Evidence map›Paper›PMID 19577567›Full record

ReviewFEBS letters2009

The GroEL/GroES cis cavity as a passive anti-aggregation device.

Arthur L Horwich, Adrian C Apetri, Wayne A Fenton

Abstract readReview
In one paragraph

Review in FEBS letters, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. A diminished hydrophobic effect inside the GroEL/ES cavity contributes to protein substrate destabilization.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Mechanisms of Cotranslational Protein Maturation in Bacteria.Frontiers in molecular biosciences · 2021
    Review
  12. Redefining Molecular Chaperones as Chaotropes.Frontiers in molecular biosciences · 2021
    Review
  13. Iterative annealing mechanism explains the functions of the GroEL and RNA chaperones.Protein science : a publication of the Protein Society · 2020
    Review
  14. Review
  15. Article
  16. Folding against the wind.Nature chemical biology · 2018
    Article
  17. Folding of maltose binding protein outside of and in GroEL.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. Article
  19. Single-Ring Intermediates Are Essential for Some Chaperonins.Frontiers in molecular biosciences · 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.

Arthur L HorwichHoward Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510, USA. arthur.horwich@yale.edu
Adrian C Apetri
Wayne A Fenton

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

The GroEL/GroES chaperonin folding chamber is an encapsulated space of approximately 65 A diameter with a hydrophilic wall, inside of which many cellular proteins reach the native state. The question of whether the cavity wall actively directs folding reactions or is playing a passive role has been open. We review past and recent observations and conclude that the chamber functions as a passive "Anfinsen cage" that prevents folding monomers from multimolecular aggregation.

Indexed as

ActinsCapsid ProteinsChaperonin 10Chaperonin 60HumansMutationProtein FoldingProteinsSubstrate SpecificityTubulinActinsCapsid ProteinsChaperonin 10Chaperonin 60gp23 protein, Bacteriophage T4ProteinsTubulin

Identifiers

PMID19577567
PMCPMC2759771

What OpenQuestion holds

Textmetadata
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.