PTEX is an essential nexus for protein export in malaria parasites
about
Recent advances in understanding apicomplexan parasitesPlasmodium falciparum Secretome in Erythrocyte and BeyondPlasmodium Rab5b is secreted to the cytoplasmic face of the tubovesicular network in infected red blood cells together with N-acylated adenylate kinase 2.The machinery underlying malaria parasite virulence is conserved between rodent and human malaria parasitesFundamental Roles of the Golgi-Associated Toxoplasma Aspartyl Protease, ASP5, at the Host-Parasite InterfacePicomolar Inhibition of Plasmepsin V, an Essential Malaria Protease, Achieved Exploiting the Prime RegionStructural basis for plasmepsin V inhibition that blocks export of malaria proteins to human erythrocytesTrafficking of PfExp1 to the parasitophorous vacuolar membrane of Plasmodium falciparum is independent of protein folding and the PTEX transloconProteomic analysis reveals novel proteins associated with the Plasmodium protein exporter PTEX and a loss of complex stability upon truncation of the core PTEX component, PTEX150Trafficking of the exported P. falciparum chaperone PfHsp70xStable Translocation Intermediates Jam Global Protein Export in Plasmodium falciparum Parasites and Link the PTEX Component EXP2 with Translocation ActivityThe Plasmodium falciparum exportome contains non-canonical PEXEL/HT proteinsA repeat sequence domain of the ring-exported protein-1 of Plasmodium falciparum controls export machinery architecture and virulence protein traffickingDiscovery of a novel and conserved Plasmodium falciparum exported protein that is important for adhesion of PfEMP1 at the surface of infected erythrocytesEvidence that the Malaria Parasite Plasmodium falciparum Putative Rhoptry Protein 2 Localizes to the Golgi Apparatus throughout the Erythrocytic CycleHost cell remodeling by pathogens: the exomembrane system in Plasmodium-infected erythrocytesTowards genome-wide experimental genetics in the in vivo malaria model parasite Plasmodium bergheiSuramin inhibits Hsp104 ATPase and disaggregase activityPlasmodium falciparum transfected with ultra bright NanoLuc luciferase offers high sensitivity detection for the screening of growth and cellular trafficking inhibitorsThe chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosolThe Plasmodium falciparum rhoptry protein RhopH3 plays essential roles in host cell invasion and nutrient uptakePlasmodium falciparum parasites deploy RhopH2 into the host erythrocyte to obtain nutrients, grow and replicateExport of virulence proteins by malaria-infected erythrocytes involves remodeling of host actin cytoskeletonThe Plasmodium rhoptry associated protein complex is important for parasitophorous vacuole membrane structure and intraerythrocytic parasite growthHost erythrocyte environment influences the localization of exported protein 2, an essential component of the Plasmodium translocon.Variant Exported Blood-Stage Proteins Encoded by Plasmodium Multigene Families Are Expressed in Liver Stages Where They Are Exported into the Parasitophorous VacuoleThe Plasmodium berghei translocon of exported proteins reveals spatiotemporal dynamics of tubular extensions.An exported protein-interacting complex involved in the trafficking of virulence determinants in Plasmodium-infected erythrocytesMalaria: Protein-export pathway illuminatedExperimental determination of the membrane topology of the Plasmodium protease Plasmepsin VHow do antimalarial drugs reach their intracellular targets?The Toxoplasma Dense Granule Proteins GRA17 and GRA23 Mediate the Movement of Small Molecules between the Host and the Parasitophorous Vacuole.Network-based gene prediction for Plasmodium falciparum malaria towards genetics-based drug discovery.In Vivo Function of PTEX88 in Malaria Parasite Sequestration and Virulence.Plasmodial HSP70s are functionally adapted to the malaria parasite life cycleContrasting Inducible Knockdown of the Auxiliary PTEX Component PTEX88 in P. falciparum and P. berghei Unmasks a Role in Parasite Virulence.Structural mapping of the ClpB ATPases of Plasmodium falciparum: Targeting protein folding and secretion for antimalarial drug designPlasmodium falciparum Protein Microarray Antibody Profiles Correlate With Protection From Symptomatic Malaria in KenyaPlasmodium knowlesi Skeleton-Binding Protein 1 Localizes to the 'Sinton and Mulligan' Stipplings in the Cytoplasm of Monkey and Human Erythrocytes.Plasmodium parasites mount an arrest response to dihydroartemisinin, as revealed by whole transcriptome shotgun sequencing (RNA-seq) and microarray study.
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P2860
PTEX is an essential nexus for protein export in malaria parasites
description
2014 nî lūn-bûn
@nan
2014 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
PTEX is an essential nexus for protein export in malaria parasites
@ast
PTEX is an essential nexus for protein export in malaria parasites
@en
type
label
PTEX is an essential nexus for protein export in malaria parasites
@ast
PTEX is an essential nexus for protein export in malaria parasites
@en
prefLabel
PTEX is an essential nexus for protein export in malaria parasites
@ast
PTEX is an essential nexus for protein export in malaria parasites
@en
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PTEX is an essential nexus for protein export in malaria parasites
@en
P2093
Catherine Q Nie
Jo-Anne Chan
Kathryn Matthews
Ming Kalanon
Natalie A Counihan
Paul R Gilson
Paul R Sanders
Philip J Shaw
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P2888
P304
P3181
P356
10.1038/NATURE13555
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P50
P577
2014-07-31T00:00:00Z
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P6179
1033050459