Skeleton-binding protein 1 functions at the parasitophorous vacuole membrane to traffic PfEMP1 to the Plasmodium falciparum-infected erythrocyte surface
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Plasmodium falciparum Secretome in Erythrocyte and BeyondThe machinery underlying malaria parasite virulence is conserved between rodent and human malaria parasitesThe malaria secretome: from algorithms to essential function in blood stage infectionThe exported protein PbCP1 localises to cleft-like structures in the rodent malaria parasite Plasmodium bergheiIdentification of new PNEPs indicates a substantial non-PEXEL exportome and underpins common features in Plasmodium falciparum protein exportA Plasmodium falciparum PHIST protein binds the virulence factor PfEMP1 and comigrates to knobs on the host cell surfaceStable Translocation Intermediates Jam Global Protein Export in Plasmodium falciparum Parasites and Link the PTEX Component EXP2 with Translocation ActivityExported proteins required for virulence and rigidity of Plasmodium falciparum-infected human erythrocytesCharacterization of the small exported Plasmodium falciparum membrane protein SEMP1A repeat sequence domain of the ring-exported protein-1 of Plasmodium falciparum controls export machinery architecture and virulence protein traffickingHost cell remodeling by pathogens: the exomembrane system in Plasmodium-infected erythrocytesAn erythrocyte vesicle protein exported by the malaria parasite promotes tubovesicular lipid import from the host cell surfacePlasmodium falciparum antigen 332 is a resident peripheral membrane protein of Maurer's cleftsInteractions between Plasmodium falciparum skeleton-binding protein 1 and the membrane skeleton of malaria-infected red blood cellsThe chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosolExport of virulence proteins by malaria-infected erythrocytes involves remodeling of host actin cytoskeletonPTEX is an essential nexus for protein export in malaria parasitesIdentification of a role for the PfEMP1 semi-conserved head structure in protein trafficking to the surface of Plasmodium falciparum infected red blood cells.Default Pathway of var2csa switching and translational repression in Plasmodium falciparumA method for visualizing surface-exposed and internal PfEMP1 adhesion antigens in Plasmodium falciparum infected erythrocytes.An upstream open reading frame controls translation of var2csa, a gene implicated in placental malaria.Dual fluorescence labeling of surface-exposed and internal proteins in erythrocytes infected with the malaria parasite Plasmodium falciparum.Gene copy number variation throughout the Plasmodium falciparum genome.Functional evaluation of Plasmodium export signals in Plasmodium berghei suggests multiple modes of protein exportEvaluation of the antigenic diversity of placenta-binding Plasmodium falciparum variants and the antibody repertoire among pregnant women.An exported protein-interacting complex involved in the trafficking of virulence determinants in Plasmodium-infected erythrocytesAn update on the rapid advances in malaria parasite cell biology.Amplification of P. falciparum Cytoadherence through induction of a pro-adhesive state in host endothelium.Antibody recognition of Plasmodium falciparum infected red blood cells by symptomatic and asymptomatic individuals in the Brazilian Amazon.Surface antigens of Plasmodium falciparum-infected erythrocytes as immune targets and malaria vaccine candidates.Maurer's clefts, the enigma of Plasmodium falciparum.Differences in gene transcriptomic pattern of Plasmodium falciparum in children with cerebral malaria and asymptomatic carriers.Experimental determination of the membrane topology of the Plasmodium protease Plasmepsin VInhibition of dendritic cell maturation by malaria is dose dependent and does not require Plasmodium falciparum erythrocyte membrane protein 1Plasmodium knowlesi Skeleton-Binding Protein 1 Localizes to the 'Sinton and Mulligan' Stipplings in the Cytoplasm of Monkey and Human Erythrocytes.Maurer's clefts of Plasmodium falciparum are secretory organelles that concentrate virulence protein reporters for delivery to the host erythrocyte.Spatial and temporal mapping of the PfEMP1 export pathway in Plasmodium falciparum.Secretion of proteins into host cells by Apicomplexan parasites.Apicomplexa in mammalian cells: trafficking to the parasitophorous vacuole.Role of the Plasmodium export element in trafficking parasite proteins to the infected erythrocyte.
P2860
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P2860
Skeleton-binding protein 1 functions at the parasitophorous vacuole membrane to traffic PfEMP1 to the Plasmodium falciparum-infected erythrocyte surface
description
2006 nî lūn-bûn
@nan
2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Skeleton-binding protein 1 fun ...... m-infected erythrocyte surface
@ast
Skeleton-binding protein 1 fun ...... m-infected erythrocyte surface
@en
type
label
Skeleton-binding protein 1 fun ...... m-infected erythrocyte surface
@ast
Skeleton-binding protein 1 fun ...... m-infected erythrocyte surface
@en
prefLabel
Skeleton-binding protein 1 fun ...... m-infected erythrocyte surface
@ast
Skeleton-binding protein 1 fun ...... m-infected erythrocyte surface
@en
P2093
P2860
P50
P921
P3181
P1433
P1476
Skeleton-binding protein 1 fun ...... m-infected erythrocyte surface
@en
P2093
Matthew T O'Neill
Matthias Marti
Melanie Rug
P2860
P304
P3181
P356
10.1182/BLOOD-2006-08-043364
P407
P577
2006-10-05T00:00:00Z