An aspartyl protease directs malaria effector proteins to the host cell.
about
That Was Then But This Is Now: Malaria Research in the Time of an Eradication AgendaPlasmodium falciparum Secretome in Erythrocyte and BeyondEukaryotic virulence determinants utilize phosphoinositides at the ER and host cell surfaceFundamental Roles of the Golgi-Associated Toxoplasma Aspartyl Protease, ASP5, at the Host-Parasite InterfaceThe exported protein PbCP1 localises to cleft-like structures in the rodent malaria parasite Plasmodium bergheiPicomolar Inhibition of Plasmepsin V, an Essential Malaria Protease, Achieved Exploiting the Prime RegionTransition of Plasmodium sporozoites into liver stage-like forms is regulated by the RNA binding protein PumilioStructure ofPlasmodium falciparumADP-ribosylation factor 1Structural basis for plasmepsin V inhibition that blocks export of malaria proteins to human erythrocytesPTEX component HSP101 mediates export of diverse malaria effectors into host erythrocytesTrafficking of PfExp1 to the parasitophorous vacuolar membrane of Plasmodium falciparum is independent of protein folding and the PTEX transloconTrafficking of the exported P. falciparum chaperone PfHsp70xAn erythrocyte cytoskeleton-binding motif in exported Plasmodium falciparum proteinsThe Plasmodium falciparum exportome contains non-canonical PEXEL/HT proteinsA conserved domain targets exported PHISTb family proteins to the periphery of Plasmodium infected erythrocytesNew Export Pathway in Plasmodium falciparum-Infected Erythrocytes: Role of the Parasite Group II Chaperonin, PfTRiCInhibition of Plasmepsin V activity demonstrates its essential role in protein export, PfEMP1 display, and survival of malaria parasitesPlasmodium falciparum transfected with ultra bright NanoLuc luciferase offers high sensitivity detection for the screening of growth and cellular trafficking inhibitorsEnzymatic Characterization of Recombinant Food Vacuole Plasmepsin 4 from the Rodent Malaria Parasite Plasmodium bergheiFunctional analysis of the exported type IV HSP40 protein PfGECO in Plasmodium falciparum gametocytesProtein export marks the early phase of gametocytogenesis of the human malaria parasite Plasmodium falciparumExport of virulence proteins by malaria-infected erythrocytes involves remodeling of host actin cytoskeletonSpatial association with PTEX complexes defines regions for effector export into Plasmodium falciparum-infected erythrocytesLong-range repulsion of colloids driven by ion exchange and diffusiophoresisThe aspartic proteinase family of three Phytophthora species.Functional evaluation of Plasmodium export signals in Plasmodium berghei suggests multiple modes of protein exportEvaluation of aminohydantoins as a novel class of antimalarial agents.An exported protein-interacting complex involved in the trafficking of virulence determinants in Plasmodium-infected erythrocytesPhylogenomic analyses of malaria parasites and evolution of their exported proteinsStructural insights into thioredoxin-2: a component of malaria parasite protein secretion machinery.Protease-associated cellular networks in malaria parasite Plasmodium falciparum.Maurer's clefts, the enigma of Plasmodium falciparum.Plasmodium Helical Interspersed Subtelomeric (PHIST) Proteins, at the Center of Host Cell Remodeling.Imperfect duplicate insertions type of mutations in plasmepsin V modulates binding properties of PEXEL motifs of export proteins in Indian Plasmodium vivax.In Silico screening on the three-dimensional model of the Plasmodium vivax SUB1 protease leads to the validation of a novel anti-parasite compoundMalaria parasite clag3 genes determine channel-mediated nutrient uptake by infected red blood cells.The conserved clag multigene family of malaria parasites: essential roles in host-pathogen interactionStructural studies of vacuolar plasmepsinsProteases in malaria parasites - a phylogenomic perspective.Experimental determination of the membrane topology of the Plasmodium protease Plasmepsin V
P2860
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P2860
An aspartyl protease directs malaria effector proteins to the host cell.
description
2010 nî lūn-bûn
@nan
2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
An aspartyl protease directs malaria effector proteins to the host cell.
@ast
An aspartyl protease directs malaria effector proteins to the host cell.
@en
type
label
An aspartyl protease directs malaria effector proteins to the host cell.
@ast
An aspartyl protease directs malaria effector proteins to the host cell.
@en
prefLabel
An aspartyl protease directs malaria effector proteins to the host cell.
@ast
An aspartyl protease directs malaria effector proteins to the host cell.
@en
P2093
P2860
P50
P921
P356
P1433
P1476
An aspartyl protease directs malaria effector proteins to the host cell.
@en
P2093
Anthony N Hodder
Eugene A Kapp
Heather Patsiouras
J Andrew Pearce
Paul R Gilson
Svenja Günther
P2860
P2888
P304
P356
10.1038/NATURE08728
P407
P577
2010-02-01T00:00:00Z
P5875
P6179
1007728912