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

By Peter Tompa, Mónika Fuxreiter. TIBS -Trends in Biochemical Sciences. Regular ed, 2008

1,042 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/3c2dc1a5c0ef1672693406711dacc5cc5a64ff62

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Materials Chemistry

In Molecular Biology

Citations in the corpus

Understanding eukaryotic linear motifs and their role in cell signaling and regulation. (2008, background): “Whilst linear motifs are found in Intrinsically Disordered Regions (IDR) it has been suggested by many authors, that motifs may form induced fit structures (for a good review see (124)).”
Shape shifting: The multiple conformational substates of the PTEN N‐terminal PIP2 ‐binding domain (2022, background): “Disordered proteins often display many conformational substates explained by a rugged energy landscape, allowing multiple binding modes.(45) Protein “energetic frustration” is a useful concept for predicting locally dynamic regions46–49 in the predicted structures.”
Structured states of disordered proteins from genomic sequences (2016, neutral): “…et al., 2004; Uversky et al., 2002), to transient ensembles, through to more stable order in specific conditions, for instance when binding a ligand, a protein, DNA, RNA or post-translational modification (Bah et al., 2015; Baker et al., 2007; Hurley et al., 2007; Tompa and Fuxreiter, 2008).”
The s2D method: simultaneous sequence-based prediction of the statistical populations of ordered and disordered regions in proteins. (2015, background): “, after binding) degree of disorder but are generally amenable for structural studies [41,42].”
Transcription factors activate genes through the phase separation capacity of their activation domains (2018, background): “The products of this type of protein-protein interaction, where the interaction interface cannot be described by a single conformation, have been termed ‘‘fuzzy complexes’’ (Tompa and Fuxreiter, 2008).”
Random-phase-approximation theory for sequence-dependent, biologically functional liquid-liquid phase separation of intrinsically disordered proteins (2016, background): “But IDPs can also form “fuzzy complexes” [18], i.”
How Random are Intrinsically Disordered Proteins? A Small Angle Scattering Perspective (2012, background): “Even when bound to a partner, they can still remain highly fluctuating, including on the interaction site, leading to what Tompa and Fuxreiter call fuzzy complexes [104].”
MobiDB 3.0: more annotations for intrinsic disorder, conformational diversity and interactions in proteins (2017, background): “Generally, the full functional characterization of IDPs and IDRs requires the description not just of their free (disordered) states (26,27), but also of their residual dynamics in the bound states (28).”
FuzDB: database of fuzzy complexes, a tool to develop stochastic structure-function relationships for protein complexes and higher-order assemblies (2016, background): “These studies demonstrated that structural multiplicity or dynamic disorder could contribute to the formation, function or regulation of the assembly, a phenomenon referred as fuzziness (10,11).”
MetaDisorder: a meta-server for the prediction of intrinsic disorder in proteins (2012, methodology): “Many proteins are functional despite they lack a stable three-dimensional structure under physiological conditions in vitro and/or in vivo [1,2].”