Evidence map›Paper›PMID 27018803›Full record

ArticleNature structural & molecular biology2016

Universality of supersaturation in protein-fiber formation.

Troy Cellmer, Frank A Ferrone, William A Eaton

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Generating the polymorph landscapes of amyloid fibrils using AI: RibbonFold.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Review
  5. Phenotypic screening of the ReFRAME drug repurposing library to discover new drugs for treating sickle cell disease.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Allosteric control of hemoglobin S fiber formation by oxygen and its relation to the pathophysiology of sickle cell disease.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Surveying the Energy Landscapes of Aβ Fibril Polymorphism.The journal of physical chemistry. B · 2018
    Article
  18. Solid nuclei and liquid droplets: A parallel treatment for 3 phase systems.Protein science : a publication of the Protein Society · 2018
    Article
  19. Article
  20. Review
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

3 authors.

Troy CellmerLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA.
Frank A FerroneDepartment of Physics, Drexel University, Philadelphia, Pennsylvania, USA.
William A EatonLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA.

Funding

Sickle cell disease molecular pathogenesis and drug therapyZIADK029053 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI EATON, WILLIAM · 2009 to 2025
$24.8M
Screening for a Drug for Sickle Cell DiseaseZ01DK029053 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI EATON, WILLIAM · 2007 to 2008
$669k
Intramural NIH HHS Z01 DK029053
6 · The paper itself

Abstract

The thermodynamics and kinetics of the aggregation of sickle-cell hemoglobin into fibers have been studied in great detail under a wide range of solution conditions. The stability of the fiber is measured by the solubility; the kinetics is characterized by a delay before the appearance of fibers. A review of data in the literature shows that there is no correlation of the delay time with fiber stability and only a weak correlation with the initial protein concentration. There is, however, a striking collapse of all the data onto a single universal curve when the delay time is plotted versus the supersaturation, which is the ratio of the initial protein concentration to the solubility, expressed as activities. Collapse onto the same universal curve is also obtained when using delay times calculated from the double-nucleation theoretical model.

Indexed as

Hemoglobin, SickleHumansKineticsModels, MolecularProtein AggregatesSolubilityThermodynamicsHemoglobin, SickleProtein Aggregates

Identifiers

PMID27018803
PMCPMC7329141

What OpenQuestion holds

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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.