The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
ZRANK: Reranking protein docking predictions with an optimized energy function
Abstract
Protein–protein docking requires fast and effective methods to quickly discriminate correct from incorrect predictions generated by initial‐stage docking. We have developed and tested a scoring function that utilizes detailed electrostatics, van der Waals, and desolvation to rescore initial‐stage docking predictions. Weights for the scoring terms were optimized for a set of test cases, and this optimized function was then tested on an independent set of nonredundant cases. This program, named ZRANK, is shown to significantly improve the success rate over the initial ZDOCK rankings across a large benchmark. The amount of test cases with No. 1 ranked hits increased from 2 to 11 and from 6 to 12 when predictions from two ZDOCK versions were considered. ZRANK can be applied either as a refinement protocol in itself or as a preprocessing stage to enrich the well‐ranked hits prior to further refinement. Proteins 2007. © 2007 Wiley‐Liss, Inc.
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Berman, H. M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.235 · Cited by 40,196
Numerical recipes in C: the art of scientific computing
(1993) · Choice Reviews Online · doi:10.5860/choice.30-5638 · Cited by 17,933
CHARMM: A program for macromolecular energy, minimization, and dynamics calculations
Brooks, B. R., Bruccoleri, R. E., Olafson, B. D., States, D. J., Swaminathan, S., & Karplus, M. (1983) · Journal of Computational Chemistry · doi:10.1002/jcc.540040211 · Cited by 14,944
Numerical Recipes in C: The Art of Scientific Computing.
Birchenhall, C., Press, W. H., Teukolsky, S. A., Vetterling, W. T., & Flannery, B. P. (1994) · The Economic Journal · doi:10.2307/2234664 · Cited by 4,355
Principles of protein-protein interactions
Jones, S., & Thornton, J. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.13 · Cited by 2,684
Crimins, F. (2003) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-003-0001-6 · Cited by 2,000
Abagyan, R., Totrov, M., & Kuznetsov, D. (1994) · Journal of Computational Chemistry · doi:10.1002/jcc.540150503 · Cited by 1,699
ZDOCK: An initial‐stage protein‐docking algorithm
Chen, R., Li, L., & Weng, Z. (2003) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.10389 · Cited by 1,393
Self-citationSimulation of activation free energies in molecular systems
Neria, E., Fischer, S., & Karplus, M. (1996) · The Journal of Chemical Physics · doi:10.1063/1.472061 · Cited by 1,322
Principles of docking: An overview of search algorithms and a guide to scoring functions
Halperin, I., Ma, B., Wolfson, H., & Nussinov, R. (2002) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.10115 · Cited by 1,294
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Pieper, U., Webb, B. M., Dong, G. Q., Schneidman-Duhovny, D., Fan, H., Kim, S. J., Khuri, N., Spill, Y. G., Weinkam, P., Hammel, M., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gkt1144 · Cited by 322
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“antibody-specific DockSorter [110] and general protein ZRANK [171], FireDock [172], SIPPER[173]) to discriminate models that are closer to the native conformation.”
BackgroundHot-spot analysis for drug discovery targeting protein-protein interactions
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“This usage is distinct from scores that may reflect energy-based evaluations, such as those generated by tools such as ZRank 31 , which are used during modeling or docking but are not direct measures of structural similarity.”
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Metadata
- Authors
- Pierce, B., & Weng, Z.
- Venue
- Proteins: Structure, Function, and Bioinformatics
- Publisher
- Wiley
- Published
- 2007-05
- Volume
- 67
- Issue
- 4
- Pages
- 1078-1086
- ISSN
- 0887-3585 (ISSN-L)
- 1097-0134
- OpenAlex
- W2129454543
- Cited by
- 444
- References
- 31
- FWCI
- 5.75
- Type
- journal article
- Language
- en
- Open access
- closed
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