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dc.contributor.author
Heusel, Moritz
dc.contributor.author
Frank, Max
dc.contributor.author
Köhler, Mario
dc.contributor.author
Amon, Sabine
dc.contributor.author
Frommelt, Fabian
dc.contributor.author
Rosenberger, George
dc.contributor.author
Bludau, Isabell
dc.contributor.author
Aulakh, Simran
dc.contributor.author
Linder, Monika I.
dc.contributor.author
Liu, Yansheng
dc.contributor.author
Collins, Ben C.
dc.contributor.author
Gstaiger, Matthias
dc.contributor.author
Kutay, Ulrike
dc.contributor.author
Aebersold, Ruedi
dc.date.accessioned
2020-03-12T12:11:40Z
dc.date.available
2020-03-12T02:37:50Z
dc.date.available
2020-03-12T12:11:40Z
dc.date.issued
2020-02-26
dc.identifier.other
10.1016/j.cels.2020.01.001
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/404471
dc.identifier.doi
10.3929/ethz-b-000404471
dc.description.abstract
Living systems integrate biochemical reactions that determine the functional state of each cell. Reactions are primarily mediated by proteins. In proteomic studies, these have been treated as independent entities, disregarding their higher-level organization into complexes that affects their activity and/or function and is thus of great interest for biological research. Here, we describe the implementation of an integrated technique to quantify cell-state-specific changes in the physical arrangement of protein complexes concurrently for thousands of proteins and hundreds of complexes. Applying this technique to a comparison of human cells in interphase and mitosis, we provide a systematic overview of mitotic proteome reorganization. The results recall key hallmarks of mitotic complex remodeling and suggest a model of nuclear pore complex disassembly, which we validate by orthogonal methods. To support the interpretation of quantitative SEC-SWATH-MS datasets, we extend the software CCprofiler and provide an interactive exploration tool, SECexplorer-cc.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
Cell Press
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.title
A Global Screen for Assembly State Changes of the Mitotic Proteome by SEC-SWATH-MS
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
dc.date.published
2020-02-05
ethz.journal.title
Cell Systems
ethz.journal.volume
10
en_US
ethz.journal.issue
2
en_US
ethz.pages.start
133
en_US
ethz.pages.end
155.e6
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
Cambridge, MA
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02517 - Institut für Biochemie / Institute of Biochemistry (IBC)::03543 - Kutay, Ulrike / Kutay, Ulrike
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02517 - Institut für Biochemie / Institute of Biochemistry (IBC)::03543 - Kutay, Ulrike / Kutay, Ulrike
ethz.date.deposited
2020-03-12T02:37:59Z
ethz.source
SCOPUS
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2020-03-12T12:11:52Z
ethz.rosetta.lastUpdated
2020-03-12T12:11:52Z
ethz.rosetta.exportRequired
true
ethz.rosetta.versionExported
true
ethz.COinS
ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.atitle=A%20Global%20Screen%20for%20Assembly%20State%20Changes%20of%20the%20Mitotic%20Proteome%20by%20SEC-SWATH-MS&rft.jtitle=Cell%20Systems&rft.date=2020-02-26&rft.volume=10&rft.issue=2&rft.spage=133&rft.epage=155.e6&rft.au=Heusel,%20Moritz&Frank,%20Max&K%C3%B6hler,%20Mario&Amon,%20Sabine&Frommelt,%20Fabian&rft.genre=article&
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