Thermodynamics Reveal that Helix Four in the NLS of NF-κB p65 Anchors IκBα, Forming a Very Stable Complex
- 7 July 2006
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 360 (2), 421-434
- https://doi.org/10.1016/j.jmb.2006.05.014
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- Molecular Recognition via Coupled Folding and Binding in a TPR DomainJournal of Molecular Biology, 2005
- Heat Capacity Effects of Water Molecules and Ions at a Protein–DNA InterfaceJournal of Molecular Biology, 2004
- Dissection of the Karyopherin α Nuclear Localization Signal (NLS)-binding GrooveJournal of Biological Chemistry, 2003
- Solvent Exposed Non-contacting Amino Acids Play a Critical Role in NF-κB/IκBα Complex FormationJournal of Molecular Biology, 2002
- The Binding Energetics of First- and Second-Generation HIV-1 Protease Inhibitors: Implications for Drug DesignArchives of Biochemistry and Biophysics, 2001
- Mechanism of IκBα Binding to NF-κB DimersOnline Journal of Public Health Informatics, 2000
- Signal-dependent and -independent Degradation of Free and NF-κB-bound IκBαOnline Journal of Public Health Informatics, 2000
- Activators and target genes of Rel/NF-κB transcription factorsOncogene, 1999
- A Thermodynamic Study of the trp Repressor—Operator InteractionJournal of Molecular Biology, 1994
- Role of the hydrophobic effect in stability of site-specific protein-DNA complexesJournal of Molecular Biology, 1989