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Journal ArticleDOI

Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions.

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TLDR
It is the view that protein disorder can be classified into four mechanistic categories, covering a continuous spectrum of structural states from static to dynamic disorder and from segmental to full disorder, and that fuzziness will become integral to understanding the interactome.
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This article is published in Trends in Biochemical Sciences.The article was published on 2008-01-01. It has received 949 citations till now. The article focuses on the topics: Intrinsically disordered proteins.

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Citations
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Intrinsically disordered proteins in cellular signalling and regulation.

TL;DR: Experimental, computational and bioinformatic analyses combine to identify and characterize disordered regions of proteins, leading to a greater appreciation of their widespread roles in biological processes.
Journal ArticleDOI

Protein Phase Separation: A New Phase in Cell Biology.

TL;DR: A combination of techniques from cell biology, biophysics, physical chemistry, structural biology, and bioinformatics are starting to help establish the molecular principles of an emerging field, thus paving the way for exciting discoveries, including novel therapeutic approaches for the treatment of age-related disorders.
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Transcription Factors Activate Genes through the Phase-Separation Capacity of Their Activation Domains.

TL;DR: It is reported that diverse ADs form phase- separated condensates with the Mediator coactivator, suggesting that diverse TFs can interact with Mediator through the phase-separating capacity of their ADs and that formation of condensate with Mediation is involved in gene activation.
References
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Journal ArticleDOI

Intrinsically unstructured proteins and their functions.

TL;DR: Many gene sequences in eukaryotic genomes encode entire proteins or large segments of proteins that lack a well-structured three-dimensional fold, whereas others constitute flexible linkers that have a role in the assembly of macromolecular arrays.
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Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm.

TL;DR: Many proteins that lack intrinsic globular structure under physiological conditions have now been recognized, and it appears likely that their rapid turnover, aided by their unstructured nature in the unbound state, provides a level of control that allows rapid and accurate responses of the cell to changing environmental conditions.
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Intrinsically unstructured proteins.

TL;DR: In this review, recent findings are surveyed to illustrate that this novel but rapidly advancing field has reached a point where proteins can be comprehensively classified on the basis of structure and function.
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Prediction and functional analysis of native disorder in proteins from the three kingdoms of life.

TL;DR: An automatic method for recognizing natively disordered regions from amino acid sequence is described and benchmarked against predictors that were assessed at the latest critical assessment of techniques for protein structure prediction (CASP) experiment and represents a statistically significant improvement on the methods evaluated on the same targets at CASP.
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The importance of intrinsic disorder for protein phosphorylation

TL;DR: A new web-based tool for the prediction of protein phosphorylation sites, DISPHOS (DISorder-enhanced PHOSphorylation predictor, http://www.ist. edu/DISPHOS), which observes that amino acid compositions, sequence complexity, hydrophobicity, charge and other sequence attributes of regions adjacent to phosphate sites are very similar to those of intrinsically disordered protein regions.
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