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dc.contributor.authorBery, N
dc.contributor.authorCruz-Migoni, A
dc.contributor.authorBataille, CJ
dc.contributor.authorQuevedo, CE
dc.contributor.authorTulmin, H
dc.contributor.authorMiller, A
dc.contributor.authorRussell, A
dc.contributor.authorPhillips, SE
dc.contributor.authorCarr, SB
dc.contributor.authorRabbitts, TH
dc.date.accessioned2020-12-21T14:04:37Z
dc.date.issued2018-07-10
dc.identifier.citationeLife, 2018, 7
dc.identifier.issn2050-084X
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/4260
dc.identifier.eissn2050-084X
dc.identifier.doi10.7554/elife.37122
dc.description.abstractThe RAS family of proteins is amongst the most highly mutated in human cancers and has so far eluded drug therapy. Currently, much effort is being made to discover mutant RAS inhibitors and in vitro screening for RAS-binding drugs must be followed by cell-based assays. Here, we have developed a robust set of bioluminescence resonance energy transfer (BRET)-based RAS biosensors that enable monitoring of RAS-effector interaction inhibition in living cells. These include KRAS, HRAS and NRAS and a variety of different mutations that mirror those found in human cancers with the major RAS effectors such as CRAF, PI3K and RALGDS. We highlighted the utility of these RAS biosensors by showing a RAS-binding compound is a potent pan-RAS-effector interactions inhibitor in cells. The RAS biosensors represent a useful tool to investigate and characterize the potency of anti-RAS inhibitors in cells and more generally any RAS protein-protein interaction (PPI) in cells.
dc.formatElectronic
dc.languageeng
dc.language.isoeng
dc.publisherELIFE SCIENCES PUBLICATIONS LTD
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.subjectHumans
dc.subjectBiosensing Techniques
dc.subjectSignal Transduction
dc.subjectEnergy Transfer
dc.subjectProtein Binding
dc.subjectMutation
dc.subjectProto-Oncogene Proteins p21(ras)
dc.subjectProtein Interaction Domains and Motifs
dc.subjectSmall Molecule Libraries
dc.subjectHEK293 Cells
dc.subjectBioluminescence Resonance Energy Transfer Techniques
dc.titleBRET-based RAS biosensors that show a novel small molecule is an inhibitor of RAS-effector protein-protein interactions.
dc.typeJournal Article
dcterms.dateAccepted2018-06-16
rioxxterms.versionofrecord10.7554/elife.37122
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by/4.0
rioxxterms.licenseref.startdate2018-07-10
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfeLife
pubs.notesNot known
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Cancer Therapeutics
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Cancer Therapeutics/Chromosomal Translocations and Intracellular Antibody Therapeutics
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Cancer Therapeutics
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Cancer Therapeutics/Chromosomal Translocations and Intracellular Antibody Therapeutics
pubs.publication-statusPublished
pubs.volume7
pubs.embargo.termsNot known
icr.researchteamChromosomal Translocations and Intracellular Antibody Therapeutics
dc.contributor.icrauthorRabbitts, Terence


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