A two-compartment model of osmotic lysis in Plasmodium falciparum-infected erythrocytes.
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Erythrocyte G protein as a novel target for malarial chemotherapyThe 'permeome' of the malaria parasite: an overview of the membrane transport proteins of Plasmodium falciparum.Ion and nutrient uptake by malaria parasite-infected erythrocytesSynergistic Malaria Parasite Killing by Two Types of Plasmodial Surface Anion Channel InhibitorsPlasmodium falciparum parasites deploy RhopH2 into the host erythrocyte to obtain nutrients, grow and replicateIdentification of inhibitors that dually target the new permeability pathway and dihydroorotate dehydrogenase in the blood stage of Plasmodium falciparumImproved perfusion conditions for patch-clamp recordings on human erythrocytes.Malaria parasites tolerate a broad range of ionic environments and do not require host cation remodellingProteolysis at a specific extracellular residue implicates integral membrane CLAG3 in malaria parasite nutrient channelsA cell-based high-throughput screen validates the plasmodial surface anion channel as an antimalarial target.Solute transport via the new permeability pathways in Plasmodium falciparum-infected human red blood cells is not consistent with a simple single-channel modelMalaria parasite mutants with altered erythrocyte permeability: a new drug resistance mechanism and important molecular tool.A kinetic fluorescence assay reveals unusual features of Ca⁺⁺ uptake in Plasmodium falciparum-infected erythrocytes.Altered plasmodial surface anion channel activity and in vitro resistance to permeating antimalarial compounds.High guanidinium permeability reveals dehydration-dependent ion selectivity in the plasmodial surface anion channel.The plasmodial surface anion channel is functionally conserved in divergent malaria parasites.Malaria parasite clag3 genes determine channel-mediated nutrient uptake by infected red blood cells.The conserved clag multigene family of malaria parasites: essential roles in host-pathogen interactionSpecific inhibition of the plasmodial surface anion channel by dantroleneA CLAG3 mutation in an amphipathic transmembrane domain alters malaria parasite nutrient channels and confers leupeptin resistance.A blasticidin S-resistant Plasmodium falciparum mutant with a defective plasmodial surface anion channelMicrofluidic approaches to malaria detection.Changes in the plasmodial surface anion channel reduce leupeptin uptake and can confer drug resistance in Plasmodium falciparum-infected erythrocytes.An epigenetic antimalarial resistance mechanism involving parasite genes linked to nutrient uptakeTwo distinct mechanisms of transport through the plasmodial surface anion channel.Complex inheritance of the plasmodial surface anion channel in a Plasmodium falciparum genetic cross.Plasmodial surface anion channel-independent phloridzin resistance in Plasmodium falciparum.Extracellular Methemoglobin Mediated Early ROS Spike Triggers Osmotic Fragility and RBC Destruction: An Insight into the Enhanced Hemolysis During Malaria.Epigenetic switches in clag3 genes mediate blasticidin S resistance in malaria parasites.Plasmodium falciparum-activated chloride channels are defective in erythrocytes from cystic fibrosis patients.Kinetics of ADP dissociation from the trail and lead heads of actomyosin V following the power stroke.Malaria parasite proteins involved in nutrient channels at the host erythrocyte membrane: advances and questions for future research
P2860
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P2860
A two-compartment model of osmotic lysis in Plasmodium falciparum-infected erythrocytes.
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
A two-compartment model of osmotic lysis in Plasmodium falciparum-infected erythrocytes.
@ast
A two-compartment model of osmotic lysis in Plasmodium falciparum-infected erythrocytes.
@en
A two-compartment model of osmotic lysis in Plasmodium falciparum-infected erythrocytes.
@nl
type
label
A two-compartment model of osmotic lysis in Plasmodium falciparum-infected erythrocytes.
@ast
A two-compartment model of osmotic lysis in Plasmodium falciparum-infected erythrocytes.
@en
A two-compartment model of osmotic lysis in Plasmodium falciparum-infected erythrocytes.
@nl
prefLabel
A two-compartment model of osmotic lysis in Plasmodium falciparum-infected erythrocytes.
@ast
A two-compartment model of osmotic lysis in Plasmodium falciparum-infected erythrocytes.
@en
A two-compartment model of osmotic lysis in Plasmodium falciparum-infected erythrocytes.
@nl
P2093
P2860
P1433
P1476
A two-compartment model of osmotic lysis in Plasmodium falciparum-infected erythrocytes.
@en
P2093
Biree Andemariam
Marissa A Wagner
Sanjay A Desai
P2860
P304
P356
10.1016/S0006-3495(03)74836-X
P407
P577
2003-01-01T00:00:00Z