Evidence map›Paper›PMID 37794023›Full record

ArticleNature communications2023

Intermolecular interactions underlie protein/peptide phase separation irrespective of sequence and structure at crowded milieu.

Manisha Poudyal, Komal Patel, Laxmikant Gadhe, Ajay Singh Sawner, Pradeep Kadu, Debalina Datta, Semanti Mukherjee, Soumik Ray, Ambuja Navalkar, Siddhartha Maiti and 7 more

Abstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing 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

68 citing papers in PubMed.

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  19. Dilute but Dense - Reversible Crosslinking Enables Water-Rich (Bio)polymer Condensates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  20. Article

8 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

17 authors.

Manisha Poudyal *Department of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai, 400076, India.
Komal Patel *Department of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai, 400076, India.
Laxmikant GadheDepartment of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai, 400076, India.
Ajay Singh SawnerDepartment of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai, 400076, India.
Pradeep KaduDepartment of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai, 400076, India.
Debalina DattaDepartment of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai, 400076, India.
Semanti MukherjeeDepartment of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai, 400076, India.
Soumik RayDepartment of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai, 400076, India.
Ambuja NavalkarDepartment of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai, 400076, India.
Siddhartha MaitiDepartment of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai, 400076, India.
Debdeep ChatterjeeDepartment of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai, 400076, India.
Jyoti DeviDepartment of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai, 400076, India.
Riya BeraDepartment of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai, 400076, India.
Nitisha GahlotDepartment of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai, 400076, India.
Jennifer JosephDepartment of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai, 400076, India.ORCID 0000-0002-0441-8856
Ranjith PadinhateeriDepartment of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai, 400076, India.ORCID 0000-0001-5485-1474
Samir K MajiDepartment of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai, 400076, India. samirmaji@iitb.ac.in.ORCID 0000-0002-9110-1565

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Liquid-liquid phase separation (LLPS) has emerged as a crucial biological phenomenon underlying the sequestration of macromolecules (such as proteins and nucleic acids) into membraneless organelles in cells. Unstructured and intrinsically disordered domains are known to facilitate multivalent interactions driving protein LLPS. We hypothesized that LLPS could be an intrinsic property of proteins/polypeptides but with distinct phase regimes irrespective of their sequence and structure. To examine this, we studied many (a total of 23) proteins/polypeptides with different structures and sequences for LLPS study in the presence and absence of molecular crowder, polyethylene glycol (PEG-8000). We showed that all proteins and even highly charged polypeptides (under study) can undergo liquid condensate formation, however with different phase regimes and intermolecular interactions. We further demonstrated that electrostatic, hydrophobic, and H-bonding or a combination of such intermolecular interactions plays a crucial role in individual protein/peptide LLPS.

Indexed as

Intrinsically Disordered ProteinsPeptidesIntrinsically Disordered ProteinsPeptides

Identifiers

PMID37794023
PMCPMC10550955

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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.