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itc data analysis module origin 7.0  (OriginLab corp)


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    OriginLab corp itc data analysis module origin 7.0
    Itc Data Analysis Module Origin 7.0, supplied by OriginLab corp, 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/itc+data+analysis+module+origin+7%2E0/itc+data+analysis+software+origin+7+0/pm36519893-54-15-17
    Average 90 stars, based on 1 article reviews
    itc data analysis module origin 7.0 - by Bioz Stars, 2026-09
    90/100 stars

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    Related Articles

    Binding Assay:

    Article Title: Recognition of unmethylated histone H3 lysine 4 links BHC80 to LSD1-mediated gene repression
    Article Snippet: .. Binding constants were calculated by fitting the data using the ITC data analysis module of Origin 7.0 (OriginLab Corporation). ..

    Article Title: Bisubstrate Inhibitors of Nicotinamide N -Methyltransferase (NNMT) with Enhanced Activity
    Article Snippet: .. Binding constants were calculated by fitting the data using the ITC data analysis module in Origin 7.0 (OriginLab Corp.). .. Docking computations were performed using Autodock 4.2.

    Article Title: Discovery of a Potent and Selective Fragment-like Inhibitor of Methyllysine Reader Protein Spindlin 1 (SPIN1).
    Article Snippet: .. Binding constants were calculated by fitting the data using the ITC data analysis module in Origin 7.0 (OriginLab Corp.). ..

    Article Title: Functional Analysis of a Methyltransferase Involved in Anthocyanin Biosynthesis from Blueberries ( Vaccinium corymbosum ).
    Article Snippet: Anthocyanins are natural water-soluble pigments that widely exist in plants, with various biological activities, including antioxidant, anti-obesity, and anti-diabetic activities.. Currently, monomeric anthocyanins are mainly obtained through natural sources, which limits their availability.. In the biosynthesis of anthocyanins, anthocyanin methyltransferases are recognized to play important roles in the water solubility and structural stability of anthocyanins.

    other:


    Article Title: Tudor domains of the PRC2 components PHF1 and PHF19 selectively bind to histone H3K36me3.
    Article Snippet: 0006-291X/$ see front matter 2012 Elsevier Inc. A http://dx.doi.org/10.1016/j.bbrc.2012.11.116 ⇑ Corresponding author at: Structural Genomics Toronto, 101 College St., Toronto, Ontario M5G 1L7, C E-mail address: jr.min@utoronto.ca (J. Min).. PRC2 is the major H3K27 methyltransferase and is responsible for maintaining repressed gene expression patterns throughout development.. It contains four core components: EZH2, EED, SUZ12 and RbAp46/48 and some cell-type specific components.



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    The hMEX-3C KH domains bind the MRE10 RNA. A, sequence alignment of the KH domains of human MEX-3C and C. elegans MEX-3. Conserved residues are highlighted in gray. The GXXG motif is indicated by a red dashed box. The secondary structure elements of human MEX-3C KH domain assigned on the basis of the X-ray structure are shown at the top. B, the domain architecture of human MEX-3C and the sequence of MRE10 RNA. The black lines represent the hMEX-3C constructs used for <t>ITC</t> and structure determination. C, the ITC fitting result of hMEX-3C KH1/2 domains with MRE10 RNA. D, the ITC fitting results of individual hMEX-3C KH domain with MRE10a or MRE10b.
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    The hMEX-3C KH domains bind the MRE10 RNA. A, sequence alignment of the KH domains of human MEX-3C and C. elegans MEX-3. Conserved residues are highlighted in gray. The GXXG motif is indicated by a red dashed box. The secondary structure elements of human MEX-3C KH domain assigned on the basis of the X-ray structure are shown at the top. B, the domain architecture of human MEX-3C and the sequence of MRE10 RNA. The black lines represent the hMEX-3C constructs used for ITC and structure determination. C, the ITC fitting result of hMEX-3C KH1/2 domains with MRE10 RNA. D, the ITC fitting results of individual hMEX-3C KH domain with MRE10a or MRE10b.

