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control atazanavir  (Gilead Sciences)

 
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    Structured Review

    Gilead Sciences control atazanavir
    (A) Superposition of the monomeric unit of M pro (in gray, PDB code 7K40) with FXa (on the left in violet, PDB code 2P16) and thrombin (on the right in purple, PDB code 1KTS). The crystallographic structure of apixaban into FXa structure, dabigatran into thrombin structure, and catalytic dyad of M pro (His-41 and Cys-145 residues) are as spheres in pink, cyan, and orange, respectively. For better interpretation the catalytic water (H 2 O cat ) of M pro is not shown. The enzymatic inhibition profile for apixaban, rivaroxaban, and dabigatran (0, 0.08, 0.16, 0.31, 0.63, 1.25, 2.5, 5.0, and 10 mM) into (B) PL pro (8.19 nM) and (C) M pro (88.8 nM) velocity. The positive controls GRL0617 (PL pro ) and GC376 (M pro ) were used under the same condition of anticoagulants. (D) Michaelis-Menten enzymatic mechanism for M pro without and in the presence of a fixed apixaban or <t>atazanavir</t> concentration (2.5 mM) for different substrate concentrations (0, 0.76, 1.56, 3.12, 6.25, 12.5, 25.0, 50.0, and 100 mM). (E) Enzymatic scheme for the experimental mechanism of M pro inhibition by anticoagulants. Best docking pose (ChemPLP function) for the interaction between M pro (F) substrate, and (G) substrate-apixaban into the active site of protease. Best docking pose (ChemPLP function) for the interaction between the dimer interface of M pro (H) apixaban and rivaroxaban, while (I) shows the selected amino acid residues which interact with apixaban. Substrate, rivaroxaban, dabigatran, and apixaban are in stick representation in beige, green, cyan, and pink, respectively, while the catalytic water (H 2 O cat ) is in sphere. Elements’ color: hydrogen, nitrogen, oxygen, sulfur, and chloro are in white, dark blue, red, yellow, and dark green, respectively.
    Control Atazanavir, supplied by Gilead Sciences, used in various techniques. Bioz Stars score: 99/100, based on 15423 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/control+atazanavir/VEKLURY/bio_rxiv__2021__09__23__461605-46-16-19
    Average 99 stars, based on 15423 article reviews
    control atazanavir - by Bioz Stars, 2026-09
    99/100 stars

    Images

    1) Product Images from "Apixaban, an orally available anticoagulant, inhibits SARS-CoV-2 replication by targeting its major protease in a non-competitive way"

    Article Title: Apixaban, an orally available anticoagulant, inhibits SARS-CoV-2 replication by targeting its major protease in a non-competitive way

