Structural Insights into Conformational Stability of Wild-Type and Mutant β1-Adrenergic Receptor
- 21 July 2010
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 99 (2) , 568-577
- https://doi.org/10.1016/j.bpj.2010.04.075
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- Ligand-specific regulation of the extracellular surface of a G-protein-coupled receptorNature, 2010
- G‐protein‐coupled receptor structures were not built in a dayProtein Science, 2009
- Identification of two distinct inactive conformations of the β 2 -adrenergic receptor reconciles structural and biochemical observationsProceedings of the National Academy of Sciences, 2009
- Agonist-Induced Conformational Changes in Bovine Rhodopsin: Insight into Activation of G-Protein-Coupled ReceptorsJournal of Molecular Biology, 2008
- Structure of a β1-adrenergic G-protein-coupled receptorNature, 2008
- Conformational thermostabilization of the β1-adrenergic receptor in a detergent-resistant formProceedings of the National Academy of Sciences, 2008
- Scalable molecular dynamics with NAMDJournal of Computational Chemistry, 2005
- A graph‐theory algorithm for rapid protein side‐chain predictionProtein Science, 2003
- All-Atom Empirical Potential for Molecular Modeling and Dynamics Studies of ProteinsThe Journal of Physical Chemistry B, 1998
- VMD: Visual molecular dynamicsJournal of Molecular Graphics, 1996