@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 {44,
	title = {CASP6 data processing and automatic evaluation at the protein structure prediction center.},
	journal = {Proteins},
	volume = {61 Suppl 7},
	year = {2005},
	month = {2005},
	pages = {19-23},
	abstract = {We present a short overview of the system governing data processing and automatic evaluation of predictions in CASP6, implemented at the Livermore Protein Structure Prediction Center. The system incorporates interrelated facilities for registering participants, collecting prediction targets from crystallographers and NMR spectroscopists and making them available to the CASP6 participants, accepting predictions and providing their preliminary evaluation, and finally, storing and visualizing results. We have automatically evaluated predictions submitted to CASP6 using criteria and methods developed over the successive CASP experiments. Also, we have tested a new evaluation technique based on non-rigid-body type superpositions. Approximately the same number of predictions has been submitted to CASP6 as to all previous CASPs combined, making navigation through and understanding of the data particularly challenging. To facilitate this, we have substantially modernized all data handling procedures, including implementation of a dedicated relational database. An overview of our redesigned website is also presented (http://predictioncenter.org/casp6/).},
	keywords = {Algorithms, Automation, Computational Biology, Crystallography, X-Ray, Internet, Magnetic Resonance Spectroscopy, Models, Molecular, Protein Conformation, Protein Folding, Protein Structure, Secondary, Protein Structure, Tertiary, Proteins, Proteomics, Software},
	issn = {1097-0134},
	doi = {10.1002/prot.20718},
	author = {Kryshtafovych, Andriy and Milostan, Maciej and Szajkowski, Lukasz and Daniluk, Pawe{\l} and Fidelis, Krzysztof}
}
