Aquaporin Water and Solute Channels from Malaria Parasites and Other Pathogenic Protozoa
Identifieur interne : 001D72 ( Main/Exploration ); précédent : 001D71; suivant : 001D73Aquaporin Water and Solute Channels from Malaria Parasites and Other Pathogenic Protozoa
Auteurs : Eric Beitz [Allemagne]Source :
- ChemMedChem [ 1860-7179 ] ; 2006-06-12.
English descriptors
- Teeft :
- Amino acid triad, Amino acids, Aqp1, Aquaglyceroporin, Aquaglyceroporins, Aquaporin, Aquaporin pore, Aquaporin water, Aquaporins, Asparagine residues, Available aquaporin, Beitz, Biol, Channel axis, Coli, Coli aqpz, Coli aquaglyceroporin glpf, Coli glpf, Constriction, Crystal structure, Drug resistance, Electrochemical gradient, Extracellular side, Glpf, Glycerol, Human aqp0, Human aqp1, Human aquaporins, Inhibitor, Larger molecules, Malaria parasites, Mutation, Orthodox aquaporins, Parasite, Permeability, Pfaqp, Plasmodium, Point mutations, Pore, Protozoan, Protozoan aquaporins, Single aquaglyceroporin, Solute, Solute channels, Toxoplasma gondii, Trypanosoma cruzi, Verlag gmbh, Water permeability, Weinheim chemmedchem.
Abstract
The treatment of malaria and other such diseases, which are caused by protozoa, is faced with problems from the rapid spread of resistant parasites. Aquaporins, cellular water and solute channels of the parasite–host interface, are potential novel drug targets. Research on protozoan aquaporin physiology and protein structure and function is currently taking up speed.
Url:
DOI: 10.1002/cmdc.200500105
Affiliations:
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Le document en format XML
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