Attenuation of West Nile Virus NS2B/NS3 Protease by Amino Terminal Copper and Nickel Binding (ATCUN) Peptides

Dataset UNKNOWN
Pinkham, Andrew M.; Yu, Zhen; Cowan, J. A.;
(2018)
  • Publisher: Figshare
  • Related identifiers: doi: 10.1021/acs.jmedchem.7b01409.s003, doi: 10.1021/acs.jmedchem.7b01409.s002
  • Subject: Molecular Biology | West Nile Virus NS 2B Protease | S 2 binding pocket | LC-MS | peptide-based inhibitors | oxidative damage | DNPH-based assay | Amino Terminal Copper | Nickel Binding | copper-binding ATCUN motif | substrate binding | Biochemistry | Pharmacology | attenuating WNVP activity | Peptides West Nile virus NS 2B protease | Biophysics | oxidative chemistry | metallopeptide
    • FOR: 69999 Biological Sciences not elsewhere classified | 60506 Virology | 39999 Chemical Sciences not elsewhere classified

West Nile virus NS2B/NS3 protease (WNVP) is a viable target for the development of antiviral compounds. To that end, catalytic metallopeptides that incorporate the copper-binding ATCUN motif into either the N- or C-terminus of known WNVP targeting peptides h... View more
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