Argininamide Binding Arrests Global Motions in HIV-1 TAR RNA: Comparison with Mg2+-induced Conformational Stabilization
- 1 April 2004
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 338 (1) , 7-16
Abstract
No abstract availableKeywords
This publication has 49 references indexed in Scilit:
- Probing Motions between Equivalent RNA Domains Using Magnetic Field Induced Residual Dipolar Couplings: Accounting for Correlations between Motions and AlignmentJournal of the American Chemical Society, 2003
- Mg2+-induced Variations in the Conformation and Dynamics of HIV-1 TAR RNA Probed Using NMR Residual Dipolar CouplingsJournal of Molecular Biology, 2003
- Molecular dynamics simulations of biomoleculesNature Structural & Molecular Biology, 2002
- Investigation of RNA-Protein and RNA-Metal Ion Interactions by Electron Paramagnetic Resonance SpectroscopyChemistry & Biology, 2002
- Base flexibility in HIV-2 TAR RNA mapped by solution 15N, 13C NMR relaxationJournal of Molecular Biology, 2002
- How RNA foldsJournal of Molecular Biology, 1999
- Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactionsNature Structural & Molecular Biology, 1998
- Solution structure of the HIV-2 TAR-argininamide complexJournal of Molecular Biology, 1997
- The Structure of the Human Immunodeficiency Virus Type-1 TAR RNA Reveals Principles of RNA Recognition by Tat ProteinJournal of Molecular Biology, 1995
- Trans-activation of human immunodeficiency virus occurs via a bimodal mechanismCell, 1986