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Proteomics of nucleocytoplasmic partitioning

Author(s): Nguyen, Thao; Pappireddi, Nishant; Wühr, Martin

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dc.contributor.authorNguyen, Thao-
dc.contributor.authorPappireddi, Nishant-
dc.contributor.authorWühr, Martin-
dc.date.accessioned2023-12-14T19:08:03Z-
dc.date.available2023-12-14T19:08:03Z-
dc.date.issued2019-02en_US
dc.identifier.citationNguyen, Thao, Pappireddi, Nishant, Wühr, Martin. (2019). Proteomics of nucleocytoplasmic partitioning. Current opinion in chemical biology, 48 (55 - 63). doi:10.1016/j.cbpa.2018.10.027en_US
dc.identifier.issn1367-5931-
dc.identifier.urihttp://arks.princeton.edu/ark:/88435/pr1sb3wz5f-
dc.description.abstractThe partitioning of the proteome between nucleus and cytoplasm affects nearly every aspect of eukaryotic biology. Despite this central role, we still have a poor understanding of which proteins localize in the nucleus and how this varies in different cell types and conditions. Recent advances in quantitative proteomics and high-throughput imaging are starting to close this knowledge gap. Studies on protein interaction are beginning to reveal the spectrum of cargos of nuclear import and export receptors. We anticipate that it will soon be possible to predict each protein's nucleocytoplasmic localization based on its importin/exportin interactions and its estimated diffusion rate through the nuclear pore. This insight is likely to provide us with a fundamental understanding of how cells use nucleocytoplasmic partitioning to encode and relay information.en_US
dc.format.extent55 - 63en_US
dc.languageengen_US
dc.language.isoen_USen_US
dc.relation.ispartofCurrent Opinion in Chemical Biologyen_US
dc.rightsAuthor's manuscripten_US
dc.titleProteomics of nucleocytoplasmic partitioningen_US
dc.typeJournal Articleen_US
dc.identifier.doidoi:10.1016/j.cbpa.2018.10.027-
dc.identifier.eissn1879-0402-
pu.type.symplectichttp://www.symplectic.co.uk/publications/atom-terms/1.0/journal-articleen_US

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