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curve fitting analyses  (GraphPad Software Inc)


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    GraphPad Software Inc curve fitting analyses
    Curve Fitting Analyses, supplied by GraphPad Software Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/curve+fitting+analyses/curve+fitting+analysis/pm39739807-365-0-16
    Average 90 stars, based on 1 article reviews
    curve fitting analyses - by Bioz Stars, 2026-10
    90/100 stars

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    Related Articles

    other:

    Article Title: SPANXN2 functions a cell migration inhibitor in testicular germ cell tumor cells
    Article Snippet: Curve fitting analyses were performed with GraphPad Prism Software5.0 (GraphPad Software, USA).

    Article Title: Synthesis and biological evaluation of novel SIPI-7623 derivatives as farnesoid X receptor (FXR) antagonists.
    Article Snippet: Most of reported steroidal FXR antagonists are restricted due to low potency.. We described the design and synthesis of novel nonsteroidal scaffold SIPI-7623 derivatives as FXR antagonists.. The most potent compound A-11 (IC50= 7.8 ± 1.1 lM) showed better activity compared to SIPI-7623 (IC50 = 40.8 ± 1.7 lM) and guggulsterone (IC50= 45.9 ± 1.1 lM).

    Article Title: Disparate patterns of thermal adaptation between life stages in temperate vs. tropical Drosophila melanogaster.
    Article Snippet: We conducted these curve fitting analyses in GraphPad Prism 7.

    Article Title: Disparate patterns of thermal adaptation between life stages in temperate vs. tropical Drosophila melanogaster.
    Article Snippet: We conducted these curve fitting analyses in GraphPad Prism 7 for Mac OS X (GraphPad Software, La Jolla, CA, USA).

    Article Title: Dynamic clamping human and rabbit atrial calcium current: narrowing <i>I</i><sub>CaL</sub> window abolishes early afterdepolarizations
    Article Snippet: All statistical and curve fitting analyses were done using Graphpad Prism 7.00.

    Software:

    Article Title: High Expression of lncRNA AFAP1-AS1 Promotes the Progression of Colon Cancer and Predicts Poor Prognosis
    Article Snippet: .. Curve fitting analyses were performed with GraphPad Prism Software (GraphPad Software, San Diego, CA, USA), and the results of the analyses were considered significant if P < 0.05. ..

    Article Title: Epstein-Barr virus-encoded miR-BART6-3p inhibits cancer cell metastasis and invasion by targeting long non-coding RNA LOC553103
    Article Snippet: .. Curve fitting analyses were performed using GraphPad Prism Software (GraphPad Software, San Diego, CA, USA). ..

    IF-P:

    Article Title: High Expression of lncRNA AFAP1-AS1 Promotes the Progression of Colon Cancer and Predicts Poor Prognosis
    Article Snippet: .. Curve fitting analyses were performed with GraphPad Prism Software (GraphPad Software, San Diego, CA, USA), and the results of the analyses were considered significant if P < 0.05. ..

    In Vitro:

    Article Title: Tamsulosin ameliorates bone loss by inhibiting the release of Cl - through wedging into an allosteric site of TMEM16A.
    Article Snippet: With the global population aging at an increasing rate, osteoporosis is emerging as a progressively significant public health concern.. TMEM16A is an important target for osteoporosis, however, the development of potent inhibitors remains challenging due to the poorly understood regulatory mechanisms.. We have uncovered an inhibition mechanism of TMEM16A by presenting its high-resolution cryo-Electron Microscopy (cryo-EM) structure in complex with Tamsulosin, an inhibitor that we identified.

    In Vivo:

    Article Title: Tamsulosin ameliorates bone loss by inhibiting the release of Cl - through wedging into an allosteric site of TMEM16A.
    Article Snippet: With the global population aging at an increasing rate, osteoporosis is emerging as a progressively significant public health concern.. TMEM16A is an important target for osteoporosis, however, the development of potent inhibitors remains challenging due to the poorly understood regulatory mechanisms.. We have uncovered an inhibition mechanism of TMEM16A by presenting its high-resolution cryo-Electron Microscopy (cryo-EM) structure in complex with Tamsulosin, an inhibitor that we identified.



