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mutation encoding midh1 r132h  (ATCC)


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    Structured Review

    ATCC mutation encoding midh1 r132h
    <t>mIDH1-selective</t> quinolinone-based inhibitors selected as lead structures (left) and radiolabeled analogs prepared in the present study (right). IC 50 values indicated below the lead structures correspond to the reported potency for inhibition of the most frequent mIDH1 <t>R132H</t> mutation in biochemical assays, while the selectivity factors correspond to the ratio of the biochemical IC 50 values for mIDH1 R132H and the wildtype enzyme.
    Mutation Encoding Midh1 R132h, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 10564 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/mutation+encoding+midh1+r132h/U-87+MG/pmc11356819-160-7-22
    Average 99 stars, based on 10564 article reviews
    mutation encoding midh1 r132h - by Bioz Stars, 2026-10
    99/100 stars

    Images

    1) Product Images from "Preparation and Preclinical Evaluation of 18 F-Labeled Olutasidenib Derivatives for Non-Invasive Detection of Mutated Isocitrate Dehydrogenase 1 (mIDH1)"

    Article Title: Preparation and Preclinical Evaluation of 18 F-Labeled Olutasidenib Derivatives for Non-Invasive Detection of Mutated Isocitrate Dehydrogenase 1 (mIDH1)

    Journal: Molecules

    doi: 10.3390/molecules29163939

    mIDH1-selective quinolinone-based inhibitors selected as lead structures (left) and radiolabeled analogs prepared in the present study (right). IC 50 values indicated below the lead structures correspond to the reported potency for inhibition of the most frequent mIDH1 R132H mutation in biochemical assays, while the selectivity factors correspond to the ratio of the biochemical IC 50 values for mIDH1 R132H and the wildtype enzyme.
    Figure Legend Snippet: mIDH1-selective quinolinone-based inhibitors selected as lead structures (left) and radiolabeled analogs prepared in the present study (right). IC 50 values indicated below the lead structures correspond to the reported potency for inhibition of the most frequent mIDH1 R132H mutation in biochemical assays, while the selectivity factors correspond to the ratio of the biochemical IC 50 values for mIDH1 R132H and the wildtype enzyme.

    Techniques Used: Inhibition, Mutagenesis

    Dose-response curves and half-maximal inhibitory concentrations (IC 50 ) for suppression of mIDH1 R132H by the fluorinated olutasidenib derivatives. Data are shown as mean ± standard deviation (n = 3). For additional fit parameters and 95% confidence intervals, see .
    Figure Legend Snippet: Dose-response curves and half-maximal inhibitory concentrations (IC 50 ) for suppression of mIDH1 R132H by the fluorinated olutasidenib derivatives. Data are shown as mean ± standard deviation (n = 3). For additional fit parameters and 95% confidence intervals, see .

    Techniques Used: Standard Deviation

    Related Articles

    Knock-In:

    Article Title: Preparation and Preclinical Evaluation of 18 F-Labeled Olutasidenib Derivatives for Non-Invasive Detection of Mutated Isocitrate Dehydrogenase 1 (mIDH1)
    Article Snippet: .. Human glioblastoma cells with a c.395G>A knock-in mutation encoding mIDH1 R132H (HTB-14IGTM) and the corresponding wildtype cells (HTB-14TM) were purchased from the American Type Culture Collection (ATCC). .. The cells were grown under standard culture conditions (5% CO 2 and 95% air at 37 °C) in Eagle’s Minimum Essential Medium (MEM) supplemented with 10% fetal bovine serum (FBS) and antibiotics (penicillin–streptomycin mixed solution, Gibco, Thermo Fisher Scientific, Oberhausen, Germany).

