: Setd1a an
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Neumann, Katrin. "H3K4 methyltransferases Mll1 and Mll2 have distinct roles and cooperate in neural differentiation and reprogramming." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2014. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-154556.

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Methylation of lysine residues in histone tails is an intensively studied epigenetic signal that regulates transcription throughout development. Methylation of histone 3 lysine 4 (H3K4) is usually associated with promoters of actively transcribed genes whereas H3K27 or H3K9 methylation silences genes. Yeast possess only one H3K4 methyltransferase, Set1. In contrast, there are six enzymes capable of catalyzing this modification in mammals implying a certain specialization or division of labor. The present study examined the functions of the mouse H3K4 methyltransferase paralogs, Mixed Lineage L
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Neumann, Katrin [Verfasser], Konstantinos [Akademischer Betreuer] Anastassiadis, Francis [Akademischer Betreuer] Stewart, and Frank [Akademischer Betreuer] Buchholz. "H3K4 methyltransferases Mll1 and Mll2 have distinct roles and cooperate in neural differentiation and reprogramming / Katrin Neumann. Gutachter: Francis Stewart ; Frank Buchholz. Betreuer: Konstantinos Anastassiadis." Dresden : Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2014. http://d-nb.info/1068448938/34.

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Pick-Franke, Patricia A. "SETD1 HISTONE 3 LYSINE 4 METHYLTRANSFERASE COMPLEX COMPONENTS IN EPIGENETIC REGULATION." Thesis, 2011. http://hdl.handle.net/1805/2511.

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Indiana University-Purdue University Indianapolis (IUPUI)<br>Setd1 histone 3 lysine 4 methyltransferases are critical for epigenetic regulation and gene expression. Setd1a is multiprotein complex comprised of several critical subunits including wdr82, which is essential for embryonic development, and cfp1, critical for regulation of both activation and repression of transcriptional programs required in basic and developmental cellular processes.
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Drouin, Simon. "Caractérisation de la fonction des complexes histone déacétylases Rpd3S et Set3C." Thèse, 2011. http://hdl.handle.net/1866/5176.

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La chromatine est essentielle au maintien de l’intégrité du génome, mais, ironiquement, constitue l’obstacle principal à la transcription des gènes. Plusieurs mécanismes ont été développés par la cellule pour pallier ce problème, dont l’acétylation des histones composant les nucléosomes. Cette acétylation, catalysée par des histones acétyl transférases (HATs), permet de réduire la force de l’interaction entre les nucléosomes et l’ADN, ce qui permet à la machinerie transcriptionnelle de faire son travail. Toutefois, on ne peut laisser la chromatine dans cet état permissif sans conséquence néfas
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Chen, Min-Wei, and 陳民瑋. "H3K9 Histone Methyltransferase G9a Promotes Cancer Cell Invasion and Metastasis." Thesis, 2010. http://ndltd.ncl.edu.tw/handle/23603814540857504865.

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博士<br>國立臺灣大學<br>毒理學研究所<br>99<br>G9a is a mammalian histone methyltransferase that contributes to the epigenetic silencing of tumor suppressor genes. Emerging evidence suggests that G9a is required to maintain the malignant phenotype, but the role of G9a function in mediating tumor metastasis has not been explored. Here, we show that G9a is expressed in aggressive lung cancer cells, and its elevated expression correlates with poor prognosis. RNAi-mediated knockdown of G9a in highly invasive lung cancer cells inhibited cell migration and invasion in vitro and metastasis in vivo. Conversely, ecto
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Koch, Carmen. "Molekulare und funktionelle Analyse von Windei (CG12340) als Bindungspartner der Histonmethyltransferase Eggless während der Oogenese von Drosophila." Doctoral thesis, 2009. http://hdl.handle.net/11858/00-1735-0000-0006-AD30-D.

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Book chapters on the topic "H3K4 methyltransferase"

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Cho, Young-Wook, SunHwa Hong, and Kai Ge. "Affi nity Purifi cation of MLL3/MLL4 Histone H3K4 Methyltransferase Complex." In Methods in Molecular Biology. Springer New York, 2011. http://dx.doi.org/10.1007/978-1-61779-376-9_30.

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Zacarias, Ericka, Juliana Almeida, and J. Armando Casas-Mollano. "Evolution of Epigenetic Mechanisms in Plants: Insights From H3K4 and H3K27 Methyltransferases." In Handbook of Epigenetics. Elsevier, 2017. http://dx.doi.org/10.1016/b978-0-12-805388-1.00026-2.

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Conference papers on the topic "H3K4 methyltransferase"

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Wang, Ya-fang, Jie Zhang, Yi Su, et al. "Abstract 4680: H3K9 methyltransferase G9a epigenetically regulates breast cancer cell iron homeostasisviarepressing ferroxidase hephaestin expression, promotes breast cancer growth." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-4680.

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Chen, Min Wei, Kuo-Tai Hua, Hsin-Jung Kao, et al. "Abstract 5324: H3K9 histone methyltransferase G9a promotes lung cancer invasion and metastasis by silencing the cell adhesion molecule Ep-CAM." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-5324.

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Tzeng, Tsai-Yu. "Abstract 78: Epigenetic regulation of the metastatic progression of non-small cell lung cancer by the histone H3K9 methyltransferase SETDB1." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-78.

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Rowbotham, Samuel P., and Carla F. Kim. "Abstract A39: H3K9 methyltransferases G9a/Glp link the chromatin regulation of lung adenocarcinoma tumor propagating cells and lung bronchiolaveolar stem cells." In Abstracts: AACR Special Conference: Chromatin and Epigenetics in Cancer; September 24-27, 2015; Atlanta, GA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.chromepi15-a39.

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