chrysin and benzothiophene

chrysin has been researched along with benzothiophene* in 2 studies

Other Studies

2 other study(ies) available for chrysin and benzothiophene

Article	Year
Effects of substituent pattern on the intracellular target of antiproliferative benzo[b]thiophenyl chromone derivatives. European journal of medicinal chemistry, 2021, Oct-15, Volume: 222 Topics: Antineoplastic Agents; Cell Proliferation; Chromones; Dose-Response Relationship, Drug; Drug Screening Assays, Antitumor; Humans; Models, Molecular; Molecular Structure; Structure-Activity Relationship; Thiophenes; Tumor Cells, Cultured	2021
Casein kinase II is a selective target of HIV-1 transcriptional inhibitors. Proceedings of the National Academy of Sciences of the United States of America, 1997, Jun-10, Volume: 94, Issue:12 The identification of cellular factors that are required to complete various steps of the HIV-1 life cycle may lead to the development of new therapeutics. One key step, transcription from the integrated provirus, is inhibited by members of two distinct classes of compounds, the flavonoids and the benzothiophenes, via an unknown mechanism, possibly involving a cellular factor. A marked specificity toward inhibiting HIV-1 transcription is evidenced by the ability of drug-treated cells to retain their proliferative and differentiation capabilities. In addition, the compounds do not impede the activation and function of the transcriptional factor NF-kappaB. Here we report on the identification of several cellular proteins that mediate the HIV-1 transcriptional inhibitory property of the flavonoid chrysin. Chemical and immunologic analyses identified these cellular proteins as the individual subunits of casein kinase II (CKII). Though structurally unrelated to chrysin, an HIV-1 inhibitory benzothiophene also bound selectively to CKII. Both chrysin and the benzothiophenes inhibited human recombinant CKII enzymatic activity and showed competitive kinetics with respect to ATP, analogous to the classic CKII inhibitor 5, 6-dichloro-1-beta-D-ribofuranosylbenzimidazole (DRB). Moreover, DRB potently inhibited HIV-1 expression in chronically infected cells. CKII may regulate HIV-1 transcription by phosphorylating cellular proteins involved in HIV-1 transactivation that contain multiple CKII phosphorylation consensus sequences. Topics: Anti-HIV Agents; Carrier Proteins; Casein Kinase II; Catechin; Cell Line; Chamomile; Chromatography, Affinity; Flavonoids; Hesperidin; HIV-1; HL-60 Cells; Humans; Kinetics; NF-kappa B; Oils, Volatile; Plants, Medicinal; Protein Serine-Threonine Kinases; Recombinant Proteins; Thiophenes; Transcription, Genetic; Virus Integration; Virus Replication	1997

Article

Year

Effects of substituent pattern on the intracellular target of antiproliferative benzo[b]thiophenyl chromone derivatives.

European journal of medicinal chemistry, 2021, Oct-15, Volume: 222

Topics: Antineoplastic Agents; Cell Proliferation; Chromones; Dose-Response Relationship, Drug; Drug Screening Assays, Antitumor; Humans; Models, Molecular; Molecular Structure; Structure-Activity Relationship; Thiophenes; Tumor Cells, Cultured

2021

Casein kinase II is a selective target of HIV-1 transcriptional inhibitors.

Proceedings of the National Academy of Sciences of the United States of America, 1997, Jun-10, Volume: 94, Issue:12

The identification of cellular factors that are required to complete various steps of the HIV-1 life cycle may lead to the development of new therapeutics. One key step, transcription from the integrated provirus, is inhibited by members of two distinct classes of compounds, the flavonoids and the benzothiophenes, via an unknown mechanism, possibly involving a cellular factor. A marked specificity toward inhibiting HIV-1 transcription is evidenced by the ability of drug-treated cells to retain their proliferative and differentiation capabilities. In addition, the compounds do not impede the activation and function of the transcriptional factor NF-kappaB. Here we report on the identification of several cellular proteins that mediate the HIV-1 transcriptional inhibitory property of the flavonoid chrysin. Chemical and immunologic analyses identified these cellular proteins as the individual subunits of casein kinase II (CKII). Though structurally unrelated to chrysin, an HIV-1 inhibitory benzothiophene also bound selectively to CKII. Both chrysin and the benzothiophenes inhibited human recombinant CKII enzymatic activity and showed competitive kinetics with respect to ATP, analogous to the classic CKII inhibitor 5, 6-dichloro-1-beta-D-ribofuranosylbenzimidazole (DRB). Moreover, DRB potently inhibited HIV-1 expression in chronically infected cells. CKII may regulate HIV-1 transcription by phosphorylating cellular proteins involved in HIV-1 transactivation that contain multiple CKII phosphorylation consensus sequences.

Topics: Anti-HIV Agents; Carrier Proteins; Casein Kinase II; Catechin; Cell Line; Chamomile; Chromatography, Affinity; Flavonoids; Hesperidin; HIV-1; HL-60 Cells; Humans; Kinetics; NF-kappa B; Oils, Volatile; Plants, Medicinal; Protein Serine-Threonine Kinases; Recombinant Proteins; Thiophenes; Transcription, Genetic; Virus Integration; Virus Replication

1997