Probing the Active Site Steric Flexibility of HIV-1 Reverse Transcriptase: Different Constraints for DNA- versus RNA-Templated Synthesis
Author:
Affiliation:
1. Department of Chemistry, Stanford University, Stanford, California 94305-5080, and Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York 10461
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi702427y
Reference34 articles.
1. Specificity and Mechanism of Error-prone Replication by Human Immunodeficiency Virus-1 Reverse Transcriptase
2. Exploiting Structurally Diverse Nucleoside Analogs as Probes of Reverse Transcription Complexes
3. Effects of Nucleotides and Nucleotide Analogue Inhibitors of HIV-1 Reverse Transcriptase in a Ratchet Model of Polymerase Translocation
4. Comparison of HIV-1 and avian myeloblastosis virus reverse transcriptase fidelity on RNA and DNA templates.
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