Now showing 1 - 2 of 2
  • 2019Journal Article Research Paper
    [["dc.bibliographiccitation.firstpage","3333"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Nature Protocols"],["dc.bibliographiccitation.lastpage","3365"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Alevra, Mihai"],["dc.contributor.author","Mandad, Sunit"],["dc.contributor.author","Ischebeck, Till"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Rizzoli, Silvio O."],["dc.contributor.author","Fornasiero, Eugenio F."],["dc.date.accessioned","2020-12-10T18:10:05Z"],["dc.date.available","2020-12-10T18:10:05Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1038/s41596-019-0222-y"],["dc.identifier.pmid","31685960"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73844"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/110"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/80"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | A03: Dynamische Analyse der Remodellierung der extrazellulären Matrix (ECM) als Mechanismus der Synapsenorganisation und Plastizität"],["dc.relation.workinggroup","RG Rizzoli (Quantitative Synaptology in Space and Time)"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.title","A mass spectrometry workflow for measuring protein turnover rates in vivo"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]
    Details DOI PMID PMC
  • 2022Journal Article
    [["dc.bibliographiccitation.artnumber","eabn4437"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Science Advances"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Kluever, Verena"],["dc.contributor.author","Russo, Belisa"],["dc.contributor.author","Mandad, Sunit"],["dc.contributor.author","Kumar, Nisha Hemandhar"],["dc.contributor.author","Alevra, Mihai"],["dc.contributor.author","Ori, Alessandro"],["dc.contributor.author","Rizzoli, Silvio O."],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Schneider, Anja"],["dc.contributor.author","Fornasiero, Eugenio F."],["dc.date.accessioned","2022-06-01T09:39:33Z"],["dc.date.available","2022-06-01T09:39:33Z"],["dc.date.issued","2022"],["dc.description.abstract","Aging is a prominent risk factor for neurodegenerative disorders (NDDs); however, the molecular mechanisms rendering the aged brain particularly susceptible to neurodegeneration remain unclear. Here, we aim to determine the link between physiological aging and NDDs by exploring protein turnover using metabolic labeling and quantitative pulse-SILAC proteomics. By comparing protein lifetimes between physiologically aged and young adult mice, we found that in aged brains protein lifetimes are increased by ~20% and that aging affects distinct pathways linked to NDDs. Specifically, a set of neuroprotective proteins are longer-lived in aged brains, while some mitochondrial proteins linked to neurodegeneration are shorter-lived. Strikingly, we observed a previously unknown alteration in proteostasis that correlates to parsimonious turnover of proteins with high biosynthetic costs, revealing an overall metabolic adaptation that preludes neurodegeneration. Our findings suggest that future therapeutic paradigms, aimed at addressing these metabolic adaptations, might be able to delay NDD onset."],["dc.description.abstract","Physiological brain aging affects protein turnover, altering the stability of proteins linked to neurodegenerative diseases."],["dc.identifier.doi","10.1126/sciadv.abn4437"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/108506"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-572"],["dc.relation.eissn","2375-2548"],["dc.title","Protein lifetimes in aged brains reveal a proteostatic adaptation linking physiological aging to neurodegeneration"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]
    Details DOI