Plasmodium falciparum-activated chloride channels are defective in erythrocytes from cystic fibrosis patients. - Wikidata - awgldk - TriplyDB

Plasmodium falciparum-activated chloride channels are defective in erythrocytes from cystic fibrosis patients.

Plasmodium falciparum-activated chloride channels are defective in erythrocytes from cystic fibrosis patients.

http://www.wikidata.org/entity/Q44695930

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Ion and nutrient uptake by malaria parasite-infected erythrocytes Synergistic Malaria Parasite Killing by Two Types of Plasmodial Surface Anion Channel Inhibitors Malaria Parasite CLAG3, a Protein Linked to Nutrient Channels, Participates in High Molecular Weight Membrane-Associated Complexes in the Infected Erythrocyte Plasmodium falciparum regulatory subunit of cAMP-dependent PKA and anion channel conductance Improved perfusion conditions for patch-clamp recordings on human erythrocytes.Solute transport via the new permeability pathways in Plasmodium falciparum-infected human red blood cells is not consistent with a simple single-channel model Altered plasmodial surface anion channel activity and in vitro resistance to permeating antimalarial compounds.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.Specific inhibition of the plasmodial surface anion channel by dantrolene A blasticidin S-resistant Plasmodium falciparum mutant with a defective plasmodial surface anion channel Toward a unifying model of malaria-induced channel activity.Electrophysiological studies of malaria parasite-infected erythrocytes: current status.Two distinct mechanisms of transport through the plasmodial surface anion channel.Why do malaria parasites increase host erythrocyte permeability?Cyclic nucleotide signalling in malaria parasites.Membrane transport in the malaria parasite and its host erythrocyte.Signaling Strategies of Malaria Parasite for Its Survival, Proliferation, and Infection during Erythrocytic Stage.Plasmodial surface anion channel-independent phloridzin resistance in Plasmodium falciparum.Erythrocytes of humans with cystic fibrosis fail to stimulate nitric oxide synthesis in isolated rabbit lungs.Reduced DIDS-sensitive chloride conductance in Ae1-/- mouse erythrocytes.Babesia and plasmodia increase host erythrocyte permeability through distinct mechanisms.Studying Mechanisms of Eryptosis.Identification and functional characterization of EhClC-A, an Entamoeba histolytica ClC chloride channel located at plasma membrane.Evidence for the involvement of Plasmodium falciparum proteins in the formation of new permeability pathways in the erythrocyte membrane.IADS, a decomposition product of DIDS activates a cation conductance in Xenopus oocytes and human erythrocytes: new compound for the diagnosis of cystic fibrosis.Reduced number of CFTR molecules in erythrocyte plasma membrane of cystic fibrosis patients.

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P2860

Plasmodium falciparum-activated chloride channels are defective in erythrocytes from cystic fibrosis patients.

http://www.wikidata.org/entity/Q44695930

description

2003 nî lūn-bûn

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2003年の論文

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年學術文章

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2003年學術文章

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name

Plasmodium falciparum-activate ...... from cystic fibrosis patients.

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Plasmodium falciparum-activate ...... from cystic fibrosis patients.

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type

label

Plasmodium falciparum-activate ...... from cystic fibrosis patients.

@en

Plasmodium falciparum-activate ...... from cystic fibrosis patients.

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prefLabel

Plasmodium falciparum-activate ...... from cystic fibrosis patients.

@en

Plasmodium falciparum-activate ...... from cystic fibrosis patients.

@nl

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P1433

Journal of Biological Chemistry

P1476

Plasmodium falciparum-activate ...... from cystic fibrosis patients

@en

P2093

Alan W Thomas

http://www.w3.org/2001/XMLSchema#string

Annemarie Van der Wel

http://www.w3.org/2001/XMLSchema#string

Ben C Tilly

http://www.w3.org/2001/XMLSchema#string

Boris M Hogema

http://www.w3.org/2001/XMLSchema#string

Hugo R De Jonge

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Maarten Sinaasappel

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Patrick Verloo

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P2860

Isolation and characterisation of a cAMP-dependent protein kinase catalytic subunit gene from Plasmodium falciparum

Human malaria parasites in continuous culture

ClC-3B, a novel ClC-3 splicing variant that interacts with EBP50 and facilitates expression of CFTR-regulated ORCC

Plasmodium falciparum activates endogenous Cl(-) channels of human erythrocytes by membrane oxidation.

Toxoplasma gondii cyclic GMP-dependent kinase: chemotherapeutic targeting of an essential parasite protein kinase.

Purification and functional reconstitution of the cystic fibrosis transmembrane conductance regulator (CFTR).

A two-compartment model of osmotic lysis in Plasmodium falciparum-infected erythrocytes.

The role of two novel regulatory sites in the activation of the cGMP-dependent protein kinase from Plasmodium falciparum

New permeability pathways induced by the malarial parasite in the membrane of its host erythrocyte: potential routes for targeting of drugs into infected cells.

Generation of cAMP-activated chloride currents by expression of CFTR.

P304

10316-10322

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10.1074/JBC.M311540200

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P433

11

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279

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2003-12-16T00:00:00Z

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14679190

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P921

cystic fibrosis

Plasmodium falciparum