ArticleeLife2017
The liquid structure of elastin.
Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
91 citing papers in PubMed.
- The emerging synergy of experimental and computational approaches for therapeutic modulation of biomolecular condensates.SLAS discovery : advancing life sciences R & D · 2026Review
- Article
- Condensates as Conformation Editors of Disordered Client Proteins.Journal of the American Chemical Society · 2026Article
- Folded domains impose structural heterogeneity and attenuated dynamics in biomolecular condensates.Nature communications · 2026Article
- Functions of prolyl hydroxylation in elastin.The Journal of biological chemistry · 2026Article
- Dynamic yet well-defined organization of the FUS RGG3 dense phase.Communications chemistry · 2026Article
- Biomimetic Approach to the Formation of Protein Materials via Complex Coacervation of Engineered Polypeptides.ACS synthetic biology · 2026Article
- Harnessing Phase Separation in the Extracellular Matrix: From Mechanisms to Therapeutic Opportunities.BioMed research international · 2026Review
- Evolutionary constraints on positional sequence, collective properties and sequence style of tropoelastin dictated by fundamental requirements for formation and function of the extracellular elastic matrix.Matrix biology plus · 2025Review
- Residue-Resolved Liquid-State Hyperpolarized NMR of Peptide Condensate Surfaces.Journal of the American Chemical Society · 2025Article
- Review
- Amino acid transfer free energies reveal thermodynamic driving forces in biomolecular condensate formation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Toward understanding biomolecular materials comprising intrinsically disordered proteinsMolecular systems design & engineering · 2025Review
- Selective engineering of condensation properties of single-stranded DNA binding (SSB) protein via its intrinsically disordered linker region.Nucleic acids research · 2025Article
- Functional Biomaterials Derived from Protein Liquid-Liquid Phase Separation and Liquid-to-Solid Transition.Advanced materials (Deerfield Beach, Fla.) · 2025Review
- Determining the Role of Electrostatics in the Making and Breaking of the Caprin1-ATP Nanocondensate.The journal of physical chemistry. B · 2025Article
- R5 Peptides Constitute Condensed Phases with Liquid-Like Properties in Biomimetic Silica Capsules.The journal of physical chemistry letters · 2025Article
- Microphase separation produces interfacial environment within diblock biomolecular condensates.eLife · 2025Article
- Article
- The Internal Structural Dynamics of Elastin-Like Polypeptide Assemblies byAnalytical chemistry · 2025Article
31 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.
Funding
Abstract
The protein elastin imparts extensibility, elastic recoil, and resilience to tissues including arterial walls, skin, lung alveoli, and the uterus. Elastin and elastin-like peptides are hydrophobic, disordered, and undergo liquid-liquid phase separation upon self-assembly. Despite extensive study, the structure of elastin remains controversial. We use molecular dynamics simulations on a massive scale to elucidate the structural ensemble of aggregated elastin-like peptides. Consistent with the entropic nature of elastic recoil, the aggregated state is stabilized by the hydrophobic effect. However, self-assembly does not entail formation of a hydrophobic core. The polypeptide backbone forms transient, sparse hydrogen-bonded turns and remains significantly hydrated even as self-assembly triples the extent of non-polar side chain contacts. Individual chains in the assembly approach a maximally-disordered, melt-like state which may be called the liquid state of proteins. These findings resolve long-standing controversies regarding elastin structure and function and afford insight into the phase separation of disordered proteins.
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What OpenQuestion holds
Registered trials
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.