The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
FoXS, FoXSDock and MultiFoXS: Single-state and multi-state structural modeling of proteins and their complexes based on SAXS profiles
Open accessAbstract
Small Angle X-ray Scattering (SAXS) is an increasingly common and useful technique for structural characterization of molecules in solution. A SAXS experiment determines the scattering intensity of a molecule as a function of spatial frequency, termed SAXS profile. Here, we describe three web servers for modeling atomic structures based on SAXS profiles. FoXS (Fast X-Ray Scattering) rapidly computes a SAXS profile of a given atomistic model and fits it to an experimental profile. FoXSDock docks two rigid protein structures based on a SAXS profile of their complex. MultiFoXS computes a population-weighted ensemble starting from a single input structure by fitting to a SAXS profile of the protein in solution. We describe the interfaces and capabilities of the servers (salilab.org/foxs), followed by demonstrating their application on Interleukin-33 (IL-33) and its primary receptor ST2.
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
Accurate assessment of mass, models and resolution by small-angle scattering
Rambo, R. P., & Tainer, J. A. (2013) · Nature · doi:10.1038/nature12070 · Cited by 750
Self-citation
Cited by
Mechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2
Pádua, R. A. P., Sun, Y., Marko, I., Pitsawong, W., Stiller, J. B., Otten, R., & Kern, D. (2018) · Nature Communications · doi:10.1038/s41467-018-06814-w · Cited by 133
Conformational buffering underlies functional selection in intrinsically disordered protein regions
González-Foutel, N. S., Glavina, J., Borcherds, W. M., Safranchik, M., Barrera-Vilarmau, S., Sagar, A., Estaña, A., Barozet, A., Garrone, N. A., Fernandez-Ballester, G., et al. (2022) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00811-w · Cited by 118
Wei, K. Y., Moschidi, D., Bick, M. J., Nerli, S., McShan, A. C., Carter, L. P., Huang, P.-S., Fletcher, D. A., Sgourakis, N. G., Boyken, S. E., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1914808117 · Cited by 57
Artificial intelligence guided conformational mining of intrinsically disordered proteins
Gupta, A., Dey, S., Hicks, A., & Zhou, H.-X. (2022) · Communications Biology · doi:10.1038/s42003-022-03562-y · Cited by 56
Integrative Structural Biology in the Era of Accurate Structure Prediction
Masrati, G., Landau, M., Ben-Tal, N., Lupas, A., Kosloff, M., & Kosinski, J. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167127 · Cited by 53
Metadata
- Authors
- Schneidman-Duhovny, D., Hammel, M., Tainer, J. A., & Sali, A.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2016-05-05
- Volume
- 44
- Issue
- W1
- Pages
- W424-W429
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W2346627216
- Cited by
- 517
- References
- 1
- FWCI
- 20.52
- Type
- journal article
- Language
- en
- Open access
- gold
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: FoXS, FoXSDock and MultiFoXS: Single-state and multi-state structural modeling of proteins and their complexes based on SAXS profiles. https://app.cochat.ai/papers/10.1093/nar/gkw389
- The paper
- Schneidman-Duhovny, D., Hammel, M., Tainer, J. A., & Sali, A. (2016). FoXS, FoXSDock and MultiFoXS: Single-state and multi-state structural modeling of proteins and their complexes based on SAXS profiles. Nucleic Acids Research. https://doi.org/10.1093/nar/gkw389
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.
