The malaria parasite, Plasmodium falciparum, requires large amounts of nutrients to sustain its rapid growth within the human red blood cell. A recently identified ion channel on the surface of the intraerythrocytic parasite may provide direct access to these nutrients in the red blood cell cytosol. Evidence supporting this role was obtained by incorporating this channel into planar lipid bilayers. In bilayers, this channel has conductance and gating properties identical to the in situ channel, passes soluble macromolecules of up to 1400 Da, and functions as a high capacity, low affinity molecular sieve. These properties, remarkably similar to those of a pore on Toxoplasma gondii (another protozoan parasite causing human disease), suggest a...
Current malaria research is geared toward identifying novel targets for malaria chemotherapy because...
The plasmodial surface anion channel (PSAC) increases eryth-rocyte permeability to many solutes in m...
Malaria parasites activate a broad-selectivity ion channel on their host erythrocyte membrane to obt...
The malaria parasite, Plasmodium falciparum, requires large amounts of nutrients to sustain its rapi...
SummaryDevelopment of malaria parasites within vertebrate erythrocytes requires nutrient uptake at t...
AbstractErythrocytes infected with malaria parasites have increased permeability to various solutes....
Plasmodium parasites responsible for the disease malaria reside within erythrocytes. Inside this nic...
AbstractThe properties of the malaria parasite-induced permeability pathways in the host red blood c...
The human malaria parasite Plasmodium falciparum increases red blood cell membrane permeability duri...
AbstractThe human malaria parasite, Plasmodium falciparum, induces in the plasma membrane of its hos...
The pathology of malaria is caused by infection of red blood cells with unicellular Plasmodium paras...
rn al o f P hy si ol og y Until recently, electrophysiological studies on human RBCs have been diffi...
ABSTRACT The plasmodial surface anion channel (PSAC) increases erythrocyte permeability to many solu...
ABSTRACT Malaria parasites increase host erythrocyte permeability to ions and nutrients via a broad-...
AbstractWe recently identified a voltage-dependent anion channel on the surface of human red blood c...
Current malaria research is geared toward identifying novel targets for malaria chemotherapy because...
The plasmodial surface anion channel (PSAC) increases eryth-rocyte permeability to many solutes in m...
Malaria parasites activate a broad-selectivity ion channel on their host erythrocyte membrane to obt...
The malaria parasite, Plasmodium falciparum, requires large amounts of nutrients to sustain its rapi...
SummaryDevelopment of malaria parasites within vertebrate erythrocytes requires nutrient uptake at t...
AbstractErythrocytes infected with malaria parasites have increased permeability to various solutes....
Plasmodium parasites responsible for the disease malaria reside within erythrocytes. Inside this nic...
AbstractThe properties of the malaria parasite-induced permeability pathways in the host red blood c...
The human malaria parasite Plasmodium falciparum increases red blood cell membrane permeability duri...
AbstractThe human malaria parasite, Plasmodium falciparum, induces in the plasma membrane of its hos...
The pathology of malaria is caused by infection of red blood cells with unicellular Plasmodium paras...
rn al o f P hy si ol og y Until recently, electrophysiological studies on human RBCs have been diffi...
ABSTRACT The plasmodial surface anion channel (PSAC) increases erythrocyte permeability to many solu...
ABSTRACT Malaria parasites increase host erythrocyte permeability to ions and nutrients via a broad-...
AbstractWe recently identified a voltage-dependent anion channel on the surface of human red blood c...
Current malaria research is geared toward identifying novel targets for malaria chemotherapy because...
The plasmodial surface anion channel (PSAC) increases eryth-rocyte permeability to many solutes in m...
Malaria parasites activate a broad-selectivity ion channel on their host erythrocyte membrane to obt...