Evidence map›Paper›PMID 31146333›Full record

ArticleInternational journal of molecular sciences2019

Yeast Sup35 Prion Structure: Two Types, Four Parts, Many Variants.

Alexander A Dergalev, Alexander I Alexandrov, Roman I Ivannikov, Michael D Ter-Avanesyan, Vitaly V Kushnirov

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Chemical reviews · 2026
    Review
  3. Review
  4. Yeast Prions: Discovery, Nature, Cellular Manipulation and Implication.Journal of microbiology and biotechnology · 2025
    Review
  5. Article
  6. Article
  7. Mapping of Prion Structures in the Yeast Rnq1.International journal of molecular sciences · 2024
    Article
  8. Prions in Microbes: The Least in the Most.Journal of microbiology (Seoul, Korea) · 2023
    Review
  9. Anti-Prion Systems inViruses · 2022
    Review
  10. Review
  11. Antiprion systems in yeast cooperate to cure or prevent the generation of nearly all [Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Structural Bases of Prion Variation in Yeast.International journal of molecular sciences · 2022
    Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Review
  18. Normal levels of ribosome-associated chaperones cure two groups of [PSI+] prion variants.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  19. How Do Yeast Cells Contend with Prions?International journal of molecular sciences · 2020
    Review
  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

5 authors.

Alexander A DergalevA.N. Bach Institute of Biochemistry, Federal Research Center "Fundamentals of Biotechnology" of the Russian Academy of Sciences, Moscow 119071, Russia. alexanderdergalioff@gmail.com.ORCID 0000-0002-0696-923X
Alexander I AlexandrovA.N. Bach Institute of Biochemistry, Federal Research Center "Fundamentals of Biotechnology" of the Russian Academy of Sciences, Moscow 119071, Russia. alexvir@gmail.com.
Roman I IvannikovA.N. Bach Institute of Biochemistry, Federal Research Center "Fundamentals of Biotechnology" of the Russian Academy of Sciences, Moscow 119071, Russia. ivannikov_ra@mail.ru.
Michael D Ter-AvanesyanA.N. Bach Institute of Biochemistry, Federal Research Center "Fundamentals of Biotechnology" of the Russian Academy of Sciences, Moscow 119071, Russia.
Vitaly V KushnirovA.N. Bach Institute of Biochemistry, Federal Research Center "Fundamentals of Biotechnology" of the Russian Academy of Sciences, Moscow 119071, Russia. vvkushnirov@gmail.com.ORCID 0000-0003-0316-0766

Funding

Ministry of Science and Higher Education of the Russian Federation N/ARussian Foundation for Basic Research #17-04-00032Russian Science Foundation #17-14-01092
6 · The paper itself

Abstract

The yeast [

Indexed as

Endopeptidase KHeat-Shock ProteinsPeptide Termination FactorsPrionsProtein DomainsProtein MultimerizationProteolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsEndopeptidase KHeat-Shock ProteinsHsP104 protein, S cerevisiaePeptide Termination FactorsPrionsSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiaeamyloidprionprion coreprion variantsproteinase KRnq1Sup35

Identifiers

PMID31146333
PMCPMC6600473

What OpenQuestion holds

Textmetadata
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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.