Please use this identifier to cite or link to this item: https://doi.org/10.15480/882.1937
DC FieldValueLanguage
dc.contributor.authorSievert, Henning-
dc.contributor.authorVenz, Simone-
dc.contributor.authorPlatas Barradas, Oscar-
dc.contributor.authorDhople, Vishnu Mukund-
dc.contributor.authorSchaletzky, Martin-
dc.contributor.authorNagel, Claus-Henning-
dc.contributor.authorBraig, Melanie-
dc.contributor.authorPreukschas, Michael-
dc.contributor.authorPällmann, Nora-
dc.contributor.authorBokemeyer, Carsten-
dc.contributor.authorBrümmendorf, Tim H.-
dc.contributor.authorPörtner, Ralf-
dc.contributor.authorWalther, Reinhard-
dc.contributor.authorDuncan, Kent E.-
dc.contributor.authorHauber, Joachim-
dc.contributor.authorBalabanov, Stefan-
dc.date.accessioned2019-01-21T10:10:57Z-
dc.date.available2019-01-21T10:10:57Z-
dc.date.issued2012-08-10-
dc.identifier.citationMolecular & cellular proteomics : MCP 11 (11): 1289-1305 (2012)de_DE
dc.identifier.issn1535-9484de_DE
dc.identifier.urihttps://tubdok.tub.tuhh.de/handle/11420/1940-
dc.description.abstractHypusine modification of eukaryotic initiation factor 5A (eIF-5A) represents a unique and highly specific post-translational modification with regulatory functions in cancer, diabetes, and infectious diseases. However, the specific cellular pathways that are influenced by the hypusine modification remain largely unknown. To globally characterize eIF-5A and hypusine-dependent pathways, we used an approach that combines large-scale bioreactor cell culture with tandem affinity purification and mass spectrometry: "bioreactor-TAP-MS/MS." By applying this approach systematically to all four components of the hypusine modification system (eIF-5A1, eIF-5A2, DHS, and DOHH), we identified 248 interacting proteins as components of the cellular hypusine network, with diverse functions including regulation of translation, mRNA processing, DNA replication, and cell cycle regulation. Network analysis of this data set enabled us to provide a comprehensive overview of the protein-protein interaction landscape of the hypusine modification system. In addition, we validated the interaction of eIF-5A with some of the newly identified associated proteins in more detail. Our analysis has revealed numerous novel interactions, and thus provides a valuable resource for understanding how this crucial homeostatic signaling pathway affects different cellular functions.en
dc.language.isoende_DE
dc.publisherAmerican Society for Biochemistry and Molecular Biology, HighWire Pressde_DE
dc.relation.ispartofMolecular & cellular proteomicsde_DE
dc.rightsCC BY 4.0de_DE
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.subjectAnimalsde_DE
dc.subjectComputational Biologyde_DE
dc.subjectDNA-Binding Proteinsde_DE
dc.subjectHumansde_DE
dc.subjectLysinede_DE
dc.subjectMass Spectrometryde_DE
dc.subjectMicede_DE
dc.subjectMixed Function Oxygenasesde_DE
dc.subjectMultivesicular Bodiesde_DE
dc.subjectNIH 3T3 Cellsde_DE
dc.subjectNuclear Proteinsde_DE
dc.subjectOxidoreductases Acting on CH-NH Group Donorsde_DE
dc.subjectPeptide Fragmentsde_DE
dc.subjectPeptide Initiation Factorsde_DE
dc.subjectProtein Transportde_DE
dc.subjectRNA-Binding Proteinsde_DE
dc.subjectRecombinant Fusion Proteinsde_DE
dc.subjectReproducibility of Resultsde_DE
dc.subjectRibosomal Proteinsde_DE
dc.subjectSubcellular Fractionsde_DE
dc.subjectProtein Interaction Mapsde_DE
dc.subjectProtein Processing, Post-Translationalde_DE
dc.subject.ddc570: Biowissenschaften, Biologiede_DE
dc.subject.ddc610: Medizinde_DE
dc.titleProtein-protein-interaction network organization of the hypusine modification systemde_DE
dc.typeArticlede_DE
dc.identifier.urnurn:nbn:de:gbv:830-882.024994-
dc.identifier.doi10.15480/882.1937-
dc.type.diniarticle-
dc.subject.ddccode570-
dc.subject.ddccode610-
dcterms.DCMITypeText-
tuhh.identifier.urnurn:nbn:de:gbv:830-882.024994de_DE
tuhh.oai.showtruede_DE
