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MedChemExpress
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Santa Cruz Biotechnology
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Selleck Chemicals
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Biomol GmbH
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Enzo Biochem
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NanoCarrier Co
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Sinopharm ltd
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University of Pittsburgh - Drug Discovery Institute
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Biopharm GmbH
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NanoCarrier Co
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BioMimetic Therapeutics
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Nanotherapeutics
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Image Search Results
Journal: Frontiers in Pharmacology
Article Title: β-lapachone suppresses carcinogenesis of cervical cancer via interaction with AKT1
doi: 10.3389/fphar.2025.1509568
Figure Lengend Snippet: β-Lapachone inhibits the proliferation of cervical cancer cells. (A) Chemical structures of β-lapachone. (B) Expression of NQO1 in cervical cancer and normal tissues were analyzed by GEPIA database. (C) NQO1 protein levels in cancer cell lines and normal cells were detected by Western blot. (D) Cell viability was detected by MTT assay after treatment of cervical cancer cells with different concentrations of β-lapachone. (E) The expression of NQO1 protein in SiHa and C33a cells treated with β-lapachone for 24 h. (F) The effect of β-lapachone on cell proliferation was detected by colony formation assay. Error bars represent the means ± SD of three independent experiments. * P < 0.05, ** P < 0.01 vs. 0 μM β-lapachone group.
Article Snippet:
Techniques: Expressing, Western Blot, MTT Assay, Colony Assay
Journal: Frontiers in Pharmacology
Article Title: β-lapachone suppresses carcinogenesis of cervical cancer via interaction with AKT1
doi: 10.3389/fphar.2025.1509568
Figure Lengend Snippet: β-Lapachone attenuated cervical cancer cell migration, invasion, EMT and angiogenesis. (A, B) Wound healing assay was used to reflect the migration ability of SiHa and C33a cells after treatment with the indicated concentrations (0–6 µM) of β-lapachone. (C, D) Transwell assay was used to detect the effect of the indicated concentrations of β-lapachone treatment on the migration and invasion ability of CC cells. (E, F) Cells were treated with β-lapachone (0–6 µM) for 24 h, and protein levels of E-cadherin, Vimentin, and Snail were analyzed by Western blot. (G) The supernatant from cells treated with β-lapachone (0–6 μM) for 24 h was collected for the tube formation assay. (H) After treating cells with β-lapachone (0–6 µM), VEGF protein expression was detected by Western blot. Error bars represent the means ± SD of three independent experiments. * P < 0.05, ** P < 0.01 vs. 0 μM β-lapachone group.
Article Snippet:
Techniques: Migration, Wound Healing Assay, Transwell Assay, Western Blot, Tube Formation Assay, Expressing
Journal: Frontiers in Pharmacology
Article Title: β-lapachone suppresses carcinogenesis of cervical cancer via interaction with AKT1
doi: 10.3389/fphar.2025.1509568
Figure Lengend Snippet: β-lapachone regulates glucose metabolism reprogramming in cervical cancer cells. (A, B) SiHa and C33a cells were treated with the indicated concentrations of β-lapachone (0–6 µM) for 24 h. Relative levels of ATP, Lactate and Glucose were determined. (C, D) After treating cells with β-lapachone (0–6 µM), PKM2 and G6PC protein expression was detected by Western blot. Error bars represent the means ± SD of three independent experiments. * P < 0.05, ** P < 0.01 vs. 0 μM β-lapachone group.
Article Snippet:
Techniques: Expressing, Western Blot
Journal: Frontiers in Pharmacology
Article Title: β-lapachone suppresses carcinogenesis of cervical cancer via interaction with AKT1
doi: 10.3389/fphar.2025.1509568
Figure Lengend Snippet: β-lapachone inhibits cervical cancer progression and metastasis via the PI3K/AKT/mTOR signaling pathway. (A) Prediction of β-lapachone related target genes in cervical cancer. (B) KEGG pathway enrichment analysis. (C) After treating cells with β-lapachone (0–6 µM), p-AKT/t-AKT, p-mTOR/t-mTOR protein expression was detected by Western blot. (D) The expression of proteins related to the PI3K/AKT/mTOR pathway and EMT process in CC cells was detected by Western blot after treating with β-lapachone and the pathway activator 740 Y-P. Error bars represent the means ± SD of three independent experiments. * P < 0.05, ** P < 0.01 vs. DMSO group, # P < 0.05, ## P < 0.01 vs. β-lapachone group.
