Evidence map›Paper›PMID 38316988›Full record

ArticleNature chemistry2024

Determinants that enable disordered protein assembly into discrete condensed phases.

Rachel M Welles, Kandarp A Sojitra, Mikael V Garabedian, Boao Xia, Wentao Wang, Muyang Guan, Roshan M Regy, Elizabeth R Gallagher, Daniel A Hammer, Jeetain Mittal and 1 more

Abstract read
In one paragraph

Article in Nature chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing 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

62 citing papers in PubMed.

  1. Article
  2. Article
  3. Spatially Encoded Protocell Network for Non-Cascaded Parallel Biocomputation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Programmable artificial RNA condensates in mammalian cells.bioRxiv : the preprint server for biology · 2026
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Internal Phase Separation in Synthetic DNA Condensates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  19. Article
  20. Article

2 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors.

Rachel M Welles *Department of Cell and Developmental Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.ORCID 0009-0005-6636-1946
Kandarp A Sojitra *Artie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX, USA.ORCID 0009-0002-8801-699X
Mikael V GarabedianDepartment of Cell and Developmental Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.ORCID 0000-0001-7826-7491
Boao XiaBioengineering Graduate Program, Rice University, Houston, TX, USA.ORCID 0000-0002-4967-5389
Wentao WangBioengineering Graduate Program, University of Pennsylvania, Philadelphia, PA, USA.
Muyang GuanChemical and Biomolecular Engineering Graduate Program, University of Pennsylvania, Philadelphia, PA, USA.
Roshan M RegyArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX, USA.
Elizabeth R GallagherCell and Molecular Biology Graduate Program, University of Pennsylvania, Philadelphia, PA, USA.ORCID 0000-0002-2951-1969
Daniel A HammerBioengineering Graduate Program, University of Pennsylvania, Philadelphia, PA, USA.ORCID 0000-0002-3522-3154
Jeetain MittalArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX, USA. jeetain@tamu.edu.ORCID 0000-0002-9725-6402
Matthew C GoodDepartment of Cell and Developmental Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA. mattgood@pennmedicine.upenn.edu.ORCID 0000-0002-6367-1034

Funding

Programmable Synthetic Organelles Built from Disordered Proteins for Cellular EngineeringR01EB028320 · NIBIB · UNIVERSITY OF PENNSYLVANIA · PI GOOD, MATTHEW CHARLTON, HAMMER, DANIEL A · 2019 to 2022
$1.7M
Liquid-Liquid Phase Separation in Heterochromatin OrganizationR01GM136917 · NIGMS · TEXAS ENGINEERING EXPERIMENT STATION · PI MITTAL, JEETAIN · 2020 to 2023
$1.4M
Multiscale Computational Models to Investigate the Role of Phase Separation in BiologyR35GM153388 · NIGMS · TEXAS ENGINEERING EXPERIMENT STATION · PI Jeetain Mittal · 2024 to 2026
$1.3M
Characterizing protein condensates and nuclear organization in genomic integrityR00GM151473 · NIGMS · RUTGERS BIOMEDICAL AND HEALTH SCIENCES · PI Mikael Garabedian · 2025 to 2026
$498k
Characterizing the role of tumor suppressor phase separation and chromatin organization in maintaining genomic integrityK99GM151473 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GARABEDIAN, MIKAEL · 2023 to 2024
$240k
National Science Foundation (NSF) DMR1720530NIBIB NIH HHS R01 EB028320NIGMS NIH HHS K99 GM151473NIGMS NIH HHS R00 GM151473NIGMS NIH HHS R01 GM136917NIGMS NIH HHS R35 GM153388U.S. Department of Energy (DOE) DE-SC0007063U.S. Department of Health & Human Services | NIH | National Institute of Biomedical Imaging and Bioengineering (NIBIB) EB028320U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R01GM136917Welch Foundation A-2113-20220331
6 · The paper itself

Abstract

Cells harbour numerous mesoscale membraneless compartments that house specific biochemical processes and perform distinct cellular functions. These protein- and RNA-rich bodies are thought to form through multivalent interactions among proteins and nucleic acids, resulting in demixing via liquid-liquid phase separation. Proteins harbouring intrinsically disordered regions (IDRs) predominate in membraneless organelles. However, it is not known whether IDR sequence alone can dictate the formation of distinct condensed phases. We identified a pair of IDRs capable of forming spatially distinct condensates when expressed in cells. When reconstituted in vitro, these model proteins do not co-partition, suggesting condensation specificity is encoded directly in the polypeptide sequences. Through computational modelling and mutagenesis, we identified the amino acids and chain properties governing homotypic and heterotypic interactions that direct selective condensation. These results form the basis of physicochemical principles that may direct subcellular organization of IDRs into specific condensates and reveal an IDR code that can guide construction of orthogonal membraneless compartments.

Indexed as

Intrinsically Disordered ProteinsIntrinsically Disordered Proteins

Identifiers

PMID38316988
PMCPMC11929961

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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.