Self-Association of Models of Transmembrane Domains of ErbB Receptors in a Lipid Bilayer
- 1 December 2010
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 99 (11) , 3657-3665
- https://doi.org/10.1016/j.bpj.2010.10.023
Abstract
No abstract availableKeywords
This publication has 71 references indexed in Scilit:
- Lipid-Modulated Sequence-Specific Association of Glycophorin A in MembranesBiophysical Journal, 2010
- Molecular Dynamics Simulations of the Dimerization of Transmembrane α-HelicesAccounts of Chemical Research, 2009
- Transmembrane Helix Association Affinity Can Be Modulated by Flanking and Noninterfacial ResiduesBiophysical Journal, 2009
- Energetics of ErbB1 Transmembrane Domain Dimerization in Lipid BilayersBiophysical Journal, 2009
- The strong dimerization of the transmembrane domain of the fibroblast growth factor receptor (FGFR) is modulated by C‐terminal juxtamembrane residuesProtein Science, 2009
- Protein modulation of lipids, and vice-versa, in membranesPublished by Elsevier ,2008
- GROMACS: Fast, flexible, and freeJournal of Computational Chemistry, 2005
- ERBB receptors and cancer: the complexity of targeted inhibitorsNature Reviews Cancer, 2005
- EGF Activates Its Receptor by Removing Interactions that Autoinhibit Ectodomain DimerizationPublished by Elsevier ,2003
- The effect of point mutations on the free energy of transmembrane α-helix dimerizationJournal of Molecular Biology, 1997