Evidence map›Paper›PMID 34725341›Full record

ArticleNature communications2021

Sustained enzymatic activity and flow in crowded protein droplets.

Andrea Testa, Mirco Dindo, Aleksander A Rebane, Babak Nasouri, Robert W Style, Ramin Golestanian, Eric R Dufresne, Paola Laurino

Abstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing 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

55 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Nucleation Kinetics Reveals a Distinct Biological Function Space of Biomolecular Condensates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  6. Review
  7. A Self-Organized Liquid Reaction Container for Cellular Memory.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Emergent Chemical Reactivity and Complexity of RNA Condensates.Angewandte Chemie (International ed. in English) · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

8 authors.

Andrea Testa *Department of Materials, ETH Zürich, 8093, Zürich, Switzerland.
Mirco Dindo *Protein Engineering and Evolution Unit, Okinawa Institute of Science and Technology Graduate University, 1919-1 Tancha, Onna, 904-0495, Okinawa, Japan.
Aleksander A RebaneDepartment of Materials, ETH Zürich, 8093, Zürich, Switzerland.
Babak NasouriMax Planck Institute for Dynamics and Self-Organization (MPIDS), D-37077, Göttingen, Germany.ORCID http://orcid.org/0000-0002-4376-2510
Robert W StyleDepartment of Materials, ETH Zürich, 8093, Zürich, Switzerland.ORCID http://orcid.org/0000-0001-5305-7658
Ramin GolestanianMax Planck Institute for Dynamics and Self-Organization (MPIDS), D-37077, Göttingen, Germany.ORCID http://orcid.org/0000-0002-3149-4002
Eric R DufresneDepartment of Materials, ETH Zürich, 8093, Zürich, Switzerland. eric.dufresne@mat.ethz.ch.
Paola LaurinoProtein Engineering and Evolution Unit, Okinawa Institute of Science and Technology Graduate University, 1919-1 Tancha, Onna, 904-0495, Okinawa, Japan. paola.laurino@oist.jp.ORCID http://orcid.org/0000-0002-3725-2645

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Living cells harvest energy from their environments to drive the chemical processes that enable life. We introduce a minimal system that operates at similar protein concentrations, metabolic densities, and length scales as living cells. This approach takes advantage of the tendency of phase-separated protein droplets to strongly partition enzymes, while presenting minimal barriers to transport of small molecules across their interface. By dispersing these microreactors in a reservoir of substrate-loaded buffer, we achieve steady states at metabolic densities that match those of the hungriest microorganisms. We further demonstrate the formation of steady pH gradients, capable of driving microscopic flows. Our approach enables the investigation of the function of diverse enzymes in environments that mimic cytoplasm, and provides a flexible platform for studying the collective behavior of matter driven far from equilibrium.

Indexed as

Artificial CellsCatalysisHumansHydro-LyasesModels, BiologicalNanoparticlesUreaseHydro-Lyaseslactate dehydrataseUrease

Identifiers

PMID34725341
PMCPMC8560906

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.