Identification of phosphinate dipeptide analog inhibitors directed against the Plasmodium falciparum M17 leucine aminopeptidase as lead antimalarial compounds.
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Structural basis for the inhibition of the essential Plasmodium falciparum M1 neutral aminopeptidaseStructure of the Plasmodium falciparum M17 aminopeptidase and significance for the design of drugs targeting the neutral exopeptidases.X-ray crystal structures of an orally available aminopeptidase inhibitor, Tosedostat, bound to anti-malarial drug targets PfA-M1 and PfA-M17Aminopeptidase fingerprints, an integrated approach for identification of good substrates and optimal inhibitors.Fingerprinting the substrate specificity of M1 and M17 aminopeptidases of human malaria, Plasmodium falciparum.Emerging principles in protease-based drug discovery.An integrated approach to the ligand binding specificity of Neisseria meningitidis M1 alanine aminopeptidase by fluorogenic substrate profiling, inhibitory studies and molecular modeling.Structure-guided, single-point modifications in the phosphinic dipeptide structure yield highly potent and selective inhibitors of neutral aminopeptidases.Molecular Characterization of Babesia bovis M17 Leucine Aminopeptidase and Inhibition of Babesia Growth by Bestatin.The aminopeptidase inhibitor CHR-2863 is an orally bioavailable inhibitor of murine malaria.Chemical target validation studies of aminopeptidase in malaria parasites using alpha-aminoalkylphosphonate and phosphonopeptide inhibitorsRecent highlights in antimalarial drug resistance and chemotherapy research.Plasmodium falciparum: new molecular targets with potential for antimalarial drug development.Trafficked Proteins-Druggable in Plasmodium falciparum?From crystal to compound: structure-based antimalarial drug discovery.M1 aminopeptidases as drug targets: broad applications or therapeutic niche?Generation of AMBER force field parameters for zinc centres of M1 and M17 family aminopeptidases.Selective inhibition of PfA-M1, over PfA-M17, by an amino-benzosuberone derivative blocks malaria parasites development in vitro and in vivo.Combinatorial multicomponent access to natural-products-inspired peptidomimetics: discovery of selective inhibitors of microbial metallo-aminopeptidases.
P2860
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P2860
Identification of phosphinate dipeptide analog inhibitors directed against the Plasmodium falciparum M17 leucine aminopeptidase as lead antimalarial compounds.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Identification of phosphinate ...... s lead antimalarial compounds.
@en
type
label
Identification of phosphinate ...... s lead antimalarial compounds.
@en
prefLabel
Identification of phosphinate ...... s lead antimalarial compounds.
@en
P2093
P356
P1476
Identification of phosphinate ...... as lead antimalarial compounds
@en
P2093
Artur Mucha
Colin M Stack
Donald L Gardiner
Franka Teuscher
John P Dalton
Jolanta Grembecka
Jonathan Lowther
Katharine R Trenholme
Pawel Kafarski
P304
P356
10.1021/JM070733V
P407
P577
2007-10-26T00:00:00Z