@article {2010|1789,
	title = {Single-spanning transmembrane domains in cell growth and cell-cell interactions: More than meets the eye?},
	journal = {Cell Adh. Migr.},
	volume = {4},
	number = {2},
	year = {2010},
	month = {apr},
	pages = {313{\textendash}324},
	abstract = {<p>As a whole, integral membrane proteins represent about one third of sequenced genomes, and more than 50\% of currently available drugs target membrane proteins, often cell surface receptors. Some membrane protein classes, with a defined number of transmembrane (TM) helices, are receiving much attention because of their great functional and pharmacological importance, such as G protein-coupled receptors possessing 7 TM segments. Although they represent roughly half of all membrane proteins, bitopic proteins (with only 1 TM helix) have so far been less well characterized. Though they include many essential families of receptors, such as adhesion molecules and receptor tyrosine kinases, many of which are excellent targets for biopharmaceuticals (peptides, antibodies, et al.). A growing body of evidence suggests a major role for interactions between TM domains of these receptors in signaling, through homo and heteromeric associations, conformational changes, assembly of signaling platforms, etc. Significantly, mutations within single domains are frequent in human disease, such as cancer or developmental disorders. This review attempts to give an overview of current knowledge about these interactions, from structural data to therapeutic perspectives, focusing on bitopic proteins involved in cell signaling.</p>},
	keywords = {Animals, Biological, Humans, Membrane Proteins, Models, Protein Structure, Secondary, Signal Transduction, Tertiary},
	issn = {1933-6926},
	doi = {10.4161/cam.4.2.12430},
	author = {Pierre Hubert and Paul Sawma and Jean-Pierre Duneau and Jonathan Khao and J{\'e}r{\^o}me H{\'e}nin and Dominique Bagnard and James Sturgis}
}
@article {2009|1830,
	title = {Replica exchange molecular dynamics simulations of coarse-grained proteins in implicit solvent.},
	journal = {J. Phys. Chem. B},
	volume = {113},
	number = {1},
	year = {2009},
	month = {jan},
	pages = {267{\textendash}274},
	keywords = {Amino Acid Sequence, Computer Simulation, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Peptides, Protein Folding, Protein Structure, Proteins, Secondary, Solvents, Temperature, Thermodynamics},
	doi = {10.1021/jp805309e},
	author = {Y Chebaro and Xiao Dong and Rozita Laghaei and Philippe Derreumaux and Normand Mousseau}
}
@article {2009|2019,
	title = {Thermodynamics and dynamics of amyloid peptide oligomerization are sequence dependent},
	journal = {Proteins: Struct., Funct., Bioinf.},
	volume = {75},
	number = {4},
	year = {2009},
	month = {jun},
	pages = {954{\textendash}963},
	keywords = {Amino Acid Sequence, Amyloid beta-Protein, beta 2-Microglobulin, Cluster Analysis, Computer Simulation, Models, Molecular, Peptide Fragments, Protein Multimerization, Protein Structure, Secondary, Structure-Activity Relationship, Thermodynamics},
	doi = {10.1002/prot.22305},
	author = {Lu, Yan and Philippe Derreumaux and Guo, Zhi and Mousseau, Normand and Wei, Guanghong}
}
