Evidence map›Paper›PMID 28798124›Full record

ArticleScience (New York, N.Y.)2017

Eye patches: Protein assembly of index-gradient squid lenses.

J Cai, J P Townsend, T C Dodson, P A Heiney, A M Sweeney

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed.

  1. Comparative analysis of the structure and crystallin composition of the lenses of freshwater fish and gastropods with respect to their vision.Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology · 2025
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Manipulating polydispersity of lens β-crystallins using divalent cations demonstrates evidence of calcium regulation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Review
  11. Article
  12. Article
  13. Nanocrystalline protein domains via salting-out.Acta crystallographica. Section F, Structural biology communications · 2021
    Article
  14. Review
  15. The intracellular environment affects protein-protein interactions.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

J CaiUniversity of Pennsylvania, Department of Physics and Astronomy, Philadelphia, PA, USA.ORCID 0000-0002-2970-0567
J P TownsendUniversity of Pennsylvania, Department of Biochemistry and Biophysics, Philadelphia, PA, USA.ORCID 0000-0002-4782-6083
T C DodsonUniversity of Pennsylvania, Department of Physics and Astronomy, Philadelphia, PA, USA.ORCID 0000-0003-1423-0088
P A HeineyUniversity of Pennsylvania, Department of Physics and Astronomy, Philadelphia, PA, USA.
A M SweeneyUniversity of Pennsylvania, Department of Physics and Astronomy, Philadelphia, PA, USA. alisonsw@physics.upenn.edu.ORCID 0000-0002-6009-8551

Funding

STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008275 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI WAND, A. JOSHUA · 1988 to 2018
$6.0M
NIGMS NIH HHS T32 GM008275
6 · The paper itself

Abstract

A parabolic relationship between lens radius and refractive index allows spherical lenses to avoid spherical aberration. We show that in squid, patchy colloidal physics resulted from an evolutionary radiation of globular S-crystallin proteins. Small-angle x-ray scattering experiments on lens tissue show colloidal gels of S-crystallins at all radial positions. Sparse lens materials form via low-valence linkages between disordered loops protruding from the protein surface. The loops are polydisperse and bind via a set of hydrogen bonds between disordered side chains. Peripheral lens regions with low particle valence form stable, volume-spanning gels at low density, whereas central regions with higher average valence gel at higher densities. The proteins demonstrate an evolved set of linkers for self-assembly of nanoparticles into volumetric materials.

Indexed as

DecapodiformesAmino Acid SequenceAnimalsCrystallinsLens, CrystallineMolecular Dynamics SimulationProtein ConformationProtein Interaction MapsRNA, MessengerScattering, Small AngleSequence Analysis, RNACrystallinsRNA, Messenger

Identifiers

PMID28798124
PMCPMC5682922

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.