@article {43,
	title = {New tools and expanded data analysis capabilities at the Protein Structure Prediction Center.},
	journal = {Proteins},
	volume = {69 Suppl 8},
	year = {2007},
	month = {2007},
	pages = {19-26},
	abstract = {We outline the main tasks performed by the Protein Structure Prediction Center in support of the CASP7 experiment and provide a brief review of the major measures used in the automatic evaluation of predictions. We describe in more detail the software developed to facilitate analysis of modeling success over and beyond the available templates and the adopted Java-based tool enabling visualization of multiple structural superpositions between target and several models/templates. We also give an overview of the CASP infrastructure provided by the Center and discuss the organization of the results web pages available through http://predictioncenter.org.},
	keywords = {Computational Biology, Internet, Models, Molecular, Protein Conformation, Protein Folding, Proteins, Software, Structure-Activity Relationship},
	issn = {1097-0134},
	doi = {10.1002/prot.21653},
	author = {Kryshtafovych, Andriy and Prlic, Andreas and Dmytriv, Zinoviy and Daniluk, Pawe{\l} and Milostan, Maciej and Eyrich, Volker and Hubbard, Tim and Fidelis, Krzysztof}
}
@article {53,
	title = {A concept for G protein activation by G protein-coupled receptor dimers: the transducin/rhodopsin interface.},
	journal = {Photochemical \& photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology},
	volume = {3},
	year = {2004},
	month = {2004 Jun},
	pages = {628-38},
	abstract = {G protein-coupled receptors (GPCRs) are ubiquitous and essential in modulating virtually all physiological processes. These receptors share a similar structural design consisting of the seven-transmembrane alpha-helical segments. The active conformations of the receptors are stabilized by an agonist and couple to structurally highly conserved heterotrimeric G proteins. One of the most important unanswered questions is how GPCRs couple to their cognate G proteins. Phototransduction represents an excellent model system for understanding G protein signaling, owing to the high expression of rhodopsin in rod photoreceptors and the multidisciplinary experimental approaches used to study this GPCR. Here, we describe how a G protein (transducin) docks on to an oligomeric GPCR (rhodopsin), revealing structural details of this critical interface in the signal transduction process. This conceptual model takes into account recent structural information on the receptor and G protein, as well as oligomeric states of GPCRs.},
	keywords = {Animals, Dimerization, Models, Molecular, Protein Conformation, Protein Structure, Secondary, Receptors, G-Protein-Coupled, Rhodopsin},
	issn = {1474-905X},
	doi = {10.1039/b315661c},
	author = {Filipek, S{\l}awomir and Krzy{\'s}ko, Krystiana A and Fotiadis, Dimitrios and Liang, Yan and Saperstein, David A and Engel, Andreas and Palczewski, Krzysztof}
}
