ReviewCurrent research in structural biology2024
Experimental methods to study the structure and dynamics of intrinsically disordered regions in proteins.
Review in Current research in structural biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- MultilevelCurrent research in structural biology · 2026Article
- Beyond the structure-function paradigm: A comprehensive review of intrinsically disordered proteins.Biochemistry and biophysics reports · 2026Review
- xCELLigence™ RTCA system in cancer biology: innovations in real-time functional profiling.Cytotechnology · 2026Review
- A Disorder-Aware Computational Framework to Identify Structurally Tractable Targets in Proliferative Vitreoretinopathy.Ophthalmology science · 2026Article
- Complete NMR assignment for 275 of the most common dipeptides in intrinsically disordered proteins.Scientific data · 2026Article
- Structural and immunogenic evaluation of silk proteins from Bombyx mori using advanced bioinformatics and deep learning for biomaterials applications.Journal, genetic engineering & biotechnology · 2026Article
- A Modular Design of a Cholera Toxin B Subunit-Scaffolded Sub-Virion Nanoparticle Vaccine Against West Nile Virus.Microbial biotechnology · 2026Article
- Backbone rigidity of disordered protein linkers from NMR experiments and MD simulations.Biophysical journal · 2026Article
- In vitro, cellular and in vivo studies of amyloid oligomers structure and toxicity: Challenges and advances.Protein science : a publication of the Protein Society · 2026Review
- Atomic resolution ensembles of intrinsically disordered proteins with Alphafold.Nature communications · 2026Article
- The Core-Shell Conformational Space of Compartmentalized Single-Chain Nanoparticles by Paramagnetic and Hyperpolarized NMR Spectroscopy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Detection of Mutation-Induced Conformational Changes in an Intrinsically Disordered Protein by Double Quantum Coherence Electron Spin Resonance Methodology.Journal of the American Chemical Society · 2026Article
- Disordered DNA-binding motif forms a modulation site for inhibiting the cancer immunotherapy target TREX1.Nucleic acids research · 2026Article
- Decoding intrinsically disordered regions in biomolecular condensates.Fundamental research · 2026Review
- Computational and Experimental Approaches and Applications of Biological NMR.Advances in experimental medicine and biology · 2026Review
- Microproteins in Metabolic Biology: Emerging Functions and Potential Roles as Nutrient-Linked Biomarkers.International journal of molecular sciences · 2025Review
- An update for AlphaFold3 versus experimental structures: assessing the precision of small molecule binding in GPCRs.Acta pharmacologica Sinica · 2025Article
- Pathogenic Proteins Through the Lens of NMR Spectroscopy: Structural and Functional Insights into Disease.Cell biochemistry and biophysics · 2025Review
- Mycobacterium tuberculosis uses intrinsically disordered, fast evolving proteins to interact with conserved host factors.Genome biology · 2025Article
- Ist2 promotes lipid transfer by Osh6 via its membrane tethering and lipid scramblase activities.Science advances · 2025Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eukaryotic proteins often feature long stretches of amino acids that lack a well-defined three-dimensional structure and are referred to as intrinsically disordered proteins (IDPs) or regions (IDRs). Although these proteins challenge conventional structure-function paradigms, they play vital roles in cellular processes. Recent progress in experimental techniques, such as NMR spectroscopy, single molecule FRET, high speed AFM and SAXS, have provided valuable insights into the biophysical basis of IDP function. This review discusses the advancements made in these techniques particularly for the study of disordered regions in proteins. In NMR spectroscopy new strategies such as
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