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pha 793887  (Selleck Chemicals)


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    Structured Review

    Selleck Chemicals pha 793887
    Pha 793887, supplied by Selleck Chemicals, used in various techniques. Bioz Stars score: 93/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/pha+793887/PHA-793887/pm40526635-62-4-14
    Average 93 stars, based on 14 article reviews
    pha 793887 - by Bioz Stars, 2026-10
    93/100 stars

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    Article Title: Methods and materials for identifying and treating BET inhibitor-resistant cancers
    Article Snippet: Examples of CDK inhibitors that can be used as described herein to increase the susceptibility of that cancer to treatment with a BET inhibitor include, without limitation, Palbociclib (6-acetyl-8-cyclopentyl-5-methyl-2-[(5-piperazin-1-ylpyridin-2-yl) amino]pyrido[2,3-d]pyrimidin-7-one), Palbociclib HCl (PD-0332991; available commercially from Selleck Chemicals, Houston, TX; Catalog #S1116), Palbociclib Isethionate (PD0332991; available commercially from Selleck Chemicals, Houston, TX; Catalog #S1579), Abemaciclib (LY2835219; N-[5-[(4-ethylpiperazin-1-yl)methyl]pyridin-2-yl]-5-fluoro-4-(7-fluoro-2-methyl-3-propan-2-ylbenzimidazol-5-yl)pyrimidin-2-amine; available commercially from Selleck Chemicals, Houston, TX; Catalog #7158), Ribociclib (LEE011; 7-cyclopentyl-N,N-dimethyl-2-[(5-piperazin-1-ylpyridin-2-yl) amino]pyrrolo[2,3-d]pyrimidine-6-carboxamide; available commercially from Selleck Chemicals, Houston, TX; Catalog #7440), Flavopiridol (Alvocidib; available commercially from Selleck Chemicals, Houston, TX; Catalog #S1230), AT7519 (available commercially from Selleck Chemicals, Houston, TX; Catalog #S1524), Flavopiridol HCl (available commercially from Selleck Chemicals, Houston, TX; Catalog #S2679), JNJ-7706621 (available commercially from Selleck Chemicals, Houston, TX; Catalog #S1249), PHA-793887 (available commercially from Selleck Chemicals, Houston, TX; Catalog #S1487), BMS-265246 (available commercially from Selleck Chemicals, Houston, TX; Catalog #S2014), Milciclib (PHA-848125 (available commercially from Selleck Chemicals, Houston, TX; Catalog #S2751), R547 (available commercially from Selleck Chemicals, Houston, TX; Catalog #S2688), P276-00 (available commercially from Selleck Chemicals, Houston, TX; Catalog #S8058), ON123300 (available commercially from Selleck Chemicals, Houston, TX; Catalog #S8161), AT7519 HCL (available commercially from Selleck Chemicals, Houston, TX; Catalog #S7808), Purvalanol A (available commercially from Selleck Chemicals, Houston, TX; Catalog #S7793), and SU9516 (available commercially from Selleck Chemicals, Houston, TX; Catalog #S7636).


    Article Title: Sigma non-opioid receptor 1 is a potential therapeutic target for long QT syndrome.
    Article Snippet: All components used for the above recording solutions were purchased from Sigma-Aldrich except (−)-[3R,4S]-chromanol 293B (Tocris).

    Article Title: Identification and subsequent validation of transcriptomic signature associated with metabolic status in endometrial cancer.
    Article Snippet: Sapanisertib (Selleckchem, Munich, Germany), PHA-793887 (Selleckchem), ciclopirox (SigmaAldrich), sulfasalazine (Sigma-Aldrich), cytarabine (Sigma-Aldrich), and 17β-estradiol (Sigma-Aldrich) were dissolved in dimethyl sulfoxide (DMSO) purchased from Sigma-Aldrich.

    Article Title: Identification and subsequent validation of transcriptomic signature associated with metabolic status in endometrial cancer
    Article Snippet: Sapanisertib (Selleckchem, Munich, Germany), PHA-793887 (Selleckchem), ciclopirox (Sigma-Aldrich), sulfasalazine (Sigma-Aldrich), cytarabine (Sigma-Aldrich), and 17β-estradiol (Sigma-Aldrich) were dissolved in dimethyl sulfoxide (DMSO) purchased from Sigma-Aldrich.