    Journal: bioRxiv

    doi: 10.1101/2021.09.23.461605

    (A) Superposition of the monomeric unit of M pro (in gray, PDB code 7K40) with FXa (on the left in violet, PDB code 2P16) and thrombin (on the right in purple, PDB code 1KTS). The crystallographic structure of apixaban into FXa structure, dabigatran into thrombin structure, and catalytic dyad of M pro (His-41 and Cys-145 residues) are as spheres in pink, cyan, and orange, respectively. For better interpretation the catalytic water (H 2 O cat ) of M pro is not shown. The enzymatic inhibition profile for apixaban, rivaroxaban, and dabigatran (0, 0.08, 0.16, 0.31, 0.63, 1.25, 2.5, 5.0, and 10 mM) into (B) PL pro (8.19 nM) and (C) M pro (88.8 nM) velocity. The positive controls GRL0617 (PL pro ) and GC376 (M pro ) were used under the same condition of anticoagulants. (D) Michaelis-Menten enzymatic mechanism for M pro without and in the presence of a fixed apixaban or atazanavir concentration (2.5 mM) for different substrate concentrations (0, 0.76, 1.56, 3.12, 6.25, 12.5, 25.0, 50.0, and 100 mM). (E) Enzymatic scheme for the experimental mechanism of M pro inhibition by anticoagulants. Best docking pose (ChemPLP function) for the interaction between M pro (F) substrate, and (G) substrate-apixaban into the active site of protease. Best docking pose (ChemPLP function) for the interaction between the dimer interface of M pro (H) apixaban and rivaroxaban, while (I) shows the selected amino acid residues which interact with apixaban. Substrate, rivaroxaban, dabigatran, and apixaban are in stick representation in beige, green, cyan, and pink, respectively, while the catalytic water (H 2 O cat ) is in sphere. Elements’ color: hydrogen, nitrogen, oxygen, sulfur, and chloro are in white, dark blue, red, yellow, and dark green, respectively.
    Figure Legend Snippet: (A) Superposition of the monomeric unit of M pro (in gray, PDB code 7K40) with FXa (on the left in violet, PDB code 2P16) and thrombin (on the right in purple, PDB code 1KTS). The crystallographic structure of apixaban into FXa structure, dabigatran into thrombin structure, and catalytic dyad of M pro (His-41 and Cys-145 residues) are as spheres in pink, cyan, and orange, respectively. For better interpretation the catalytic water (H 2 O cat ) of M pro is not shown. The enzymatic inhibition profile for apixaban, rivaroxaban, and dabigatran (0, 0.08, 0.16, 0.31, 0.63, 1.25, 2.5, 5.0, and 10 mM) into (B) PL pro (8.19 nM) and (C) M pro (88.8 nM) velocity. The positive controls GRL0617 (PL pro ) and GC376 (M pro ) were used under the same condition of anticoagulants. (D) Michaelis-Menten enzymatic mechanism for M pro without and in the presence of a fixed apixaban or atazanavir concentration (2.5 mM) for different substrate concentrations (0, 0.76, 1.56, 3.12, 6.25, 12.5, 25.0, 50.0, and 100 mM). (E) Enzymatic scheme for the experimental mechanism of M pro inhibition by anticoagulants. Best docking pose (ChemPLP function) for the interaction between M pro (F) substrate, and (G) substrate-apixaban into the active site of protease. Best docking pose (ChemPLP function) for the interaction between the dimer interface of M pro (H) apixaban and rivaroxaban, while (I) shows the selected amino acid residues which interact with apixaban. Substrate, rivaroxaban, dabigatran, and apixaban are in stick representation in beige, green, cyan, and pink, respectively, while the catalytic water (H 2 O cat ) is in sphere. Elements’ color: hydrogen, nitrogen, oxygen, sulfur, and chloro are in white, dark blue, red, yellow, and dark green, respectively.

    Techniques Used: Inhibition, Concentration Assay

    Antiviral activity of anticoagulants, atazanavir, and remdesivir in Calu-3 cells (densities of 2.0 × 10 5 cells/well) infected with SARS-CoV-2 (MOI 0.1) in 96-well plates. The data is presented as (A) virus production (PFU/mL) and (B) percentage of viral replication inhibition. The data represent means ± SEM of three independent experiments.
    Figure Legend Snippet: Antiviral activity of anticoagulants, atazanavir, and remdesivir in Calu-3 cells (densities of 2.0 × 10 5 cells/well) infected with SARS-CoV-2 (MOI 0.1) in 96-well plates. The data is presented as (A) virus production (PFU/mL) and (B) percentage of viral replication inhibition. The data represent means ± SEM of three independent experiments.

    Techniques Used: Activity Assay, Infection, Inhibition


    Figure Legend Snippet:

