Capece, Vincenzo

[["dc.bibliographiccitation.artnumber","373"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.journal","Frontiers in Cellular Neuroscience"],["dc.bibliographiccitation.lastpage","15"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Stilling, Roman Manuel"],["dc.contributor.author","Benito-Garagorri, Eva"],["dc.contributor.author","Gertig, Michael"],["dc.contributor.author","Barth, Jonas"],["dc.contributor.author","Capece, Vincenzo"],["dc.contributor.author","Burkhardt, Susanne"],["dc.contributor.author","Bonn, Stefan"],["dc.contributor.author","Fischer, Andre"],["dc.date.accessioned","2017-09-07T11:45:24Z"],["dc.date.available","2017-09-07T11:45:24Z"],["dc.date.issued","2014"],["dc.description.abstract","Aging is accompanied by gradually increasing impairment of cognitive abilities and constitutes the main risk factor of neurodegenerative conditions like Alzheimer's disease (AD). The underlying mechanisms are however not well understood. Here we analyze the hippocampal transcriptome of young adult mice and two groups of mice at advanced age using RNA sequencing. This approach enabled us to test differential expression of coding and non-coding transcripts, as well as differential splicing and RNA editing. We report a specific age-associated gene expression signature that is associated with major genetic risk factors for late-onset AD (LOAD). This signature is dominated by neuroinflammatory processes, specifically activation of the complement system at the level of increased gene expression, while de-regulation of neuronal plasticity appears to be mediated by compromised RNA splicing."],["dc.identifier.doi","10.3389/fncel.2014.00373"],["dc.identifier.gro","3142019"],["dc.identifier.isi","000345840200001"],["dc.identifier.pmid","25431548"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11463"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3645"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1662-5102"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","De-regulation of gene expression and alternative splicing affects distinct cellular pathways in the aging hippocampus"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","e1239"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Translational psychiatry"],["dc.bibliographiccitation.lastpage","e1239"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Benito, E."],["dc.contributor.author","Ramachandran, B."],["dc.contributor.author","Schroeder, H."],["dc.contributor.author","Schmidt, G."],["dc.contributor.author","Urbanke, H."],["dc.contributor.author","Burkhardt, S."],["dc.contributor.author","Capece, V."],["dc.contributor.author","Dean, C."],["dc.contributor.author","Fischer, A."],["dc.date.accessioned","2019-07-09T11:44:50Z"],["dc.date.available","2019-07-09T11:44:50Z"],["dc.date.issued","2017-09-26"],["dc.description.abstract","Histone acetylation is essential for memory formation and its deregulation contributes to the pathogenesis of Alzheimer's disease. Thus, targeting histone acetylation is discussed as a novel approach to treat dementia. The histone acetylation landscape is shaped by chromatin writer and eraser proteins, while readers link chromatin state to cellular function. Chromatin readers emerged novel drug targets in cancer research but little is known about the manipulation of readers in the adult brain. Here we tested the effect of JQ1-a small-molecule inhibitor of the chromatin readers BRD2, BRD3, BRD4 and BRDT-on brain function and show that JQ1 is able to enhance cognitive performance and long-term potentiation in wild-type animals and in a mouse model for Alzheimer's disease. Systemic administration of JQ1 elicited a hippocampal gene expression program that is associated with ion channel activity, transcription and DNA repair. Our findings suggest that JQ1 could be used as a therapy against dementia and should be further tested in the context of learning and memory."],["dc.identifier.doi","10.1038/tp.2017.202"],["dc.identifier.pmid","28949335"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14924"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59110"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","info:eu-repo/grantAgreement/EC/H2020/648898/EU//DEPICODE"],["dc.relation.issn","2158-3188"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","612"],["dc.title","The BET/BRD inhibitor JQ1 improves brain plasticity in WT and APP mice."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","54"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","European Journal of Heart Failure"],["dc.bibliographiccitation.lastpage","66"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Berulava, Tea"],["dc.contributor.author","Buchholz, Eric"],["dc.contributor.author","Elerdashvili, Vakhtang"],["dc.contributor.author","Pena, Tonatiuh"],["dc.contributor.author","Islam, Md Rezaul"],["dc.contributor.author","Lbik, Dawid"],["dc.contributor.author","Mohamed, Belal A."],["dc.contributor.author","Renner, Andre"],["dc.contributor.author","Lewinski, Dirk"],["dc.contributor.author","Sacherer, Michael"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Jain, Gaurav"],["dc.contributor.author","Capece, Vincenzo"],["dc.contributor.author","Cleve, Nicole"],["dc.contributor.author","Burkhardt, Susanne"],["dc.contributor.author","Hasenfuss, Gerd"],["dc.contributor.author","Fischer, Andre"],["dc.contributor.author","Toischer, Karl"],["dc.date.accessioned","2020-12-10T14:06:19Z"],["dc.date.available","2020-12-10T14:06:19Z"],["dc.date.issued","2019"],["dc.description.abstract","ABSTRACT Aims Deregulation of epigenetic