Evidence map›Paper›PMID 32619404›Full record

ArticleBiophysical journal2020

Connecting Coil-to-Globule Transitions to Full Phase Diagrams for Intrinsically Disordered Proteins.

Xiangze Zeng, Alex S Holehouse, Ashutosh Chilkoti, Tanja Mittag, Rohit V Pappu

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2020. 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
7.2field-weighted citation impact, top 2% 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

62 citing papers in PubMed, 124 citations in OpenAlex.

  1. Article
  2. Distinguishing near- versus off-critical phase behaviors of intrinsically disordered proteins.Reports on progress in physics. Physical Society (Great Britain) · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Accurate prediction of thermoresponsive phase behavior of disordered proteins.Protein science : a publication of the Protein Society · 2025
    Article
  8. Article
  9. Article
  10. Prediction of phase-separation propensities of disordered proteins from sequence.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Article
  13. Sequence complexity and monomer rigidity control the morphologies and aging dynamics of protein aggregates.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Molecular insights into the interaction between a disordered protein and a folded RNA.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Article

2 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

5 authors at 4 institutions in 1 country.

Xiangze ZengDepartment of Biomedical Engineering, Washington University in St. Louis, St. Louis, Missouri; Center for Science & Engineering of Living Systems, Washington University in St. Louis, St. Louis, Missouri.
Alex S HolehouseCenter for Science & Engineering of Living Systems, Washington University in St. Louis, St. Louis, Missouri; Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri.
Ashutosh ChilkotiDepartment of Biomedical Engineering, Duke University, Durham, North Carolina.
Tanja MittagDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, Tennessee.
Rohit V PappuDepartment of Biomedical Engineering, Washington University in St. Louis, St. Louis, Missouri; Center for Science & Engineering of Living Systems, Washington University in St. Louis, St. Louis, Missouri. Electronic address: pappu@wustl.edu.
Washington University in St. Louis · USDuke University · USLiving Systems (United States) · USSt. Jude Children's Research Hospital · US

Funding

ROLE OF CHAIN LENGTH AND SEQUENCE CONTEXTS ON POLYGLUTAMINE OLIGOMERIZATIONR01NS056114 · NINDS · WASHINGTON UNIVERSITY · PI PAPPU, ROHIT V · 2007 to 2020
$4.4M
NINDS NIH HHS R01 NS056114
6 · The paper itself

Abstract

Phase separation is thought to underlie spatial and temporal organization that is required for controlling biochemical reactions in cells. Multivalence of interaction motifs, also known as stickers, is a defining feature of proteins that drive phase separation. Intrinsically disordered proteins with stickers uniformly distributed along the linear sequence can serve as scaffold molecules that drive phase separation. The sequence-intrinsic contributions of disordered proteins to phase separation can be discerned by computing or measuring sequence-specific phase diagrams. These help to delineate the combinations of protein concentration and a suitable control parameter, such as temperature, that support phase separation. Here, we present an approach that combines detailed simulations with a numerical adaptation of an analytical Gaussian cluster theory to enable the calculation of sequence-specific phase diagrams. Our approach leverages the known equivalence between the driving forces for single-chain collapse in dilute solutions and the driving forces for phase separation in concentrated solutions. We demonstrate the application of the theory-aided computations through calculation of phase diagrams for a set of archetypal intrinsically disordered low-complexity domains. We also leverage theories to compute sequence-specific percolation lines and thereby provide a thermodynamic framework for hardening transitions that have been observed for many biomolecular condensates.

Indexed as

Intrinsically Disordered ProteinsPhase TransitionTemperatureThermodynamicsIntrinsically Disordered Proteins

Identifiers

PMID32619404
PMCPMC7376131
OpenAlexW3035871125

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.