Evidence map›Paper›PMID 33510441›Full record

ReviewNature reviews. Molecular cell biology2021

Biomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing.

Simon Alberti, Anthony A Hyman

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Molecular cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 664 papers.

0numbers the graph read from it
0cells of the map it votes in
664citing papers in PubMed
63.5field-weighted citation impact, top 1% 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

664 citing papers in PubMed, 1,149 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Protein rheostasis: quality control in metastable proteomes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  5. Article
  6. A New Soaking Protocol to Live StainbioRxiv : the preprint server for biology · 2026
    Article
  7. Cellular and systemic modifiers of alpha-synuclein proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  8. Differential proteostasis imbalance and the molecular basis of distinct synucleinopathies and tauopathies.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  9. Review
  10. Article
  11. New perspectives on plant water sensing.Science China. Life sciences · 2026
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Principles and mechanisms of plant acclimation to heat stress.Nature reviews. Molecular cell biology · 2026
    Review
  20. Article

604 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

2 authors at 2 institutions in 1 country.

Simon AlbertiTechnische Universität Dresden, Biotechnology Center (BIOTEC) and Center for Molecular and Cellular Engineering (CMCB), Dresden, Germany. simon.alberti@tu-dresden.de.ORCID http://orcid.org/0000-0003-4017-6505
Anthony A HymanMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany. hyman@mpi-cbg.de.
Center for Systems Biology Dresden · DEMax Planck Institute of Molecular Cell Biology and Genetics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biomolecular condensates are membraneless intracellular assemblies that often form via liquid-liquid phase separation and have the ability to concentrate biopolymers. Research over the past 10 years has revealed that condensates play fundamental roles in cellular organization and physiology, and our understanding of the molecular principles, components and forces underlying their formation has substantially increased. Condensate assembly is tightly regulated in the intracellular environment, and failure to control condensate properties, formation and dissolution can lead to protein misfolding and aggregation, which are often the cause of ageing-associated diseases. In this Review, we describe the mechanisms and regulation of condensate assembly and dissolution, highlight recent advances in understanding the role of biomolecular condensates in ageing and disease, and discuss how cellular stress, ageing-related loss of homeostasis and a decline in protein quality control may contribute to the formation of aberrant, disease-causing condensates. Our improved understanding of condensate pathology provides a promising path for the treatment of protein aggregation diseases.

Indexed as

AgingAnimalsCell Physiological PhenomenaHumansMacromolecular SubstancesMultiprotein ComplexesProtein AggregatesProtein Aggregation, PathologicalStress, PhysiologicalMacromolecular SubstancesMultiprotein ComplexesProtein Aggregates

Identifiers

PMID33510441
OpenAlexW3123015207

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.