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https://hdl.handle.net/1959.11/57207
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DC Field | Value | Language |
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dc.contributor.author | Glover, Stephen A | en |
dc.date.accessioned | 2024-01-08T06:49:42Z | - |
dc.date.available | 2024-01-08T06:49:42Z | - |
dc.date.issued | 2023-01-19 | - |
dc.identifier.citation | Australian Journal of Chemistry, 76(1), p. 1-24 | en |
dc.identifier.issn | 1445-0038 | en |
dc.identifier.issn | 0004-9425 | en |
dc.identifier.uri | https://hdl.handle.net/1959.11/57207 | - |
dc.description.abstract | <p>This account describes the origins of our extensive investigations into the mutagenicity of N-acyloxy-N-alkoxyamides. Since their discovery as biologically active anomeric amides that mutate DNA in the Ames reverse mutation assay without the need for metabolic activation, we have used activities in the Ames test to understand the impact of structural variation on cellular access to, binding to and reactivity with DNA. We have developed an understanding of the roles played by hydrophobicity, electrophilic reactivity, steric effects and, importantly, intercalation on mutagenicity levels and therefore interactions with DNA. The evolution and application of meaningful quantitative structure–activity relationships is described, and examples of their utility in explaining molecule–DNA interactions are given. Their ability to explain previous mutagenicity data and, importantly, to predict meaningful mutagenic behaviour is also demonstrated.</p> | en |
dc.language | en | en |
dc.publisher | CSIRO Publishing | en |
dc.relation.ispartof | Australian Journal of Chemistry | en |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 International | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.title | Mutagenicity of N-acyloxy-N-alkoxyamides – QSAR determination of factors controlling activity | en |
dc.type | Journal Article | en |
dc.identifier.doi | 10.1071/CH22205 | en |
dcterms.accessRights | UNE Green | en |
local.contributor.firstname | Stephen A | en |
local.profile.school | School of Science and Technology | en |
local.profile.email | sglover@une.edu.au | en |
local.output.category | C1 | en |
local.record.place | au | en |
local.record.institution | University of New England | en |
local.publisher.place | Australia | en |
local.format.startpage | 1 | en |
local.format.endpage | 24 | en |
local.peerreviewed | Yes | en |
local.identifier.volume | 76 | en |
local.identifier.issue | 1 | en |
local.access.fulltext | Yes | en |
local.contributor.lastname | Glover | en |
dc.identifier.staff | une-id:sglover | en |
local.profile.orcid | 0000-0002-9344-8669 | en |
local.profile.role | author | en |
local.identifier.unepublicationid | une:1959.11/57207 | en |
dc.identifier.academiclevel | Academic | en |
local.title.maintitle | Mutagenicity of N-acyloxy-N-alkoxyamides – QSAR determination of factors controlling activity | en |
local.output.categorydescription | C1 Refereed Article in a Scholarly Journal | en |
local.search.author | Glover, Stephen A | en |
local.open.fileurl | https://rune.une.edu.au/web/retrieve/e16bb113-8349-43c7-9516-672d36a592a9 | en |
local.uneassociation | Yes | en |
local.atsiresearch | No | en |
local.sensitive.cultural | No | en |
local.year.published | 2023 | en |
local.fileurl.open | https://rune.une.edu.au/web/retrieve/e16bb113-8349-43c7-9516-672d36a592a9 | en |
local.fileurl.openpublished | https://rune.une.edu.au/web/retrieve/e16bb113-8349-43c7-9516-672d36a592a9 | en |
local.subject.for2020 | 340402 Biomolecular modelling and design | en |
local.subject.for2020 | 340401 Biologically active molecules | en |
local.subject.for2020 | 340701 Computational chemistry | en |
local.subject.seo2020 | 280105 Expanding knowledge in the chemical sciences | en |
local.subject.seo2020 | 280102 Expanding knowledge in the biological sciences | en |
local.profile.affiliationtype | UNE Affiliation | en |
Appears in Collections: | Journal Article School of Science and Technology |
Files in This Item:
File | Description | Size | Format | |
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openpublished/MutagenicityGlover2023JournalArticle.pdf | Published version | 2.09 MB | Adobe PDF Download Adobe | View/Open |
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