Article Snippet:
Techniques: Expressing, Western Blot
Journal: Frontiers in Pharmacology
Article Title: β-lapachone suppresses carcinogenesis of cervical cancer via interaction with AKT1
doi: 10.3389/fphar.2025.1509568
Figure Lengend Snippet: β-lapachone inhibits glucose metabolism and EMT process in CC cells by targeting AKT1. (A) Docking analysis for predicting the binding mode of β-lapachone to AKT1. (B) Western blot analysis of AKT1 in CC cells transfected with siRNA-control, siRNA-AKT1-1、siRNA-AKT1-2 and siRNA-AKT1-3. (C, D) CC cells with AKT1 knockdown were treated with β-lapachone for 24 h, and protein expression levels were analyzed by Western blot. * P < 0.05, ** P < 0.01 vs. β-lapachone group.
Article Snippet:
Techniques: Binding Assay, Western Blot, Transfection, Control, Knockdown, Expressing
Journal: Frontiers in Pharmacology
Article Title: β-lapachone suppresses carcinogenesis of cervical cancer via interaction with AKT1
doi: 10.3389/fphar.2025.1509568
Figure Lengend Snippet: β-Lapachone inhibits tumor growth in vivo . (A) Images of subcutaneous xenograft tumors in the treatment group β-lapachone and control group. (B) Weight statistics of subcutaneous xenograft tumors in the treatment and control groups. (C) Growth volume statistics of subcutaneous xenograft tumors in the treatment and control groups during treatment with β-lapachone. (D) Representative immunohistochemical staining images of Ki67 expression in grafted tumor tissues from various groups of mice; Representative H&E stained images of liver, kidney and lung tissues from each group of mice. Scale bar: 50 μm * P < 0.05, ** P < 0.01.
Article Snippet:
Techniques: In Vivo, Control, Immunohistochemical staining, Staining, Expressing
Journal: Frontiers in Pharmacology
Article Title: β-lapachone suppresses carcinogenesis of cervical cancer via interaction with AKT1
doi: 10.3389/fphar.2025.1509568
Figure Lengend Snippet: Schematic illustration of the mechanisms by which β-lapachone regulates glucose metabolism, EMT process and angiogenesis in cervical cancer through the PI3K/AKT/mTOR signaling pathway.
Article Snippet:
Techniques:
Journal: Assay and Drug Development Technologies
Article Title: Profiling the NIH Small Molecule Repository for Compounds That Generate H 2 O 2 by Redox Cycling in Reducing Environments
doi: 10.1089/adt.2009.0247
Figure Lengend Snippet: Screening the Library of Pharmacologically Active Compounds (LOPAC) set to identify redox cycling compounds (RCCs). (A) The 4 × 384-well plate overlay scatter plot of the % activation of H2O2 production data from the first iteration of the LOPAC screen. An ActivityBase™ HTS template was written to calculate the % activation based on the maximum (n = 32) and minimum (n = 24) plate controls for the HRP-PR H2O2 detection assay. A Spotfire® visualization of the % activation data from 4 × 384-well plates of the HRP-PR H2O2 production data for the first iteration of the LOPAC screen overlaid in a single scatter plot is presented; () maximum (100 μM H2O2 in 1% Dimethyl Sulfoxide (DMSO), n = 32) plate controls, () minimum (1% DMSO, n = 24) plate controls, () 50% (50 μM H2O2 in 1% DMSO, n = 8) plate controls, and () 10 μM compounds in 0.8 mM DTT (1% DMSO, n = 320). (B) Chemical structures, names, and PubChem substance identity numbers (SIDs) of the RCCs identified in the LOPAC set. The chemical structures of 2,3-bis(2-hydroxyethylthio)naphthalene-1,4-dione (NSC 95397, PubChem-SID 400206), and 2,2-dimethyl-3,4-dihydro-2H-benzo[h]chromene-5,6-dione (β-lapachone, PubChem-SID 207115) are presented.
Article Snippet:
Techniques: Activation Assay, Detection Assay