dc.contributor.author | Liu, M | |
dc.contributor.author | Mallinger, A | |
dc.contributor.author | Tortorici, M | |
dc.contributor.author | Newbatt, Y | |
dc.contributor.author | Richards, M | |
dc.contributor.author | Mirza, A | |
dc.contributor.author | van Montfort, RLM | |
dc.contributor.author | Burke, R | |
dc.contributor.author | Blagg, J | |
dc.contributor.author | Kaserer, T | |
dc.date.accessioned | 2018-09-17T09:17:21Z | |
dc.date.issued | 2018-09-21 | |
dc.identifier.citation | ACS chemical biology, 2018, 13 (9), pp. 2427 - 2432 | |
dc.identifier.issn | 1554-8929 | |
dc.identifier.uri | https://repository.icr.ac.uk/handle/internal/2695 | |
dc.identifier.eissn | 1554-8937 | |
dc.identifier.doi | 10.1021/acschembio.8b00639 | |
dc.description.abstract | APOBEC3B (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.format | Print-Electronic | |
dc.format.extent | 2427 - 2432 | |
dc.language | eng | |
dc.language.iso | eng | |
dc.publisher | AMER CHEMICAL SOC | |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0 | |
dc.subject | Humans | |
dc.subject | Cytidine Deaminase | |
dc.subject | Nucleotides | |
dc.subject | DNA, Single-Stranded | |
dc.subject | Minor Histocompatibility Antigens | |
dc.subject | Nuclear Magnetic Resonance, Biomolecular | |
dc.subject | Substrate Specificity | |
dc.subject | Models, Molecular | |
dc.title | Evaluation of APOBEC3B Recognition Motifs by NMR Reveals Preferred Substrates. | |
dc.type | Journal Article | |
rioxxterms.versionofrecord | 10.1021/acschembio.8b00639 | |
rioxxterms.licenseref.uri | https://creativecommons.org/licenses/by/4.0 | |
rioxxterms.licenseref.startdate | 2018-09 | |
rioxxterms.type | Journal Article/Review | |
dc.relation.isPartOf | ACS chemical biology | |
pubs.issue | 9 | |
pubs.notes | No 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-status | Published | |
pubs.volume | 13 | |
pubs.embargo.terms | No embargo | |
pubs.oa-location | https://pubs.acs.org/doi/full/10.1021/acschembio.8b00639 | |
icr.researchteam | Hit Discovery & Structural Design | |
dc.contributor.icrauthor | Van Montfort, Robert | |
dc.contributor.icrauthor | Burke, Rosemary | |