    In Vitro:

    Article Title: Efficacy of NAMPT inhibition in T-cell acute lymphoblastic leukemia.
    Article Snippet: .. For in vitro studies, PHA-793887, AZD7762, FK866, STF-118804, gedatolisib, and doxorubicin were purchased from Selleckchem (Houston, TX, USA), and LY3023414, AZD2014, and AT7519 were purchased from MedChem Express (Monmouth Junction, NJ, USA). ..

    Article Title: Efficacy of NAMPT inhibition in T-cell acute lymphoblastic leukemia
    Article Snippet: .. For in vitro studies, PHA-793887, AZD7762, FK866, STF-118804, gedatolisib, and doxorubicin were purchased from Selleckchem (Houston, TX, USA), and LY3023414, AZD2014, and AT7519 were purchased from MedChem Express (Monmouth Junction, NJ, USA). ..

    Concentration Assay:

    Article Title: Sigma non-opioid receptor 1 is a potential therapeutic target for long QT syndrome
    Article Snippet: .. The stock of PHA-793887 (Selleckchem) was diluted with DMSO and added to the corresponding samples in the PHA-793887 treated Timothy syndrome groups at the concentration of 5 μM. ..



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    Structural basis of CDK5/p25 inhibition by pyrazole-based kinase inhibitors. (A) Close-up view of the ATP-binding pocket of the CDK5/p25 complex (chain A: red; chain D: blue) with Dinaciclib (cyan) bound. Key residues Leu83 and Asp86 (pink sticks) form hydrogen bonds (orange lines, distances in Å) with the inhibitor’s heterocyclic core and substituents. The surrounding protein surface is rendered semi-transparently in pink to highlight the binding cleft. (B) Global view of the CDK5/p25–Dinaciclib complex. Chain A (CDK5) is depicted as red ribbons, chain D (p25) as blue ribbons, and the molecular surface is shown in pink to delineate the active site region. Dinaciclib (cyan) occupies the canonical ATP-binding site between the N- and C-terminal lobes, consistent with its mechanism as a competitive ATP-mimetic inhibitor. (C) Chemical structures of representative pyrazole derivatives: Dinaciclib, Milciclib, <t>PHA-793887,</t> AT7519. 3D model created using SwissDock.
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    Structural basis of CDK5/p25 inhibition by pyrazole-based kinase inhibitors. (A) Close-up view of the ATP-binding pocket of the CDK5/p25 complex (chain A: red; chain D: blue) with Dinaciclib (cyan) bound. Key residues Leu83 and Asp86 (pink sticks) form hydrogen bonds (orange lines, distances in Å) with the inhibitor’s heterocyclic core and substituents. The surrounding protein surface is rendered semi-transparently in pink to highlight the binding cleft. (B) Global view of the CDK5/p25–Dinaciclib complex. Chain A (CDK5) is depicted as red ribbons, chain D (p25) as blue ribbons, and the molecular surface is shown in pink to delineate the active site region. Dinaciclib (cyan) occupies the canonical ATP-binding site between the N- and C-terminal lobes, consistent with its mechanism as a competitive ATP-mimetic inhibitor. (C) Chemical structures of representative pyrazole derivatives: Dinaciclib, Milciclib, <t>PHA-793887,</t> AT7519. 3D model created using SwissDock.
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    Structural basis of CDK5/p25 inhibition by pyrazole-based kinase inhibitors. (A) Close-up view of the ATP-binding pocket of the CDK5/p25 complex (chain A: red; chain D: blue) with Dinaciclib (cyan) bound. Key residues Leu83 and Asp86 (pink sticks) form hydrogen bonds (orange lines, distances in Å) with the inhibitor’s heterocyclic core and substituents. The surrounding protein surface is rendered semi-transparently in pink to highlight the binding cleft. (B) Global view of the CDK5/p25–Dinaciclib complex. Chain A (CDK5) is depicted as red ribbons, chain D (p25) as blue ribbons, and the molecular surface is shown in pink to delineate the active site region. Dinaciclib (cyan) occupies the canonical ATP-binding site between the N- and C-terminal lobes, consistent with its mechanism as a competitive ATP-mimetic inhibitor. (C) Chemical structures of representative pyrazole derivatives: Dinaciclib, Milciclib, <t>PHA-793887,</t> AT7519. 3D model created using SwissDock.
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    Structural basis of CDK5/p25 inhibition by pyrazole-based kinase inhibitors. (A) Close-up view of the ATP-binding pocket of the CDK5/p25 complex (chain A: red; chain D: blue) with Dinaciclib (cyan) bound. Key residues Leu83 and Asp86 (pink sticks) form hydrogen bonds (orange lines, distances in Å) with the inhibitor’s heterocyclic core and substituents. The surrounding protein surface is rendered semi-transparently in pink to highlight the binding cleft. (B) Global view of the CDK5/p25–Dinaciclib complex. Chain A (CDK5) is depicted as red ribbons, chain D (p25) as blue ribbons, and the molecular surface is shown in pink to delineate the active site region. Dinaciclib (cyan) occupies the canonical ATP-binding site between the N- and C-terminal lobes, consistent with its mechanism as a competitive ATP-mimetic inhibitor. (C) Chemical structures of representative pyrazole derivatives: Dinaciclib, Milciclib, <t>PHA-793887,</t> AT7519. 3D model created using SwissDock.
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    Structural basis of CDK5/p25 inhibition by pyrazole-based kinase inhibitors. (A) Close-up view of the ATP-binding pocket of the CDK5/p25 complex (chain A: red; chain D: blue) with Dinaciclib (cyan) bound. Key residues Leu83 and Asp86 (pink sticks) form hydrogen bonds (orange lines, distances in Å) with the inhibitor’s heterocyclic core and substituents. The surrounding protein surface is rendered semi-transparently in pink to highlight the binding cleft. (B) Global view of the CDK5/p25–Dinaciclib complex. Chain A (CDK5) is depicted as red ribbons, chain D (p25) as blue ribbons, and the molecular surface is shown in pink to delineate the active site region. Dinaciclib (cyan) occupies the canonical ATP-binding site between the N- and C-terminal lobes, consistent with its mechanism as a competitive ATP-mimetic inhibitor. (C) Chemical structures of representative pyrazole derivatives: Dinaciclib, Milciclib, <t>PHA-793887,</t> AT7519. 3D model created using SwissDock.
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    Image Search Results


