ArticleEssays in biochemistry2022
NMR insights into dynamic, multivalent interactions of intrinsically disordered regions: from discrete complexes to condensates.
Article in Essays in biochemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 28 citations in OpenAlex.
- Disordered but rhythmic-the role of intrinsic protein disorder in eukaryotic circadian timing.FEBS letters · 2026Review
- In situ NMR and integrative proteomics reveal the interaction signature of serum α-synuclein.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Sequence and length-scale dependent dynamics in biocondensates of highly charged disordered proteins.Communications chemistry · 2026Article
- Diffusion-based size determination of solute particles: a method adapted for postsynaptic proteins.FEBS open bio · 2026Article
- Biological insights from integrative modeling of intrinsically disordered protein systems.Current opinion in structural biology · 2025Review
- Exploring the complexity of MECP2 function in Rett syndrome.Nature reviews. Neuroscience · 2025Review
- From molecular descriptions to cellular functions of intrinsically disordered protein regions.Biophysics reviews · 2024Review
- Perspective: on the importance of extensive, high-quality and reliable deposition of biomolecular NMR data in the age of artificial intelligence.Journal of biomolecular NMR · 2024Article
- Article
- AlphaFold-Multimer accurately captures interactions and dynamics of intrinsically disordered protein regions.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Disentangling the Complexity in Protein Complexes Using Complementary Isotope-Labeling and Multiple-Receiver NMR Spectroscopy.Journal of the American Chemical Society · 2024Article
- The acidic intrinsically disordered region of the inflammatory mediator HMGB1 mediates fuzzy interactions with CXCL12.Nature communications · 2024Article
- Exploring the World of Membrane Proteins: Techniques and Methods for Understanding Structure, Function, and Dynamics.Molecules (Basel, Switzerland) · 2023Review
- Extreme dynamics in a biomolecular condensate.Nature · 2023Article
- Protein Binding: A Fuzzy Concept.Life (Basel, Switzerland) · 2023Article
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2 authors at 2 institutions in 1 country.
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Abstract
The spatial and temporal organization of interactions between proteins underlie the regulation of most cellular processes. The requirement for such interactions to be specific predisposes a view that protein-protein interactions are relatively static and are formed through the stable complementarity of the interacting partners. A growing body of reports indicate, however, that many interactions lead to fuzzy complexes with an ensemble of conformations in dynamic exchange accounting for the observed binding. Here, we discuss how NMR has facilitated the characterization of these discrete, dynamic complexes and how such characterization has aided the understanding of dynamic, condensed phases of phase-separating proteins with exchanging multivalent interactions.
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