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Intrinsically unstructured proteins and their functions
  • H. Dyson, P. Wright
  • Biology, Medicine
  • Nature Reviews Molecular Cell Biology
  • 1 March 2005
Many gene sequences in eukaryotic genomes encode entire proteins or large segments of proteins that lack a well-structured three-dimensional fold. Disordered regions can be highly conserved betweenExpand
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm.
A major challenge in the post-genome era will be determination of the functions of the encoded protein sequences. Since it is generally assumed that the function of a protein is closely linked to itsExpand
Solution Structure of the KIX Domain of CBP Bound to the Transactivation Domain of CREB: A Model for Activator:Coactivator Interactions
The nuclear factor CREB activates transcription of target genes in part through direct interactions with the KIX domain of the coactivator CBP in a phosphorylation-dependent manner. The solutionExpand
Recognition of the mRNA AU-rich element by the zinc finger domain of TIS11d
The tandem zinc finger (TZF) domain of the protein TIS11d binds to the class II AU-rich element (ARE) in the 3′ untranslated region (3′ UTR) of target mRNAs and promotes their deadenylation andExpand
Classification of Intrinsically Disordered Regions and Proteins
1.1. Uncharacterized Protein Segments Are a Source of Functional Novelty Over the past decade, we have observed a massive increase in the amount of information describing protein sequences from aExpand
Intrinsically disordered proteins in cellular signalling and regulation
Intrinsically disordered proteins (IDPs) are important components of the cellular signalling machinery, allowing the same polypeptide to undertake different interactions with different consequences.Expand
Coupling of folding and binding for unstructured proteins.
  • H. Dyson, P. Wright
  • Biology, Medicine
  • Current opinion in structural biology
  • 1 February 2002
There are now numerous examples of proteins that are unstructured or only partially structured under physiological conditions and yet are nevertheless functional. Such proteins are especiallyExpand
Linking folding and binding.
  • P. Wright, H. Dyson
  • Biology, Medicine
  • Current opinion in structural biology
  • 1 February 2009
Many cellular proteins are intrinsically disordered and undergo folding, in whole or in part, upon binding to their physiological targets. The past few years have seen an exponential increase inExpand
The Dynamic Energy Landscape of Dihydrofolate Reductase Catalysis
We used nuclear magnetic resonance relaxation dispersion to characterize higher energy conformational substates of Escherichia coli dihydrofolate reductase. Each intermediate in the catalytic cycleExpand
Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators
Nuclear hormone receptors are ligand-activated transcription factors that regulate the expression of genes that are essential for development, reproduction and homeostasis. The hormone response isExpand