    Techniques Used: Concentration Assay



    Similar Products

    control atazanavir  (Gilead Sciences)
    99
    Gilead Sciences control atazanavir
    (A) Superposition of the monomeric unit of M pro (in gray, PDB code 7K40) with FXa (on the left in violet, PDB code 2P16) and thrombin (on the right in purple, PDB code 1KTS). The crystallographic structure of apixaban into FXa structure, dabigatran into thrombin structure, and catalytic dyad of M pro (His-41 and Cys-145 residues) are as spheres in pink, cyan, and orange, respectively. For better interpretation the catalytic water (H 2 O cat ) of M pro is not shown. The enzymatic inhibition profile for apixaban, rivaroxaban, and dabigatran (0, 0.08, 0.16, 0.31, 0.63, 1.25, 2.5, 5.0, and 10 mM) into (B) PL pro (8.19 nM) and (C) M pro (88.8 nM) velocity. The positive controls GRL0617 (PL pro ) and GC376 (M pro ) were used under the same condition of anticoagulants. (D) Michaelis-Menten enzymatic mechanism for M pro without and in the presence of a fixed apixaban or <t>atazanavir</t> concentration (2.5 mM) for different substrate concentrations (0, 0.76, 1.56, 3.12, 6.25, 12.5, 25.0, 50.0, and 100 mM). (E) Enzymatic scheme for the experimental mechanism of M pro inhibition by anticoagulants. Best docking pose (ChemPLP function) for the interaction between M pro (F) substrate, and (G) substrate-apixaban into the active site of protease. Best docking pose (ChemPLP function) for the interaction between the dimer interface of M pro (H) apixaban and rivaroxaban, while (I) shows the selected amino acid residues which interact with apixaban. Substrate, rivaroxaban, dabigatran, and apixaban are in stick representation in beige, green, cyan, and pink, respectively, while the catalytic water (H 2 O cat ) is in sphere. Elements’ color: hydrogen, nitrogen, oxygen, sulfur, and chloro are in white, dark blue, red, yellow, and dark green, respectively.
    Control Atazanavir, supplied by Gilead Sciences, 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/control+atazanavir/VEKLURY/bio_rxiv__2021__09__23__461605-46-16-19
    Average 99 stars, based on 1 article reviews
    control atazanavir - by Bioz Stars, 2026-09
    99/100 stars
    		  Buy from Supplier

    Image Search Results


    (A) Superposition of the monomeric unit of M pro (in gray, PDB code 7K40) with FXa (on the left in violet, PDB code 2P16) and thrombin (on the right in purple, PDB code 1KTS). The crystallographic structure of apixaban into FXa structure, dabigatran into thrombin structure, and catalytic dyad of M pro (His-41 and Cys-145 residues) are as spheres in pink, cyan, and orange, respectively. For better interpretation the catalytic water (H 2 O cat ) of M pro is not shown. The enzymatic inhibition profile for apixaban, rivaroxaban, and dabigatran (0, 0.08, 0.16, 0.31, 0.63, 1.25, 2.5, 5.0, and 10 mM) into (B) PL pro (8.19 nM) and (C) M pro (88.8 nM) velocity. The positive controls GRL0617 (PL pro ) and GC376 (M pro ) were used under the same condition of anticoagulants. (D) Michaelis-Menten enzymatic mechanism for M pro without and in the presence of a fixed apixaban or atazanavir concentration (2.5 mM) for different substrate concentrations (0, 0.76, 1.56, 3.12, 6.25, 12.5, 25.0, 50.0, and 100 mM). (E) Enzymatic scheme for the experimental mechanism of M pro inhibition by anticoagulants. Best docking pose (ChemPLP function) for the interaction between M pro (F) substrate, and (G) substrate-apixaban into the active site of protease. Best docking pose (ChemPLP function) for the interaction between the dimer interface of M pro (H) apixaban and rivaroxaban, while (I) shows the selected amino acid residues which interact with apixaban. Substrate, rivaroxaban, dabigatran, and apixaban are in stick representation in beige, green, cyan, and pink, respectively, while the catalytic water (H 2 O cat ) is in sphere. Elements’ color: hydrogen, nitrogen, oxygen, sulfur, and chloro are in white, dark blue, red, yellow, and dark green, respectively.

