Show simple item record

dc.contributor.authorPettinger, J
dc.contributor.authorJones, K
dc.contributor.authorCheeseman, MD
dc.date.accessioned2017-08-30T10:53:10Z
dc.date.issued2017-11-27
dc.identifier.citationAngewandte Chemie (International ed. in English), 2017, 56 (48), pp. 15200 - 15209
dc.identifier.issn1433-7851
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/800
dc.identifier.eissn1521-3773
dc.identifier.doi10.1002/anie.201707630
dc.description.abstractTargeted covalent inhibitors have gained widespread attention in drug discovery as a validated method to circumvent acquired resistance in oncology. This strategy exploits small-molecule/protein crystal structures to design tightly binding ligands with appropriately positioned electrophilic warheads. Whilst most focus has been on targeting binding-site cysteine residues, targeting nucleophilic lysine residues can also represent a viable approach to irreversible inhibition. However, owing to the basicity of the ϵ-amino group in lysine, this strategy generates a number of specific challenges. Herein, we review the key principles for inhibitor design, give historical examples, and present recent developments that demonstrate the potential of lysine targeting for future drug discovery.
dc.formatPrint-Electronic
dc.format.extent15200 - 15209
dc.languageeng
dc.language.isoeng
dc.publisherWILEY-V C H VERLAG GMBH
dc.rights.urihttps://www.rioxx.net/licenses/all-rights-reserved
dc.titleLysine-Targeting Covalent Inhibitors.
dc.typeJournal Article
dcterms.dateAccepted2017-08-29
rioxxterms.funderThe Institute of Cancer Research
rioxxterms.identifier.projectUnspecified
rioxxterms.versionofrecord10.1002/anie.201707630
rioxxterms.licenseref.urihttps://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.licenseref.startdate2017-11
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfAngewandte Chemie (International ed. in English)
pubs.issue48
pubs.notesIndefinite
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/Medicinal Chemistry 3
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/Medicinal Chemistry 3
pubs.publication-statusPublished
pubs.volume56
pubs.embargo.termsIndefinite
icr.researchteamMedicinal Chemistry 3
dc.contributor.icrauthorPettinger, Jonathan
dc.contributor.icrauthorJones, Keith
dc.contributor.icrauthorCheeseman, Matthew


Files in this item

Thumbnail

This item appears in the following collection(s)

Show simple item record