Mutated K65R recombinant reverse transcriptase of human immunodeficiency virus type 1 shows diminished chain termination in the presence of 2',3'-dideoxycytidine 5'-triphosphate and other drugs

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Phys Rev B | / 24卷 / 2760期
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  • [1] MUTATED K65R RECOMBINANT REVERSE-TRANSCRIPTASE OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 SHOWS DIMINISHED CHAIN TERMINATION IN THE PRESENCE OF 2',3'-DIDEOXYCYTIDINE 5'-TRIPHOSPHATE AND OTHER DRUGS
    GU, ZX
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  • [2] Kinetics and chain termination studies performed with recombinant mutated M184V and K65R HIV reverse transcriptase
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    JOURNAL OF ACQUIRED IMMUNE DEFICIENCY SYNDROMES AND HUMAN RETROVIROLOGY, 1995, 10 : 5 - 5
  • [3] In vitro activity of structurally diverse nucleoside analogs against human immunodeficiency virus type 1 with the K65R mutation in reverse transcriptase
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  • [4] Diminished replicative fitness of primary human immunodeficiency virus type 1 isolates harboring the K65R mutation
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  • [6] Template Usage Is Responsible for the Preferential Acquisition of the K65R Reverse Transcriptase Mutation in Subtype C Variants of Human Immunodeficiency Virus Type 1
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  • [7] RESISTANCE TO 2',3'-DIDEOXYCYTIDINE CONFERRED BY A MUTATION IN CODON-65 OF THE HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 REVERSE-TRANSCRIPTASE
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    ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 1994, 38 (02) : 282 - 287
  • [8] Molecular mechanisms of resistance to human immunodeficiency virus type 1 with reverse transcriptase mutations K65R and K65R+M184V and their effects on enzyme function and viral replication capacity
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