m sodium pyrophosphate Search Results


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  • 99
    Thermo Fisher phosphatase inhibitors
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    Model for <t>ATP-dependent</t> G4 destabilization by RHAU. RHAU (represented by its two RecA-like domains, the conserved C-terminal domain and the N-terminal RSM domain) binds to the G4 substrate in both (i) nucleotide-free and (ii) ATP-bound states. G4 destabilization occurs during (iii and iv) ATP hydrolysis and the following <t>ADP</t> or phosphate release steps. The RHAU–ssDNA binding interface is drawn based on the structure of a closely related DEAH-box helicase ( 29 ). The binding interface of RSM domain with G4 is drawn based on a recent NMR-solved structure ( 26 ).
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    Qiagen lysis buffer
    Model for <t>ATP-dependent</t> G4 destabilization by RHAU. RHAU (represented by its two RecA-like domains, the conserved C-terminal domain and the N-terminal RSM domain) binds to the G4 substrate in both (i) nucleotide-free and (ii) ATP-bound states. G4 destabilization occurs during (iii and iv) ATP hydrolysis and the following <t>ADP</t> or phosphate release steps. The RHAU–ssDNA binding interface is drawn based on the structure of a closely related DEAH-box helicase ( 29 ). The binding interface of RSM domain with G4 is drawn based on a recent NMR-solved structure ( 26 ).
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    Image Search Results


    Model for ATP-dependent G4 destabilization by RHAU. RHAU (represented by its two RecA-like domains, the conserved C-terminal domain and the N-terminal RSM domain) binds to the G4 substrate in both (i) nucleotide-free and (ii) ATP-bound states. G4 destabilization occurs during (iii and iv) ATP hydrolysis and the following ADP or phosphate release steps. The RHAU–ssDNA binding interface is drawn based on the structure of a closely related DEAH-box helicase ( 29 ). The binding interface of RSM domain with G4 is drawn based on a recent NMR-solved structure ( 26 ).

    Journal: Nucleic Acids Research

    Article Title: RHAU helicase stabilizes G4 in its nucleotide-free state and destabilizes G4 upon ATP hydrolysis

    doi: 10.1093/nar/gkw881

    Figure Lengend Snippet: Model for ATP-dependent G4 destabilization by RHAU. RHAU (represented by its two RecA-like domains, the conserved C-terminal domain and the N-terminal RSM domain) binds to the G4 substrate in both (i) nucleotide-free and (ii) ATP-bound states. G4 destabilization occurs during (iii and iv) ATP hydrolysis and the following ADP or phosphate release steps. The RHAU–ssDNA binding interface is drawn based on the structure of a closely related DEAH-box helicase ( 29 ). The binding interface of RSM domain with G4 is drawn based on a recent NMR-solved structure ( 26 ).

    Article Snippet: The ADP·AlF \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{upgreek} \usepackage{mathrsfs} \setlength{\oddsidemargin}{-69pt} \begin{document} }{}$_4^-$\end{document} was prepared by incubating 10 mM ATP-depleted ADP, 50 mM NaF (Sigma 67414) and 10 mM AlCl3 (Sigma 563919) as described previously ( ).

    Techniques: Binding Assay, Nuclear Magnetic Resonance