Binding Kinetics and Affinities of Heterodimeric versus Homodimeric HIV-1 Reverse Transcriptase on DNA–DNA Substrates at the Single-Molecule Level-Reference-Cited by-同舟云学术

Binding Kinetics and Affinities of Heterodimeric versus Homodimeric HIV-1 Reverse Transcriptase on DNA–DNA Substrates at the Single-Molecule Level

Published:2013-02-01 Issue:16 Volume:117 Page:4560-4567
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Marko Ryan A.¹,Liu Hsiao-Wei¹,Ablenas Christopher J.²,Ehteshami Maryam³,Götte Matthias³²⁴,Cosa Gonzalo¹

Affiliation:

1. Department of Chemistry and Center for Self Assembled Chemical Structures (CSACS/CRMAA), McGill University, 801 Sherbrooke Street West, Montreal, QC, H3A 0B8, Canada

2. Department of Biochemistry, McGill University, 3655 Promenade Sir William Osler, Montreal, QC, H3G 1Y6, Canada

3. Department of Microbiology and Immunology, McGill University, 3775 University Street, Montreal, QC, H3A 2B4, Canada

4. Department of Medicine, McGill University, 3655 Promenade Sir William Osler, Montreal, QC, H3G 1Y6, Canada

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp308674g

Reference48 articles.

1. Characterization of Highly Immunogenic p66/p51 as the Reverse Transcriptase of HTLV-III/LAV

2. Enzyme activity gel analysis of human immunodeficiency virus reverse transcriptase.

3. Subunit-selective mutagenesis indicates minimal polymerase activity in heterodimer-associated p51 HIV-1 reverse transcriptase.

4. Crystal Structure at 3.5 Å Resolution of HIV-1 Reverse Transcriptase Complexed with an Inhibitor

5. Structural basis of asymmetry in the human immunodeficiency virus type 1 reverse transcriptase heterodimer.

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