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brequinar dhodh inhibitor  (MedChemExpress)


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    MedChemExpress brequinar dhodh inhibitor
    Brequinar Dhodh Inhibitor, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 95/100, based on 59 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/brequinar/Brequinar/pm42561532-77-191-194
    Average 95 stars, based on 59 article reviews
    brequinar dhodh inhibitor - by Bioz Stars, 2026-09
    95/100 stars

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    Related Articles

    Xenograft Assay:

    Article Title: Japanese encephalitis virus reprograms host pyrimidine metabolism to facilitate viral replication
    Article Snippet: Brequinar (BQR, HY-108325), GOT1 inhibitor-1 (GOT1i, HY-122723), L-aspartic acid sodium (HY-N0666C) and V9302 (HY-112683) were purchased from MedChem Express (Monmouth Junction, USA).

    Polyacrylamide Gel Electrophoresis:

    Article Title: Japanese encephalitis virus reprograms host pyrimidine metabolism to facilitate viral replication
    Article Snippet: Brequinar (BQR, HY-108325), GOT1 inhibitor-1 (GOT1i, HY-122723), L-aspartic acid sodium (HY-N0666C) and V9302 (HY-112683) were purchased from MedChem Express (Monmouth Junction, USA).

    Recombinant:

    Article Title: Japanese encephalitis virus reprograms host pyrimidine metabolism to facilitate viral replication
    Article Snippet: Brequinar (BQR, HY-108325), GOT1 inhibitor-1 (GOT1i, HY-122723), L-aspartic acid sodium (HY-N0666C) and V9302 (HY-112683) were purchased from MedChem Express (Monmouth Junction, USA).

    Binding Assay:

    Article Title: Japanese encephalitis virus reprograms host pyrimidine metabolism to facilitate viral replication
    Article Snippet: Brequinar (BQR, HY-108325), GOT1 inhibitor-1 (GOT1i, HY-122723), L-aspartic acid sodium (HY-N0666C) and V9302 (HY-112683) were purchased from MedChem Express (Monmouth Junction, USA).

    Purification:

    Article Title: Japanese encephalitis virus reprograms host pyrimidine metabolism to facilitate viral replication
    Article Snippet: Brequinar (BQR, HY-108325), GOT1 inhibitor-1 (GOT1i, HY-122723), L-aspartic acid sodium (HY-N0666C) and V9302 (HY-112683) were purchased from MedChem Express (Monmouth Junction, USA).

    Incubation:

    Article Title: Japanese encephalitis virus reprograms host pyrimidine metabolism to facilitate viral replication
    Article Snippet: Brequinar (BQR, HY-108325), GOT1 inhibitor-1 (GOT1i, HY-122723), L-aspartic acid sodium (HY-N0666C) and V9302 (HY-112683) were purchased from MedChem Express (Monmouth Junction, USA).

    Western Blot:

    Article Title: Japanese encephalitis virus reprograms host pyrimidine metabolism to facilitate viral replication
    Article Snippet: Brequinar (BQR, HY-108325), GOT1 inhibitor-1 (GOT1i, HY-122723), L-aspartic acid sodium (HY-N0666C) and V9302 (HY-112683) were purchased from MedChem Express (Monmouth Junction, USA).

    Immunoprecipitation:

    Article Title: Japanese encephalitis virus reprograms host pyrimidine metabolism to facilitate viral replication
    Article Snippet: Brequinar (BQR, HY-108325), GOT1 inhibitor-1 (GOT1i, HY-122723), L-aspartic acid sodium (HY-N0666C) and V9302 (HY-112683) were purchased from MedChem Express (Monmouth Junction, USA).

    Control:

    Article Title: Japanese encephalitis virus reprograms host pyrimidine metabolism to facilitate viral replication
    Article Snippet: Brequinar (BQR, HY-108325), GOT1 inhibitor-1 (GOT1i, HY-122723), L-aspartic acid sodium (HY-N0666C) and V9302 (HY-112683) were purchased from MedChem Express (Monmouth Junction, USA).

    Two Tailed Test:

    Article Title: Japanese encephalitis virus reprograms host pyrimidine metabolism to facilitate viral replication
    Article Snippet: Brequinar (BQR, HY-108325), GOT1 inhibitor-1 (GOT1i, HY-122723), L-aspartic acid sodium (HY-N0666C) and V9302 (HY-112683) were purchased from MedChem Express (Monmouth Junction, USA).

    Labeling:

    Article Title: Japanese encephalitis virus reprograms host pyrimidine metabolism to facilitate viral replication
    Article Snippet: Brequinar (BQR, HY-108325), GOT1 inhibitor-1 (GOT1i, HY-122723), L-aspartic acid sodium (HY-N0666C) and V9302 (HY-112683) were purchased from MedChem Express (Monmouth Junction, USA).

