YTHDF

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  1. Multi-Kinase PROTAC

    SK-3-91 is a multi-kinase degrader functioning through the ubiquitin biotinylation (E-STUB) pathway to induce the degradation of over 125 unique kinases. This PROTAC effectively reduces the levels of YTHDF2, contributing to the inhibition of cell proliferation and morphological alterations in treated cells. Its design facilitates the selective targeting and degradation of diverse kinases, making it a valuable tool for studying kinase function and exploring therapeutic applications in cancer research.
  2. Natural Product

    Curdione, a naturally occurring sesquiterpenoid, exhibits significant anti-platelet aggregation activity and plays a pivotal role in modulating ferroptosis in colorectal cancer through m6A methylation processes involving METTL14 and YTHDF2. This compound is effective in alleviating myocardial infarction-induced oxidative stress via the Keap1/Trx1/GPX4 signaling pathway and mitigating Doxorubicin-induced cardiotoxicity through activation of the Nrf2/HO-1 pathway. Additionally, Curdione demonstrates protective properties against sepsis-induced lung injury, pulmonary fibrosis, and focal cerebral ischemia, while also exhibiting antiproliferative effects against human uterine leiomyosarcoma by targeting IDO1. Its modulation of DNMT1-mediated ERBB4 promoter methylation further supports its vascular protective effects.
  3. YTH domain Inhibitor

    YTH-IN-1 is a pan-YTH domain inhibitor that targets various YTH domain-containing proteins. It exhibits IC50 values of 39 μM, 34 μM, 35 μM, 48 μM, and 30 μM for human YTHDF1, YTHDF2, YTHDF3, YTHDC1, and YTHDC2 respectively. This compound is utilized in research to explore the role of YTH domain proteins in RNA metabolism and epitranscriptomics, making it a valuable tool for studying gene regulation and cellular responses.
  4. YTHDF2 Ligand

    YTHDF2 ligand-1 is a selective and high-affinity ligand that targets YTHDF2, with an IC50 of 11 μM and a Kd of 1.3 μM. This compound effectively competes with m6A-RNA for the binding site on YTHDF2, making it a valuable tool for studies involving RNA methylation and its implications in cancer research. Researchers can utilize YTHDF2 ligand-1 to explore the role of YTHDF2 in various cellular processes and potential therapeutic interventions.

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