Evidence map›Paper›PMID 31199001›Full record

ArticleAnnals of the New York Academy of Sciences2019

Phase separation in biology and disease-a symposium report.

Jennifer Cable, Clifford Brangwynne, Geraldine Seydoux, David Cowburn, Rohit V Pappu, Carlos A Castañeda, Luke E Berchowitz, Zhijuan Chen, Martin Jonikas, Abby Dernburg and 2 more

Open access · greenAbstract read
In one paragraph

Article in Annals of the New York Academy of Sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

17 citing papers in PubMed, 24 citations in OpenAlex.

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  10. Article
  11. Liquid-liquid phase separation in tumor biology.Signal transduction and targeted therapy · 2022
    Review
  12. Review
  13. Membrane signalosome: where biophysics meets systems biology.Current opinion in systems biology · 2021
    Article
  14. Review
  15. Review
  16. Article
  17. 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

12 authors at 9 institutions in 1 country.

Jennifer CableScience Writer, New York, New York.
Clifford BrangwynneDepartment of Chemical and Biological Engineering, Princeton University, Princeton, New Jersey.
Geraldine SeydouxDepartment of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, Maryland.
David CowburnDepartments of Biochemistry and Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York.
Rohit V PappuDepartment of Biomedical Engineering, Center for Science and Engineering of Living Systems, McKelvey School of Engineering, St. Louis, Missouri.
Carlos A CastañedaDepartments of Biology and Chemistry, Program in Neuroscience, Syracuse University, Syracuse, New York.
Luke E BerchowitzDepartments of Genetics and Development, Columbia University, New York, New York.
Zhijuan ChenUniversity of Texas Southwestern Medical Center, Dallas, Texas.
Martin JonikasDepartment of Molecular Biology, Princeton University, Princeton, New Jersey.
Abby DernburgDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California.
Tanja MittagDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, Tennessee.
Nicolas L FawziDepartment of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, Rhode Island.
Princeton University · USAlbert Einstein College of Medicine · USBrown University · USColumbia University · USJohns Hopkins Medicine · USSt. Jude Children's Research Hospital · USSyracuse University · USThe University of Texas Southwestern Medical Center · USUniversity of California, Berkeley · US

Funding

Elucidation of regulation and function of amyloid-like assembliesR35GM124633 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Luke E Berchowitz · 2017 to 2026
$4.2M
The dynamic mechanism of nuclear transport visualized at the atomic scaleR01GM117212 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI COWBURN, DAVID · 2016 to 2023
$3.7M
The role of weak multivalent interactions and phase separation in SPOP tumor suppressor functionR01GM112846 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI MITTAG, TANJA · 2015 to 2023
$3.0M
Transforming our understanding of eukaryotic gene functions through chemical genetics in the green alga Chlamydomonas reinhardtiiDP2GM119137 · NIGMS · PRINCETON UNIVERSITY · PI JONIKAS, MARTIN CASIMIR · 2015 to 2015
$2.4M
Turning off the molecular switch for pathological self-assembly of FUSR01GM118530 · NIGMS · BROWN UNIVERSITY · PI FAWZI, NICOLAS LUX · 2016 to 2020
$1.6M
ALS Association 17-IIP-369ALS Association 18-IIP-400American Lebanese Syrian Associated CharitiesHuman Frontiers Science Program RGP0045/2018National Science Foundation 1750462National Science Foundation 1845734National Science Foundation EF-1105617National Science Foundation IOS-1359682National Science Foundation MCB-1146621NIGMS NIH HHS DP2 GM119137NIGMS NIH HHS R01 GM112846NIGMS NIH HHS R01 GM117212NIGMS NIH HHS R01 GM118530NIGMS NIH HHS R35 GM124633Simons Foundation and Howard Hughes Medical Institute 55108535St. Jude Children's Research Hospital
6 · The paper itself

Abstract

Phase separation of multivalent protein and RNA molecules enables cells the formation of reversible nonstoichiometric, membraneless assemblies. These assemblies, referred to as biomolecular condensates, help with the spatial organization and compartmentalization of cellular matter. Each biomolecular condensate is defined by a distinct macromolecular composition. Distinct condensates have distinct preferential locations within cells, and they are associated with distinct biological functions, including DNA replication, RNA metabolism, signal transduction, synaptic transmission, and stress response. Several proteins found in biomolecular condensates have also been implicated in disease, including Huntington's disease, amyotrophic lateral sclerosis, and several types of cancer. Disease-associated mutations in these proteins have been found to affect the material properties of condensates as well as the driving forces for phase separation. Understanding the intrinsic and extrinsic forces driving the formation and dissolution of biomolecular condensates via spontaneous and driven phase separation is an important step in understanding the processes associated with biological regulation in health and disease.

Indexed as

Macromolecular SubstancesCytoplasmHumansOrganellesMacromolecular Substancesbiomolecular condensatesgranulesmembraneless organellesphase diagramphase separationprotein disorder

Identifiers

PMID31199001
PMCPMC6751006
OpenAlexW2952667761

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.