Evidence map›Paper›PMID 33315891›Full record

ArticlePLoS computational biology2020

Proteostasis is adaptive: Balancing chaperone holdases against foldases.

Adam Mr de Graff, David E Mosedale, Tilly Sharp, Ken A Dill, David J Grainger

Open access · goldAbstract read
In one paragraph

Article in PLoS computational biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. A population threshold for dedicated teaching.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. G-quadruplexes catalyze protein folding by reshaping the energetic landscape.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Physiological adventures inMicrobiology and molecular biology reviews : MMBR · 2024
    Review
  15. Review
  16. The Functionality of IbpA fromInternational journal of molecular sciences · 2023
    Article
  17. Review
  18. Review
  19. Review
  20. The Protein Folding Problem: The Role of Theory.Journal of molecular biology · 2021
    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

5 authors at 1 institution in 1 country.

Adam Mr de GraffMethuselah Health UK Ltd, Cambridge, United Kingdom.ORCID 0000-0001-8529-8587
David E MosedaleMethuselah Health UK Ltd, Cambridge, United Kingdom.ORCID 0000-0002-2075-0699
Tilly SharpMethuselah Health UK Ltd, Cambridge, United Kingdom.ORCID 0000-0002-3389-2119
Ken A DillLaufer Center for Physical & Quantitative Biology, Stony Brook University, Stony Brook, New York, United States of America.ORCID 0000-0002-2390-2002
David J GraingerMethuselah Health UK Ltd, Cambridge, United Kingdom.ORCID 0000-0002-3211-2045
Stony Brook University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Because a cell must adapt to different stresses and growth rates, its proteostasis system must too. How do cells detect and adjust proteome folding to different conditions? Here, we explore a biophysical cost-benefit principle, namely that the cell should keep its proteome as folded as possible at the minimum possible energy cost. This can be achieved by differential expression of chaperones-balancing foldases (which accelerate folding) against holdases (which act as parking spots). The model captures changes in the foldase-holdase ratio observed both within organisms during aging and across organisms of varying metabolic rates. This work describes a simple biophysical mechanism by which cellular proteostasis adapts to meet the needs of a changing growth environment.

Indexed as

Protein FoldingProteostasisAnimalsHumansKineticsMammalsModels, TheoreticalMolecular ChaperonesProtein BindingMolecular Chaperones

Identifiers

PMID33315891
PMCPMC7769611
OpenAlexW3110739506

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.