    Fluorescence:

    Article Title: Japanese encephalitis virus reprograms host pyrimidine metabolism to facilitate viral replication
    Article Snippet: Brequinar (BQR, HY-108325), GOT1 inhibitor-1 (GOT1i, HY-122723), L-aspartic acid sodium (HY-N0666C) and V9302 (HY-112683) were purchased from MedChem Express (Monmouth Junction, USA).

    Microscopy:

    Article Title: Japanese encephalitis virus reprograms host pyrimidine metabolism to facilitate viral replication
    Article Snippet: Brequinar (BQR, HY-108325), GOT1 inhibitor-1 (GOT1i, HY-122723), L-aspartic acid sodium (HY-N0666C) and V9302 (HY-112683) were purchased from MedChem Express (Monmouth Junction, USA).

    Concentration Assay:

    Article Title: Japanese encephalitis virus reprograms host pyrimidine metabolism to facilitate viral replication
    Article Snippet: Brequinar (BQR, HY-108325), GOT1 inhibitor-1 (GOT1i, HY-122723), L-aspartic acid sodium (HY-N0666C) and V9302 (HY-112683) were purchased from MedChem Express (Monmouth Junction, USA).



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    a . AlphaLisa binding assay measuring apparent binding affinity ( K d app ) for PPAT–NUDT5 binding in the absence and presence of AMP (1 mM). Data represent the mean ± s.e.m. from n = 3 independent experiments. The AMP (1 mM) condition is also shown in Fig. . b . AlphaLisa binding assay quantifying the stabilization of PPAT–NUDT5 binding by AMP in the presence of PRPP (1 mM). Data represent the mean ± s.e.m. from n = 3 independent experiments. c – e . Mass photometry analysis of purified PPAT and NUDT5 and PPAT incubated with the indicated metabolites: buffer only ( c ), AMP ( d ), or PRPP ( e ). Data in c – e are representative of two independent experiments. f . Left – Representative Western blot of immunoprecipitations from endogenous NUDT5 3×Flag HEK293T cells treated with indicated drugs for 16 h: methotrexate (MTX; 2 µM), lometrexol (LMX; 10 µM), 6-mercaptopurine (6-MP; 50 µM), MLN4924 (1 µM), <t>brequinar</t> (2 µM), and rapamycin (1 µM). Right, quantification of PPAT co-immunoprecipitation relative to NUDT5–3×Flag bait and normalized to a DMSO-treated control condition. Data represent the mean ± s.e.m. with individual values from n = 3 biological replicates. g . Time-course immunoprecipitation of endogenous NUDT5–3×Flag from HEK293T cells treated with MTX (2 µM). Blot shown is representative of two independent experiments. Values for K d app in a were compared by global nonlinear regression using an extra sum-of-squares F-test. Statistical significance in f was determined using two-tailed one-sample t -tests relative to the DMSO control. Significance is indicated as ns (not significant), * P < 0.05, ** P < 0.01 and *** P < 0.001. Exact P values are included as source data.
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    a . AlphaLisa binding assay measuring apparent binding affinity ( K d app ) for PPAT–NUDT5 binding in the absence and presence of AMP (1 mM). Data represent the mean ± s.e.m. from n = 3 independent experiments. The AMP (1 mM) condition is also shown in Fig. . b . AlphaLisa binding assay quantifying the stabilization of PPAT–NUDT5 binding by AMP in the presence of PRPP (1 mM). Data represent the mean ± s.e.m. from n = 3 independent experiments. c – e . Mass photometry analysis of purified PPAT and NUDT5 and PPAT incubated with the indicated metabolites: buffer only ( c ), AMP ( d ), or PRPP ( e ). Data in c – e are representative of two independent experiments. f . Left – Representative Western blot of immunoprecipitations from endogenous NUDT5 3×Flag HEK293T cells treated with indicated drugs for 16 h: methotrexate (MTX; 2 µM), lometrexol (LMX; 10 µM), 6-mercaptopurine (6-MP; 50 µM), MLN4924 (1 µM), <t>brequinar</t> (2 µM), and rapamycin (1 µM). Right, quantification of PPAT co-immunoprecipitation relative to NUDT5–3×Flag bait and normalized to a DMSO-treated control condition. Data represent the mean ± s.e.m. with individual values from n = 3 biological replicates. g . Time-course immunoprecipitation of endogenous NUDT5–3×Flag from HEK293T cells treated with MTX (2 µM). Blot shown is representative of two independent experiments. Values for K d app in a were compared by global nonlinear regression using an extra sum-of-squares F-test. Statistical significance in f was determined using two-tailed one-sample t -tests relative to the DMSO control. Significance is indicated as ns (not significant), * P < 0.05, ** P < 0.01 and *** P < 0.001. Exact P values are included as source data.
