Structural basis for the role of the K65R mutation in HIV-1 reverse transcriptase polymerization, excision antagonism, and tenofovir resistance.
Das K, Bandwar RP, White KL, Feng JY, Sarafianos SG, Tuske S, Tu X, Clark AD, Boyer PL, Hou X, Gaffney BL, Jones RA, Miller MD, Hughes SH, Arnold E
The Journal of biological chemistry (2009), Volume 284, Page 35092
Abstract:
Polymerases:
Topics:
Structure and Structure/Function, Reverse Transcriptase
Status:
new | topics/pols set | partial results | complete | validated |
Results:
Polymerase | Reference | Property | Result | Context |
---|---|---|---|---|
HIV RT | Structural basis for the role of the K65R mutation in HIV-1 reverse transcriptase polymerization, excision antagonism, and tenofovir resistance. | Reverse Transcriptase Activity | Yes | |
HIV RT K65R | Structural basis for the role of the K65R mutation in HIV-1 reverse transcriptase polymerization, excision antagonism, and tenofovir resistance. | Reverse Transcriptase Activity | Yes |