dc.identifier.hdl11420/1940-
tuhh.abstract.englishHypusine modification of eukaryotic initiation factor 5A (eIF-5A) represents a unique and highly specific post-translational modification with regulatory functions in cancer, diabetes, and infectious diseases. However, the specific cellular pathways that are influenced by the hypusine modification remain largely unknown. To globally characterize eIF-5A and hypusine-dependent pathways, we used an approach that combines large-scale bioreactor cell culture with tandem affinity purification and mass spectrometry: "bioreactor-TAP-MS/MS." By applying this approach systematically to all four components of the hypusine modification system (eIF-5A1, eIF-5A2, DHS, and DOHH), we identified 248 interacting proteins as components of the cellular hypusine network, with diverse functions including regulation of translation, mRNA processing, DNA replication, and cell cycle regulation. Network analysis of this data set enabled us to provide a comprehensive overview of the protein-protein interaction landscape of the hypusine modification system. In addition, we validated the interaction of eIF-5A with some of the newly identified associated proteins in more detail. Our analysis has revealed numerous novel interactions, and thus provides a valuable resource for understanding how this crucial homeostatic signaling pathway affects different cellular functions.de_DE
tuhh.publisher.doi10.1074/mcp.M112.019059-
tuhh.publication.instituteBioprozess- und Biosystemtechnik V-1de_DE
tuhh.identifier.doi10.15480/882.1937-
tuhh.type.opus(wissenschaftlicher) Artikel-
tuhh.institute.germanBioprozess- und Biosystemtechnik V-1de
tuhh.institute.englishBioprozess- und Biosystemtechnik V-1de_DE
tuhh.gvk.hasppnfalse-
openaire.rightsinfo:eu-repo/semantics/openAccessde_DE
dc.type.driverarticle-
dc.rights.ccbyde_DE
dc.rights.ccversion4.0de_DE
dc.type.casraiJournal Article-
tuhh.container.issue11de_DE
tuhh.container.volume11de_DE
tuhh.container.startpage1289de_DE
tuhh.container.endpage1305de_DE
dc.rights.nationallicensefalsede_DE
item.fulltextWith Fulltext-
item.creatorGNDSievert, Henning-
item.creatorGNDVenz, Simone-
item.creatorGNDPlatas Barradas, Oscar-
item.creatorGNDDhople, Vishnu Mukund-
item.creatorGNDSchaletzky, Martin-
item.creatorGNDNagel, Claus-Henning-
item.creatorGNDBraig, Melanie-
item.creatorGNDPreukschas, Michael-
item.creatorGNDPällmann, Nora-
item.creatorGNDBokemeyer, Carsten-
item.creatorGNDBrümmendorf, Tim H.-
item.creatorGNDPörtner, Ralf-
item.creatorGNDWalther, Reinhard-
item.creatorGNDDuncan, Kent E.-
item.creatorGNDHauber, Joachim-
item.creatorGNDBalabanov, Stefan-
item.languageiso639-1en-
item.openairetypeArticle-
item.openairecristypehttp://purl.org/coar/resource_type/c_6501-
item.creatorOrcidSievert, Henning-
item.creatorOrcidVenz, Simone-
item.creatorOrcidPlatas Barradas, Oscar-
item.creatorOrcidDhople, Vishnu Mukund-
item.creatorOrcidSchaletzky, Martin-
item.creatorOrcidNagel, Claus-Henning-
item.creatorOrcidBraig, Melanie-
item.creatorOrcidPreukschas, Michael-
item.creatorOrcidPällmann, Nora-
item.creatorOrcidBokemeyer, Carsten-
item.creatorOrcidBrümmendorf, Tim H.-
item.creatorOrcidPörtner, Ralf-
item.creatorOrcidWalther, Reinhard-
item.creatorOrcidDuncan, Kent E.-
item.creatorOrcidHauber, Joachim-
item.creatorOrcidBalabanov, Stefan-
item.cerifentitytypePublications-
item.grantfulltextopen-
crisitem.author.deptBioprozess- und Biosystemtechnik V-1-
crisitem.author.deptBioprozess- und Biosystemtechnik V-1-
crisitem.author.deptBioprozess- und Biosystemtechnik V-1-
crisitem.author.orcid0000-0003-1163-9718-
crisitem.author.orcid0000-0003-4290-2670-
crisitem.author.orcid0000-0001-6219-9527-
crisitem.author.parentorgStudiendekanat Verfahrenstechnik-
crisitem.author.parentorgStudiendekanat Verfahrenstechnik-
crisitem.author.parentorgStudiendekanat Verfahrenstechnik-
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