During reverse transcription, an RNA polypurine tract (PPT) resists digestion by reverse transcriptase (RT) and primes plus-strand DNA synthesis. In this issue of Chemistry & Biology, Yi-Brunozzi et al. (2008) report structural studies of PPTs, illuminating how they are recognized by RT
Despite extensive study, the mechanism by which retroviral reverse transciptases (RTs) specifically ...
In synthesizing a double-stranded DNA from viral RNA, HIV-1 reverse transcriptase (RT) generates an ...
Despite extensive study, the mechanism by which retroviral reverse transciptases (RTs) specifically ...
During reverse transcription, an RNA polypurine tract (PPT) resists digestion by reverse transcripta...
HIV-1 reverse transcriptase (HIV-1 RT) possesses both DNA polymerase activity and RNase H activity t...
SummaryA purine-rich region of the plus-strand RNA genome of retroviruses and long terminal repeat (...
AbstractThe RNase H cleavages that generate and remove the polypurine tract (PPT) primer during retr...
We have determined the 3.0 A resolution structure of wild-type HIV-1 reverse transcriptase in comple...
Retroviral conversion of single-stranded RNA into double-stranded DNA requires priming for each stra...
AbstractThe recognition and precise cleavage of the polypurine tract (PPT) of the human immunodefici...
catalyzes the hydrolysis of the RNA strand in the hybrid form. The polypurine tract (PPT) in human i...
AbstractA stretch of purine residues, the polypurine tract (PPT), is found in all retroviruses and i...
AbstractBackground: DNA–RNA hybrids are substrates for RNase H. This enzyme catalyzes the hydrolysis...
AbstractThe RNase H cleavages that generate and remove the polypurine tract (PPT) primer during retr...
Despite extensive study, the mechanism by which retroviral reverse transciptases (RTs) specifically ...
Despite extensive study, the mechanism by which retroviral reverse transciptases (RTs) specifically ...
In synthesizing a double-stranded DNA from viral RNA, HIV-1 reverse transcriptase (RT) generates an ...
Despite extensive study, the mechanism by which retroviral reverse transciptases (RTs) specifically ...
During reverse transcription, an RNA polypurine tract (PPT) resists digestion by reverse transcripta...
HIV-1 reverse transcriptase (HIV-1 RT) possesses both DNA polymerase activity and RNase H activity t...
SummaryA purine-rich region of the plus-strand RNA genome of retroviruses and long terminal repeat (...
AbstractThe RNase H cleavages that generate and remove the polypurine tract (PPT) primer during retr...
We have determined the 3.0 A resolution structure of wild-type HIV-1 reverse transcriptase in comple...
Retroviral conversion of single-stranded RNA into double-stranded DNA requires priming for each stra...
AbstractThe recognition and precise cleavage of the polypurine tract (PPT) of the human immunodefici...
catalyzes the hydrolysis of the RNA strand in the hybrid form. The polypurine tract (PPT) in human i...
AbstractA stretch of purine residues, the polypurine tract (PPT), is found in all retroviruses and i...
AbstractBackground: DNA–RNA hybrids are substrates for RNase H. This enzyme catalyzes the hydrolysis...
AbstractThe RNase H cleavages that generate and remove the polypurine tract (PPT) primer during retr...
Despite extensive study, the mechanism by which retroviral reverse transciptases (RTs) specifically ...
Despite extensive study, the mechanism by which retroviral reverse transciptases (RTs) specifically ...
In synthesizing a double-stranded DNA from viral RNA, HIV-1 reverse transcriptase (RT) generates an ...
Despite extensive study, the mechanism by which retroviral reverse transciptases (RTs) specifically ...
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