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- W1999205763 abstract "DNA-templated reversible assembly of an enzyme–inhibitor complex is presented as a new and highly modular approach to control enzyme activity. TEM1-β-lactamase and its inhibitor protein BLIP were conjugated to different oligonucleotides, resulting in enzyme inhibition in the presence of template strand. Formation of a rigid dsDNA linker upon addition of a complementary target strand disrupts the enzyme–inhibitor complex and results in the restoration of enzyme activity, enabling detection of as little as 2 fmol DNA. The noncovalent assembly of the complex allows easy tuning of target and template strands without changing the oligonucleotide-functionalized enzyme and inhibitor domains. Using a panel of eight different template sequences, restoration of enzyme activity was only observed in the presence of the target viral DNA sequence. The use of stable, well-characterized protein domains and the intrinsic modularity of our system should allow easy integration with DNA/RNA-based logic circuits for applications in biomedicine and molecular diagnostics." @default.
- W1999205763 created "2016-06-24" @default.
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- W1999205763 date "2014-09-19" @default.
- W1999205763 modified "2023-10-16" @default.
- W1999205763 title "DNA-Directed Control of Enzyme–Inhibitor Complex Formation: A Modular Approach to Reversibly Switch Enzyme Activity" @default.
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- W1999205763 doi "https://doi.org/10.1021/sb500278z" @default.
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