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Martinez-Hernandez, Ana
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Martinez-Hernandez, Ana
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Martinez-Hernandez, Ana
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Martinez-Hernandez, A.
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2007Journal Article [["dc.bibliographiccitation.firstpage","232"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","BMC Genomics"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Cankaya, Murat"],["dc.contributor.author","Hernandez, Ana"],["dc.contributor.author","Ciftci, Mehmet"],["dc.contributor.author","Beydemir, Sukru"],["dc.contributor.author","Ozdemir, Hasan"],["dc.contributor.author","Budak, Harun"],["dc.contributor.author","Gulcin, Ilhami"],["dc.contributor.author","Comakli, Veysel"],["dc.contributor.author","Emircupani, Tufan"],["dc.contributor.author","Kufrevioglu, Omer"],["dc.date.accessioned","2021-06-01T10:47:59Z"],["dc.date.available","2021-06-01T10:47:59Z"],["dc.date.issued","2007"],["dc.identifier.doi","10.1186/1471-2164-8-232"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/85786"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.issn","1471-2164"],["dc.title","An analysis of expression patterns of genes encoding proteins with catalytic activities"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]Details DOI2014Journal Article Research Paper [["dc.bibliographiccitation.firstpage","1912"],["dc.bibliographiccitation.issue","17"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","1927"],["dc.bibliographiccitation.volume","33"],["dc.contributor.author","Stilling, Roman Manuel"],["dc.contributor.author","Roenicke, Raik"],["dc.contributor.author","Benito-Garagorri, Eva"],["dc.contributor.author","Urbanke, Hendrik"],["dc.contributor.author","Capece, Vincenzo"],["dc.contributor.author","Burkhardt, Susanne"],["dc.contributor.author","Bahari-Javan, Sanaz"],["dc.contributor.author","Barth, Jonas"],["dc.contributor.author","Sananbenesi, Farahnaz"],["dc.contributor.author","Schuetz, Anna L."],["dc.contributor.author","Dyczkowski, Jerzy"],["dc.contributor.author","Martinez-Hernandez, Ana"],["dc.contributor.author","Kerimoglu, Cemil"],["dc.contributor.author","Dent, Sharon Y. R."],["dc.contributor.author","Bonn, Stefan"],["dc.contributor.author","Reymann, Klaus G."],["dc.contributor.author","Fischer, Andre"],["dc.date.accessioned","2017-09-07T11:45:35Z"],["dc.date.available","2017-09-07T11:45:35Z"],["dc.date.issued","2014"],["dc.description.abstract","Neuronal histone acetylation has been linked to memory consolidation, and targeting histone acetylation has emerged as a promising therapeutic strategy for neuropsychiatric diseases. However, the role of histone-modifying enzymes in the adult brain is still far from being understood. Here we use RNA sequencing to screen the levels of all known histone acetyltransferases (HATs) in the hippocampal CA1 region and find that K-acetyltransferase 2a (Kat2a)-a HAT that has not been studied for its role in memory function so far-shows highest expression. Mice that lack Kat2a show impaired hippocampal synaptic plasticity and long-term memory consolidation. We furthermore show that Kat2a regulates a highly interconnected hippocampal gene expression network linked to neuroactive receptor signaling via a mechanism that involves nuclear factor kappa-light-chain-enhancer of activated B cells (NF-kappa B). In conclusion, our data establish Kat2a as a novel and essential regulator of hippocampal memory consolidation."],["dc.identifier.doi","10.15252/embj.201487870"],["dc.identifier.gro","3142062"],["dc.identifier.isi","000341839500009"],["dc.identifier.pmid","25024434"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4123"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1460-2075"],["dc.relation.issn","0261-4189"],["dc.title","K-Lysine acetyltransferase 2a regulates a hippocampal gene expression network linked to memory formation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2010Journal Article [["dc.bibliographiccitation.firstpage","6058"],["dc.bibliographiccitation.issue","13"],["dc.bibliographiccitation.journal","PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA"],["dc.bibliographiccitation.lastpage","6063"],["dc.bibliographiccitation.volume","107"],["dc.contributor.author","Heneka, Michael T."],["dc.contributor.author","Nadrigny, Fabian"],["dc.contributor.author","Regen, Tommy"],["dc.contributor.author","Martinez-Hernandez, Ana"],["dc.contributor.author","Dumitrescu-Ozimek, Lucia"],["dc.contributor.author","Terwel, Dick"],["dc.contributor.author","Jardanhazi-Kurutz, Daniel"],["dc.contributor.author","Walter, Jochen"],["dc.contributor.author","Kirchhoff, Frank"],["dc.contributor.author","Hanisch, Uwe-Karsten"],["dc.contributor.author","Kummer, Markus P."],["dc.date.accessioned","2018-11-07T08:44:59Z"],["dc.date.available","2018-11-07T08:44:59Z"],["dc.date.issued","2010"],["dc.description.abstract","Locus ceruleus (LC)-supplied norepinephrine (NE) suppresses neuroinflammation in the brain. To elucidate the effect of LC degeneration and subsequent NE deficiency on Alzheimer's disease pathology, we evaluated NE effects on microglial key functions. NE stimulation of mouse microglia suppressed A beta-induced cytokine and chemokine production and increased microglial migration and phagocytosis of A beta. Induced degeneration of the locus ceruleus increased expression of inflammatory mediators in APP-transgenic mice and resulted in elevated A beta deposition. In vivo laser microscopy confirmed a reduced recruitment of microglia to A beta plaque sites and impaired microglial A beta phagocytosis in NE-depleted APP-transgenic mice. Supplying the mice the norepinephrine precursor L-threo-DOPS restored microglial functions in NE-depleted mice. This indicates that decrease of NE in locus ceruleus projection areas facilitates the inflammatory reaction of microglial cells in AD and impairs microglial migration and phagocytosis, thereby contributing to reduced A beta clearance. Consequently, therapies targeting microglial phagocytosis should be tested under NE depletion."],["dc.identifier.doi","10.1073/pnas.0909586107"],["dc.identifier.isi","000276159500066"],["dc.identifier.pmid","20231476"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/20326"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Natl Acad Sciences"],["dc.relation.issn","0027-8424"],["dc.title","Locus ceruleus controls Alzheimer's disease pathology by modulating microglial functions through norepinephrine"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS