@ARTICLE{Janssen2014-ws,
  title    = "{DNA-directed} control of enzyme-inhibitor complex formation: a
              modular approach to reversibly switch enzyme activity",
  author   = "Janssen, Brian M G and Engelen, Wouter and Merkx, Maarten",
  abstract = "DNA-templated reversible assembly of an enzyme-inhibitor complex
              is presented as a new and highly modular approach to control
              enzyme activity. TEM1-$\beta$-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.",
  journal  = "ACS Synth Biol",
  volume   =  4,
  number   =  5,
  pages    = "547--553",
  month    =  sep,
  year     =  2014,
  address  = "United States",
  keywords = "bionanotechnology; molecular switch; reporter enzyme;
              self-assembly; $\beta$-lactamase",
  language = "en"
}

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