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Plasmodium falciparum glutathione S-transferase—Structural and mechanistic studies on ligand binding and enzyme inhibition
Glutathione S-transferase of the malarial parasite Plasmodium falciparum (PfGST) represents a novel class of GST isoenzymes. Since the architecture of the PfGST substrate binding site differs significantly from its human counterparts and there is only this one isoenzyme present in the parasite, PfGS...
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| Huvudupphovsmän: | , , , , , |
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| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
Cold Spring Harbor Laboratory Press
2006
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2242455/ https://ncbi.nlm.nih.gov/pubmed/16385005 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.051891106 |
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