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foxo3  (Addgene inc)


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    Structured Review

    Addgene inc foxo3
    Foxo3, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/flag+foxo3/FLAG-FOXO3a+TM+(Plasmid+%238361)/pm41920736-552-17-19
    Average 93 stars, based on 14 article reviews
    foxo3 - by Bioz Stars, 2026-09
    93/100 stars

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    a. Structure of the FOXO4 DBD–DNA complex. The FOXO-DBD is shown in blue ribbon (upper) and the DNA double helix is shown as orange and green ( lower ) ( https://www.rcsb.org/structure/3L2C ). b. Structure of ActD. c. The result of a luciferase reporter assay shows that ActD inhibited FOXO4 activity. d. The result of a luciferase reporter assay shows that ActD did not inhibit <t>FOXO3</t> activity. e & f. The results of computational protein-ligand docking advocated helix H3 as the major site of inhibition. g. SwissDock-based AutoDock Vina execution exhibited active residues Arg78, His79 and Ser82 interacting with ActD. h. AlphaFold3-based Protenix predicted similar heavy atom contacts with ligand to H2 (Leu47), H3 (Asn75, Arg78, His79, Ser82 and Leu83) and S3 (Lys89) domains of FOXO4. All numerical data are shown as mean ± SD. N = 3, *p <0.05, ns, no significant difference.
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    a. Structure of the FOXO4 DBD–DNA complex. The FOXO-DBD is shown in blue ribbon (upper) and the DNA double helix is shown as orange and green ( lower ) ( https://www.rcsb.org/structure/3L2C ). b. Structure of ActD. c. The result of a luciferase reporter assay shows that ActD inhibited FOXO4 activity. d. The result of a luciferase reporter assay shows that ActD did not inhibit <t>FOXO3</t> activity. e & f. The results of computational protein-ligand docking advocated helix H3 as the major site of inhibition. g. SwissDock-based AutoDock Vina execution exhibited active residues Arg78, His79 and Ser82 interacting with ActD. h. AlphaFold3-based Protenix predicted similar heavy atom contacts with ligand to H2 (Leu47), H3 (Asn75, Arg78, His79, Ser82 and Leu83) and S3 (Lys89) domains of FOXO4. All numerical data are shown as mean ± SD. N = 3, *p <0.05, ns, no significant difference.
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    Image Search Results


    a. Structure of the FOXO4 DBD–DNA complex. The FOXO-DBD is shown in blue ribbon (upper) and the DNA double helix is shown as orange and green ( lower ) ( https://www.rcsb.org/structure/3L2C ). b. Structure of ActD. c. The result of a luciferase reporter assay shows that ActD inhibited FOXO4 activity. d. The result of a luciferase reporter assay shows that ActD did not inhibit FOXO3 activity. e & f. The results of computational protein-ligand docking advocated helix H3 as the major site of inhibition. g. SwissDock-based AutoDock Vina execution exhibited active residues Arg78, His79 and Ser82 interacting with ActD. h. AlphaFold3-based Protenix predicted similar heavy atom contacts with ligand to H2 (Leu47), H3 (Asn75, Arg78, His79, Ser82 and Leu83) and S3 (Lys89) domains of FOXO4. All numerical data are shown as mean ± SD. N = 3, *p <0.05, ns, no significant difference.

    Journal: bioRxiv

    Article Title: Validating FOXO4 as a therapeutic target for protecting against ischemia-reperfusion-caused neuronal injury

    doi: 10.1101/2025.03.13.643180

    Figure Lengend Snippet: a. Structure of the FOXO4 DBD–DNA complex. The FOXO-DBD is shown in blue ribbon (upper) and the DNA double helix is shown as orange and green ( lower ) ( https://www.rcsb.org/structure/3L2C ). b. Structure of ActD. c. The result of a luciferase reporter assay shows that ActD inhibited FOXO4 activity. d. The result of a luciferase reporter assay shows that ActD did not inhibit FOXO3 activity. e & f. The results of computational protein-ligand docking advocated helix H3 as the major site of inhibition. g. SwissDock-based AutoDock Vina execution exhibited active residues Arg78, His79 and Ser82 interacting with ActD. h. AlphaFold3-based Protenix predicted similar heavy atom contacts with ligand to H2 (Leu47), H3 (Asn75, Arg78, His79, Ser82 and Leu83) and S3 (Lys89) domains of FOXO4. All numerical data are shown as mean ± SD. N = 3, *p <0.05, ns, no significant difference.

    Article Snippet: Moreover, to eliminate the compounds that also showed inhibitory effect on FOXO1 and FOXO3, we performed additional reporter assays with HEK293 cells co-transfected with the 3XIRS luciferase (Luc) reporter that contains 3 copies of the insulin-responsive sequence or FHRE-Luc together with FOXO3 plasmid (Addgene #8360) .

    Techniques: Luciferase, Reporter Assay, Activity Assay, Inhibition