Minimum information guidelines for experiments structurally characterizing intrinsically disordered protein regions
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Molecular Biology,Biochemistry,Biotechnology
Link
https://www.nature.com/articles/s41592-023-01915-x.pdf
Reference56 articles.
1. Quaglia, F. et al. DisProt in 2022: improved quality and accessibility of protein intrinsic disorder annotation. Nucleic Acids Res. 50, D480–D487 (2021).
2. Fukuchi, S. et al. IDEAL in 2014 illustrates interaction networks composed of intrinsically disordered proteins and their binding partners. Nucleic Acids Res. 42, D320–D325 (2014).
3. Dyson, H. J. & Wright, P. E. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 6, 197–208 (2005). A highly influential review describing the structure–function relationship in the context of IDRs.
4. Davey, N. E. The functional importance of structure in unstructured protein regions. Curr. Opin. Struct. Biol. 56, 155–163 (2019).
5. Schad, E. et al. DIBS: a repository of disordered binding sites mediating interactions with ordered proteins. Bioinformatics 34, 535–537 (2018).
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