Brefeldin A inhibits transport of the glycophorin-binding protein from Plasmodium falciparum into the host erythrocyte.
about
A newly discovered protein export machine in malaria parasitesPlasmodium falciparum AMA1 binds a rhoptry neck protein homologous to TgRON4, a component of the moving junction in Toxoplasma gondiiPlasmodium falciparum Sec24 marks transitional ER that exports a model cargo via a diacidic motifA Plasmodium falciparum dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradationAnalyses of interactions between heparin and the apical surface proteins of Plasmodium falciparumThe signal sequence of exported protein-1 directs the green fluorescent protein to the parasitophorous vacuole of transfected malaria parasitesReturn to sender: use of Plasmodium ER retrieval sequences to study protein transport in the infected erythrocyte and predict putative ER protein familiesEvidence for catalytic roles for Plasmodium falciparum aminopeptidase P in the food vacuole and cytosolpfmdr2 confers heavy metal resistance to Plasmodium falciparumA homologue of N-ethylmaleimide-sensitive factor in the malaria parasite Plasmodium falciparum is exported and localized in vesicular structures in the cytoplasm of infected erythrocytes in the brefeldin A-sensitive pathwayTrafficking of the phosphoprotein PfCRT to the digestive vacuolar membrane in Plasmodium falciparumProteases and chaperones are the most abundant proteins in the parasitophorous vacuole of Plasmodium falciparum-infected erythrocytes.The Plasmodium export element revisitedCatestatin, an endogenous chromogranin A-derived peptide, inhibits in vitro growth of Plasmodium falciparumTrafficking and assembly of the cytoadherence complex in Plasmodium falciparum-infected human erythrocytes.Experimental determination of the membrane topology of the Plasmodium protease Plasmepsin VProtein targeting from malaria parasites to host erythrocytes.A novel alternate secretory pathway for the export of Plasmodium proteins into the host erythrocyte.Protein export from Plasmodium parasites.Knockout of the peroxiredoxin 5 homologue PFAOP does not affect the artemisinin susceptibility of Plasmodium falciparum.Protein sorting in Plasmodium falciparum-infected red blood cells permeabilized with the pore-forming protein streptolysin O.The significant role of the Golgi apparatus in cardiovascular diseases.Parasite-regulated membrane transport processes and metabolic control in malaria-infected erythrocytes.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.Plasmodium falciparum-infected erythrocytes utilize a synthetic truncated ceramide precursor for synthesis and secretion of truncated sphingomyelin.Apicomplexan parasites possess distinct nuclear-encoded, but apicoplast-localized, plant-type ferredoxin-NADP+ reductase and ferredoxin.A point mutation in an unusual Sec7 domain is linked to brefeldin A resistance in a Plasmodium falciparum line generated by drug selection.A nonpermeant biotin derivative gains access to the parasitophorous vacuole in Plasmodium falciparum-infected erythrocytes permeabilized with streptolysin O.A potential novel mechanism for the insertion of a membrane protein revealed by a biochemical analysis of the Plasmodium falciparum cytoadherence molecule PfEMP-1.Export of PfSBP1 to the Plasmodium falciparum Maurer's clefts.The cytosolic glyoxalases of Plasmodium falciparum are dispensable during asexual blood-stage development.Evidence for the involvement of Plasmodium falciparum proteins in the formation of new permeability pathways in the erythrocyte membrane.Protein unfolding is an essential requirement for transport across the parasitophorous vacuolar membrane of Plasmodium falciparum.Trafficking determinants for PfEMP3 export and assembly under the Plasmodium falciparum-infected red blood cell membrane.
P2860
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P2860
Brefeldin A inhibits transport of the glycophorin-binding protein from Plasmodium falciparum into the host erythrocyte.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年学术文章
@wuu
1994年学术文章
@zh-cn
1994年学术文章
@zh-hans
1994年学术文章
@zh-my
1994年学术文章
@zh-sg
1994年學術文章
@yue
1994年學術文章
@zh
1994年學術文章
@zh-hant
name
Brefeldin A inhibits transport ...... rum into the host erythrocyte.
@en
type
label
Brefeldin A inhibits transport ...... rum into the host erythrocyte.
@en
prefLabel
Brefeldin A inhibits transport ...... rum into the host erythrocyte.
@en
P2093
P2860
P356
P1433
P1476
Brefeldin A inhibits transport ...... rum into the host erythrocyte.
@en
P2093
P2860
P304
P356
10.1042/BJ3000821
P407
P478
300 ( Pt 3)
P577
1994-06-01T00:00:00Z