Evidence map›Paper›PMID 26438827›Full record

ArticleThe Journal of cell biology2015

Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery.

Jonathan O'Driscoll, Daniel Clare, Helen Saibil

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2015. 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
2.3field-weighted citation impact, top 12% 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, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Big versus small: The impact of aggregate size in disease.Protein science : a publication of the Protein Society · 2023
    Review
  6. Article
  7. Article
  8. Review
  9. Nuclear envelope budding is a response to cellular stress.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Recent Insights on Alzheimer's Disease Originating from Yeast Models.International journal of molecular sciences · 2018
    Review
  17. Article
  18. Article
  19. The Insoluble Protein Deposit (IPOD) in Yeast.Frontiers in molecular neuroscience · 2018
    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

3 authors at 2 institutions in 1 country.

Jonathan O'DriscollCrystallography, Department of Biological Sciences, Institute of Structural and Molecular Biology, Birkbeck College, London WC1E 7HX, UK.
Daniel ClareCrystallography, Department of Biological Sciences, Institute of Structural and Molecular Biology, Birkbeck College, London WC1E 7HX, UK.
Helen SaibilCrystallography, Department of Biological Sciences, Institute of Structural and Molecular Biology, Birkbeck College, London WC1E 7HX, UK h.saibil@mail.cryst.bbk.ac.uk.
Institute of Structural and Molecular Biology · GBBirkbeck, University of London · GB

Funding

Wellcome Trust 079605Wellcome Trust 086018Wellcome Trust 089050Wellcome Trust 101488
6 · The paper itself

Abstract

Prions consist of misfolded proteins that have adopted an infectious amyloid conformation. In vivo, prion biogenesis is intimately associated with the protein quality control machinery. Using electron tomography, we probed the effects of the heat shock protein Hsp70 chaperone system on the structure of a model yeast [PSI+] prion in situ. Individual Hsp70 deletions shift the balance between fibril assembly and disassembly, resulting in a variable shell of nonfibrillar, but still immobile, aggregates at the surface of the [PSI+] prion deposits. Both Hsp104 (an Hsp100 disaggregase) and Sse1 (the major yeast form of Hsp110) were localized to this surface shell of [PSI+] deposits in the deletion mutants. Elevation of Hsp104 expression promoted the appearance of this novel, nonfibrillar form of the prion aggregate. Moreover, Sse1 was found to regulate prion fibril length. Our studies reveal a key role for Sse1 (Hsp110), in cooperation with Hsp104, in regulating the length and assembly state of [PSI+] prion fibrils in vivo.

Indexed as

Heat-Shock ProteinsHSP110 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsPrionsProtein AggregatesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsHeat-Shock ProteinsHsP104 protein, S cerevisiaeHSP110 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsPrionsProtein AggregatesSaccharomyces cerevisiae ProteinsSSE1 protein, S cerevisiae

Identifiers

PMID26438827
PMCPMC4602031
OpenAlexW1930229629

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.