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    a . AlphaLisa binding assay measuring apparent binding affinity ( K d app ) for PPAT–NUDT5 binding in the absence and presence of AMP (1 mM). Data represent the mean ± s.e.m. from n = 3 independent experiments. The AMP (1 mM) condition is also shown in Fig. . b . AlphaLisa binding assay quantifying the stabilization of PPAT–NUDT5 binding by AMP in the presence of PRPP (1 mM). Data represent the mean ± s.e.m. from n = 3 independent experiments. c – e . Mass photometry analysis of purified PPAT and NUDT5 and PPAT incubated with the indicated metabolites: buffer only ( c ), AMP ( d ), or PRPP ( e ). Data in c – e are representative of two independent experiments. f . Left – Representative Western blot of immunoprecipitations from endogenous NUDT5 3×Flag HEK293T cells treated with indicated drugs for 16 h: methotrexate (MTX; 2 µM), lometrexol (LMX; 10 µM), 6-mercaptopurine (6-MP; 50 µM), MLN4924 (1 µM), <t>brequinar</t> (2 µM), and rapamycin (1 µM). Right, quantification of PPAT co-immunoprecipitation relative to NUDT5–3×Flag bait and normalized to a DMSO-treated control condition. Data represent the mean ± s.e.m. with individual values from n = 3 biological replicates. g . Time-course immunoprecipitation of endogenous NUDT5–3×Flag from HEK293T cells treated with MTX (2 µM). Blot shown is representative of two independent experiments. Values for K d app in a were compared by global nonlinear regression using an extra sum-of-squares F-test. Statistical significance in f was determined using two-tailed one-sample t -tests relative to the DMSO control. Significance is indicated as ns (not significant), * P < 0.05, ** P < 0.01 and *** P < 0.001. Exact P values are included as source data.
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    a . AlphaLisa binding assay measuring apparent binding affinity ( K d app ) for PPAT–NUDT5 binding in the absence and presence of AMP (1 mM). Data represent the mean ± s.e.m. from n = 3 independent experiments. The AMP (1 mM) condition is also shown in Fig. . b . AlphaLisa binding assay quantifying the stabilization of PPAT–NUDT5 binding by AMP in the presence of PRPP (1 mM). Data represent the mean ± s.e.m. from n = 3 independent experiments. c – e . Mass photometry analysis of purified PPAT and NUDT5 and PPAT incubated with the indicated metabolites: buffer only ( c ), AMP ( d ), or PRPP ( e ). Data in c – e are representative of two independent experiments. f . Left – Representative Western blot of immunoprecipitations from endogenous NUDT5 3×Flag HEK293T cells treated with indicated drugs for 16 h: methotrexate (MTX; 2 µM), lometrexol (LMX; 10 µM), 6-mercaptopurine (6-MP; 50 µM), MLN4924 (1 µM), <t>brequinar</t> (2 µM), and rapamycin (1 µM). Right, quantification of PPAT co-immunoprecipitation relative to NUDT5–3×Flag bait and normalized to a DMSO-treated control condition. Data represent the mean ± s.e.m. with individual values from n = 3 biological replicates. g . Time-course immunoprecipitation of endogenous NUDT5–3×Flag from HEK293T cells treated with MTX (2 µM). Blot shown is representative of two independent experiments. Values for K d app in a were compared by global nonlinear regression using an extra sum-of-squares F-test. Statistical significance in f was determined using two-tailed one-sample t -tests relative to the DMSO control. Significance is indicated as ns (not significant), * P < 0.05, ** P < 0.01 and *** P < 0.001. Exact P values are included as source data.
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    Image Search Results


    a . AlphaLisa binding assay measuring apparent binding affinity ( K d app ) for PPAT–NUDT5 binding in the absence and presence of AMP (1 mM). Data represent the mean ± s.e.m. from n = 3 independent experiments. The AMP (1 mM) condition is also shown in Fig. . b . AlphaLisa binding assay quantifying the stabilization of PPAT–NUDT5 binding by AMP in the presence of PRPP (1 mM). Data represent the mean ± s.e.m. from n = 3 independent experiments. c – e . Mass photometry analysis of purified PPAT and NUDT5 and PPAT incubated with the indicated metabolites: buffer only ( c ), AMP ( d ), or PRPP ( e ). Data in c – e are representative of two independent experiments. f . Left – Representative Western blot of immunoprecipitations from endogenous NUDT5 3×Flag HEK293T cells treated with indicated drugs for 16 h: methotrexate (MTX; 2 µM), lometrexol (LMX; 10 µM), 6-mercaptopurine (6-MP; 50 µM), MLN4924 (1 µM), brequinar (2 µM), and rapamycin (1 µM). Right, quantification of PPAT co-immunoprecipitation relative to NUDT5–3×Flag bait and normalized to a DMSO-treated control condition. Data represent the mean ± s.e.m. with individual values from n = 3 biological replicates. g . Time-course immunoprecipitation of endogenous NUDT5–3×Flag from HEK293T cells treated with MTX (2 µM). Blot shown is representative of two independent experiments. Values for K d app in a were compared by global nonlinear regression using an extra sum-of-squares F-test. Statistical significance in f was determined using two-tailed one-sample t -tests relative to the DMSO control. Significance is indicated as ns (not significant), * P < 0.05, ** P < 0.01 and *** P < 0.001. Exact P values are included as source data.

