Conformational ensembles of the human intrinsically disordered proteome
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
https://www.nature.com/articles/s41586-023-07004-5.pdf
Reference98 articles.
1. Holehouse, A. S. & Kragelund, B. B. The molecular basis for cellular function of intrinsically disordered protein regions. Nat. Rev. Mol. Cell Biol. https://doi.org/10.1038/s41580-023-00673-0 (2023).
2. Akdel, M. et al. A structural biology community assessment of AlphaFold2 applications. Nat. Struct. Mol. Biol. 29, 1056–1067 (2022).
3. Ghafouri, H. et al. PED in 2024: improving the community deposition of structural ensembles for intrinsically disordered proteins. Nucleic Acids Res. 52, D536–D544 (2024).
4. Tesei, G., Schulze, T. K., Crehuet, R. & Lindorff-Larsen, K. Accurate model of liquid–liquid phase behavior of intrinsically disordered proteins from optimization of single-chain properties. Proc. Natl Acad. Sci. USA 118, e2111696118 (2021).
5. Tesei, G. & Lindorff-Larsen, K. Improved predictions of phase behaviour of intrinsically disordered proteins by tuning the interaction range. Open Res. Europe 2, 94 (2023).
Cited by 2 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. An easy-to-use computational tool for predicting 3D properties of disordered proteins;Nature Methods;2024-01-31
2. Direct prediction of intrinsically disordered protein conformational properties from sequences;Nature Methods;2024-01-31
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