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standard slope dose response function with plateaus  (GraphPad Software Inc)

 
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    GraphPad Software Inc standard slope dose response function with plateaus
    Fungal Cdc14 homologs can be specifically inhibited by a substrate mimetic. ( a ) Structure of the synthetic peptide used for inhibition assays (sequence Glu-Val-pCF 2 Ser-Pro-Thr-Lys-Arg-amide). ( b ) <t>Dose</t> <t>response</t> with the pCF 2 Ser peptide from A and the indicated fungal Cdc14 enzymes using DiFMUP as substrate. Data represent the average of 5 or 6 independent trials. It was not practical to show error bars on the graph, however error values for replicate K i measurements are provided in ( c ). Best fit lines were generated with a <t>standard</t> <t>slope</t> dose response <t>function</t> with plateaus set at 100% and 0% in Graphpad Prism. We did not have enough pCF 2 Ser peptide to perform the full analysis on all 8 plant fungal pathogen homologs. ( c ) Each individual trial from the experiment in ( b ) was fit as described in b to generate IC 50 , from which K i was calculated (see “ ”). Values represent the mean ± standard deviation. ( d ) Comparison of pCF 2 Ser peptide inhibition of human tyrosine phosphatase PTP1B and dual specificity phosphatase VHR to ScCdc14 and human Cdc14A using DiFMUP at the measured K M for each enzyme. Percent activity relative to a no inhibitor control was calculated and plotted. Data are means of 3 independent experiments and error bars are standard deviations. Numbers over the bars are p values from a t- test (unpaired, one-tail) comparing 0 and 200 µM inhibitor data.
    Standard Slope Dose Response Function With Plateaus, 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/result/standard slope dose response function with plateaus/product/GraphPad Software Inc
    Average 90 stars, based on 1 article reviews
    standard slope dose response function with plateaus - by Bioz Stars, 2026-03
    90/100 stars

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    1) Product Images from "Conservation of Cdc14 phosphatase specificity in plant fungal pathogens: implications for antifungal development"

    Article Title: Conservation of Cdc14 phosphatase specificity in plant fungal pathogens: implications for antifungal development

    Journal: Scientific Reports

    doi: 10.1038/s41598-020-68921-3

    Fungal Cdc14 homologs can be specifically inhibited by a substrate mimetic. ( a ) Structure of the synthetic peptide used for inhibition assays (sequence Glu-Val-pCF 2 Ser-Pro-Thr-Lys-Arg-amide). ( b ) Dose response with the pCF 2 Ser peptide from A and the indicated fungal Cdc14 enzymes using DiFMUP as substrate. Data represent the average of 5 or 6 independent trials. It was not practical to show error bars on the graph, however error values for replicate K i measurements are provided in ( c ). Best fit lines were generated with a standard slope dose response function with plateaus set at 100% and 0% in Graphpad Prism. We did not have enough pCF 2 Ser peptide to perform the full analysis on all 8 plant fungal pathogen homologs. ( c ) Each individual trial from the experiment in ( b ) was fit as described in b to generate IC 50 , from which K i was calculated (see “ ”). Values represent the mean ± standard deviation. ( d ) Comparison of pCF 2 Ser peptide inhibition of human tyrosine phosphatase PTP1B and dual specificity phosphatase VHR to ScCdc14 and human Cdc14A using DiFMUP at the measured K M for each enzyme. Percent activity relative to a no inhibitor control was calculated and plotted. Data are means of 3 independent experiments and error bars are standard deviations. Numbers over the bars are p values from a t- test (unpaired, one-tail) comparing 0 and 200 µM inhibitor data.
    Figure Legend Snippet: Fungal Cdc14 homologs can be specifically inhibited by a substrate mimetic. ( a ) Structure of the synthetic peptide used for inhibition assays (sequence Glu-Val-pCF 2 Ser-Pro-Thr-Lys-Arg-amide). ( b ) Dose response with the pCF 2 Ser peptide from A and the indicated fungal Cdc14 enzymes using DiFMUP as substrate. Data represent the average of 5 or 6 independent trials. It was not practical to show error bars on the graph, however error values for replicate K i measurements are provided in ( c ). Best fit lines were generated with a standard slope dose response function with plateaus set at 100% and 0% in Graphpad Prism. We did not have enough pCF 2 Ser peptide to perform the full analysis on all 8 plant fungal pathogen homologs. ( c ) Each individual trial from the experiment in ( b ) was fit as described in b to generate IC 50 , from which K i was calculated (see “ ”). Values represent the mean ± standard deviation. ( d ) Comparison of pCF 2 Ser peptide inhibition of human tyrosine phosphatase PTP1B and dual specificity phosphatase VHR to ScCdc14 and human Cdc14A using DiFMUP at the measured K M for each enzyme. Percent activity relative to a no inhibitor control was calculated and plotted. Data are means of 3 independent experiments and error bars are standard deviations. Numbers over the bars are p values from a t- test (unpaired, one-tail) comparing 0 and 200 µM inhibitor data.

