Structural basis for the inhibition of the essential Plasmodium falciparum M1 neutral aminopeptidase
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Structure of the Plasmodium falciparum M17 aminopeptidase and significance for the design of drugs targeting the neutral exopeptidases.Synthesis of New (−)-Bestatin-Based Inhibitor Libraries Reveals a Novel Binding Mode in the S1 Pocket of the Essential Malaria M1 MetalloaminopeptidaseBestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidasesThe X-ray Crystal Structure of Human Aminopeptidase N Reveals a Novel Dimer and the Basis for Peptide ProcessingStructural basis for multifunctional roles of mammalian aminopeptidase NA Novel Family of Soluble Minimal Scaffolds Provides Structural Insight into the Catalytic Domains of Integral Membrane MetallopeptidasesA Naturally Variable Residue in the S1 Subsite of M1 Family Aminopeptidases Modulates Catalytic Properties and Promotes Functional SpecializationX-ray crystal structures of an orally available aminopeptidase inhibitor, Tosedostat, bound to anti-malarial drug targets PfA-M1 and PfA-M17Distribution and biochemical properties of an M1-family aminopeptidase in Plasmodium falciparum indicate a role in vacuolar hemoglobin catabolismEvidence for catalytic roles for Plasmodium falciparum aminopeptidase P in the food vacuole and cytosolThe Plasmodium falciparum malaria M1 alanyl aminopeptidase (PfA-M1): insights of catalytic mechanism and function from MD simulationsIdentification and Validation of a Potent Dual Inhibitor of the P. falciparum M1 and M17 Aminopeptidases Using Virtual ScreeningPurification and functional characterisation of rhiminopeptidase A, a novel aminopeptidase from the venom of Bitis gabonica rhinoceros.CD13 is dispensable for normal hematopoiesis and myeloid cell functions in the mouseAminopeptidase N1 (EtAPN1), an M1 metalloprotease of the apicomplexan parasite Eimeria tenella, participates in parasite development.Clinical proteomics of the neglected human malarial parasite Plasmodium vivax.Fingerprinting the substrate specificity of M1 and M17 aminopeptidases of human malaria, Plasmodium falciparum.An integrated approach to the ligand binding specificity of Neisseria meningitidis M1 alanine aminopeptidase by fluorogenic substrate profiling, inhibitory studies and molecular modeling.1H-NMR metabolite profiles of different strains of Plasmodium falciparum.Structure-guided, single-point modifications in the phosphinic dipeptide structure yield highly potent and selective inhibitors of neutral aminopeptidases.Identification and development of specific inhibitors for insulin-regulated aminopeptidase as a new class of cognitive enhancers.Screening the Medicines for Malaria Venture "Malaria Box" against the Plasmodium falciparum aminopeptidases, M1, M17 and M18.Engagement of the S1, S1' and S2' subsites drives efficient catalysis of peptide bond hydrolysis by the M1-family aminopeptidase from Plasmodium falciparum.The Anopheles-midgut APN1 structure reveals a new malaria transmission-blocking vaccine epitopeThe aminopeptidase inhibitor CHR-2863 is an orally bioavailable inhibitor of murine malaria.Inactivation of Caenorhabditis elegans aminopeptidase DNPP-1 restores endocytic sorting and recycling in tat-1 mutantsPlasmodium falciparum: new molecular targets with potential for antimalarial drug development.Proteases as regulators of pathogenesis: examples from the Apicomplexa.Novel antimalarial drug targets: hope for new antimalarial drugs.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?Exploration of Sitagliptin as a potential inhibitor for the M1 Alanine aminopeptidase enzyme in Plasmodium falciparum using computational docking.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.Modeling of human M1 aminopeptidases for in silico screening of potential Plasmodium falciparum alanine aminopeptidase (PfA-M1) specific inhibitors.Glu121-Lys319 salt bridge between catalytic and N-terminal domains is pivotal for the activity and stability of Escherichia coli aminopeptidase N.Sitagliptin does not inhibit the M1 alanyl aminopeptidase from Plasmodium falciparum.Plasmodium falciparum PfA-M1 aminopeptidase is trafficked via the parasitophorous vacuole and marginally delivered to the food vacuoleCrystal structure of leukotriene A4 hydrolase in complex with kelatorphan, implications for design of zinc metallopeptidase inhibitors.
P2860
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P2860
Structural basis for the inhibition of the essential Plasmodium falciparum M1 neutral aminopeptidase
description
2009 nî lūn-bûn
@nan
2009 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Structural basis for the inhib ...... arum M1 neutral aminopeptidase
@ast
Structural basis for the inhib ...... arum M1 neutral aminopeptidase
@en
Structural basis for the inhib ...... arum M1 neutral aminopeptidase
@nl
type
label
Structural basis for the inhib ...... arum M1 neutral aminopeptidase
@ast
Structural basis for the inhib ...... arum M1 neutral aminopeptidase
@en
Structural basis for the inhib ...... arum M1 neutral aminopeptidase
@nl
prefLabel
Structural basis for the inhib ...... arum M1 neutral aminopeptidase
@ast
Structural basis for the inhib ...... arum M1 neutral aminopeptidase
@en
Structural basis for the inhib ...... arum M1 neutral aminopeptidase
@nl
P2093
P2860
P50
P921
P356
P1476
Structural basis for the inhib ...... arum M1 neutral aminopeptidase
@en
P2093
Artur Mucha
Colin M Stack
Corrine J Porter
Donald L Gardiner
Franka Teuscher
John P Dalton
Jolanta Grembecka
Jonathan Lowther
Katharine R Trenholme
Pawel Kafarski
P2860
P304
P356
10.1073/PNAS.0807398106
P407
P50
P577
2009-02-05T00:00:00Z