Evidence map›Paper›PMID 19519517›Full record

ReviewProtein and peptide letters2009

Hsp104 and prion propagation.

Nina V Romanova, Yury O Chernoff

Abstract readReview
In one paragraph

Review in Protein and peptide letters, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed.

  1. Review
  2. [PRIONPathogens (Basel, Switzerland) · 2022
    Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Recent Insights on Alzheimer's Disease Originating from Yeast Models.International journal of molecular sciences · 2018
    Review
  9. Article
  10. Review
  11. Analysis of [SWIMolecular microbiology · 2017
    Article
  12. Substrate Discrimination by ClpB and Hsp104.Frontiers in molecular biosciences · 2017
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

2 authors.

Nina V RomanovaSchool of Biology and Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, GA, USA.
Yury O Chernoff

Funding

GENETIC STUDY OF THE YEAST PRION INTERACTING PROTEINSR01GM058763 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI CHERNOFF, YURY O · 1999 to 2010
$2.6M
NIGMS NIH HHS R01 GM058763NIGMS NIH HHS R01GM58763
6 · The paper itself

Abstract

High-ordered aggregates (amyloids) may disrupt cell functions, cause toxicity at certain conditions and provide a basis for self-perpetuated, protein-based infectious heritable agents (prions). Heat shock proteins acting as molecular chaperones counteract protein aggregation and influence amyloid propagation. The yeast Hsp104/Hsp70/Hsp40 chaperone complex plays a crucial role in interactions with both ordered and unordered aggregates. The main focus of this review will be on the Hsp104 chaperone, a molecular "disaggregase".

Indexed as

AmyloidHeat-Shock ProteinsPrionsSaccharomyces cerevisiae ProteinsAmyloidHeat-Shock ProteinsHsP104 protein, S cerevisiaePrionsSaccharomyces cerevisiae Proteins

Identifiers

PMID19519517
PMCPMC2791106

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.