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dc.contributor.author
Varjosalo, Markku
dc.contributor.author
Keskitalo, Salla
dc.contributor.author
van Drogen, Audrey
dc.contributor.author
Nurkkala, Helka
dc.contributor.author
Vichalkovski, Anton
dc.contributor.author
Aebersold, Ruedi
dc.contributor.author
Gstaiger, Matthias
dc.date.accessioned
2018-09-25T14:37:33Z
dc.date.available
2017-06-10T20:07:10Z
dc.date.available
2018-09-25T14:37:33Z
dc.date.issued
2013-04
dc.identifier.other
10.1016/j.celrep.2013.03.027
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/70524
dc.identifier.doi
10.3929/ethz-b-000070524
dc.description.abstract
Cellular information processing via reversible protein phosphorylation requires tight control of the localization, activity, and substrate specificity of protein kinases, which to a large extent is accomplished by complex formation with other proteins. Despite their critical role in cellular regulation and pathogenesis, protein interaction information is available for only a subset of the 518 human protein kinases. Here we present a global proteomic analysis of complexes of the human CMGC kinase group. In addition to subgroup-specific functional enrichment and modularity, the identified 652 high-confidence kinase-protein interactions provide a specific biochemical context for many poorly studied CMGC kinases. Furthermore, the analysis revealed a kinase-kinase subnetwork and candidate substrates for CMGC kinases. Finally, the presented interaction proteome uncovered a large set of interactions with proteins genetically linked to a range of human diseases, including cancer, suggesting additional routes for analyzing the role of CMGC kinases in controlling human disease pathways.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
Elsevier
en_US
dc.rights.uri
http://creativecommons.org/licenses/by-nc-nd/3.0/
dc.title
The Protein Interaction Landscape of the Human CMGC Kinase Group
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution-NonCommercial-NoDerivs 3.0 Unported
dc.date.published
2013-04-18
ethz.journal.title
Cell Reports
ethz.journal.volume
3
en_US
ethz.journal.issue
4
en_US
ethz.pages.start
1306
en_US
ethz.pages.end
1320
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.nebis
007612702
ethz.publication.place
New York, NY
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::02538 - Institut für Molekulare Systembiologie / Institute for Molecular Systems Biology::03663 - Aebersold, Rudolf / Aebersold, Rudolf
en_US
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02538 - Institut für Molekulare Systembiologie / Institute for Molecular Systems Biology::03663 - Aebersold, Rudolf / Aebersold, Rudolf
ethz.date.deposited
2017-06-10T20:07:49Z
ethz.source
ECIT
ethz.identifier.importid
imp593650e2a0df626017
ethz.ecitpid
pub:111669
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2017-07-19T08:03:05Z
ethz.rosetta.lastUpdated
2018-09-25T14:37:40Z
ethz.rosetta.versionExported
true
ethz.COinS
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