Evidence map›Paper›PMID 21454575›Full record

ArticleThe Journal of biological chemistry2011

Recruitment of class I hydrophobins to the air:water interface initiates a multi-step process of functional amyloid formation.

Vanessa K Morris, Qin Ren, Ingrid Macindoe, Ann H Kwan, Nolene Byrne, Margaret Sunde

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. 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
–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

25 citing papers in PubMed.

  1. Establishment of CRISPR/Cas9 Genome Editing inJournal of fungi (Basel, Switzerland) · 2026
    Article
  2. What makes functional amyloids work?Critical reviews in biochemistry and molecular biology · 2022
    Review
  3. Microorganisms · 2022
    Review
  4. Article
  5. Article
  6. Assembly and disassembly ofCell surface (Amsterdam, Netherlands) · 2019
    Article
  7. Review
  8. The Journal of biological chemistry · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. BslA is a self-assembling bacterial hydrophobin that coats the Bacillus subtilis biofilm.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  19. Article
  20. Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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

6 authors.

Vanessa K MorrisSchool of Molecular Bioscience, University of Sydney, Sydney, New South Wales, Australia.
Qin Ren
Ingrid Macindoe
Ann H Kwan
Nolene Byrne
Margaret Sunde

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Class I fungal hydrophobins form amphipathic monolayers composed of amyloid rodlets. This is a remarkable case of functional amyloid formation in that a hydrophobic:hydrophilic interface is required to trigger the self-assembly of the proteins. The mechanism of rodlet formation and the role of the interface in this process have not been well understood. Here, we have studied the effect of a range of additives, including ionic liquids, alcohols, and detergents, on rodlet formation by two class I hydrophobins, EAS and DewA. Although the conformation of the hydrophobins in these different solutions is not altered, we observe that the rate of rodlet formation is slowed as the surface tension of the solution is decreased, regardless of the nature of the additive. These results suggest that interface properties are of critical importance for the recruitment, alignment, and structural rearrangement of the amphipathic hydrophobin monomers. This work gives insight into the forces that drive macromolecular assembly of this unique family of proteins and allows us to propose a three-stage model for the interface-driven formation of rodlets.

Indexed as

AmyloidAspergillus nidulansFungal ProteinsNeurospora crassaPhase TransitionRecombinant ProteinsAmyloidDEWA protein, Asperigillus nidulansFungal ProteinsRecombinant Proteins

Identifiers

PMID21454575
PMCPMC3091204

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.