Evidence map›Paper›PMID 19491937›Full record

ArticleNature structural & molecular biology2009

Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI+].

Peter M Tessier, Susan Lindquist

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing 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

43 citing papers in PubMed.

  1. Article
  2. Article
  3. Trans-seeding of Alzheimer-related tau protein by a yeast prion.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2022
    Article
  4. A bacteria-based genetic assay detects prion formation.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Mechanisms of amyloid formation revealed by solution NMR.Progress in nuclear magnetic resonance spectroscopy · 2015
    Review
  11. Article
  12. Review
  13. Looked at life from both sides now.Life (Basel, Switzerland) · 2014
    Review
  14. Article
  15. Article
  16. Ion-specific effects on prion nucleation and strain formation.The Journal of biological chemistry · 2013
    Article
  17. Article
  18. Article
  19. Article
  20. Prions in yeast.Genetics · 2012
    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

2 authors.

Peter M TessierCenter of Biotechnology and Interdisciplinary Studies, Department of Chemical & Biological Engineering, Rensselaer Polytechnic Institute, Troy, New York, USA. tessier@rpi.edu
Susan Lindquist

Funding

THE FUNCTION OF HEAT SHOCK RESPONSE IN DROSOPHILAR01GM025874 · NIGMS · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI WHITESELL, LUKE J · 1985 to 2016
$4.7M
CHAPERONE PROTEIN AND PROTEIN CONFORMATIONAL SWITCHESR37GM025874 · NIGMS · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI LINDQUIST, SUSAN L. · 1997 to 2006
$2.7M
Howard Hughes Medical InstituteNIGMS NIH HHS GM25874NIGMS NIH HHS R01 GM025874NIGMS NIH HHS R37 GM025874
6 · The paper itself

Abstract

Prions are proteins that can access multiple conformations, at least one of which is beta-sheet rich, infectious and self-perpetuating in nature. These infectious proteins show several remarkable biological activities, including the ability to form multiple infectious prion conformations, also known as strains or variants, encoding unique biological phenotypes, and to establish and overcome prion species (transmission) barriers. In this Perspective, we highlight recent studies of the yeast prion [PSI(+)], using various biochemical and structural methods, that have begun to illuminate the molecular mechanisms by which self-perpetuating prions encipher such biological activities. We also discuss several aspects of prion conformational change and structure that remain either unknown or controversial, and we propose approaches to accelerate the understanding of these enigmatic, infectious conformers.

Indexed as

Amino Acid SequenceAmyloidBinding SitesCrystallizationFungal ProteinsGenetic VariationModels, MolecularMolecular Sequence DataPeptide Termination FactorsPrionsProtein ConformationProtein FoldingProtein Structure, SecondarySaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSpecies SpecificityAmyloidFungal ProteinsPeptide Termination FactorsPrionsSaccharomyces cerevisiae ProteinsSup35 protein, Candida albicansSUP35 protein, S cerevisiae

Identifiers

PMID19491937
PMCPMC4502417

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.