    Journal: Nature

    Article Title: Metabolite glues as a means of purine sensing and chemotherapeutic response

    doi: 10.1038/s41586-026-10790-3

    Figure Lengend Snippet: a . AlphaLisa binding assay measuring apparent binding affinity ( K d app ) for PPAT–NUDT5 binding in the absence and presence of AMP (1 mM). Data represent the mean ± s.e.m. from n = 3 independent experiments. The AMP (1 mM) condition is also shown in Fig. . b . AlphaLisa binding assay quantifying the stabilization of PPAT–NUDT5 binding by AMP in the presence of PRPP (1 mM). Data represent the mean ± s.e.m. from n = 3 independent experiments. c – e . Mass photometry analysis of purified PPAT and NUDT5 and PPAT incubated with the indicated metabolites: buffer only ( c ), AMP ( d ), or PRPP ( e ). Data in c – e are representative of two independent experiments. f . Left – Representative Western blot of immunoprecipitations from endogenous NUDT5 3×Flag HEK293T cells treated with indicated drugs for 16 h: methotrexate (MTX; 2 µM), lometrexol (LMX; 10 µM), 6-mercaptopurine (6-MP; 50 µM), MLN4924 (1 µM), brequinar (2 µM), and rapamycin (1 µM). Right, quantification of PPAT co-immunoprecipitation relative to NUDT5–3×Flag bait and normalized to a DMSO-treated control condition. Data represent the mean ± s.e.m. with individual values from n = 3 biological replicates. g . Time-course immunoprecipitation of endogenous NUDT5–3×Flag from HEK293T cells treated with MTX (2 µM). Blot shown is representative of two independent experiments. Values for K d app in a were compared by global nonlinear regression using an extra sum-of-squares F-test. Statistical significance in f was determined using two-tailed one-sample t -tests relative to the DMSO control. Significance is indicated as ns (not significant), * P < 0.05, ** P < 0.01 and *** P < 0.001. Exact P values are included as source data.

    Article Snippet: The following drugs and chemicals were used in this study at amounts specified in figures and legends: pevonedistat (MLN4924; MedChemExpress, HY-70062), MTX (MedChemExpress, HY-14519), lometrexol (LMX; MedChemExpress, HY-14521), brequinar (MedChemExpress, HY-108325), rapamycin (Adooq Biosciences, A10782), 5-phospho- d -ribose 1-diphosphate (PRPP; Sigma-Aldrich, P8296), l -glutamine (Sigma-Aldrich, G8540); adenosine-5′-monophosphate; (AMP; Sigma-Aldrich 01930), inosine-5′-monophosphate (IMP; MedChemExpress, HY-W010759), guanosine-5′-monophosphate (GMP; Sigma-Aldrich, G8377), AICA-ribonucleotide (Cayman Chemicals, 33907), adenine (Thermo Fisher Scientific, A17622.14), hypoxanthine (MedChemExpress, HY-N0091), 6-TG (Thermo Fisher Scientific, B21280.03), 6-MP (Adooq Biosciences, A15898), 6-thioinosine-5′-monophosphate (6-TIMP; Jena Biosciences, NU-1148), 6-methylthioinosine-5′-monophosphate (6-meTIMP; Jena Biosciences, NU-1226), 6-methylthioguanosine-5′-monophosphate (6-meTGMP; Jena Biosciences, NU-1128), 6-benzylthioinosine-5′-monophosphate (6-benzylTIMP; WuXi, custom synthesis); staurosporine (Selleckchem, AM-2282); 6-ethylthioinosine-5′-monophosphate (6-etTIMP; WuXi, custom synthesis) amd 6-ethylmercaptopurine riboside (6-EMPR; WuXi, custom synthesis).

    Techniques: Binding Assay, Purification, Incubation, Western Blot, Immunoprecipitation, Control, Two Tailed Test