Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/90305
Full metadata record
DC FieldValueLanguage
dc.contributor.authorDai, Lingyunen
dc.contributor.authorZhao, Tianyunen
dc.contributor.authorBisteau, Xavieren
dc.contributor.authorSun, Wendien
dc.contributor.authorPrabhu, Nayanaen
dc.contributor.authorLim, Yan Tingen
dc.contributor.authorSobota, Radoslaw M.en
dc.contributor.authorKaldis, Philippen
dc.contributor.authorNordlund, Pären
dc.date.accessioned2019-05-30T04:21:17Zen
dc.date.accessioned2019-12-06T17:45:19Z-
dc.date.available2019-05-30T04:21:17Zen
dc.date.available2019-12-06T17:45:19Z-
dc.date.issued2018en
dc.identifier.citationDai, L., Zhao, T., Bisteau, X., Sun, W., Prabhu, N., Lim, Y. T., . . . Nordlund, P. (2018). Modulation of Protein-Interaction States through the Cell Cycle. Cell, 173(6), 1481-1494. doi:10.1016/j.cell.2018.03.065en
dc.identifier.issn0092-8674en
dc.identifier.urihttps://hdl.handle.net/10356/90305-
dc.identifier.urihttp://hdl.handle.net/10220/48485en
dc.description.abstractGlobal profiling of protein expression through the cell cycle has revealed subsets of periodically expressed proteins. However, expression levels alone only give a partial view of the biochemical processes determining cellular events. Using a proteome-wide implementation of the cellular thermal shift assay (CETSA) to study specific cell-cycle phases, we uncover changes of interaction states for more than 750 proteins during the cell cycle. Notably, many protein complexes are modulated in specific cell-cycle phases, reflecting their roles in processes such as DNA replication, chromatin remodeling, transcription, translation, and disintegration of the nuclear envelope. Surprisingly, only small differences in the interaction states were seen between the G1 and the G2 phase, suggesting similar hardwiring of biochemical processes in these two phases. The present work reveals novel molecular details of the cell cycle and establishes proteome-wide CETSA as a new strategy to study modulation of protein-interaction states in intact cells.en
dc.description.sponsorshipASTAR (Agency for Sci., Tech. and Research, S’pore)en
dc.description.sponsorshipMOH (Min. of Health, S’pore)en
dc.format.extent61 p.en
dc.language.isoenen
dc.relation.ispartofseriesCellen
dc.rights© 2018 Elsevier Inc. All rights reserved. This paper was published in Cell and is made available with permission of Elsevier Inc.en
dc.subjectDRNTU::Science::Biological sciencesen
dc.subjectCellular Thermal Shift Assayen
dc.subjectCell Cycleen
dc.titleModulation of protein-interaction states through the cell cycleen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen
dc.identifier.doihttp://dx.doi.org/10.1016/j.cell.2018.03.065en
dc.description.versionAccepted versionen
item.grantfulltextopen-
item.fulltextWith Fulltext-
Appears in Collections:SBS Journal Articles
Files in This Item:
File Description SizeFormat 
Modulation of Protein-Interaction States through the Cell Cycle.pdf6.01 MBAdobe PDFThumbnail
View/Open

Google ScholarTM

Check

Altmetric

Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.