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- W2077487109 endingPage "950" @default.
- W2077487109 startingPage "930" @default.
- W2077487109 abstract "Structural disorder of functional proteins under physiological conditions is widespread within eukaryotic proteomes. The lack of stable tertiary and secondary structure offers a variety of functional advantages to intrinsically disordered proteins (IDPs): their malleability of interaction with different partners, specific but low-affinity binding, and their fine modulation by post-translational modifications. IDPs are therefore central players in key processes such as cell-cycle control and signal-transduction pathways, and impairment of their function is associated with many disease states such as cancer and neurodegenerative disorders. Fascinating progress in the experimental characterization of IDPs has been made in the last decade, especially in NMR spectroscopy and small-angle X-ray scattering as well as in single-molecule techniques. It has been accompanied by the development of powerful computational tools to translate experimental results in explicit ensemble representations of IDPs. With the aid of bioinformatics tools, these advances have paved the way to targeting IDP interactions in rational drug-discovery projects." @default.
- W2077487109 created "2016-06-24" @default.
- W2077487109 creator A5001250430 @default.
- W2077487109 creator A5033249566 @default.
- W2077487109 creator A5036082816 @default.
- W2077487109 date "2012-04-13" @default.
- W2077487109 modified "2023-09-25" @default.
- W2077487109 title "Intrinsically Disordered Proteins: From Sequence and Conformational Properties toward Drug Discovery" @default.
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