Nucleotide-dependent conformational change governs specificity and analog discrimination by HIV reverse transcriptase

Proceedings of the National Academy of Sciences of the United States of America

Volumn 107, Issue 17, 2010, Pages 7734-7739

  Kellinger, Matthew W ^a   Johnson, Kenneth A ^a  

^a UNIVERSITY OF TEXAS AT AUSTIN   (United States)

Author keywords

Human immunodeficiency virus; Nucleoside analogs; Polymerase fidelity; Pre steady state kinetics; Substrate specificity

Indexed keywords

LAMIVUDINE TRIPHOSPHATE; NUCLEOSIDE ANALOG; RNA DIRECTED DNA POLYMERASE; UNCLASSIFIED DRUG;

ARTICLE; CONFORMATIONAL TRANSITION; ENZYME BINDING; ENZYME KINETICS; ENZYME STRUCTURE; POLYMERIZATION; PRIORITY JOURNAL;

CHROMATOGRAPHY, AFFINITY; CHROMATOGRAPHY, ION EXCHANGE; CYTIDINE TRIPHOSPHATE; DIDEOXYNUCLEOTIDES; DNA PRIMERS; FLUOROMETRY; HIV REVERSE TRANSCRIPTASE; KINETICS; LAMIVUDINE; MODELS, CHEMICAL; MUTAGENESIS; PROTEIN BINDING; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY;

HUMAN IMMUNODEFICIENCY VIRUS;

EID: 77952388742     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0913946107     Document Type: Article

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