Hexose permeation pathways in Plasmodium falciparum-infected erythrocytes - Wikidata - awgldk - TriplyDB

Hexose permeation pathways in Plasmodium falciparum-infected erythrocytes

Hexose permeation pathways in Plasmodium falciparum-infected erythrocytes

http://www.wikidata.org/entity/Q37389641

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Genome sequence of the human malaria parasite Plasmodium falciparum Sugar activation and glycosylation in Plasmodium The malaria parasite cation ATPase PfATP4 and its role in the mechanism of action of a new arsenal of antimalarial drugs Biosynthesis of GDP-fucose and other sugar nucleotides in the blood stages of Plasmodium falciparum Comparative characterization of hexose transporters of Plasmodium knowlesi, Plasmodium yoelii and Toxoplasma gondii highlights functional differences within the apicomplexan family Studies with the Plasmodium falciparum hexokinase reveal that PfHT limits the rate of glucose entry into glycolysis Identification and functional analysis of the primary pantothenate transporter, PfPAT, of the human malaria parasite Plasmodium falciparum A lactate and formate transporter in the intraerythrocytic malaria parasite, Plasmodium falciparum Plant homologs of the Plasmodium falciparum chloroquine-resistance transporter, PfCRT, are required for glutathione homeostasis and stress responses A two-compartment model of osmotic lysis in Plasmodium falciparum-infected erythrocytes.Membrane transport in the malaria-infected erythrocyte.A constitutive pan-hexose permease for the Plasmodium life cycle and transgenic models for screening of antimalarial sugar analogs Plasmodial sugar transporters as anti-malarial drug targets and comparisons with other protozoa.Validation of the hexose transporter of Plasmodium falciparum as a novel drug target.Why is the Plasmodium falciparum hexose transporter a promising new drug target?Identification, expression and characterisation of a Babesia bovis hexose transporter.GLUT1-mediated glucose uptake plays a crucial role during Plasmodium hepatic infection.Central carbon metabolism of Plasmodium parasites.Glucose-6-phosphate metabolism in Plasmodium falciparum.Membrane transport in the malaria parasite and its host erythrocyte.Transport proteins of parasitic protists and their role in nutrient salvage.Novel Plasmodium falciparum metabolic network reconstruction identifies shifts associated with clinical antimalarial resistance.Construction and validation of a detailed kinetic model of glycolysis in Plasmodium falciparum.Analysis of the antimalarial drug resistance protein Pfcrt expressed in yeast.New insight into the mechanism of accumulation and intraerythrocytic compartmentation of albitiazolium, a new type of antimalarial.Analysis of Plasmodium vivax hexose transporters and effects of a parasitocidal inhibitor.Characterisation of exogenous folate transport in Plasmodium falciparum.Comparison of effects of green tea catechins on apicomplexan hexose transporters and mammalian orthologues.Glucose transporters in parasitic protozoa.Mutational analysis of the hexose transporter of Plasmodium falciparum and development of a three-dimensional model.Inhibition of hexose transport and abrogation of pH homeostasis in the intraerythrocytic malaria parasite by an O-3-hexose derivative.Phylogeny and Evolution

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P2860

Hexose permeation pathways in Plasmodium falciparum-infected erythrocytes

http://www.wikidata.org/entity/Q37389641

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on August 2000

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Hexose permeation pathways in Plasmodium falciparum-infected erythrocytes

@en

Hexose permeation pathways in Plasmodium falciparum-infected erythrocytes.

@nl

type

label

Hexose permeation pathways in Plasmodium falciparum-infected erythrocytes

@en

Hexose permeation pathways in Plasmodium falciparum-infected erythrocytes.

@nl

prefLabel

Hexose permeation pathways in Plasmodium falciparum-infected erythrocytes

@en

Hexose permeation pathways in Plasmodium falciparum-infected erythrocytes.

@nl

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Hexose permeation pathways in Plasmodium falciparum-infected erythrocytes

@en

P2093

Burchmore RJ

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

Krishna S

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Woodrow CJ

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P2860

QLS motif in transmembrane helix VII of the glucose transporter family interacts with the C-1 position of D-glucose and is involved in substrate selection at the exofacial binding site

Different functional domains of GLUT2 glucose transporter are required for glucose affinity and substrate specificity.

Glucose transporter isoforms GLUT1 and GLUT3 transport dehydroascorbic acid

Sequence and structure of a human glucose transporter

Intraerythrocytic Plasmodium falciparum expresses a high affinity facilitative hexose transporter

Pore size of the malaria parasite's nutrient channel

Site-directed mutagenesis of GLUT1 in helix 7 residue 282 results in perturbation of exofacial ligand binding.

Plasmodium falciparum: in vitro studies of the pharmacodynamic properties of drugs used for the treatment of severe malaria.

The glucose transporter family: structure, function and tissue-specific expression.

Amino acid substitutions at tryptophan 388 and tryptophan 412 of the HepG2 (Glut1) glucose transporter inhibit transport activity and targeting to the plasma membrane in Xenopus oocytes.

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9931-9936

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scholarly article

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10.1073/PNAS.170153097

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18

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2000-08-01T00:00:00Z

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12365740

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10954735

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Plasmodium falciparum

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27630

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