Targeted gene disruption shows that knobs enable malaria-infected red cells to cytoadhere under physiological shear stress.
about
That Was Then But This Is Now: Malaria Research in the Time of an Eradication AgendaStructural analysis of the Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) intracellular domain reveals a conserved interaction epitopeImpaired cytoadherence of Plasmodium falciparum-infected erythrocytes containing sickle hemoglobinA newly discovered protein export machine in malaria parasitesPlasmodium falciparum Secretome in Erythrocyte and BeyondRAP1 controls rhoptry targeting of RAP2 in the malaria parasite Plasmodium falciparumPlasmodium falciparum merozoite invasion is inhibited by antibodies that target the PfRh2a and b binding domainsParasite Calcineurin Regulates Host Cell Recognition and Attachment by ApicomplexansRheopathologic Consequence of Plasmodium vivax Rosette FormationThe malaria secretome: from algorithms to essential function in blood stage infectionMicrofluidic modeling of cell-cell interactions in malaria pathogenesisPicomolar Inhibition of Plasmepsin V, an Essential Malaria Protease, Achieved Exploiting the Prime RegionStructure ofPlasmodium falciparumADP-ribosylation factor 1Insights into Duffy Binding-like Domains through the Crystal Structure and Function of the Merozoite Surface Protein MSPDBL2 from Plasmodium falciparumA recombinant peptide based on PfEMP-1 blocks and reverses adhesion of malaria-infected red blood cells to CD36 under flowPTEX component HSP101 mediates export of diverse malaria effectors into host erythrocytesThe ring-infected erythrocyte surface antigen (RESA) of Plasmodium falciparum stabilizes spectrin tetramers and suppresses further invasionExpansion of Lysine-rich Repeats in Plasmodium Proteins Generates Novel Localisation Sequences that Target the Periphery of the Host ErythrocyteRoles for two aminopeptidases in vacuolar hemoglobin catabolism in Plasmodium falciparumThe Plasmodium translocon of exported proteins (PTEX) component thioredoxin-2 is important for maintaining normal blood-stage growthFunctional alteration of red blood cells by a megadalton protein of Plasmodium falciparumExported proteins required for virulence and rigidity of Plasmodium falciparum-infected human erythrocytesA conserved domain targets exported PHISTb family proteins to the periphery of Plasmodium infected erythrocytesCharacterization of two putative protein translocation components in the apicoplast of Plasmodium falciparumclag9: A cytoadherence gene in Plasmodium falciparum essential for binding of parasitized erythrocytes to CD36A repeat sequence domain of the ring-exported protein-1 of Plasmodium falciparum controls export machinery architecture and virulence protein traffickingA subset of Plasmodium falciparum SERA genes are expressed and appear to play an important role in the erythrocytic cycleTruncation of merozoite surface protein 3 disrupts its trafficking and that of acidic-basic repeat protein to the surface of Plasmodium falciparum merozoitesCharacterization of Plasmodium falciparum adenylyl cyclase-β and its role in erythrocytic stage parasitesModeling cytoadhesion of Plasmodium falciparum-infected erythrocytes and leukocytes-common principles and distinctive featuresHost cell remodeling by pathogens: the exomembrane system in Plasmodium-infected erythrocytesInteraction of Plasmodium falciparum knob-associated histidine-rich protein (KAHRP) with erythrocyte ankyrin R is required for its attachment to the erythrocyte membraneBiophysics of malarial parasite exit from infected erythrocytesSystematic analysis of FKBP inducible degradation domain tagging strategies for the human malaria parasite Plasmodium falciparumInteractions between Plasmodium falciparum skeleton-binding protein 1 and the membrane skeleton of malaria-infected red blood cellsAn exported heat shock protein 40 associates with pathogenesis-related knobs in Plasmodium falciparum infected erythrocytesPlasmodium falciparum erythrocyte membrane protein 3 (PfEMP3) destabilizes erythrocyte membrane skeletonTargeted mutagenesis of Plasmodium falciparum erythrocyte membrane protein 3 (PfEMP3) disrupts cytoadherence of malaria-infected red blood cellsPlasmodium falciparum Plasmodium helical interspersed subtelomeric proteins contribute to cytoadherence and anchor P. falciparum erythrocyte membrane protein 1 to the host cell cytoskeletonThe Plasmodium falciparum rhoptry protein RhopH3 plays essential roles in host cell invasion and nutrient uptake
P2860
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P2860
Targeted gene disruption shows that knobs enable malaria-infected red cells to cytoadhere under physiological shear stress.
description
1997 nî lūn-bûn
@nan
1997 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Targeted gene disruption shows ...... er physiological shear stress.
@ast
Targeted gene disruption shows ...... er physiological shear stress.
@en
Targeted gene disruption shows ...... er physiological shear stress.
@nl
type
label
Targeted gene disruption shows ...... er physiological shear stress.
@ast
Targeted gene disruption shows ...... er physiological shear stress.
@en
Targeted gene disruption shows ...... er physiological shear stress.
@nl
prefLabel
Targeted gene disruption shows ...... er physiological shear stress.
@ast
Targeted gene disruption shows ...... er physiological shear stress.
@en
Targeted gene disruption shows ...... er physiological shear stress.
@nl
P2093
P1433
P1476
Targeted gene disruption shows ...... der physiological shear stress
@en
P2093
A F Cowman
K M Davern
M E Wickham
R L Coppel
S R Caruana
P304
P356
10.1016/S0092-8674(00)80207-X
P407
P577
1997-04-01T00:00:00Z