Evidence map›Paper›PMID 29716768›Full record

ReviewTrends in biochemical sciences2018

Why Do Disordered and Structured Proteins Behave Differently in Phase Separation?

Huan-Xiang Zhou, Valery Nguemaha, Konstantinos Mazarakos, Sanbo Qin

Open access · greenAbstract readComparative StudyReview
In one paragraph

Review in Trends in biochemical sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
6.8field-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

64 citing papers in PubMed, 148 citations in OpenAlex.

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  13. CytochromeiScience · 2024
    Article
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  17. Surface Charge Can Modulate Phase Separation of Multidomain Proteins.Journal of the American Chemical Society · 2024
    Article
  18. Article
  19. Article
  20. Review

4 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

4 authors at 2 institutions in 1 country.

Huan-Xiang ZhouDepartment of Chemistry and Department of Physics, University of Illinois at Chicago, Chicago, IL 60607, USA; Department of Physics and Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306, USA. Electronic address: hzhou43@uic.edu.
Valery NguemahaDepartment of Physics and Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306, USA.
Konstantinos MazarakosDepartment of Physics and Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306, USA.
Sanbo QinDepartment of Physics and Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306, USA.
Florida State University · USUniversity of Illinois Chicago · US

Funding

Quantitative, Mechanistic Studies of Biomolecular RecognitionR35GM118091 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI Huan-Xiang Zhou · 2016 to 2026
$6.5M
NIGMS NIH HHS R35 GM118091
6 · The paper itself

Abstract

Intracellular membraneless organelles and their myriad cellular functions have garnered tremendous recent interest. It is becoming well accepted that they form via liquid-liquid phase separation (LLPS) of protein mixtures (often including RNA), where the organelles correspond to a protein-rich droplet phase coexisting with a protein-poor bulk phase. The major protein components contain disordered regions and often also RNA-binding domains, and the disordered fragments on their own easily undergo LLPS. By contrast, LLPS for structured proteins has been observed infrequently. The contrasting phase behaviors can be explained by modeling disordered and structured proteins, respectively, as polymers and colloids. These physical models also provide a better understanding of the regulation of droplet formation by cellular signals and its dysregulation leading to diseases.

Indexed as

Models, MolecularAmino Acid MotifsAnimalsHumansHydrophobic and Hydrophilic InteractionsIntrinsically Disordered ProteinsKineticsProtein Interaction Domains and MotifsProteinsProtein StabilityRNA, MessengerSolubilityIntrinsically Disordered ProteinsProteinsRNA, Messengermembraneless organellephase separationtransient bonding network

Identifiers

PMID29716768
PMCPMC6014895
OpenAlexW2802429563

What OpenQuestion holds

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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.