ArticleProtein science : a publication of the Protein Society2018
Prediction of protein disorder based on IUPred.
Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.
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122 citing papers in PubMed.
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- Optimized ND4 allotopic expression for gene therapy of Leber's hereditary optic neuropathy.Frontiers in bioengineering and biotechnology · 2026Article
- Investigating the Role of OsHDT701 and Other Blast-Associated Negative Regulatory Genes in Indica Rice Cultivar Ranjit Using Combined Wet Lab and Computational Approaches.Molecular biotechnology · 2025Article
- Combination of in vivo and in vitro phosphoproteomics determines the PP2A target repertoire on proteome scale.Cell reports methods · 2025Article
- Integration of protein stability and AlphaMissense scores improves bioinformatic impact prediction for p53 missense and in-frame amino acid deletion variants.American journal of human genetics · 2025Article
- Deep learning tools predict variants in disordered regions with lower sensitivity.BMC genomics · 2025Article
- Navigating centriolar satellites: the role of PCM1 in cellular and organismal processes.The FEBS journal · 2025Review
- Evolution of intrinsic disorder in the structural domains of viral and cellular proteomes.Scientific reports · 2025Article
62 more citing papers are in PubMed but not listed here.
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Abstract
Many proteins contain intrinsically disordered regions (IDRs), functional polypeptide segments that in isolation adopt a highly flexible conformational ensemble instead of a single, well-defined structure. Disorder prediction methods, which can discriminate ordered and disordered regions from the amino acid sequence, have contributed significantly to our current understanding of the distinct properties of intrinsically disordered proteins by enabling the characterization of individual examples as well as large-scale analyses of these protein regions. One popular method, IUPred provides a robust prediction of protein disorder based on an energy estimation approach that captures the fundamental difference between the biophysical properties of ordered and disordered regions. This paper reviews the energy estimation method underlying IUPred and the basic properties of the web server. Through an example, it also illustrates how the prediction output can be interpreted in a more complex case by taking into account the heterogeneous nature of IDRs. Various applications that benefited from IUPred to provide improved disorder predictions, complementing domain annotations and aiding the identification of functional short linear motifs are also described here. IUPred is freely available for noncommercial users through the web server (http://iupred.enzim.hu and http://iupred.elte.hu) . The program can also be downloaded and installed locally for large-scale analyses.
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