Evidence map›Paper›PMID 37084706›Full record

ArticleNano letters2023

Liquid-Liquid Phase Separation Primes Spider Silk Proteins for Fiber Formation via a Conditional Sticker Domain.

Axel Leppert, Gefei Chen, Dilraj Lama, Cagla Sahin, Vaida Railaite, Olga Shilkova, Tina Arndt, Erik G Marklund, David P Lane, Anna Rising and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Nano letters, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
8.3field-weighted citation impact, top 2% of its field
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

25 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Liquid-liquid phase separation enables chromatography-free purification and high-performance spidroin-amyloid hybrid silk fibers.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Arg-Tyr cation-π interactions drive phase separation and β-sheet assembly in native spider dragline silk.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Nanostructured Protein Surfaces Inspired by Spider Silk.Advanced materials (Deerfield Beach, Fla.) · 2025
    Review
  9. Article
  10. Developing anACS synthetic biology · 2025
    Article
  11. Article
  12. Exploring the functional properties ofMaterials today. Communications · 2025
    Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
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  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

11 authors at 3 institutions in 2 countries.

Axel LeppertDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, S-17165 Solna, Sweden.ORCID 0000-0001-6223-3350
Gefei ChenDepartment of Biosciences and Nutrition, Karolinska Institutet, S-14157 Huddinge, Sweden.ORCID 0000-0002-5543-5963
Dilraj LamaDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, S-17165 Solna, Sweden.
Cagla SahinDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, S-17165 Solna, Sweden.ORCID 0000-0002-2889-5200
Vaida RailaiteDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, S-17165 Solna, Sweden.
Olga ShilkovaDepartment of Biosciences and Nutrition, Karolinska Institutet, S-14157 Huddinge, Sweden.
Tina ArndtDepartment of Biosciences and Nutrition, Karolinska Institutet, S-14157 Huddinge, Sweden.ORCID 0000-0002-5190-0039
Erik G MarklundDepartment of Chemistry - BMC, Uppsala University, S-75123 Uppsala, Sweden.ORCID 0000-0002-9804-5009
David P LaneDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, S-17165 Solna, Sweden.
Anna RisingDepartment of Biosciences and Nutrition, Karolinska Institutet, S-14157 Huddinge, Sweden.ORCID 0000-0002-1872-1207
Michael LandrehDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, S-17165 Solna, Sweden.ORCID 0000-0002-7958-4074
Karolinska Institutet · SEUppsala University · SEUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many protein condensates can convert to fibrillar aggregates, but the underlying mechanisms are unclear. Liquid-liquid phase separation (LLPS) of spider silk proteins, spidroins, suggests a regulatory switch between both states. Here, we combine microscopy and native mass spectrometry to investigate the influence of protein sequence, ions, and regulatory domains on spidroin LLPS. We find that salting out-effects drive LLPS via low-affinity stickers in the repeat domains. Interestingly, conditions that enable LLPS simultaneously cause dissociation of the dimeric C-terminal domain (CTD), priming it for aggregation. Since the CTD enhances LLPS of spidroins but is also required for their conversion into amyloid-like fibers, we expand the stickers and spacers-model of phase separation with the concept of folded domains as conditional stickers that represent regulatory units.

Indexed as

FibroinsSilkAmino Acid SequenceArthropod ProteinsArthropod ProteinsFibroinsSilkfunctional amyloidnative mass spectrometryPhase separationstickers and spacers-model

Identifiers

PMID37084706
PMCPMC10311596
OpenAlexW4366605540

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.