A potential novel mechanism for the insertion of a membrane protein revealed by a biochemical analysis of the Plasmodium falciparum cytoadherence molecule PfEMP-1.
about
Unifying themes in microbial associations with animal and plant hosts described using the gene ontologyAn unusual ERAD-like complex is targeted to the apicoplast of Plasmodium falciparumExported proteins required for virulence and rigidity of Plasmodium falciparum-infected human erythrocytesRON12, a novel Plasmodium-specific rhoptry neck protein important for parasite proliferation.Host cell remodeling by pathogens: the exomembrane system in Plasmodium-infected erythrocytesPlasmodium falciparum antigen 332 is a resident peripheral membrane protein of Maurer's cleftsSkeleton-binding protein 1 functions at the parasitophorous vacuole membrane to traffic PfEMP1 to the Plasmodium falciparum-infected erythrocyte surfaceCell biological characterization of the malaria vaccine candidate trophozoite exported protein 1Export of virulence proteins by malaria-infected erythrocytes involves remodeling of host actin cytoskeletonSubcellular location, phosphorylation and assembly into the motor complex of GAP45 during Plasmodium falciparum schizont developmentTrafficking of the major virulence factor to the surface of transfected P. falciparum-infected erythrocytesA method for visualizing surface-exposed and internal PfEMP1 adhesion antigens in Plasmodium falciparum infected erythrocytes.The Plasmodium falciparum STEVOR multigene family mediates antigenic variation of the infected erythrocyteAn exported protein-interacting complex involved in the trafficking of virulence determinants in Plasmodium-infected erythrocytesMalaria: Protein-export pathway illuminatedMaurer's clefts, the enigma of Plasmodium falciparum.The role of KAHRP domains in knob formation and cytoadherence of P falciparum-infected human erythrocytesDelivery of the malaria virulence protein PfEMP1 to the erythrocyte surface requires cholesterol-rich domains.Transcriptional profiling defines dynamics of parasite tissue sequestration during malaria infectionHypervariability within the Rifin, Stevor and Pfmc-2TM superfamilies in Plasmodium falciparum.A comparative study of the localization and membrane topology of members of the RIFIN, STEVOR and PfMC-2TM protein families in Plasmodium falciparum-infected erythrocytesSerum lipoproteins promote efficient presentation of the malaria virulence protein PfEMP1 at the erythrocyte surface.Six genes are preferentially transcribed by the circulating and sequestered forms of Plasmodium falciparum parasites that infect pregnant women.A Maurer's cleft-associated protein is essential for expression of the major malaria virulence antigen on the surface of infected red blood cellsProtein targeting from malaria parasites to host erythrocytes.Signal-mediated export of proteins from the malaria parasite to the host erythrocyte.The exported Plasmodium berghei protein IBIS1 delineates membranous structures in infected red blood cells.Maurer's clefts of Plasmodium falciparum are secretory organelles that concentrate virulence protein reporters for delivery to the host erythrocyte.Variant antigen gene expression in malaria.Protein export from Plasmodium parasites.Plasmodium falciparum STEVOR proteins are highly expressed in patient isolates and located in the surface membranes of infected red blood cells and the apical tips of merozoites.Protein transport across the parasitophorous vacuole of Plasmodium falciparum: into the great wide open.Spatial and temporal mapping of the PfEMP1 export pathway in Plasmodium falciparum.Protein export in malaria parasites: many membranes to cross.Role of the Plasmodium export element in trafficking parasite proteins to the infected erythrocyte.Human erythrocyte remodelling during Plasmodium falciparum malaria parasite growth and egress.Protein export in malaria parasites: an update.Ticket to ride: export of proteins to the Plasmodium falciparum-infected erythrocyte.Trafficking of STEVOR to the Maurer's clefts in Plasmodium falciparum-infected erythrocytes.Diversion at the ER: How Plasmodium falciparum exports proteins into host erythrocytes.
P2860
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P2860
A potential novel mechanism for the insertion of a membrane protein revealed by a biochemical analysis of the Plasmodium falciparum cytoadherence molecule PfEMP-1.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
A potential novel mechanism fo ...... ytoadherence molecule PfEMP-1.
@en
A potential novel mechanism fo ...... ytoadherence molecule PfEMP-1.
@nl
type
label
A potential novel mechanism fo ...... ytoadherence molecule PfEMP-1.
@en
A potential novel mechanism fo ...... ytoadherence molecule PfEMP-1.
@nl
prefLabel
A potential novel mechanism fo ...... ytoadherence molecule PfEMP-1.
@en
A potential novel mechanism fo ...... ytoadherence molecule PfEMP-1.
@nl
P1476
A potential novel mechanism fo ...... ytoadherence molecule PfEMP-1.
@en
P2093
Janni Papakrivos
Klaus Lingelbach
P2860
P304
P356
10.1111/J.1365-2958.2004.04468.X
P407
P577
2005-02-01T00:00:00Z