Intersubunit Interactions in Human Cytidine Deaminase

@article{Vincenzetti2003IntersubunitII,
  title={Intersubunit Interactions in Human Cytidine Deaminase},
  author={Silvia Vincenzetti and Stefano Costanzi and Gloria Cristalli and Pierluigi Mariani and B. Quadrini and Natalina Cammertoni and Alberto Vita},
  journal={Nucleosides, Nucleotides \& Nucleic Acids},
  year={2003},
  volume={22},
  pages={1535 - 1538}
}
Abstract In order to design new efficient cytidine based drugs, an intersubunit interactions study related to the active site has been performed on the wild-type cytidine deaminase (CDA) and on the mutant enzyme F137W/W113F. F137 is the homologous to the Bacillus subtilis CDA F125 involved in the subunit interactions. In presence of the dissociating agent SDS, wild-type human CDA dissociate into enzymatically inactive monomers without intermediate forms via a non-cooperative transition… 

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TLDR
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TLDR
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TLDR
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TLDR
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