Conformational changes of HIV reverse transcriptase subunits on formation of the heterodimer. Correlation with kcat and Km
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00150a015
Reference38 articles.
1. HIV-1 reverse transcriptase specifically interacts with the anticodon domain of its cognate primer tRNA.
2. Isolation of a T-Lymphotropic Retrovirus from a Patient at Risk for Acquired Immune Deficiency Syndrome (AIDS)
3. Protein-protein interactions of HIV-1 reverse transcriptase: implication of central and C-terminal regions in subunit binding
4. Denaturation/Refolding of Purified Recombinant HIV Reverse Transcriptase Yields Monomeric Enzyme with High Enzymatic Activity
5. Characterization of Highly Immunogenic p66/p51 as the Reverse Transcriptase of HTLV-III/LAV
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1. Polyols have unique ability to refold protein as compared to other osmolyte types;Biochemistry (Moscow);2017-04
2. Asymmetric conformational maturation of HIV-1 reverse transcriptase;eLife;2015-06-03
3. Selective unfolding of one Ribonuclease H domain of HIV reverse transcriptase is linked to homodimer formation;Nucleic Acids Research;2014-02-25
4. Virion Instability of Human Immunodeficiency Virus Type 1 Reverse Transcriptase (RT) Mutated in the Protease Cleavage Site between RT p51 and the RT RNase H Domain;Journal of Virology;2005-09-15
5. Osmolyte-induced folding enhances tryptic enzyme activity;Archives of Biochemistry and Biophysics;2005-04
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