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THE STRUCTURE OF PNEUMOCYSTIS CARINII DIHYDROFOLATE REDUCTASE TO 1.9 ANGSTROMS RESOLUTION

The structure of Pneumocystis carinii dihydrofolate reductase to 1.9 A resolution. - Champness JN, Achari A, Ballantine SP, Bryant PK, Delves CJ, Stammers DK Structure (2) 915-24 (1994)
www.ebi.ac.uk

S. aureus F98Y DHFR complexed with TMP

Increased hydrophobic interactions of iclaprim with Staphylococcus aureus dihydrofolate reductase are responsible for the increase in affinity and antibacterial activity. - Oefner C, Dale-Glenn E J Antimicrob Chemother (63) 687-98 (2009)
www.ebi.ac.uk

pcDHFR K37S/F69N double mutant TMP NADPH ternary complex

Kinetic and structural analysis for potent antifolate inhibition of Pneumocystis jirovecii, Pneumocystis carinii, and human dihydrofolate reductases and their active-site variants. - Cody V Antimicrob Agents Chemother (57) 2669-77 (2013)
www.ebi.ac.uk

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Story collected by a student at Yellow Furze school (Yellow Furze, Co. Meath) (no informant identified).
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