processes and aberrant gene expression are important mechanisms in heart failure. Here we studied the potential relevance of m6A RNA methylation in heart failure development. Methods and results We analysed m6A RNA methylation via next‐generation sequencing. We found that approximately one quarter of the transcripts in the healthy mouse and human heart exhibit m6A RNA methylation. During progression to heart failure we observed that changes in m6A RNA methylation exceed changes in gene expression both in mouse and human. RNAs with altered m6A RNA methylation were mainly linked to metabolic and regulatory pathways, while changes in RNA expression level mainly represented changes in structural plasticity. Mechanistically, we could link m6A RNA methylation to altered RNA translation and protein production. Interestingly, differentially methylated but not differentially expressed RNAs showed differential polysomal occupancy, indicating transcription‐independent modulation of translation. Furthermore, mice with a cardiomyocyte restricted knockout of the RNA demethylase Fto exhibited an impaired cardiac function compared to control mice. Conclusions We could show that m6A landscape is altered in heart hypertrophy and heart failure. m6A RNA methylation changes lead to changes in protein abundance, unconnected to mRNA levels. This uncovers a new transcription‐independent mechanisms of translation regulation. Therefore, our data suggest that modulation of epitranscriptomic processes such as m6A methylation might be an interesting target for therapeutic interventions."],["dc.description.sponsorship","German Center for cardiovascular research (DZHK)"],["dc.description.sponsorship","German Center for Neurodegenerative Diseases (DZNE) http://dx.doi.org/10.13039/501100005224"],["dc.description.sponsorship","BMBF http://dx.doi.org/10.13039/501100002347"],["dc.description.sponsorship","German Research Foundation (DFG"],["dc.identifier.doi","10.1002/ejhf.1672"],["dc.identifier.pmid","31849158"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17076"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/69851"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/11"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/334"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | D01: Erholung aus der Herzinsuffizienz – Einfluss von Fibrose und Transkriptionssignatur"],["dc.relation","SFB 1002 | D04: Bedeutung der Methylierung von RNA (m6A) und des Histons H3 (H3K4) in der Herzinsuffizienz"],["dc.relation.workinggroup","RG M. Bohnsack (Molecular Biology)"],["dc.relation.workinggroup","RG A. Fischer (Epigenetics and Systems Medicine in Neurodegenerative Diseases)"],["dc.relation.workinggroup","RG Hasenfuß"],["dc.relation.workinggroup","RG Toischer (Kardiales Remodeling)"],["dc.rights","CC BY-NC 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/4.0"],["dc.title","Changes in m6A RNA methylation contribute to heart failure progression by modulating translation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1071"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.lastpage","1086"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Murdoch, John D."],["dc.contributor.author","Rostosky, Christine M."],["dc.contributor.author","Gowrisankaran, Sindhuja"],["dc.contributor.author","Arora, Amandeep S."],["dc.contributor.author","Soukup, Sandra-Fausia"],["dc.contributor.author","Vidal, Ramon"],["dc.contributor.author","Capece, Vincenzo"],["dc.contributor.author","Freytag, Siona"],["dc.contributor.author","Fischer, Andre"],["dc.contributor.author","Verstreken, Patrik"],["dc.contributor.author","Bonn, Stefan"],["dc.contributor.author","Raimundo, Nuno"],["dc.contributor.author","Milosevic, Ira"],["dc.date.accessioned","2018-04-23T11:47:20Z"],["dc.date.available","2018-04-23T11:47:20Z"],["dc.date.issued","2016"],["dc.description.abstract","Endophilin-A, a well-characterized endocytic adaptor essential for synaptic vesicle recycling, has recently been linked to neurodegeneration. We report here that endophilin-A deficiency results in impaired movement, age-dependent ataxia, and neurodegeneration in mice. Transcriptional analysis of endophilin-A mutant mice, complemented by proteomics, highlighted ataxia- and protein-homeostasis-related genes and revealed upregulation of the E3-ubiquitin ligase FBXO32/atrogin-1 and its transcription factor FOXO3A. FBXO32 overexpression triggers apoptosis in cultured cells and neurons but, remarkably, coexpression of endophilin-A rescues it. FBXO32 interacts with all three endophilin-A proteins. Similarly to endophilin-A, FBXO32 tubulates membranes and localizes on clathrin-coated structures. Additionally, FBXO32 and endophilin-A are necessary for autophagosome formation, and both colocalize transiently with autophagosomes. Our results point to a role for endophilin-A proteins in autophagy and protein degradation, processes that are impaired in their absence, potentially contributing to neurodegeneration and ataxia."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2016"],["dc.identifier.doi","10.1016/j.celrep.2016.09.058"],["dc.identifier.gro","3142206"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13844"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13327"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.issn","2211-1247"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.title","Endophilin-A Deficiency Induces the Foxo3a-Fbxo32 Network in the Brain and Causes Dysregulation of Autophagy and the Ubiquitin-Proteasome System"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]