Structural Role of the Conserved Cysteines in the Dimerization of the Viral Transmembrane Oncoprotein E5
- 22 September 2010
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 99 (6) , 1764-1772
- https://doi.org/10.1016/j.bpj.2010.06.073
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- Artificial Transmembrane Oncoproteins Smaller than the Bovine Papillomavirus E5 Protein Redefine Sequence Requirements for Activation of the Platelet-Derived Growth Factor β ReceptorJournal of Virology, 2009
- Conformation and Membrane Orientation of Amphiphilic Helical Peptides by Oriented Circular DichroismBiophysical Journal, 2008
- De novo design of fibrils made of short α-helical coiled coil peptidesPublished by Elsevier ,2001
- Predicting transmembrane protein topology with a hidden markov model: application to complete genomes11Edited by F. CohenJournal of Molecular Biology, 2001
- How to measure and predict the molar absorption coefficient of a proteinProtein Science, 1995
- Signal transduction by receptors with tyrosine kinase activityPublished by Elsevier ,1990
- Evidence for an .alpha.II-type helical conformation for bacteriorhodopsin in the purple membraneBiochemistry, 1989
- Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptorBiochemistry, 1987
- Self-phosphorylation of epidermal growth factor receptor: evidence for a model of intermolecular allosteric activationBiochemistry, 1987
- Differential light scattering and absorption flattening optical effects are minimal in the circular dichroism spectra of small unilamellar vesiclesBiochemistry, 1984