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non-linear regression curve fit analysis using graphpad prism software version 5.01  (GraphPad Software Inc)

 
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    GraphPad Software Inc non-linear regression curve fit analysis using graphpad prism software version 5.01
    Non Linear Regression Curve Fit Analysis Using Graphpad Prism Software Version 5.01, 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/non-linear regression curve fit analysis using graphpad prism software version 5.01/product/GraphPad Software Inc
    Average 90 stars, based on 1 article reviews
    non-linear regression curve fit analysis using graphpad prism software version 5.01 - by Bioz Stars, 2026-03
    90/100 stars

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    Investigating the ligand binding mode and selectivity with biophysical methods (A) Chemical structures of probe 8 : TAMRA-labeled β-homo-tripeptide. (B) MST dose-response curves for probe 8 binding to DNMT2. (C) Fluorescence polarization assay for probe 6 binding to native DNMT2 (2 μM), DNMT2 (2 μM) preincubated with SAH (100 μM), DNMT2 (2 μM) with tRNA Asp (10 μM), and various related MTase off-targets (all 2 μM). (D) DNMT2-SAH ITC displacement experiment for compound 3 . SAH was titrated to DNMT2 in the absence resp. presence of compound 3 (100 μM), yielding a significant enthalpy reduction. (E) EMSA assay investigates the competition of hit compounds 1 – 5 with the tRNA substrate. Positive control: tRNA+DNMT2 (band at high molecular weights); negative control: only tRNA (band at low molecular weights). Hit compounds 1 – 5 (100 μM) were added to the DNMT2-tRNA complex (10 + 5 μM) and analyzed by native PAGE. No compound was able to dissociate the DNMT2-tRNA complex. Data are represented as mean ± SEM. Uncropped PAGE images can be found in .

    Journal: iScience

    Article Title: DNA-encoded library screening uncovers potent DNMT2 inhibitors targeting a cryptic allosteric binding site

    doi: 10.1016/j.isci.2025.113300

    Figure Lengend Snippet: Investigating the ligand binding mode and selectivity with biophysical methods (A) Chemical structures of probe 8 : TAMRA-labeled β-homo-tripeptide. (B) MST dose-response curves for probe 8 binding to DNMT2. (C) Fluorescence polarization assay for probe 6 binding to native DNMT2 (2 μM), DNMT2 (2 μM) preincubated with SAH (100 μM), DNMT2 (2 μM) with tRNA Asp (10 μM), and various related MTase off-targets (all 2 μM). (D) DNMT2-SAH ITC displacement experiment for compound 3 . SAH was titrated to DNMT2 in the absence resp. presence of compound 3 (100 μM), yielding a significant enthalpy reduction. (E) EMSA assay investigates the competition of hit compounds 1 – 5 with the tRNA substrate. Positive control: tRNA+DNMT2 (band at high molecular weights); negative control: only tRNA (band at low molecular weights). Hit compounds 1 – 5 (100 μM) were added to the DNMT2-tRNA complex (10 + 5 μM) and analyzed by native PAGE. No compound was able to dissociate the DNMT2-tRNA complex. Data are represented as mean ± SEM. Uncropped PAGE images can be found in .

    Article Snippet: Data analysis and displacement curve fitting were accomplished via the MicroCal PEAQ-ITC Analysis Software.

    Techniques: Ligand Binding Assay, Labeling, Binding Assay, Fluorescence, Positive Control, Negative Control, Clear Native PAGE