Evidence map›Paper›PMID 32312191›Full record

ReviewAnnual review of physical chemistry2020

Biomolecular Phase Separation: From Molecular Driving Forces to Macroscopic Properties.

Gregory L Dignon, Robert B Best, Jeetain Mittal

Open access · bronzeAbstract readReview
In one paragraph

Review in Annual review of physical chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 349 papers.

0numbers the graph read from it
0cells of the map it votes in
349citing papers in PubMed
29.7field-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

349 citing papers in PubMed, 697 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Distinguishing near- versus off-critical phase behaviors of intrinsically disordered proteins.Reports on progress in physics. Physical Society (Great Britain) · 2026
    Article

289 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 at 3 institutions in 1 country.

Gregory L DignonDepartment of Chemical and Biomolecular Engineering, Lehigh University, Bethlehem, Pennsylvania 18015, USA; email: jem309@lehigh.edu.
Robert B BestLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA; email: robert.best2@nih.gov.
Jeetain MittalDepartment of Chemical and Biomolecular Engineering, Lehigh University, Bethlehem, Pennsylvania 18015, USA; email: jem309@lehigh.edu.
Lehigh University · USNational Institute of Diabetes and Digestive and Kidney Diseases · USStony Brook University · US

Funding

Understanding protein folding, evolution and function via molecular simulationZIADK075104 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BEST, ROBERT · 2013 to 2025
$13.7M
Turning off the molecular switch for pathological self-assembly of FUSR01GM118530 · NIGMS · BROWN UNIVERSITY · PI FAWZI, NICOLAS LUX · 2016 to 2020
$1.6M
Conformational dynamics, binding and aggregation of intrinsically disordered proteinsR01GM120537 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI VAIANA, SARA M. · 2017 to 2021
$1.4M
NIGMS NIH HHS R01 GM118530NIGMS NIH HHS R01 GM120537
6 · The paper itself

Abstract

Biological phase separation is known to be important for cellular organization, which has recently been extended to a new class of biomolecules that form liquid-like droplets coexisting with the surrounding cellular or extracellular environment. These droplets are termed membraneless organelles, as they lack a dividing lipid membrane, and are formed through liquid-liquid phase separation (LLPS). Elucidating the molecular determinants of phase separation is a critical challenge for the field, as we are still at the early stages of understanding how cells may promote and regulate functions that are driven by LLPS. In this review, we discuss the role that disorder, perturbations to molecular interactions resulting from sequence, posttranslational modifications, and various regulatory stimuli play on protein LLPS, with a particular focus on insights that may be obtained from simulation and theory. We finally discuss how these molecular driving forces alter multicomponent phase separation and selectivity.

Indexed as

Intrinsically Disordered ProteinsLiquid-Liquid ExtractionOrganellesPhase TransitionIntrinsically Disordered Proteinsbiomolecular condensatesintrinsically disordered proteinsmulticomponent phase separationphase separation

Identifiers

PMID32312191
PMCPMC7469089
OpenAlexW3017333675

What OpenQuestion 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 OpenQuestion graph.