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  1. Structures revealing mechanisms of resistance and collateral ...

  2. People also ask
    The proteasome of the malaria parasite Plasmodium falciparum (Pf20S) is an advantageous drug target because its inhibition kills P. falciparum in multiple stages of its life cycle and synergizes with artemisinins.
    Many efforts have been poured into the development of oral Pf20S-selective inhibitors, with some success. Peptide boronate MPI-13 is optimized to be orally bioavailable but is only modestly selective in targeting Pf20S over human constitutive proteasome and non-selective in being equally potent against human immunoproteasome 17.
    At present, however, Pf20S inhibitors that spare both human constitutive (c-20S) and immuno-proteasomes (i-20S) are not orally bioavailable.
    Thus, Pf20S inhibitors hold the potential to reduce the emergence of resistance to and spread of ART resistance. Many efforts have been poured into the development of oral Pf20S-selective inhibitors, with some success.
    By comparing the structures of the Pf20S WT and Pf20S A117D, we unambiguously found that the A117D mutation not only causes a conformational change in the β5 inhibitor binding pockets, but also a substantial conformational change remotely in the β2 active subunit that enhances the binding affinity of a β2 inhibitor.
    The only reported orally bioavailable Pf20S inhibitor with efficacy in a humanized mouse model of malarial infection is a peptide boronate that is only modestly selective for Pf20S over c-20S and has no selectivity over i-20S 17.
  3. PF20S-11.010.T528.20.0.0000.0 | Baumer PF20S Series ...

  4. Improvement of Asparagine Ethylenediamines as Anti-malarial ...

  5. PF20S-11.010.T527.20.0.0000.0 | Baumer PF20S Series ...

  6. 8UD9 - RCSB PDB

  7. PF20S Mag-Mate | Octopart Electronic Components

  8. Selective Plasmodium proteasome inhibitors as novel multi ...

  9. Some results have been removed
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