    Mutagenesis:

    Article Title: Preparation and Preclinical Evaluation of 18 F-Labeled Olutasidenib Derivatives for Non-Invasive Detection of Mutated Isocitrate Dehydrogenase 1 (mIDH1)
    Article Snippet: .. Human glioblastoma cells with a c.395G>A knock-in mutation encoding mIDH1 R132H (HTB-14IGTM) and the corresponding wildtype cells (HTB-14TM) were purchased from the American Type Culture Collection (ATCC). .. The cells were grown under standard culture conditions (5% CO 2 and 95% air at 37 °C) in Eagle’s Minimum Essential Medium (MEM) supplemented with 10% fetal bovine serum (FBS) and antibiotics (penicillin–streptomycin mixed solution, Gibco, Thermo Fisher Scientific, Oberhausen, Germany).



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    mutation encoding midh1 r132h  (ATCC)
    99
    ATCC mutation encoding midh1 r132h
    <t>mIDH1-selective</t> quinolinone-based inhibitors selected as lead structures (left) and radiolabeled analogs prepared in the present study (right). IC 50 values indicated below the lead structures correspond to the reported potency for inhibition of the most frequent mIDH1 <t>R132H</t> mutation in biochemical assays, while the selectivity factors correspond to the ratio of the biochemical IC 50 values for mIDH1 R132H and the wildtype enzyme.
    Mutation Encoding Midh1 R132h, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/mutation+encoding+midh1+r132h/U-87+MG/pmc11356819-160-7-22
    Average 99 stars, based on 1 article reviews
    mutation encoding midh1 r132h - by Bioz Stars, 2026-10
    99/100 stars
    		  Buy from Supplier

    Image Search Results


    mIDH1-selective quinolinone-based inhibitors selected as lead structures (left) and radiolabeled analogs prepared in the present study (right). IC 50 values indicated below the lead structures correspond to the reported potency for inhibition of the most frequent mIDH1 R132H mutation in biochemical assays, while the selectivity factors correspond to the ratio of the biochemical IC 50 values for mIDH1 R132H and the wildtype enzyme.

    Journal: Molecules

    Article Title: Preparation and Preclinical Evaluation of 18 F-Labeled Olutasidenib Derivatives for Non-Invasive Detection of Mutated Isocitrate Dehydrogenase 1 (mIDH1)

    doi: 10.3390/molecules29163939

    Figure Lengend Snippet: mIDH1-selective quinolinone-based inhibitors selected as lead structures (left) and radiolabeled analogs prepared in the present study (right). IC 50 values indicated below the lead structures correspond to the reported potency for inhibition of the most frequent mIDH1 R132H mutation in biochemical assays, while the selectivity factors correspond to the ratio of the biochemical IC 50 values for mIDH1 R132H and the wildtype enzyme.

    Article Snippet: Human glioblastoma cells with a c.395G>A knock-in mutation encoding mIDH1 R132H (HTB-14IGTM) and the corresponding wildtype cells (HTB-14TM) were purchased from the American Type Culture Collection (ATCC).

    Techniques: Inhibition, Mutagenesis

    Dose-response curves and half-maximal inhibitory concentrations (IC 50 ) for suppression of mIDH1 R132H by the fluorinated olutasidenib derivatives. Data are shown as mean ± standard deviation (n = 3). For additional fit parameters and 95% confidence intervals, see .

    Journal: Molecules

    Article Title: Preparation and Preclinical Evaluation of 18 F-Labeled Olutasidenib Derivatives for Non-Invasive Detection of Mutated Isocitrate Dehydrogenase 1 (mIDH1)

    doi: 10.3390/molecules29163939

    Figure Lengend Snippet: Dose-response curves and half-maximal inhibitory concentrations (IC 50 ) for suppression of mIDH1 R132H by the fluorinated olutasidenib derivatives. Data are shown as mean ± standard deviation (n = 3). For additional fit parameters and 95% confidence intervals, see .

    Article Snippet: Human glioblastoma cells with a c.395G>A knock-in mutation encoding mIDH1 R132H (HTB-14IGTM) and the corresponding wildtype cells (HTB-14TM) were purchased from the American Type Culture Collection (ATCC).

    Techniques: Standard Deviation