Evidence map›Paper›PMID 28507126›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Direct observation of structure and dynamics during phase separation of an elastomeric protein.

Sean E Reichheld, Lisa D Muiznieks, Fred W Keeley, Simon Sharpe

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 119 papers.

0numbers the graph read from it
0cells of the map it votes in
119citing papers in PubMed
18.5field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

119 citing papers in PubMed, 266 citations in OpenAlex.

  1. Review
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  7. Arg-Tyr cation-π interactions drive phase separation and β-sheet assembly in native spider dragline silk.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  17. A Novel Gene Synthesis Platform for Designing Functional Protein Polymers.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
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  19. Review
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59 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Sean E ReichheldMolecular Medicine Program, The Hospital for Sick Children, Toronto, ON, Canada, M5G 0A4.
Lisa D MuiznieksMolecular Medicine Program, The Hospital for Sick Children, Toronto, ON, Canada, M5G 0A4.
Fred W KeeleyMolecular Medicine Program, The Hospital for Sick Children, Toronto, ON, Canada, M5G 0A4.
Simon SharpeMolecular Medicine Program, The Hospital for Sick Children, Toronto, ON, Canada, M5G 0A4; ssharpe@sickkids.ca.
Hospital for Sick Children · CAUniversity of Toronto · CA

Funding

CIHR
6 · The paper itself

Abstract

Despite its growing importance in biology and in biomaterials development, liquid-liquid phase separation of proteins remains poorly understood. In particular, the molecular mechanisms underlying simple coacervation of proteins, such as the extracellular matrix protein elastin, have not been reported. Coacervation of the elastin monomer, tropoelastin, in response to heat and salt is a critical step in the assembly of elastic fibers in vivo, preceding chemical cross-linking. Elastin-like polypeptides (ELPs) derived from the tropoelastin sequence have been shown to undergo a similar phase separation, allowing formation of biomaterials that closely mimic the material properties of native elastin. We have used NMR spectroscopy to obtain site-specific structure and dynamics of a self-assembling elastin-like polypeptide along its entire self-assembly pathway, from monomer through coacervation and into a cross-linked elastic material. Our data reveal that elastin-like hydrophobic domains are composed of transient β-turns in a highly dynamic and disordered chain, and that this disorder is retained both after phase separation and in elastic materials. Cross-linking domains are also highly disordered in monomeric and coacervated ELP

Indexed as

Biomimetic MaterialsCross-Linking ReagentsElasticityElastinIntrinsically Disordered ProteinsMicroscopy, Electron, ScanningMolecular Dynamics SimulationMultiprotein ComplexesNuclear Magnetic Resonance, BiomolecularPhase TransitionProtein ConformationProtein Structure, SecondaryTropoelastinCross-Linking ReagentsElastinIntrinsically Disordered ProteinsMultiprotein ComplexesTropoelastindynamicselastinNMRphase separationprotein structure

Identifiers

PMID28507126
PMCPMC5465911
OpenAlexW2615201923

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.