The structure of Pneumocystis carinii dihydrofolate reductase to 1.9 A resolution.
BACKGROUND: The fungal pathogen Pneumocystis carinii causes a pneumonia which is an opportunistic infection of AIDS patients. Current therapy includes the dihydrofolate reductase (DHFR) inhibitor trimethoprim which is selective but only a relatively weak inhibitor of the enzyme for P. carinii. Deter...
Váldodahkkit: | Champness, J, Achari, A, Ballantine, S, Bryant, P, Delves, C, Stammers, D |
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Materiálatiipa: | Journal article |
Giella: | English |
Almmustuhtton: |
1994
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Geahča maid
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The structure of Pneumocystis carinii dihydrofolate reductase to 1.9 A resolution.
Dahkki: Champness, J, et al.
Almmustuhtton: (1994) -
Preliminary crystallographic data for Pneumocystis carinii dihydrofolate reductase.
Dahkki: Stammers, D, et al.
Almmustuhtton: (1993) -
Refolding of recombinant Pneumocystis carinii dihydrofolate reductase and characterization of the enzyme.
Dahkki: Delves, C, et al.
Almmustuhtton: (1993) -
The binding of trimethoprim to bacterial dihydrofolate reductase.
Dahkki: Baker, D, et al.
Almmustuhtton: (1981) -
Synthesis of 2,4-Diaminopteridines with Bulky Lipophilic Groups at the 6-Position as Inhibitors of Pneumocystis carinii, Toxoplasma gondii, and Mammalian Dihydrofolate Reductase
Dahkki: Rosowsky Andre, et al.
Almmustuhtton: (1997-09-01)