Protein unfolding is an essential requirement for transport across the parasitophorous vacuolar membrane of Plasmodium falciparum.
about
A newly discovered protein export machine in malaria parasitesPlasmodium falciparum Secretome in Erythrocyte and BeyondEukaryotic virulence determinants utilize phosphoinositides at the ER and host cell surfaceIdentification of new PNEPs indicates a substantial non-PEXEL exportome and underpins common features in Plasmodium falciparum protein exportTrafficking of PfExp1 to the parasitophorous vacuolar membrane of Plasmodium falciparum is independent of protein folding and the PTEX transloconSubcellular localization of adenylate kinases in Plasmodium falciparumProteomic 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 PfHsp70xAn unusual ERAD-like complex is targeted to the apicoplast of Plasmodium falciparumStable Translocation Intermediates Jam Global Protein Export in Plasmodium falciparum Parasites and Link the PTEX Component EXP2 with Translocation ActivityThe Plasmodium translocon of exported proteins (PTEX) component thioredoxin-2 is important for maintaining normal blood-stage growthThe Plasmodium falciparum exportome contains non-canonical PEXEL/HT proteinsA conserved domain targets exported PHISTb family proteins to the periphery of Plasmodium infected erythrocytesHost cell remodeling by pathogens: the exomembrane system in Plasmodium-infected erythrocytesThe chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosolAn exported heat shock protein 40 associates with pathogenesis-related knobs in Plasmodium falciparum infected erythrocytesHost 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 VacuoleIdentification of a role for the PfEMP1 semi-conserved head structure in protein trafficking to the surface of Plasmodium falciparum infected red blood cells.Spatial association with PTEX complexes defines regions for effector export into Plasmodium falciparum-infected erythrocytesThe Plasmodium berghei translocon of exported proteins reveals spatiotemporal dynamics of tubular extensions.Proteomic analysis of exported chaperone/co-chaperone complexes of P. falciparum reveals an array of complex protein-protein interactionsThe host targeting motif in exported Plasmodium proteins is cleaved in the parasite endoplasmic reticulum.An update on the rapid advances in malaria parasite cell biology.Malaria: Protein-export pathway illuminatedMaurer's clefts, the enigma of Plasmodium falciparum.Plasmodial HSP70s are functionally adapted to the malaria parasite life cycleProbing the Biology of Giardia intestinalis Mitosomes Using In Vivo Enzymatic TaggingStructural mapping of the ClpB ATPases of Plasmodium falciparum: Targeting protein folding and secretion for antimalarial drug designHost targeting of virulence determinants and phosphoinositides in blood stage malaria parasitesAn aspartyl protease defines a novel pathway for export of Toxoplasma proteins into the host cell.Identification of an exported heat shock protein 70 in Plasmodium falciparum.Protein export in malaria parasites: many membranes to cross.Crystal structure and solution characterization of the thioredoxin-2 from Plasmodium falciparum, a constituent of an essential parasitic protein export complex.Protein export in malaria parasites: an update.Plasmodial Hsp40 and Hsp70 chaperones: current and future perspectives.Ticket to ride: export of proteins to the Plasmodium falciparum-infected erythrocyte.The exported chaperone Hsp70-x supports virulence functions for Plasmodium falciparum blood stage parasites.The aspartyl protease TgASP5 mediates the export of the Toxoplasma GRA16 and GRA24 effectors into host cells.The Exported Chaperone PfHsp70x Is Dispensable for the Plasmodium falciparum Intraerythrocytic Life Cycle.
P2860
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P2860
Protein unfolding is an essential requirement for transport across the parasitophorous vacuolar membrane of Plasmodium falciparum.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh
2008年學術文章
@zh-hant
name
Protein unfolding is an essent ...... rane of Plasmodium falciparum.
@en
Protein unfolding is an essent ...... rane of Plasmodium falciparum.
@nl
type
label
Protein unfolding is an essent ...... rane of Plasmodium falciparum.
@en
Protein unfolding is an essent ...... rane of Plasmodium falciparum.
@nl
prefLabel
Protein unfolding is an essent ...... rane of Plasmodium falciparum.
@en
Protein unfolding is an essent ...... rane of Plasmodium falciparum.
@nl
P2093
P1476
Protein unfolding is an essent ...... rane of Plasmodium falciparum.
@en
P2093
Corinna Hinrichs
Irine Montilla
Jude M Przyborski
Klaus Lingelbach
Nina Gehde
Stefan Charpian
P2860
P304
P356
10.1111/J.1365-2958.2008.06552.X
P407
P577
2008-11-24T00:00:00Z