期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 97, 期 7, 页码 3056-3061出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.97.7.3056
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资金
- NIAID NIH HHS [R37 AI027690, AI 27690, F32 AI009578, AI 09578, R01 AI027690] Funding Source: Medline
- NIGMS NIH HHS [GM 56609] Funding Source: Medline
We have examined amino acid substitutions at residues 115 and 116 in the reverse transcriptase (RT) of HIV-1, A number of properties were examined, including polymerization and processivity on both DNA and RNA templates, strand displacement, ribonucleotide misincorporation, and resistance to nucleoside analogs. The RT variants Tyr-215-Phe and Phe-116-Tyr are similar to wild-type HIV-1 RT in most but not all, respects. In contrast, the RT variant Tyr-115-Val is significantly impaired in polymerase activity compared with wild-type RT; however, Tyr-115-Val is able to incorporate ribonucleotides as well as deoxyribonucleotides during polymerization and is resistant to a variety of nucleoside analogs.
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