Evidence map›Paper›PMID 31604601›Full record

ReviewMolecular cell2019

The Control Centers of Biomolecular Phase Separation: How Membrane Surfaces, PTMs, and Active Processes Regulate Condensation.

Wilton T Snead, Amy S Gladfelter

Open access · bronzeAbstract readReview
In one paragraph

Review in Molecular cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 190 papers.

0numbers the graph read from it
0cells of the map it votes in
190citing papers in PubMed
14.0field-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

190 citing papers in PubMed, 366 citations in OpenAlex.

  1. Article
  2. Review
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  6. RBMP2 shapes specialized membranes for CObioRxiv : the preprint server for biology · 2026
    Article
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  13. Signaling architecture of the glucagon-like peptide-1 receptor.The Journal of clinical investigation · 2026
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Control of encounter kinetics by chemically active droplets.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. Review
  20. Article

130 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.

Wilton T SneadDepartment of Biology, The University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Amy S GladfelterDepartment of Biology, The University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA; Marine Biological Laboratory, Woods Hole, MA 02543, USA. Electronic address: amyglad@unc.edu.
Marine Biological Laboratory · USUniversity of North Carolina at Chapel Hill · US

Funding

Cytoplasmic Organization by phase transitionsR01GM081506 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI GLADFELTER, AMY S · 2010 to 2023
$4.0M
NIGMS NIH HHS R01 GM081506
6 · The paper itself

Abstract

Biomolecular condensation is emerging as an essential process for cellular compartmentalization. The formation of biomolecular condensates can be driven by liquid-liquid phase separation, which arises from weak, multivalent interactions among proteins and nucleic acids. A substantial body of recent work has revealed that diverse cellular processes rely on biomolecular condensation and that aberrant phase separation may cause disease. Many proteins display an intrinsic propensity to undergo phase separation. However, the mechanisms by which cells regulate phase separation to build functional condensates at the appropriate time and location are only beginning to be understood. Here, we review three key cellular mechanisms that enable the control of biomolecular phase separation: membrane surfaces, post-translational modifications, and active processes. We discuss how these mechanisms may function in concert to provide robust control over biomolecular condensates and suggest new research avenues that will elucidate how cells build and maintain these key centers of cellular compartmentalization.

Indexed as

Cell CompartmentationProtein Processing, Post-TranslationalProtein TransportAnimalsCell MembraneEndocytosisHumansIntracellular MembranesMolecular ChaperonesNucleic Acid ConformationNucleic AcidsProtein ConformationProteinsSolubilityStructure-Activity RelationshipMolecular ChaperonesNucleic AcidsProteinsbiomolecular condensatesmembranesmolecular chaperonesphase separationpost-translational modifications

Identifiers

PMID31604601
PMCPMC7173186
OpenAlexW2980184617

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.