The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Increasing the precision of comparative models with YASARA NOVA—a self‐parameterizing force field
Open accessAbstract
One of the conclusions drawn at the CASP4 meeting in Asilomar was that applying various force fields during refinement of template‐based models tends to move predictions in the wrong direction, away from the experimentally determined coordinates. We have derived an all‐atom force field aimed at protein and nucleotide optimization in vacuo (NOVA), which has been specifically designed to avoid this problem. NOVA resembles common molecular dynamics force fields but has been automatically parameterized with two major goals: (i) not to make high resolution X‐ray structures worse and (ii) to improve homology models built by WHAT IF. Force‐field parameters were not required to be physically correct; instead, they were optimized with random Monte Carlo moves in force‐field parameter space, each one evaluated by simulated annealing runs of a 50‐protein optimization set. Errors inherent to the approximate force‐field equation could thus be canceled by errors in force‐field parameters. Compared with the optimization set, the force field did equally well on an independent validation set and is shown to move in silico models closer to reality. It can be applied to modeling applications as well as X‐ray and NMR structure refinement. A new method to assign force‐field parameters based on molecular trees is also presented. A NOVA server is freely accessible at http://www.yasara.com/servers Proteins 2002;47:393–402. © 2002 Wiley‐Liss, Inc.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
Protein Structure Comparison by Alignment of Distance Matrices
Holm, L., & Sander, C. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1489 · Cited by 3,984 · cited 1×
“For each of these chains, the script searched for a modeling template in the corresponding FSSP file.(18) If a template existed that allowed modeling the chain without insertions or deletions and had 93% sequence identity, the model was built with WHAT IF(19) and added to the group of models (M); otherwise, the chain…”
Method
Cited by
Mutations in the DJ-1 Gene Associated with Autosomal Recessive Early-Onset Parkinsonism
Bonifati, V., Rizzu, P., van Baren, M. J., Schaap, O., Breedveld, G. J., Krieger, E., Dekker, M. C. J., Squitieri, F., Ibanez, P., Joosse, M., et al. (2003) · Science · doi:10.1126/science.1077209 · Cited by 2,778
Self-citationVenselaar, H., te Beek, T. A., Kuipers, R. K., Hekkelman, M. L., & Vriend, G. (2010) · BMC Bioinformatics · doi:10.1186/1471-2105-11-548 · Cited by 1,162
Self-citationWhole-genome landscape of pancreatic neuroendocrine tumours
Initiative, A. P. C. G., Scarpa, A., Chang, D. K., Nones, K., Corbo, V., Patch, A.-M., Bailey, P., Lawlor, R. T., Johns, A. L., Miller, D. K., et al. (2017) · Nature · doi:10.1038/nature21063 · Cited by 999
Making optimal use of empirical energy functions: Force‐field parameterization in crystal space
Krieger, E., Darden, T., Nabuurs, S. B., Finkelstein, A., & Vriend, G. (2004) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.20251 · Cited by 853
Self-citationThe PDB_REDO server for macromolecular structure model optimization
Joosten, R. P., Long, F., Murshudov, G. N., & Perrakis, A. (2014) · IUCrJ · doi:10.1107/s2052252514009324 · Cited by 834
Metadata
- Authors
- Krieger, E., Koraimann, G., & Vriend, G.
- Venue
- Proteins: Structure, Function, and Bioinformatics
- Publisher
- Wiley
- Published
- 2002-03-27
- Volume
- 47
- Issue
- 3
- Pages
- 393-402
- ISSN
- 0887-3585 (ISSN-L)
- 1097-0134
- OpenAlex
- W2099099776
- Cited by
- 1,514
- References
- 2
- FWCI
- 2.16
- Type
- journal article
- Language
- en
- Open access
- bronze
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.