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dc.contributor.authorLiu, M
dc.contributor.authorMallinger, A
dc.contributor.authorTortorici, M
dc.contributor.authorNewbatt, Y
dc.contributor.authorRichards, M
dc.contributor.authorMirza, A
dc.contributor.authorvan Montfort, RLM
dc.contributor.authorBurke, R
dc.contributor.authorBlagg, J
dc.contributor.authorKaserer, T
dc.date.accessioned2018-09-17T09:17:21Z
dc.date.issued2018-09-21
dc.identifier.citationACS chemical biology, 2018, 13 (9), pp. 2427 - 2432
dc.identifier.issn1554-8929
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/2695
dc.identifier.eissn1554-8937
dc.identifier.doi10.1021/acschembio.8b00639
dc.description.abstractAPOBEC3B (A3B) deamination activity on ssDNA is considered a contributing factor to tumor heterogeneity and drug resistance in a number of human cancers. Despite its clinical impact, little is known about A3B ssDNA substrate preference. We have used nuclear magnetic resonance to monitor the catalytic turnover of A3B substrates in real-time. This study reports preferred nucleotide sequences for A3B substrates, including optimized 4-mer oligonucleotides, and reveals a breadth of substrate recognition that includes DNA sequences known to be mutated in drug-resistant cancer clones. Our results are consistent with available clinical and structural data and may inform the design of substrate-based A3B inhibitors.
dc.formatPrint-Electronic
dc.format.extent2427 - 2432
dc.languageeng
dc.language.isoeng
dc.publisherAMER CHEMICAL SOC
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.subjectHumans
dc.subjectCytidine Deaminase
dc.subjectNucleotides
dc.subjectDNA, Single-Stranded
dc.subjectMinor Histocompatibility Antigens
dc.subjectNuclear Magnetic Resonance, Biomolecular
dc.subjectSubstrate Specificity
dc.subjectModels, Molecular
dc.titleEvaluation of APOBEC3B Recognition Motifs by NMR Reveals Preferred Substrates.
dc.typeJournal Article
rioxxterms.versionofrecord10.1021/acschembio.8b00639
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by/4.0
rioxxterms.licenseref.startdate2018-09
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfACS chemical biology
pubs.issue9
pubs.notesNo embargo
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/Hit Discovery & Structural Design
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology/Hit Discovery & Structural Design
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/Hit Discovery & Structural Design
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology/Hit Discovery & Structural Design
pubs.publication-statusPublished
pubs.volume13
pubs.embargo.termsNo embargo
pubs.oa-locationhttps://pubs.acs.org/doi/full/10.1021/acschembio.8b00639
icr.researchteamHit Discovery & Structural Design
dc.contributor.icrauthorVan Montfort, Robert
dc.contributor.icrauthorBurke, Rosemary


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