    Techniques Used: Inhibition, Sequencing, Generated, Standard Deviation, Comparison, Activity Assay, Control



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    standard slope dose response function with plateaus  (GraphPad Software Inc)
    90
    GraphPad Software Inc standard slope dose response function with plateaus
    Fungal Cdc14 homologs can be specifically inhibited by a substrate mimetic. ( a ) Structure of the synthetic peptide used for inhibition assays (sequence Glu-Val-pCF 2 Ser-Pro-Thr-Lys-Arg-amide). ( b ) <t>Dose</t> <t>response</t> with the pCF 2 Ser peptide from A and the indicated fungal Cdc14 enzymes using DiFMUP as substrate. Data represent the average of 5 or 6 independent trials. It was not practical to show error bars on the graph, however error values for replicate K i measurements are provided in ( c ). Best fit lines were generated with a <t>standard</t> <t>slope</t> dose response <t>function</t> with plateaus set at 100% and 0% in Graphpad Prism. We did not have enough pCF 2 Ser peptide to perform the full analysis on all 8 plant fungal pathogen homologs. ( c ) Each individual trial from the experiment in ( b ) was fit as described in b to generate IC 50 , from which K i was calculated (see “ ”). Values represent the mean ± standard deviation. ( d ) Comparison of pCF 2 Ser peptide inhibition of human tyrosine phosphatase PTP1B and dual specificity phosphatase VHR to ScCdc14 and human Cdc14A using DiFMUP at the measured K M for each enzyme. Percent activity relative to a no inhibitor control was calculated and plotted. Data are means of 3 independent experiments and error bars are standard deviations. Numbers over the bars are p values from a t- test (unpaired, one-tail) comparing 0 and 200 µM inhibitor data.
    Standard Slope Dose Response Function With Plateaus, 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/result/standard slope dose response function with plateaus/product/GraphPad Software Inc
    Average 90 stars, based on 1 article reviews
    standard slope dose response function with plateaus - by Bioz Stars, 2026-03
    90/100 stars
    		  Buy from Supplier

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    Fungal Cdc14 homologs can be specifically inhibited by a substrate mimetic. ( a ) Structure of the synthetic peptide used for inhibition assays (sequence Glu-Val-pCF 2 Ser-Pro-Thr-Lys-Arg-amide). ( b ) Dose response with the pCF 2 Ser peptide from A and the indicated fungal Cdc14 enzymes using DiFMUP as substrate. Data represent the average of 5 or 6 independent trials. It was not practical to show error bars on the graph, however error values for replicate K i measurements are provided in ( c ). Best fit lines were generated with a standard slope dose response function with plateaus set at 100% and 0% in Graphpad Prism. We did not have enough pCF 2 Ser peptide to perform the full analysis on all 8 plant fungal pathogen homologs. ( c ) Each individual trial from the experiment in ( b ) was fit as described in b to generate IC 50 , from which K i was calculated (see “ ”). Values represent the mean ± standard deviation. ( d ) Comparison of pCF 2 Ser peptide inhibition of human tyrosine phosphatase PTP1B and dual specificity phosphatase VHR to ScCdc14 and human Cdc14A using DiFMUP at the measured K M for each enzyme. Percent activity relative to a no inhibitor control was calculated and plotted. Data are means of 3 independent experiments and error bars are standard deviations. Numbers over the bars are p values from a t- test (unpaired, one-tail) comparing 0 and 200 µM inhibitor data.

    Journal: Scientific Reports

    Article Title: Conservation of Cdc14 phosphatase specificity in plant fungal pathogens: implications for antifungal development

    doi: 10.1038/s41598-020-68921-3

    Figure Lengend Snippet: Fungal Cdc14 homologs can be specifically inhibited by a substrate mimetic. ( a ) Structure of the synthetic peptide used for inhibition assays (sequence Glu-Val-pCF 2 Ser-Pro-Thr-Lys-Arg-amide). ( b ) Dose response with the pCF 2 Ser peptide from A and the indicated fungal Cdc14 enzymes using DiFMUP as substrate. Data represent the average of 5 or 6 independent trials. It was not practical to show error bars on the graph, however error values for replicate K i measurements are provided in ( c ). Best fit lines were generated with a standard slope dose response function with plateaus set at 100% and 0% in Graphpad Prism. We did not have enough pCF 2 Ser peptide to perform the full analysis on all 8 plant fungal pathogen homologs. ( c ) Each individual trial from the experiment in ( b ) was fit as described in b to generate IC 50 , from which K i was calculated (see “ ”). Values represent the mean ± standard deviation. ( d ) Comparison of pCF 2 Ser peptide inhibition of human tyrosine phosphatase PTP1B and dual specificity phosphatase VHR to ScCdc14 and human Cdc14A using DiFMUP at the measured K M for each enzyme. Percent activity relative to a no inhibitor control was calculated and plotted. Data are means of 3 independent experiments and error bars are standard deviations. Numbers over the bars are p values from a t- test (unpaired, one-tail) comparing 0 and 200 µM inhibitor data.

    Article Snippet: Best fit lines were generated with a standard slope dose response function with plateaus set at 100% and 0% in Graphpad Prism.

    Techniques: Inhibition, Sequencing, Generated, Standard Deviation, Comparison, Activity Assay, Control