Role of Residues in the Tryptophan Repeat Motif for HIV-1 Reverse Transcriptase Dimerization
- 23 January 2003
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 326 (2) , 381-396
- https://doi.org/10.1016/s0022-2836(02)01433-x
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- A New Potent HIV-1 Reverse Transcriptase InhibitorJournal of Biological Chemistry, 1999
- Anatomy of hot spots in protein interfacesJournal of Molecular Biology, 1998
- Chimeric HIV-1 and feline immunodeficiency virus reverse transcriptases: critical role of the p51 subunit in the structural integrity of heterodimeric lentiviral DNA polymerasesJournal of Molecular Biology, 1998
- Dimerization Kinetics of HIV-1 and HIV-2 Reverse Transcriptase: A Two Step ProcessJournal of Molecular Biology, 1995
- Characterization of the dimerization process of HIV‐1 reverse transcriptase heterodimer using intrinsic protein fluorescenceFEBS Letters, 1993
- RNase H activity of HIV reverse transcriptases is confined exclusively to the dimeric formsFEBS Letters, 1992
- A novel genetic system to detect protein–protein interactionsNature, 1989
- Site-specific mutagenesis of AIDS virus reverse transcriptaseNature, 1987
- Characterization of Highly Immunogenic p66/p51 as the Reverse Transcriptase of HTLV-III/LAVScience, 1986
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983