Reprogramming Caspase‑7 Specificity by Regio-Specific Mutations and Selection Provides Alternate Solutions for Substrate Recognition

E. Hill, Maureen; MacPherson, Derek J.; Wu, Peng; Julien, Olivier; Wells, James A.; Hardy, Jeanne A.;
  • Publisher: Figshare
  • Related identifiers: doi: 10.1021/acschembio.5b00971.s003, doi: 10.1021/acschembio.5b00971.s004, doi: 10.1021/acschembio.5b00971.s002
  • Subject: Molecular Biology | cell types | reprogrammed proteases | caspase | Evolutionary Biology | Selection Provides | protein substrates | lamin C | Biophysics | cell death | site loop | Medicine | intracellular cysteine protease | intracellular protease specificity | binding modes | Computational Biology | Cell Biology | nonobvious mutations | engineer protease specificity | saturation mutagenesis | specificity reprogramming | Biochemistry | Cancer | Substrate Recognition
    • FOR: 110309 Infectious Diseases

The ability to routinely engineer protease specificity can allow us to better understand and modulate their biology for expanded therapeutic and industrial applications. Here, we report a new approach based on a caged green fluorescent protein (CA-GFP) repor... View more
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