The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Practically Useful: What the R osetta Protein Modeling Suite Can Do for You
Open accessAbstract
The objective of this review is to enable researchers to use the software package Rosetta for biochemical and biomedicinal studies. We provide a brief review of the six most frequent research problems tackled with Rosetta. For each of these six tasks, we provide a tutorial that illustrates a basic Rosetta protocol. The Rosetta method was originally developed for de novo protein structure prediction and is regularly one of the best performers in the community-wide biennial Critical Assessment of Structure Prediction. Predictions for protein domains with fewer than 125 amino acids regularly have a backbone root-mean-square deviation of better than 5.0 A. More impressively, there are several cases in which Rosetta has been used to predict structures with atomic level accuracy better than 2.5 A. In addition to de novo structure prediction, Rosetta also has methods for molecular docking, homology modeling, determining protein structures from sparse experimental NMR or EPR data, and protein design. Rosetta has been used to accurately design a novel protein structure, predict the structure of protein-protein complexes, design altered specificity protein-protein and protein-DNA interactions, and stabilize proteins and protein complexes. Most recently, Rosetta has been used to solve the X-ray crystallographic phase problem.
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Cites
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
Protein backbone angle restraints from searching a database for chemical shift and sequence homology
Cornilescu, G., Delaglio, F., & Bax, A. (1999) · Journal of Biomolecular NMR · doi:10.1023/a:1008392405740 · Cited by 2,957 · cited 1×
“Chemical shift assignments for backbone atoms can be converted to φ and ψ backbone angle restraints ( 33 ) are incorporated into the scoring function used during folding.”
MethodAmbroggio, X. I., & Kuhlman, B. (2006) · Journal of the American Chemical Society · doi:10.1021/ja054718w · Cited by 200
Cited by
Leaver-Fay (2011) · doi:10.1016/b978-0-12-381270-4.00019-6 · Cited by 1,904
CEACAM1 regulates TIM-3-mediated tolerance and exhaustion
Huang, Y.-H., Zhu, C., Kondo, Y., Anderson, A. C., Gandhi, A., Russell, A., Dougan, S. K., Petersen, B.-S., Melum, E., Pertel, T., et al. (2015) · Nature · doi:10.1038/nature13848 · Cited by 717
Memdock: an α-helical membrane protein docking algorithm
Hurwitz, N., Schneidman-Duhovny, D., & Wolfson, H. J. (2016) · Bioinformatics · doi:10.1093/bioinformatics/btw184 · Cited by 40
Protein-protein and peptide-protein docking and refinement using ATTRACT in CAPRI
Schindler, C. E. M., Chauvot de Beauchêne, I., de Vries, S. J., & Zacharias, M. (2017) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25196 · Cited by 20
ESM ‐scan—A tool to guide amino acid substitutions
Totaro, M. G., Vide, U., Zausinger, R., Winkler, A., & Oberdorfer, G. (2024) · Protein Science · doi:10.1002/pro.5221 · Cited by 19
Metadata
- Authors
- Kaufmann, K. W., Lemmon, G. H., DeLuca, S. L., Sheehan, J. H., & Meiler, J.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-03-17
- Volume
- 49
- Issue
- 14
- Pages
- 2987-2998
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2033650210
- Cited by
- 402
- References
- 3
- FWCI
- 10.16
- Type
- journal article
- Language
- en
- Open access
- hybrid
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