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The discovery of penta-peptides inhibiting the activity of the formylglycine-generating enzyme and their potential antibacterial effects against Mycobacterium tuberculosis

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dc.contributor.authorAsiimwe, Nicholas-
dc.contributor.authorAl Mazid, Mohammad Faysal-
dc.contributor.authorJeong, Yong Taek-
dc.contributor.authorLee, Juyong-
dc.contributor.authorLee, Jun-Seok-
dc.date.accessioned2022-08-10T23:40:56Z-
dc.date.available2022-08-10T23:40:56Z-
dc.date.created2022-08-10-
dc.date.issued2022-06-22-
dc.identifier.issn2046-2069-
dc.identifier.urihttps://scholar.korea.ac.kr/handle/2021.sw.korea/142793-
dc.description.abstractThe formylglycine-generating enzyme is a key regulator that converts sulfatase into an active form. Despite its key role in many diseases, enzyme activity inhibitors have not yet been reported. In this study, we investigated penta-peptide ligands for FGE activity inhibition and discovered two hit peptides. In addition, the lead peptides also showed potential antibacterial effects in a Mycobacterium tuberculosis model.-
dc.languageEnglish-
dc.language.isoen-
dc.publisherROYAL SOC CHEMISTRY-
dc.subjectMOUSE MODEL-
dc.subjectSULFATASES-
dc.subjectINTERFACE-
dc.titleThe discovery of penta-peptides inhibiting the activity of the formylglycine-generating enzyme and their potential antibacterial effects against Mycobacterium tuberculosis-
dc.typeArticle-
dc.contributor.affiliatedAuthorJeong, Yong Taek-
dc.contributor.affiliatedAuthorLee, Jun-Seok-
dc.identifier.doi10.1039/d2ra03379h-
dc.identifier.scopusid2-s2.0-85134341828-
dc.identifier.wosid000818027200001-
dc.identifier.bibliographicCitationRSC ADVANCES, v.12, no.29, pp.18884 - 18888-
dc.relation.isPartOfRSC ADVANCES-
dc.citation.titleRSC ADVANCES-
dc.citation.volume12-
dc.citation.number29-
dc.citation.startPage18884-
dc.citation.endPage18888-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.isOpenAccessY-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaChemistry-
dc.relation.journalWebOfScienceCategoryChemistry, Multidisciplinary-
dc.subject.keywordPlusMOUSE MODEL-
dc.subject.keywordPlusSULFATASES-
dc.subject.keywordPlusINTERFACE-
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