    Journal: bioRxiv

    Article Title: Apixaban, an orally available anticoagulant, inhibits SARS-CoV-2 replication by targeting its major protease in a non-competitive way

    doi: 10.1101/2021.09.23.461605

    Figure Lengend Snippet: (A) Superposition of the monomeric unit of M pro (in gray, PDB code 7K40) with FXa (on the left in violet, PDB code 2P16) and thrombin (on the right in purple, PDB code 1KTS). The crystallographic structure of apixaban into FXa structure, dabigatran into thrombin structure, and catalytic dyad of M pro (His-41 and Cys-145 residues) are as spheres in pink, cyan, and orange, respectively. For better interpretation the catalytic water (H 2 O cat ) of M pro is not shown. The enzymatic inhibition profile for apixaban, rivaroxaban, and dabigatran (0, 0.08, 0.16, 0.31, 0.63, 1.25, 2.5, 5.0, and 10 mM) into (B) PL pro (8.19 nM) and (C) M pro (88.8 nM) velocity. The positive controls GRL0617 (PL pro ) and GC376 (M pro ) were used under the same condition of anticoagulants. (D) Michaelis-Menten enzymatic mechanism for M pro without and in the presence of a fixed apixaban or atazanavir concentration (2.5 mM) for different substrate concentrations (0, 0.76, 1.56, 3.12, 6.25, 12.5, 25.0, 50.0, and 100 mM). (E) Enzymatic scheme for the experimental mechanism of M pro inhibition by anticoagulants. Best docking pose (ChemPLP function) for the interaction between M pro (F) substrate, and (G) substrate-apixaban into the active site of protease. Best docking pose (ChemPLP function) for the interaction between the dimer interface of M pro (H) apixaban and rivaroxaban, while (I) shows the selected amino acid residues which interact with apixaban. Substrate, rivaroxaban, dabigatran, and apixaban are in stick representation in beige, green, cyan, and pink, respectively, while the catalytic water (H 2 O cat ) is in sphere. Elements’ color: hydrogen, nitrogen, oxygen, sulfur, and chloro are in white, dark blue, red, yellow, and dark green, respectively.

    Article Snippet: Nevertheless, apixaban was about 5- and 60-fold less potent in vitro in comparison to the positive control atazanavir and remdesivir, respectively , indicating that apixaban shows an interestingly scaffold for the design of novel compounds to increase its antiviral action.

    Techniques: Inhibition, Concentration Assay

    Antiviral activity of anticoagulants, atazanavir, and remdesivir in Calu-3 cells (densities of 2.0 × 10 5 cells/well) infected with SARS-CoV-2 (MOI 0.1) in 96-well plates. The data is presented as (A) virus production (PFU/mL) and (B) percentage of viral replication inhibition. The data represent means ± SEM of three independent experiments.

    Journal: bioRxiv

    Article Title: Apixaban, an orally available anticoagulant, inhibits SARS-CoV-2 replication by targeting its major protease in a non-competitive way

    doi: 10.1101/2021.09.23.461605

    Figure Lengend Snippet: Antiviral activity of anticoagulants, atazanavir, and remdesivir in Calu-3 cells (densities of 2.0 × 10 5 cells/well) infected with SARS-CoV-2 (MOI 0.1) in 96-well plates. The data is presented as (A) virus production (PFU/mL) and (B) percentage of viral replication inhibition. The data represent means ± SEM of three independent experiments.

    Article Snippet: Nevertheless, apixaban was about 5- and 60-fold less potent in vitro in comparison to the positive control atazanavir and remdesivir, respectively , indicating that apixaban shows an interestingly scaffold for the design of novel compounds to increase its antiviral action.

    Techniques: Activity Assay, Infection, Inhibition

    Journal: bioRxiv

    Article Title: Apixaban, an orally available anticoagulant, inhibits SARS-CoV-2 replication by targeting its major protease in a non-competitive way

    doi: 10.1101/2021.09.23.461605

    Figure Lengend Snippet:

    Article Snippet: Nevertheless, apixaban was about 5- and 60-fold less potent in vitro in comparison to the positive control atazanavir and remdesivir, respectively , indicating that apixaban shows an interestingly scaffold for the design of novel compounds to increase its antiviral action.

    Techniques: Concentration Assay