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ds 1001b  (MedChemExpress)


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    MedChemExpress ds 1001b
    Ds 1001b, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ds 1001b/product/MedChemExpress
    Average 92 stars, based on 2 article reviews
    ds 1001b - by Bioz Stars, 2026-02
    92/100 stars

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    IDH mutations and mutant IDH inhibitors. (A) Mutations in IDH1 and IDH2 increase 2-HG promoting pleotropic effects leading to tumorigenesis. 2-HG competitively inhibits α-KG binding to histone demethylases, including KDM2A, TET1 and TET2 hydroxymethylases promoting epigenetic dysregulation through hypermethylation of DNA. 2-HG also stabilises HIF1α promoting increased vascular endothelial growth factor (VEGF) signaling and angiogenesis. Additionally, the mutant IDH1 consumes NADPH for NADP + production, driving a metabolic compensation through glutaminolysis, leading to the accumulation of reactive oxidation species (ROS) and oxidative damage. In the tumor microenvironment, 2-HG exerts immunosuppressive effects through upregulation of immunosuppressive macrophages and down regulation of CD8 + T cells. (B) Safusidenib binds to the allosteric pocket in the mutant IDH1 dimer surface stabilizing the inactive form of the enzyme, thus reducing 2-HG and reversing the oncogenic effects. Created with BioRender.com .

    Journal: Future Oncology

    Article Title: A perioperative study of Safusidenib in patients with IDH1 -mutated glioma

    doi: 10.1080/14796694.2024.2383064

    Figure Lengend Snippet: IDH mutations and mutant IDH inhibitors. (A) Mutations in IDH1 and IDH2 increase 2-HG promoting pleotropic effects leading to tumorigenesis. 2-HG competitively inhibits α-KG binding to histone demethylases, including KDM2A, TET1 and TET2 hydroxymethylases promoting epigenetic dysregulation through hypermethylation of DNA. 2-HG also stabilises HIF1α promoting increased vascular endothelial growth factor (VEGF) signaling and angiogenesis. Additionally, the mutant IDH1 consumes NADPH for NADP + production, driving a metabolic compensation through glutaminolysis, leading to the accumulation of reactive oxidation species (ROS) and oxidative damage. In the tumor microenvironment, 2-HG exerts immunosuppressive effects through upregulation of immunosuppressive macrophages and down regulation of CD8 + T cells. (B) Safusidenib binds to the allosteric pocket in the mutant IDH1 dimer surface stabilizing the inactive form of the enzyme, thus reducing 2-HG and reversing the oncogenic effects. Created with BioRender.com .

    Article Snippet: Safusidenib (AB-218 / DS-1001b) is an oral, blood brain barrier penetrant IDH1 R132X enzyme inhibitor developed by Daiichi Sankyo.

    Techniques: Mutagenesis, Binding Assay

    Objective and outcomes of the study.

    Journal: Future Oncology

    Article Title: A perioperative study of Safusidenib in patients with IDH1 -mutated glioma

    doi: 10.1080/14796694.2024.2383064

    Figure Lengend Snippet: Objective and outcomes of the study.

    Article Snippet: Safusidenib (AB-218 / DS-1001b) is an oral, blood brain barrier penetrant IDH1 R132X enzyme inhibitor developed by Daiichi Sankyo.

    Techniques: Clinical Proteomics, Activity Assay, Sampling, Methylation, Gene Expression, Imaging, Diffusion-based Assay

    Pharmacokinetics of safusidenib and sample timing.

    Journal: Future Oncology

    Article Title: A perioperative study of Safusidenib in patients with IDH1 -mutated glioma

    doi: 10.1080/14796694.2024.2383064

    Figure Lengend Snippet: Pharmacokinetics of safusidenib and sample timing.

    Article Snippet: Safusidenib (AB-218 / DS-1001b) is an oral, blood brain barrier penetrant IDH1 R132X enzyme inhibitor developed by Daiichi Sankyo.

    Techniques: Drug discovery, Clinical Proteomics

    Physiologic function of IDH1 (outside the mitochondria) and IDH2 (inside the mitochondria); mIDH1 and mIDH2 are shown producing D2-HG. mIDH inhibitors are shown to inhibit mIDH1 and mIDH2 function. Created with BioRender.

    Journal: Neuro-Oncology Advances

    Article Title: Isocitrate dehydrogenase mutations in gliomas: A review of current understanding and trials

    doi: 10.1093/noajnl/vdad053

    Figure Lengend Snippet: Physiologic function of IDH1 (outside the mitochondria) and IDH2 (inside the mitochondria); mIDH1 and mIDH2 are shown producing D2-HG. mIDH inhibitors are shown to inhibit mIDH1 and mIDH2 function. Created with BioRender.

    Article Snippet: Finally, NCT03030066 (Daiichi Sankyo Co, Ltd, Japan) conducted a single-center, Phase I open-label clinical trial studying the mutant IDH1 inhibitor DS-1001b in patients with IDH1-R132-mutated gliomas, as a salvage treatment.

    Techniques:

    All Completed Peptide Vaccine and IDH-inhibitor Trials

    Journal: Neuro-Oncology Advances

    Article Title: Isocitrate dehydrogenase mutations in gliomas: A review of current understanding and trials

    doi: 10.1093/noajnl/vdad053

    Figure Lengend Snippet: All Completed Peptide Vaccine and IDH-inhibitor Trials

    Article Snippet: Finally, NCT03030066 (Daiichi Sankyo Co, Ltd, Japan) conducted a single-center, Phase I open-label clinical trial studying the mutant IDH1 inhibitor DS-1001b in patients with IDH1-R132-mutated gliomas, as a salvage treatment.

    Techniques:

    All Current Clinical Trials Targeting IDH-mutated Gliomas

    Journal: Neuro-Oncology Advances

    Article Title: Isocitrate dehydrogenase mutations in gliomas: A review of current understanding and trials

    doi: 10.1093/noajnl/vdad053

    Figure Lengend Snippet: All Current Clinical Trials Targeting IDH-mutated Gliomas

    Article Snippet: Finally, NCT03030066 (Daiichi Sankyo Co, Ltd, Japan) conducted a single-center, Phase I open-label clinical trial studying the mutant IDH1 inhibitor DS-1001b in patients with IDH1-R132-mutated gliomas, as a salvage treatment.

    Techniques: Clinical Proteomics, Mutagenesis, Adjuvant