ReviewCurrent protein & peptide science2012
How random are intrinsically disordered proteins? A small angle scattering perspective.
Review in Current protein & peptide science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 170 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
170 citing papers in PubMed, 362 citations in OpenAlex.
- Characterization of Liquid-Liquid Phase Separation of Companion of Cellulose Synthases under Stress Mimicking Conditions.bioRxiv : the preprint server for biology · 2026Article
- Programming the Optoelectronic Properties of Atomically Precise Gold Nanoclusters Using the Conformational Landscape of Intrinsically Disordered Proteins.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Unraveling G-Quadruplex and i-Motif Coexistence Within a Double-Stranded DNA.Angewandte Chemie (International ed. in English) · 2026Article
- AI-Physics-Experiment Trinity for Integrated Protein Dynamics Modeling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Intrinsically disordered protein coating for oral delivery of peptide drugs.Cell biomaterials · 2026Article
- Structural characterization of OsPDIL2-3, a rice protein disulfide isomerase involved in prolamin accumulation.The Biochemical journal · 2026Article
- Toward a unified framework for determining conformational ensembles of disordered proteins.Nature methods · 2026Review
- An intrinsically disordered region mediates RNA-binding selectivity and cellular activities of LARP6.Nature communications · 2026Article
- From TDP-43/RNA complex formation to disease-linked TDP-43 aggregation through a structural and cellular approach.Nature communications · 2026Article
- pH Sensitivity of the SERF1a Conformational Ensemble.ACS omega · 2026Article
- Ion-selective conformational stabilization of a disordered repeats-in-toxin protein domain.Biophysical journal · 2025Article
- SAXS Assistant: Automated SAXS analysis for structural discovery in biologics and polymeric nanoparticles.Biophysical journal · 2025Article
- State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025Review
- Molecular Dynamics of the Intrinsically Disordered Protein COR15A─A Force Field Validation on Structure and Dynamics.Journal of chemical theory and computation · 2025Article
- Molecular basis of Fab-dependent IgA antibody recognition by gut-bacterial metallopeptidases.The EMBO journal · 2025Article
- Solution conformational differences between conventional and CENP-A nucleosomes are accentuated by reversible deformation under high pressure.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025Article
- Article
- Structure of the nucleosome-bound human BCL7A.Nucleic acids research · 2025Article
- Dynamic Interchange of Local Residue-Residue Interactions in the Largely Extended Single Alpha-Helix in Drebrin.The Biochemical journal · 2025Article
- Structure and Dynamics of Macrophage Infectivity Potentiator Proteins from Pathogenic Bacteria and Protozoans Bound to Fluorinated Pipecolic Acid Inhibitors.Journal of medicinal chemistry · 2025Article
110 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
While the crucial role of intrinsically disordered proteins (IDPs) in the cell cycle is now recognized, deciphering their molecular mode of action at the structural level still remains highly challenging and requires a combination of many biophysical approaches. Among them, small angle X-ray scattering (SAXS) has been extremely successful in the last decade and has become an indispensable technique for addressing many of the fundamental questions regarding the activities of IDPs. After introducing some experimental issues specific to IDPs and in relation to the latest technical developments, this article presents the interest of the theory of polymer physics to evaluate the flexibility of fully disordered proteins. The different strategies to obtain 3-dimensional models of IDPs, free in solution and associated in a complex, are then reviewed. Indeed, recent computational advances have made it possible to readily extract maximum information from the scattering curve with a special emphasis on highly flexible systems, such as multidomain proteins and IDPs. Furthermore, integrated computational approaches now enable the generation of ensembles of conformers to translate the unique flexible characteristics of IDPs by taking into consideration the constraints of more and more various complementary experiment. In particular, a combination of SAXS with high-resolution techniques, such as x-ray crystallography and NMR, allows us to provide reliable models and to gain unique structural insights about the protein over multiple structural scales. The latest neutron scattering experiments also promise new advances in the study of the conformational changes of macromolecules involving more complex systems.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.