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    Binding and neutralizing activity of humanized anti-Abrin antibody S008. (A) S008 binds to abrin in a dose-dependent manner determined by ELISA. Absorbance values for different antibody concentrations (0.005 to 5 μg/mL) were detected at 450 nm. The EC50 value of S008 was 0.317 μg/mL, while that of 10D8 was 0.553 μg/mL, and EC50 values were calculated using GraphPad <t>Prism’s</t> Nonliner regression (curve fit) of XY analyses; (B) Kinetic analysis of antibody binding to abrin measured by the ForteBio method. Left: 10D8 (KD=0.2836 nmol/L); right: S008 (KD=0.2095 nmol/L). (C) Inhibition rate of protein synthesis induced by diluted recombinant abrin A chain treatment. The IC50 of protein synthesis in vitro was determined to be 0.01 μg/mL; (D) S008 and 10D8 neutralized the A chain and recovered protein synthesis in a dose-dependent manner. Left: luminescence values of 10D8 and S008. Positive control without abrin A chain, negative control without antibodies. (** P < 0.01, *** P < 0.001; ns, no significance). Right: Rates of protein synthesis by 10D8 and S008 were calculated using the equation (RLU of the experimental group)/(RLU of positive control group) ×100%. (E) Effect of different concentration of abrin on cell death. (F) S008 protected both Jurkat (left) and Vero (right) cells against abrin toxicity in a dose-dependent manner.
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    Binding and neutralizing activity of humanized anti-Abrin antibody S008. (A) S008 binds to abrin in a dose-dependent manner determined by ELISA. Absorbance values for different antibody concentrations (0.005 to 5 μg/mL) were detected at 450 nm. The EC50 value of S008 was 0.317 μg/mL, while that of 10D8 was 0.553 μg/mL, and EC50 values were calculated using GraphPad Prism’s Nonliner regression (curve fit) of XY analyses; (B) Kinetic analysis of antibody binding to abrin measured by the ForteBio method. Left: 10D8 (KD=0.2836 nmol/L); right: S008 (KD=0.2095 nmol/L). (C) Inhibition rate of protein synthesis induced by diluted recombinant abrin A chain treatment. The IC50 of protein synthesis in vitro was determined to be 0.01 μg/mL; (D) S008 and 10D8 neutralized the A chain and recovered protein synthesis in a dose-dependent manner. Left: luminescence values of 10D8 and S008. Positive control without abrin A chain, negative control without antibodies. (** P < 0.01, *** P < 0.001; ns, no significance). Right: Rates of protein synthesis by 10D8 and S008 were calculated using the equation (RLU of the experimental group)/(RLU of positive control group) ×100%. (E) Effect of different concentration of abrin on cell death. (F) S008 protected both Jurkat (left) and Vero (right) cells against abrin toxicity in a dose-dependent manner.

    Journal: Frontiers in Immunology

    Article Title: A Novel Humanized Anti-Abrin A Chain Antibody Inhibits Abrin Toxicity In Vitro and In Vivo

    doi: 10.3389/fimmu.2022.831536

    Figure Lengend Snippet: Binding and neutralizing activity of humanized anti-Abrin antibody S008. (A) S008 binds to abrin in a dose-dependent manner determined by ELISA. Absorbance values for different antibody concentrations (0.005 to 5 μg/mL) were detected at 450 nm. The EC50 value of S008 was 0.317 μg/mL, while that of 10D8 was 0.553 μg/mL, and EC50 values were calculated using GraphPad Prism’s Nonliner regression (curve fit) of XY analyses; (B) Kinetic analysis of antibody binding to abrin measured by the ForteBio method. Left: 10D8 (KD=0.2836 nmol/L); right: S008 (KD=0.2095 nmol/L). (C) Inhibition rate of protein synthesis induced by diluted recombinant abrin A chain treatment. The IC50 of protein synthesis in vitro was determined to be 0.01 μg/mL; (D) S008 and 10D8 neutralized the A chain and recovered protein synthesis in a dose-dependent manner. Left: luminescence values of 10D8 and S008. Positive control without abrin A chain, negative control without antibodies. (** P < 0.01, *** P < 0.001; ns, no significance). Right: Rates of protein synthesis by 10D8 and S008 were calculated using the equation (RLU of the experimental group)/(RLU of positive control group) ×100%. (E) Effect of different concentration of abrin on cell death. (F) S008 protected both Jurkat (left) and Vero (right) cells against abrin toxicity in a dose-dependent manner.

