The DOI matches its Crossref record.
PRODIGY: a web server for predicting the binding affinity of protein–protein complexes
Open accessAbstract
Summary: Gaining insights into the structural determinants of protein–protein interactions holds the key for a deeper understanding of biological functions, diseases and development of therapeutics. An important aspect of this is the ability to accurately predict the binding strength for a given protein–protein complex. Here we present PROtein binDIng enerGY prediction (PRODIGY), a web server to predict the binding affinity of protein–protein complexes from their 3D structure. The PRODIGY server implements our simple but highly effective predictive model based on intermolecular contacts and properties derived from non-interface surface. Availability and Implementation: PRODIGY is freely available at: http://milou.science.uu.nl/services/PRODIGY. Contact: a.m.j.j.bonvin@uu.nl, a.vangone@uu.nl
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
Cited by
Arshad, N., Laurent-Rolle, M., Ahmed, W. S., Hsu, J. C.-C., Mitchell, S. M., Pawlak, J., Sengupta, D., Biswas, K. H., & Cresswell, P. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2208525120 · Cited by 119
Shor, B., & Schneidman-Duhovny, D. (2024) · Nature Methods · doi:10.1038/s41592-024-02174-0 · Cited by 85
Zhou, Z., Yin, Y., Han, H., Jia, Y., Koh, J. H., Kong, A. W.-K., & Mu, Y. (2024) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.4c01850 · Cited by 30
Discovery, structure, and function of filamentous 3-methylcrotonyl-CoA carboxylase
Hu, J. J., Lee, J. K. J., Liu, Y.-T., Yu, C., Huang, L., Aphasizheva, I., Aphasizhev, R., & Zhou, Z. H. (2023) · Structure · doi:10.1016/j.str.2022.11.015 · Cited by 29
Ikenohuchi, Y. J., Silva, M. D. S., Rego, C. M. A., Francisco, A. F., da Silva Setúbal, S., Ferreira e Ferreira, A. A., Boeno, C. N., Santana, H. M., Felipin, K. P., de Lima, A. M., et al. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04839-z · Cited by 20
Fast, accurate ranking of engineered proteins by target-binding propensity using structure modeling
Ding, X., Chen, X., Sullivan, E. E., Shay, T. F., & Gradinaru, V. (2024) · Molecular Therapy · doi:10.1016/j.ymthe.2024.04.003 · Cited by 20
CryoEM reveals oligomeric isomers of a multienzyme complex and assembly mechanics
Lee, J. K. J., Liu, Y.-T., Hu, J. J., Aphasizheva, I., Aphasizhev, R., & Zhou, Z. H. (2023) · Journal of Structural Biology: X · doi:10.1016/j.yjsbx.2023.100088 · Cited by 16
Kumar, N., Kaushik, R., Zhang, K. Y. J., Uversky, V. N., Sahu, U., Sood, R., & Bhatia, S. (2023) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.26467 · Cited by 15
A computational toolbox for the assembly yield of complex and heterogeneous structures
Curatolo, A. I., Kimchi, O., Goodrich, C. P., Krueger, R. K., & Brenner, M. P. (2023) · Nature Communications · doi:10.1038/s41467-023-43168-4 · Cited by 15
Zheng, F., Jiang, X., Wen, Y., Yang, Y., & Li, M. (2024) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2023.12.018 · Cited by 14
TopBP1 utilises a bipartite GINS binding mode to support genome replication
Day, M., Tetik, B., Parlak, M., Almeida-Hernández, Y., Räschle, M., Kaschani, F., Siegert, H., Marko, A., Sanchez-Garcia, E., Kaiser, M., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45946-0 · Cited by 14
Structural insights into pink-eyed dilution protein (Oca2)
Mesdaghi, S., Murphy, D. L., Simpkin, A. J., & Rigden, D. J. (2023) · Bioscience Reports · doi:10.1042/bsr20230060 · Cited by 13
The Rapid Evolution of De Novo Proteins in Structure and Complex
(2024) · doi:10.1093/gbe/evae107 · Cited by 13
Kaushik, R., Kumar, N., Zhang, K. Y. J., Srivastava, P., Bhatia, S., & Malik, Y. S. (2022) · Environmental Research · doi:10.1016/j.envres.2022.113303 · Cited by 13
Kawaguchi, S., Xu, X., Soga, T., Yamaguchi, K., Kawasaki, R., Shimouchi, R., Date, S., & Kai, T. (2025) · eLife · doi:10.7554/elife.101967.3 · Cited by 10
Ferraz, M. V. F., Neto, J. C. S., Lins, R. D., & Teixeira, E. S. (2023) · Physical Chemistry Chemical Physics · doi:10.1039/d2cp05644e · Cited by 9
A paired sequence language model for protein-protein interaction modeling
Liu, J., Chen, H., & Zhang, Y. (2026) · Nature Communications · doi:10.1038/s41467-026-70457-5 · Cited by 8
Molecular investigation of TSHR gene in Bangladeshi congenital hypothyroid patients
Begum, M. N., Mahtarin, R., Islam, M. T., Ahmed, S., Konika, T. K., Mannoor, K., Akhteruzzaman, S., & Qadri, F. (2023) · PLOS ONE · doi:10.1371/journal.pone.0282553 · Cited by 6
Shishir, T. A., Jannat, T., & Naser, I. B. (2022) · doi:10.1101/2022.02.21.481269 · Cited by 5
Xiao, M., Dhungel, S., Azad, R., Favaro, D. C., Rajesh, R. P., Gardner, K. H., & Kikani, C. K. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168433 · Cited by 2
Guo, Y., Shukla, S., Minasov, G., Inniss, N. L., Klose, T., Tokars, V. L., Mondragón, A., Otwinowski, Z., Borek, D., & Satchell, K. J. F. (2026) · Protein Science · doi:10.1002/pro.70609 · Cited by 1
Mukhtar, O., Dutt, R., Panda, A., Kumari, P., Singh, S. S., Paul, G., Prakash, N., Abbas, M., Islam, M. M., Arora, P., et al. (2026) · eLife · doi:10.7554/elife.110942
Metadata
- Authors
- Xue, L. C., Rodrigues, J. P., Kastritis, P. L., Bonvin, A. M., & Vangone, A.
- Venue
- Bioinformatics
- Publisher
- Oxford University Press (OUP)
- Published
- 2016-08-08
- Volume
- 32
- Issue
- 23
- Pages
- 3676-3678
- ISSN
- 1367-4803 (ISSN-L)
- 1367-4811
- OpenAlex
- W2512372054
- Cited by
- 1,413
- References
- 0
- FWCI
- 12.34
- Type
- journal article
- Language
- en
- Open access
- green
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.