    Journal: The Journal of Biological Chemistry

    Article Title: The human RNA-binding protein and E3 ligase MEX-3C binds the MEX-3–recognition element (MRE) motif with high affinity

    doi: 10.1074/jbc.M117.797746

    Figure Lengend Snippet: The hMEX-3C KH domains bind the MRE10 RNA. A, sequence alignment of the KH domains of human MEX-3C and C. elegans MEX-3. Conserved residues are highlighted in gray. The GXXG motif is indicated by a red dashed box. The secondary structure elements of human MEX-3C KH domain assigned on the basis of the X-ray structure are shown at the top. B, the domain architecture of human MEX-3C and the sequence of MRE10 RNA. The black lines represent the hMEX-3C constructs used for ITC and structure determination. C, the ITC fitting result of hMEX-3C KH1/2 domains with MRE10 RNA. D, the ITC fitting results of individual hMEX-3C KH domain with MRE10a or MRE10b.

    Article Snippet: Data analysis was done using the ITC data analysis module Origin 7.0 (MicroCal) provided by the manufacturer.

    Techniques: Sequencing, Construct

    The key residues involved in RNA binding by MEX-3C KH domains. A, the ITC fitting curves of the wild-type hMEX-3C KH1/2 domains and its mutants to MRE10 RNA. B, the Kd value histogram of the wild-type KH1/2 domains and its mutants to MRE10. The error bars represent S.D.

    Journal: The Journal of Biological Chemistry

    Article Title: The human RNA-binding protein and E3 ligase MEX-3C binds the MEX-3–recognition element (MRE) motif with high affinity

    doi: 10.1074/jbc.M117.797746

    Figure Lengend Snippet: The key residues involved in RNA binding by MEX-3C KH domains. A, the ITC fitting curves of the wild-type hMEX-3C KH1/2 domains and its mutants to MRE10 RNA. B, the Kd value histogram of the wild-type KH1/2 domains and its mutants to MRE10. The error bars represent S.D.

    Article Snippet: Data analysis was done using the ITC data analysis module Origin 7.0 (MicroCal) provided by the manufacturer.

    Techniques: RNA Binding Assay

    Mutagenesis of MRE10 RNA. A, the MRE10 RNA was mutated systematically, and the Kd value for every single-nucleotide mutation was determined by ITC experiment. The change of standard free energy change is defined as ΔΔG0 = −RTln(1/Kd,mut) − [−RTln(1/Kd,wt)]. The bars represent the ΔΔG0 value, and the single-nucleotide mutants are indicated on the horizontal axis. The broken bars indicate the mutants that can hardly bind to hMEX-3C. B, upper, the RNA sequence of MRE10 and a series of spacing mutants with the background of cytosine are shown. The hMRE motif are shown in bold. Lower, the Kd value for each spacing mutant was determined by ITC experiment. The bars represent the ΔΔG0 value, and the spacing mutants are indicated on the horizontal axis. The error bars represent S.D.

    Journal: The Journal of Biological Chemistry

    Article Title: The human RNA-binding protein and E3 ligase MEX-3C binds the MEX-3–recognition element (MRE) motif with high affinity

    doi: 10.1074/jbc.M117.797746

    Figure Lengend Snippet: Mutagenesis of MRE10 RNA. A, the MRE10 RNA was mutated systematically, and the Kd value for every single-nucleotide mutation was determined by ITC experiment. The change of standard free energy change is defined as ΔΔG0 = −RTln(1/Kd,mut) − [−RTln(1/Kd,wt)]. The bars represent the ΔΔG0 value, and the single-nucleotide mutants are indicated on the horizontal axis. The broken bars indicate the mutants that can hardly bind to hMEX-3C. B, upper, the RNA sequence of MRE10 and a series of spacing mutants with the background of cytosine are shown. The hMRE motif are shown in bold. Lower, the Kd value for each spacing mutant was determined by ITC experiment. The bars represent the ΔΔG0 value, and the spacing mutants are indicated on the horizontal axis. The error bars represent S.D.

    Article Snippet: Data analysis was done using the ITC data analysis module Origin 7.0 (MicroCal) provided by the manufacturer.

    Techniques: Mutagenesis, Sequencing