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dc.contributor.authorCanning, P
dc.contributor.authorBataille, C
dc.contributor.authorBery, N
dc.contributor.authorMilhas, S
dc.contributor.authorHayes, A
dc.contributor.authorRaynaud, F
dc.contributor.authorMiller, A
dc.contributor.authorRabbitts, T
dc.date.accessioned2021-05-19T13:55:56Z
dc.date.available2021-05-19T13:55:56Z
dc.date.issued2021-03-29
dc.identifier.citationJournal of immunological methods, 2021, 494 pp. 113051 - ?
dc.identifier.issn0022-1759
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/4560
dc.identifier.eissn1872-7905
dc.identifier.doi10.1016/j.jim.2021.113051
dc.description.abstractThe use of intracellular antibodies as templates to derive surrogate compounds is an important objective because intracellular antibodies can be employed initially for target validation in pre-clinical assays and subsequently employed in compound library screens. LMO2 is a T cell oncogenic protein activated in the majority of T cell acute leukaemias. We have used an inhibitory intracellular antibody fragment as a competitor in a small molecule library screen using competitive surface plasmon resonance (cSPR) to identify compounds that bind to LMO2. We selected four compounds that bind to LMO2 but not when the anti-LMO2 intracellular antibody fragment is bound to it. These findings further illustrate the value of intracellular antibodies in the initial stages of drug discovery campaigns and more generally antibodies, or antibody fragments, can be the starting point for chemical compound development as surrogates of the antibody combining site.
dc.formatPrint-Electronic
dc.format.extent113051 - ?
dc.languageeng
dc.language.isoeng
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.titleCompetitive SPR using an intracellular anti-LMO2 antibody identifies novel LMO2-interacting compounds.
dc.typeJournal Article
dcterms.dateAccepted2021-03-26
rioxxterms.versionVoR
rioxxterms.versionofrecord10.1016/j.jim.2021.113051
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by/4.0
rioxxterms.licenseref.startdate2021-03-29
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfJournal of immunological methods
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/Primary Group/ICR Divisions/Cancer Therapeutics/Clinical Pharmacology & Trials (including Drug Metabolism & Pharmacokinetics Group)
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/Primary Group/ICR Divisions/Cancer Therapeutics/Clinical Pharmacology & Trials (including Drug Metabolism & Pharmacokinetics Group)
pubs.publication-statusPublished
pubs.volume494
pubs.embargo.termsNot known
icr.researchteamChromosomal Translocations and Intracellular Antibody Therapeutics
icr.researchteamClinical Pharmacology & Trials (including Drug Metabolism & Pharmacokinetics Group)
icr.researchteamChromosomal Translocations and Intracellular Antibody Therapeuticsen_US
icr.researchteamClinical Pharmacology & Trials (including Drug Metabolism & Pharmacokinetics Group)en_US
dc.contributor.icrauthorRaynaud, Florenceen
dc.contributor.icrauthorRabbitts, Terenceen


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