{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["24(1)"],"submitter":["Maslyk M"],"pubmed_abstract":["Small molecules containing quinone and/or oxime moieties have been found as promising anti-fungal agents. One of them is 4-AN, a recently reported potent anti-Candida compound, which inhibits the formation of hyphae, decreases the level of cellular phosphoproteome, and finally shows no toxicity towards human erythrocytes and zebrafish embryos. Here, further research on 4-AN is presented. The results revealed that the compound: (i) Kills Candida clinical isolates, including these with developed antibiotic resistance, (ii) affects mature biofilm, and (iii) moderately disrupts membrane permeability. Atomic force microscopy studies revealed a slight influence of 4-AN on the cell surface architecture. 4-AN was also shown to inhibit multiple various protein kinases, a characteristic shared by most of the ATP-competitive inhibitors. The presented compound can be used in novel strategies in the fight against candidiasis, and reversible protein phosphorylation should be taken into consideration as a target in designing these strategies."],"journal":["Molecules (Basel, Switzerland)"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6337409"],"repository":["biostudies-literature"],"pubmed_title":["The Anti-Candida albicans Agent 4-AN Inhibits Multiple Protein Kinases."],"pmcid":["PMC6337409"],"pubmed_authors":["Maslyk M","Bach S","Demchuk OM","Tokarska-Rodak M","Kubinski K","Chwedczuk M","Ruchaud S","Czernik S","Martyna A","Foll-Josselin B","Janeczko M"],"additional_accession":[]},"is_claimable":false,"name":"The Anti-Candida albicans Agent 4-AN Inhibits Multiple Protein Kinases.","description":"Small molecules containing quinone and/or oxime moieties have been found as promising anti-fungal agents. One of them is 4-AN, a recently reported potent anti-Candida compound, which inhibits the formation of hyphae, decreases the level of cellular phosphoproteome, and finally shows no toxicity towards human erythrocytes and zebrafish embryos. Here, further research on 4-AN is presented. The results revealed that the compound: (i) Kills Candida clinical isolates, including these with developed antibiotic resistance, (ii) affects mature biofilm, and (iii) moderately disrupts membrane permeability. Atomic force microscopy studies revealed a slight influence of 4-AN on the cell surface architecture. 4-AN was also shown to inhibit multiple various protein kinases, a characteristic shared by most of the ATP-competitive inhibitors. The presented compound can be used in novel strategies in the fight against candidiasis, and reversible protein phosphorylation should be taken into consideration as a target in designing these strategies.","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Jan","modification":"2020-11-19T14:35:39Z","creation":"2019-03-26T22:40:59Z"},"accession":"S-EPMC6337409","cross_references":{"pubmed":["30609757"],"doi":["10.3390/molecules24010153"]}}