    Structural basis of CDK5/p25 inhibition by pyrazole-based kinase inhibitors. (A) Close-up view of the ATP-binding pocket of the CDK5/p25 complex (chain A: red; chain D: blue) with Dinaciclib (cyan) bound. Key residues Leu83 and Asp86 (pink sticks) form hydrogen bonds (orange lines, distances in Å) with the inhibitor’s heterocyclic core and substituents. The surrounding protein surface is rendered semi-transparently in pink to highlight the binding cleft. (B) Global view of the CDK5/p25–Dinaciclib complex. Chain A (CDK5) is depicted as red ribbons, chain D (p25) as blue ribbons, and the molecular surface is shown in pink to delineate the active site region. Dinaciclib (cyan) occupies the canonical ATP-binding site between the N- and C-terminal lobes, consistent with its mechanism as a competitive ATP-mimetic inhibitor. (C) Chemical structures of representative pyrazole derivatives: Dinaciclib, Milciclib, PHA-793887, AT7519. 3D model created using SwissDock.

    Journal: Frontiers in Bioengineering and Biotechnology

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    Figure Lengend Snippet: Structural basis of CDK5/p25 inhibition by pyrazole-based kinase inhibitors. (A) Close-up view of the ATP-binding pocket of the CDK5/p25 complex (chain A: red; chain D: blue) with Dinaciclib (cyan) bound. Key residues Leu83 and Asp86 (pink sticks) form hydrogen bonds (orange lines, distances in Å) with the inhibitor’s heterocyclic core and substituents. The surrounding protein surface is rendered semi-transparently in pink to highlight the binding cleft. (B) Global view of the CDK5/p25–Dinaciclib complex. Chain A (CDK5) is depicted as red ribbons, chain D (p25) as blue ribbons, and the molecular surface is shown in pink to delineate the active site region. Dinaciclib (cyan) occupies the canonical ATP-binding site between the N- and C-terminal lobes, consistent with its mechanism as a competitive ATP-mimetic inhibitor. (C) Chemical structures of representative pyrazole derivatives: Dinaciclib, Milciclib, PHA-793887, AT7519. 3D model created using SwissDock.

    Article Snippet: PHA-793887 , Pyrazole derivative , CDK5, CDK2, CDK1 , ATP-competitive; nanomolar potency , Preclinical oncology studies ( ; Verastem, Inc., 2013; ) .

    Techniques: Inhibition, Binding Assay