Evidence map›Paper›PMID 11967376›Full record

ArticleProtein science : a publication of the Protein Society2002

Self-assembly of the hydrophobin SC3 proceeds via two structural intermediates.

Marcel L de Vocht, Ilya Reviakine, Wolf-Peter Ulrich, Wilma Bergsma-Schutter, Han A B Wösten, Horst Vogel, Alain Brisson, Joseph G H Wessels, George T Robillard

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Identification of Candidate Ice Nucleation Activity (INA) Genes inJournal of fungi (Basel, Switzerland) · 2022
    Article
  4. Article
  5. Review
  6. Article
  7. Crystallization and preliminary X-ray diffraction of the surfactant protein Lv-ranaspumin from the frog Leptodactylus vastus.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Structural basis for rodlet assembly in fungal hydrophobins.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  15. Article
  16. 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

9 authors.

Marcel L de VochtGroningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
Ilya Reviakine
Wolf-Peter Ulrich
Wilma Bergsma-Schutter
Han A B Wösten
Horst Vogel
Alain Brisson
Joseph G H Wessels
George T Robillard

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hydrophobins self assemble into amphipathic films at hydrophobic-hydrophilic interfaces. These proteins are involved in a broad range of processes in fungal development. We have studied the conformational changes that accompany the self-assembly of the hydrophobin SC3 with polarization-modulation infrared reflection absorption spectroscopy, attenuated total reflection Fourier transform infrared spectroscopy, and circular dichroism, and related them to changes in morphology as observed by electron microcopy. Three states of SC3 have been spectroscopically identified previously as follows: the monomeric state, the alpha-helical state that is formed upon binding to a hydrophobic solid, and the beta-sheet state, which is formed at the air-water interface. Here, we show that the formation of the beta-sheet state of SC3 proceeds via two intermediates. The first intermediate has an infrared spectrum indistinguishable from that of the alpha-helical state of SC3. The second intermediate is rich in beta-sheet structure and has a featureless appearance under the electron microscope. The end state has the same secondary structure, but is characterized by the familiar 10-nm-wide rodlets.

Indexed as

Bacterial ProteinsCircular DichroismFungal ProteinsMicroscopy, ElectronProtein Structure, SecondarySpectrophotometry, InfraredBacterial ProteinsFungal Proteins

Identifiers

PMID11967376
PMCPMC2373556

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.