    Article Snippet: EC50 values were calculated using GraphPad Prism’s Nonliner regression (curve fit) of XY analyses with the formula Y=Bottom+(Top-Bottom)/(1 + 10^((LogEC50-X) ×HillSlope)).

    Techniques: Binding Assay, Activity Assay, Enzyme-linked Immunosorbent Assay, Inhibition, Recombinant, In Vitro, Positive Control, Negative Control, Concentration Assay

    Binding and neutralizing activity of humanized anti-Abrin antibody S008. (A) S008 binds to abrin in a dose-dependent manner determined by ELISA. Absorbance values for different antibody concentrations (0.005 to 5 μg/mL) were detected at 450 nm. The EC50 value of S008 was 0.317 μg/mL, while that of 10D8 was 0.553 μg/mL, and EC50 values were calculated using GraphPad Prism’s Nonliner regression (curve fit) of XY analyses; (B) Kinetic analysis of antibody binding to abrin measured by the ForteBio method. Left: 10D8 (KD=0.2836 nmol/L); right: S008 (KD=0.2095 nmol/L). (C) Inhibition rate of protein synthesis induced by diluted recombinant abrin A chain treatment. The IC50 of protein synthesis in vitro was determined to be 0.01 μg/mL; (D) S008 and 10D8 neutralized the A chain and recovered protein synthesis in a dose-dependent manner. Left: luminescence values of 10D8 and S008. Positive control without abrin A chain, negative control without antibodies. (** P < 0.01, *** P < 0.001; ns, no significance). Right: Rates of protein synthesis by 10D8 and S008 were calculated using the equation (RLU of the experimental group)/(RLU of positive control group) ×100%. (E) Effect of different concentration of abrin on cell death. (F) S008 protected both Jurkat (left) and Vero (right) cells against abrin toxicity in a dose-dependent manner.

    Journal: Frontiers in Immunology

    Article Title: A Novel Humanized Anti-Abrin A Chain Antibody Inhibits Abrin Toxicity In Vitro and In Vivo

    doi: 10.3389/fimmu.2022.831536

    Figure Lengend Snippet: Binding and neutralizing activity of humanized anti-Abrin antibody S008. (A) S008 binds to abrin in a dose-dependent manner determined by ELISA. Absorbance values for different antibody concentrations (0.005 to 5 μg/mL) were detected at 450 nm. The EC50 value of S008 was 0.317 μg/mL, while that of 10D8 was 0.553 μg/mL, and EC50 values were calculated using GraphPad Prism’s Nonliner regression (curve fit) of XY analyses; (B) Kinetic analysis of antibody binding to abrin measured by the ForteBio method. Left: 10D8 (KD=0.2836 nmol/L); right: S008 (KD=0.2095 nmol/L). (C) Inhibition rate of protein synthesis induced by diluted recombinant abrin A chain treatment. The IC50 of protein synthesis in vitro was determined to be 0.01 μg/mL; (D) S008 and 10D8 neutralized the A chain and recovered protein synthesis in a dose-dependent manner. Left: luminescence values of 10D8 and S008. Positive control without abrin A chain, negative control without antibodies. (** P < 0.01, *** P < 0.001; ns, no significance). Right: Rates of protein synthesis by 10D8 and S008 were calculated using the equation (RLU of the experimental group)/(RLU of positive control group) ×100%. (E) Effect of different concentration of abrin on cell death. (F) S008 protected both Jurkat (left) and Vero (right) cells against abrin toxicity in a dose-dependent manner.

    Article Snippet: IC50 values were calculated using GraphPad Prism’s Nonliner regression (curve fit) of XY analyses with the formula Y=Bottom+(Top-Bottom)/(1 + 10^((LogIC50-X) ×HillSlope)).

    Techniques: Binding Assay, Activity Assay, Enzyme-linked Immunosorbent Assay, Inhibition, Recombinant, In Vitro, Positive Control, Negative Control, Concentration Assay