Evidence map›Paper›PMID 31558609›Full record

ArticleThe Journal of biological chemistry2019

Calibration between trigger and color: Neutralization of a genetically encoded coulombic switch and dynamic arrest precisely tune reflectin assembly.

Robert Levenson, Colton Bracken, Cristian Sharma, Jerome Santos, Claire Arata, Brandon Malady, Daniel E Morse

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Review
  2. Electrochemically Driven Optical Dynamics of Reflectin Protein Films.Advanced materials (Deerfield Beach, Fla.) · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Voltage-calibrated, finely tunable protein assembly.Journal of the Royal Society, Interface · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. 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
  17. Article
  18. 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

7 authors.

Robert LevensonDepartment of Molecular, Cellular and Developmental Biology and the Institute for Collaborative Biotechnologies, University of California, Santa Barbara, California 93106-5100.ORCID 0000-0001-8251-626X
Colton BrackenDepartment of Molecular, Cellular and Developmental Biology and the Institute for Collaborative Biotechnologies, University of California, Santa Barbara, California 93106-5100.
Cristian SharmaDepartment of Molecular, Cellular and Developmental Biology and the Institute for Collaborative Biotechnologies, University of California, Santa Barbara, California 93106-5100.ORCID 0000-0003-4699-623X
Jerome SantosDepartment of Molecular, Cellular and Developmental Biology and the Institute for Collaborative Biotechnologies, University of California, Santa Barbara, California 93106-5100.
Claire ArataDepartment of Molecular, Cellular and Developmental Biology and the Institute for Collaborative Biotechnologies, University of California, Santa Barbara, California 93106-5100.
Brandon MaladyDepartment of Molecular, Cellular and Developmental Biology and the Institute for Collaborative Biotechnologies, University of California, Santa Barbara, California 93106-5100.
Daniel E MorseDepartment of Molecular, Cellular and Developmental Biology and the Institute for Collaborative Biotechnologies, 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

Reflectin proteins are widely distributed in reflective structures in cephalopods. However, only in loliginid squids are they and the subwavelength photonic structures they control dynamically tunable, driving changes in skin color for camouflage and communication. The reflectins are block copolymers with repeated canonical domains interspersed with cationic linkers. Neurotransmitter-activated signal transduction culminates in catalytic phosphorylation of the tunable reflectins' cationic linkers; the resulting charge neutralization overcomes coulombic repulsion to progressively allow condensation, folding, and assembly into multimeric spheres of tunable well-defined size and low polydispersity. Here, we used dynamic light scattering, transmission EM, CD, atomic force microscopy, and fluorimetry to analyze the structural transitions of reflectins A1 and A2. We also analyzed the assembly behavior of phosphomimetic, deletion, and other mutants in conjunction with pH titration as an

Indexed as

Amino Acid SequenceAnimalsCalibrationCephalopodaColorComputational BiologyIntrinsically Disordered ProteinsIntrinsically Disordered Proteinsbiomaterialsbiophotonicsintrinsically disordered proteiniridescenceliquid-liquid phase separationprotein aggregationprotein assemblyprotein-protein interactionprotein self-assemblyreflectins

Identifiers

PMID31558609
PMCPMC6851332

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.