about
etramps, a new Plasmodium falciparum gene family coding for developmentally regulated and highly charged membrane proteins located at the parasite-host cell interfaceIdentification and localization of ERD2 in the malaria parasite Plasmodium falciparum: separation from sites of sphingomyelin synthesis and implications for organization of the GolgiThe secretory pathway of protists: spatial and functional organization and evolutionCharacterization of a membrane-associated rhoptry protein of Plasmodium falciparumIntracellular life.The antibiotic micrococcin is a potent inhibitor of growth and protein synthesis in the malaria parasite.In vivo activity of ajoene against rodent malaria.Sphingolipid synthesis as a target for chemotherapy against malaria parasites.Membrane transport in the malaria-infected erythrocyte.Toxoplasma invasion: the parasitophorous vacuole is formed from host cell plasma membrane and pinches off via a fission pore.Analysis of the high molecular weight rhoptry complex of Plasmodium falciparum using monoclonal antibodies.Protein sorting in Plasmodium falciparum-infected red blood cells permeabilized with the pore-forming protein streptolysin O.Brefeldin A inhibits transport of the glycophorin-binding protein from Plasmodium falciparum into the host erythrocyte.Localization of parasite antigens in Cryptosporidium parvum-infected epithelial cells using monoclonal antibodies.Parasite-regulated membrane transport processes and metabolic control in malaria-infected erythrocytes.Endoplasmic reticulum PI(3)P lipid binding targets malaria proteins to the host cell.Biosynthesis, export and processing of a 45 kDa protein detected in membrane clefts of erythrocytes infected with Plasmodium falciparum.PI(3)P-independent and -dependent pathways function together in a vacuolar translocation sequence to target malarial proteins to the host erythrocyte.Plasmodium falciparum-infected erythrocytes utilize a synthetic truncated ceramide precursor for synthesis and secretion of truncated sphingomyelin.Identification of novel membrane structures in Plasmodium falciparum infected erythrocytes.Biosynthesis and maturation of the malaria aspartic hemoglobinases plasmepsins I and II.Organization of ETRAMPs and EXP-1 at the parasite-host cell interface of malaria parasites.Characterization of membrane proteins exported from Plasmodium falciparum into the host erythrocyte.
P2860
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P2860
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Secretory transport in Plasmodium.
@ast
Secretory transport in Plasmodium.
@en
type
label
Secretory transport in Plasmodium.
@ast
Secretory transport in Plasmodium.
@en
prefLabel
Secretory transport in Plasmodium.
@ast
Secretory transport in Plasmodium.
@en
P1476
Secretory transport in Plasmodium.
@en
P2093
Elmendorf HG
P304
P356
10.1016/0169-4758(93)90216-3
P577
1993-03-01T00:00:00Z