Evidence map›Paper›PMID 28099852›Full record

ArticleCell reports2017

Yeast Short-Lived Actin-Associated Protein Forms a Metastable Prion in Response to Thermal Stress.

Tatiana A Chernova, Denis A Kiktev, Andrey V Romanyuk, John R Shanks, Oskar Laur, Moiez Ali, Abheek Ghosh, Dami Kim, Zhen Yang, Maggie Mang and 2 more

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

36 citing papers in PubMed, 48 citations in OpenAlex.

  1. Anti-Prion Systems in Saccharomyces cerevisiae.Journal of neurochemistry · 2025
    Review
  2. Article
  3. Article
  4. How Big Is the Yeast Prion Universe?International journal of molecular sciences · 2023
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Structural Bases of Prion Variation in Yeast.International journal of molecular sciences · 2022
    Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Neural regeneration research · 2021
    Review
  15. Review
  16. Review
  17. Mechanisms for Curing Yeast Prions.International journal of molecular sciences · 2020
    Review
  18. Article
  19. How Do Yeast Cells Contend with Prions?International journal of molecular sciences · 2020
    Review
  20. Prions: Roles in Development and Adaptive Evolution.Journal of molecular evolution · 2020
    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

12 authors at 3 institutions in 2 countries.

Tatiana A ChernovaDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA. Electronic address: tcherno@emory.edu.
Denis A KiktevSchool of Biological Sciences, Georgia Institute of Technology, Atlanta, GA 30332-2000, USA; Laboratory of Amyloid Biology and Institute of Translational Biomedicine, St. Petersburg State University, St. Petersburg 199034, Russia.
Andrey V RomanyukSchool of Biological Sciences, Georgia Institute of Technology, Atlanta, GA 30332-2000, USA.
John R ShanksDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA.
Oskar LaurDivision of Microbiology, Yerkes Research Center, Emory University, Atlanta, GA 30322, USA.
Moiez AliDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA.
Abheek GhoshDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA.
Dami KimDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA.
Zhen YangDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA.
Maggie MangDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA.
Yury O ChernoffSchool of Biological Sciences, Georgia Institute of Technology, Atlanta, GA 30332-2000, USA; Laboratory of Amyloid Biology and Institute of Translational Biomedicine, St. Petersburg State University, St. Petersburg 199034, Russia. Electronic address: yury.chernoff@biology.gatech.edu.
Keith D WilkinsonDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA. Electronic address: genekdw@emory.edu.
Emory University · USGeorgia Institute of Technology · USSt Petersburg University · RU

Funding

Ubiquitin and regulation of prion induction by a short-lived proteinR01GM093294 · NIGMS · EMORY UNIVERSITY · PI WILKINSON, KEITH D · 2011 to 2014
$1.3M
NIGMS NIH HHS R01 GM093294
6 · The paper itself

Abstract

Self-perpetuating ordered protein aggregates (amyloids and prions) are associated with a variety of neurodegenerative disorders. Although environmental agents have been linked to certain amyloid diseases, the molecular basis of their action remains unclear. We have employed endogenous yeast prions as a model system to study environmental control of amyloid formation. A short-lived actin-associated yeast protein Lsb2 can trigger prion formation by other proteins in a mode regulated by the cytoskeleton and ubiquitin-dependent processes. Here, we show that such a heterologous prion induction is due to the ability of Lsb2 to form a transient prion state, generated in response to thermal stress. Evolutionary acquisition of prion-inducing activity by Lsb2 is traced to a single amino acid change, coinciding with the acquisition of thermotolerance in the Saccharomyces yeast lineage. This raises the intriguing possibility that the transient prion formation could aid in functioning of Lsb2 at higher temperatures.

Indexed as

Amino Acid SequenceCarrier ProteinsCytoskeletonMeiosisMolecular ChaperonesMutagenesis, Site-DirectedPeptide Termination FactorsPrionsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentTemperatureUbiquitinationCarrier Proteinslas17-binding protein Lsb2, S cerevisiaeLsb1 protein, S cerevisiaeMolecular ChaperonesPeptide Termination FactorsPrionsSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiaeactinamyloidschaperoneenvironmental stressheat shockprionsSup35ubiquitination

Identifiers

PMID28099852
PMCPMC5267347
OpenAlexW2577386528

What OpenQuestion holds

Textmetadata
LicenceTDM
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.