Evidence map›Paper›PMID 26719342›Full record

ArticleThe Journal of biological chemistry2016

Cyclable Condensation and Hierarchical Assembly of Metastable Reflectin Proteins, the Drivers of Tunable Biophotonics.

Robert Levenson, Colton Bracken, Nicole Bush, Daniel E Morse

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 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. Review
  2. Neural responses to light stimulation in the octopus arm.The Journal of experimental biology · 2025
    Article
  3. Electrochemically Driven Optical Dynamics of Reflectin Protein Films.Advanced materials (Deerfield Beach, Fla.) · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Voltage-calibrated, finely tunable protein assembly.Journal of the Royal Society, Interface · 2023
    Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Structure, self-assembly, and properties of a truncated reflectin variant.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. Article
  17. Recent advances in bioelectronics chemistry.Chemical Society reviews · 2020
    Review
  18. Article
  19. 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

4 authors.

Robert LevensonFrom the Department of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, California 93106-5100.
Colton BrackenFrom the Department of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, California 93106-5100.
Nicole BushFrom the Department of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, California 93106-5100.
Daniel E MorseFrom the Department of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, California 93106-5100 d_morse@lifesci.ucsb.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reversible changes in the phosphorylation of reflectin proteins have been shown to drive the tunability of color and brightness of light reflected from specialized cells in the skin of squids and related cephalopods. We show here, using dynamic light scattering, electron microscopy, and fluorescence analyses, that reversible titration of the excess positive charges of the reflectins, comparable with that produced by phosphorylation, is sufficient to drive the reversible condensation and hierarchical assembly of these proteins. The results suggest a two-stage process in which charge neutralization first triggers condensation, resulting in the emergence of previously cryptic structures that subsequently mediate reversible, hierarchical assembly. The extent to which cyclability is seen in the in vitro formation and disassembly of complexes estimated to contain several thousand reflectin molecules suggests that intrinsic sequence- and structure-determined specificity governs the reversible condensation and assembly of the reflectins and that these processes are therefore sufficient to produce the reversible changes in refractive index, thickness, and spacing of the reflectin-containing subcellular Bragg lamellae to change the brightness and color of reflected light. This molecular mechanism points to the metastability of reflectins as the centrally important design principle governing biophotonic tunability in this system.

Indexed as

LightAnimalsDecapodiformesProteinsProtein StabilityProtein Structure, TertiaryProteinsbiomaterialsbiophotonicsintrinsically disordered proteiniridescenceprotein aggregationprotein assemblyprotein metastabilityprotein self-assemblyreflectinstunable

Identifiers

PMID26719342
PMCPMC4759182

What OpenQuestion holds

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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.