Evidence map›Paper›PMID 36067308›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Liquid to solid transition of elastin condensates.

Alfredo Vidal Ceballos, Jairo A Díaz A, Jonathan M Preston, Christo Vairamon, Christopher Shen, Ronald L Koder, Shana Elbaum-Garfinkle

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
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

24 citing papers in PubMed.

  1. Review
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  9. Review
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  14. Cellular Uptake of Phase-Separating Peptide Coacervates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Elastin recoil is driven by the hydrophobic effect.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Alfredo Vidal CeballosDepartment of Biochemistry, The Graduate Center of the City University of New York, New York, NY 10016.ORCID 0000-0003-1677-8450
Jairo A Díaz ADepartment of Chemical Engineering, Rochester Institute of Technology, Rochester, NY 14623.
Jonathan M PrestonDepartment of Physics, The City College of New York, New York, NY 10031.
Christo VairamonDepartment of Physics, The City College of New York, New York, NY 10031.
Christopher ShenDepartment of Physics, The City College of New York, New York, NY 10031.
Ronald L KoderDepartment of Physics, The City College of New York, New York, NY 10031.
Shana Elbaum-GarfinkleDepartment of Biochemistry, The Graduate Center of the City University of New York, New York, NY 10016.ORCID 0000-0002-3953-7329

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Liquid-liquid phase separation of tropoelastin has long been considered to be an important early step in the complex process of elastin fiber assembly in the body and has inspired the development of elastin-like peptides with a wide range of industrial and biomedical applications. Despite decades of study, the material state of the condensed liquid phase of elastin and its subsequent maturation remain poorly understood. Here, using a model minielastin that mimics the alternating domain structure of full-length tropoelastin, we examine the elastin liquid phase. We combine differential interference contrast (DIC), fluorescence, and scanning electron microscopy with particle-tracking microrheology to resolve the material transition occurring within elastin liquids over time in the absence of exogenous cross-linking. We find that this transition is accompanied by an intermediate stage marked by the coexistence of insoluble solid and dynamic liquid phases giving rise to significant spatial heterogeneities in material properties. We further demonstrate that varying the length of the terminal hydrophobic domains of minielastins can tune the maturation process. This work not only resolves an important step in the hierarchical assembly process of elastogenesis but further contributes mechanistic insight into the diverse repertoire of protein condensate maturation pathways with emerging importance across biology.

Indexed as

ElastinTropoelastinHydrophobic and Hydrophilic InteractionsPeptidesElastinPeptidesTropoelastinbiomolecular condensatesmaturationmicrorheology

Identifiers

PMID36067308
PMCPMC9477396

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Registered trials

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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.