Raimundo, Nuno

[["dc.bibliographiccitation.artnumber","54"],["dc.bibliographiccitation.journal","Frontiers in Cell and Developmental Biology"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Raimundo, Nuno"],["dc.contributor.author","Krisko, Anita"],["dc.date.accessioned","2019-07-09T11:51:27Z"],["dc.date.available","2019-07-09T11:51:27Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.3389/fcell.2019.00054"],["dc.identifier.pmid","31032256"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16125"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59946"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","Frontiers Media S.A."],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/337327/EU//MITOPEXLYSONETWORK"],["dc.relation.eissn","2296-634X"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","610"],["dc.title","Editorial: Mitochondrial Communication in Physiology, Disease and Aging"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","editorial_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Sathyanarayanan, Udhayabhaskar"],["dc.contributor.author","Musa, Marina"],["dc.contributor.author","Bou Dib, Peter"],["dc.contributor.author","Raimundo, Nuno"],["dc.contributor.author","Milosevic, Ira"],["dc.contributor.author","Krisko, Anita"],["dc.date.accessioned","2021-04-14T08:31:49Z"],["dc.date.available","2021-04-14T08:31:49Z"],["dc.date.issued","2020"],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.1038/s41467-020-19104-1"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83720"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","2041-1723"],["dc.relation.orgunit","Abteilung Experimentelle Neurodegeneration"],["dc.rights","CC BY 4.0"],["dc.title","ATP hydrolysis by yeast Hsp104 determines protein aggregate dissolution and size in vivo"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e202201737"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Life Science Alliance"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Musa, Marina"],["dc.contributor.author","Dionisio, Pedro A"],["dc.contributor.author","Casqueiro, Ricardo"],["dc.contributor.author","Milosevic, Ira"],["dc.contributor.author","Raimundo, Nuno"],["dc.contributor.author","Krisko, Anita"],["dc.date.accessioned","2022-12-01T08:31:29Z"],["dc.date.available","2022-12-01T08:31:29Z"],["dc.date.issued","2022"],["dc.description.abstract","Exact mechanisms of heat shock–induced lifespan extension, although documented across species, are still not well understood. Here, we show that fully functional peroxisomes, specifically peroxisomal catalase, are needed for the activation of canonical heat shock response and heat-induced hormesis in\r\n Caenorhabditis elegans\r\n . Although during heat shock, the HSP-70 chaperone is strongly up-regulated in the WT and in the absence of peroxisomal catalase (\r\n ctl-2(ua90)II\r\n ), the small heat shock proteins display modestly increased expression in the mutant. Nuclear foci formation of HSF-1 is reduced in the\r\n ctl-2(ua90)II\r\n mutant. In addition, heat-induced lifespan extension, observed in the WT, is absent in the\r\n ctl-2(ua90)II\r\n strain. Activation of the antioxidant response and pentose phosphate pathway are the most prominent changes observed during heat shock in the WT worm but not in the\r\n ctl-2(ua90)II\r\n mutant. Involvement of peroxisomes in the cell-wide cellular response to transient heat shock reported here gives new insight into the role of organelle communication in the organism’s stress response."],["dc.description.sponsorship"," Deutsche Forschungsgemeinschaft 501100001659"],["dc.description.sponsorship","Mediterranean Institute for Life Sciences"],["dc.description.sponsorship","European Research Council"],["dc.description.sponsorship"," John Black Charitable Foundation 501100020400"],["dc.description.sponsorship"," H2020 100010661"],["dc.identifier.doi","10.26508/lsa.202201737"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/118182"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-621"],["dc.relation.eissn","2575-1077"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Lack of peroxisomal catalase affects heat shock response in\n Caenorhabditis elegans"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Sathyanarayanan, Udhayabhaskar"],["dc.contributor.author","Musa, Marina"],["dc.contributor.author","Dib, Peter Bou"],["dc.contributor.author","Raimundo, Nuno"],["dc.contributor.author","Milosevic, Ira"],["dc.contributor.author","Krisko, Anita"],["dc.date.accessioned","2021-06-01T10:50:39Z"],["dc.date.available","2021-06-01T10:50:39Z"],["dc.date.issued","2020"],["dc.description.abstract","A Correction to this paper has been published: https://doi.org/10.1038/s41467-020-20394-8"],["dc.identifier.doi","10.1038/s41467-020-20394-8"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86737"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.eissn","2041-1723"],["dc.title","Author Correction: ATP hydrolysis by yeast Hsp104 determines protein aggregate dissolution and size in vivo"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","28751"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Peric, Matea"],["dc.contributor.author","Dib, Peter Bou"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Musa, Marina"],["dc.contributor.author","Rudan, Marina"],["dc.contributor.author","Lovric, Anita"],["dc.contributor.author","Nikolic, Andrea"],["dc.contributor.author","Saric, Ana"],["dc.contributor.author","Sobocanec, Sandra"],["dc.contributor.author","Macak, Zeljka"],["dc.contributor.author","Raimundo, Nuno"],["dc.contributor.author","Krisko, Anita"],["dc.date.accessioned","2018-11-07T10:12:38Z"],["dc.date.available","2018-11-07T10:12:38Z"],["dc.date.issued","2016"],["dc.description.abstract","In cells living under optimal conditions, protein folding defects are usually prevented by the action of chaperones. Here, we investigate the cell-wide consequences of loss of chaperone function in cytosol, mitochondria or the endoplasmic reticulum (ER) in budding yeast. We find that the decline in chaperone activity in each compartment results in loss of respiration, demonstrating the dependence of mitochondrial activity on cell-wide proteostasis. Furthermore, each chaperone deficiency triggers a response, presumably via the communication among the folding environments of distinct cellular compartments, termed here the cross-organelle stress response (CORE). The proposed CORE pathway encompasses activation of protein conformational maintenance machineries, antioxidant enzymes, and metabolic changes simultaneously in the cytosol, mitochondria, and the ER. CORE induction extends replicative and chronological lifespan in budding yeast, highlighting its protective role against moderate proteotoxicity and its consequences such as the decline in respiration. Our findings accentuate that organelles do not function in isolation, but are integrated in a functional crosstalk, while also highlighting the importance of organelle communication in aging and age-related diseases."],["dc.identifier.doi","10.1038/srep28751"],["dc.identifier.isi","000378491700002"],["dc.identifier.pmid","27346163"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13472"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40278"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","2045-2322"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Crosstalk between cellular compartments protects against proteotoxicity and extends lifespan"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]