Evidence map›Paper›PMID 30733602›Full record

ReviewNature reviews. Molecular cell biology2019

The proteostasis network and its decline in ageing.

Mark S Hipp, Prasad Kasturi, F Ulrich Hartl

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Molecular cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 893 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
893citing papers in PubMed, 1 pooled it
–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

893 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Protein rheostasis: quality control in metastable proteomes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  11. From aggregate structure to disease trajectory: the role of the proteostasis network.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  12. Cellular and systemic modifiers of alpha-synuclein proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  13. Article
  14. Article
  15. Article
  16. Translation fidelity mechanisms and their changes in aging.bioRxiv : the preprint server for biology · 2026
    Article
  17. Article
  18. Article
  19. The Hallmarks of Aging: From Molecular Mechanisms to Clinical Translation.International journal of molecular sciences · 2026
    Review
  20. Article

833 more citing papers are in PubMed but not listed here.

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.

Mark S HippMax Planck Institute of Biochemistry, Department of Cellular Biochemistry, Martinsried, Germany.ORCID http://orcid.org/0000-0002-0497-3016
Prasad KasturiMax Planck Institute of Biochemistry, Department of Cellular Biochemistry, Martinsried, Germany.
F Ulrich HartlMax Planck Institute of Biochemistry, Department of Cellular Biochemistry, Martinsried, Germany. uhartl@biochem.mpg.de.ORCID http://orcid.org/0000-0002-7941-135X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ageing is a major risk factor for the development of many diseases, prominently including neurodegenerative disorders such as Alzheimer disease and Parkinson disease. A hallmark of many age-related diseases is the dysfunction in protein homeostasis (proteostasis), leading to the accumulation of protein aggregates. In healthy cells, a complex proteostasis network, comprising molecular chaperones and proteolytic machineries and their regulators, operates to ensure the maintenance of proteostasis. These factors coordinate protein synthesis with polypeptide folding, the conservation of protein conformation and protein degradation. However, sustaining proteome balance is a challenging task in the face of various external and endogenous stresses that accumulate during ageing. These stresses lead to the decline of proteostasis network capacity and proteome integrity. The resulting accumulation of misfolded and aggregated proteins affects, in particular, postmitotic cell types such as neurons, manifesting in disease. Recent analyses of proteome-wide changes that occur during ageing inform strategies to improve proteostasis. The possibilities of pharmacological augmentation of the capacity of proteostasis networks hold great promise for delaying the onset of age-related pathologies associated with proteome deterioration and for extending healthspan.

Indexed as

Protein FoldingProteolysisProteostasisAlzheimer DiseaseAnimalsHumansMolecular ChaperonesParkinson DiseaseMolecular Chaperones

Identifiers

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.