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000139386 041__ $$aEnglish
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000139386 1001_ $$0P:(DE-HGF)0$$aKerimoglu, Cemil$$b0
000139386 245__ $$aKMT2A and KMT2B Mediate Memory Function by Affecting Distinct Genomic Regions.
000139386 260__ $$a[New York, NY]$$bElsevier$$c2017
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000139386 520__ $$aKmt2a and Kmt2b are H3K4 methyltransferases of the Set1/Trithorax class. We have recently shown the importance of Kmt2b for learning and memory. Here, we report that Kmt2a is also important in memory formation. We compare the decrease in H3K4 methylation and de-regulation of gene expression in hippocampal neurons of mice with knockdown of either Kmt2a or Kmt2b. Kmt2a and Kmt2b control largely distinct genomic regions and different molecular pathways linked to neuronal plasticity. Finally, we show that the decrease in H3K4 methylation resulting from Kmt2a knockdown partially recapitulates the pattern previously reported in CK-p25 mice, a model for neurodegeneration and memory impairment. Our findings point to the distinct functions of even closely related histone-modifying enzymes and provide essential insight for the development of more efficient and specific epigenetic therapies against brain diseases.
000139386 536__ $$0G:(DE-HGF)POF3-342$$a342 - Disease Mechanisms and Model Systems (POF3-342)$$cPOF3-342$$fPOF III$$x0
000139386 542__ $$2Crossref$$i2017-07-01$$uhttps://www.elsevier.com/tdm/userlicense/1.0/
000139386 542__ $$2Crossref$$i2017-06-26$$uhttp://creativecommons.org/licenses/by-nc-nd/4.0/
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000139386 650_7 $$0149025-06-9$$2NLM Chemicals$$aMyeloid-Lymphoid Leukemia Protein
000139386 650_7 $$0EC 2.1.1.43$$2NLM Chemicals$$aHistone-Lysine N-Methyltransferase
000139386 650_7 $$0EC 2.1.1.43$$2NLM Chemicals$$aKmt2a protein, mouse
000139386 650_2 $$2MeSH$$aAnimals
000139386 650_2 $$2MeSH$$aGene Expression Regulation, Enzymologic
000139386 650_2 $$2MeSH$$aHippocampus: enzymology
000139386 650_2 $$2MeSH$$aHistone-Lysine N-Methyltransferase: biosynthesis
000139386 650_2 $$2MeSH$$aHistone-Lysine N-Methyltransferase: genetics
000139386 650_2 $$2MeSH$$aMemory
000139386 650_2 $$2MeSH$$aMethylation
000139386 650_2 $$2MeSH$$aMice
000139386 650_2 $$2MeSH$$aMyeloid-Lymphoid Leukemia Protein: biosynthesis
000139386 650_2 $$2MeSH$$aMyeloid-Lymphoid Leukemia Protein: genetics
000139386 650_2 $$2MeSH$$aNeurons: enzymology
000139386 7001_ $$0P:(DE-2719)2812054$$aSakib, M Sadman$$b1$$udzne
000139386 7001_ $$0P:(DE-2719)2811223$$aJain, Gaurav$$b2$$udzne
000139386 7001_ $$0P:(DE-2719)2810482$$aBenito, Eva$$b3$$udzne
000139386 7001_ $$0P:(DE-2719)2810773$$aBurkhardt, Susanne$$b4$$udzne
000139386 7001_ $$0P:(DE-2719)2810626$$aCapece, Vincenzo$$b5$$udzne
000139386 7001_ $$0P:(DE-2719)2812832$$aKaurani, Lalit$$b6$$udzne
000139386 7001_ $$0P:(DE-2719)2810512$$aHalder, Rashi$$b7$$udzne
000139386 7001_ $$0P:(DE-2719)9000006$$aAgís-Balboa, Roberto Carlos$$b8$$udzne
000139386 7001_ $$0P:(DE-2719)9000302$$aStilling, Roman$$b9$$udzne
000139386 7001_ $$0P:(DE-2719)2811034$$aUrbanke, Hendrik$$b10$$udzne
000139386 7001_ $$0P:(DE-HGF)0$$aKranz, Andrea$$b11
000139386 7001_ $$0P:(DE-HGF)0$$aStewart, A Francis$$b12
000139386 7001_ $$0P:(DE-2719)2000047$$aFischer, Andre$$b13$$eLast author$$udzne
000139386 77318 $$2Crossref$$3journal-article$$a10.1016/j.celrep.2017.06.072$$b : Elsevier BV, 2017-07-01$$n3$$p538-548$$tCell Reports$$v20$$x2211-1247$$y2017
000139386 773__ $$0PERI:(DE-600)2649101-1$$a10.1016/j.celrep.2017.06.072$$gVol. 20, no. 3, p. 538 - 548$$n3$$p538-548$$q20:3<538 - 548$$tCell reports$$v20$$x2211-1247$$y2017
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