Evidence map›Paper›PMID 37710047›Full record

ArticleNature chemistry2024

Assembling membraneless organelles from de novo designed proteins.

Alexander T Hilditch, Andrey Romanyuk, Stephen J Cross, Richard Obexer, Jennifer J McManus, Derek N Woolfson

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 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. Article
  2. Article
  3. Reversible Nucleolar Complex Coacervation by Short Cationic Peptides.Journal of the American Chemical Society · 2026
    Article
  4. The Polymers of Life: Exploring Cellular Function Through Polymer Concepts.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Interfacing bacterial microcompartment shell proteins with genetically encoded condensates.Protein science : a publication of the Protein Society · 2025
    Article
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

6 authors.

Alexander T HilditchSchool of Chemistry, University of Bristol, Bristol, UK.ORCID 0000-0002-0529-3215
Andrey RomanyukSchool of Chemistry, University of Bristol, Bristol, UK.ORCID 0000-0002-4526-3598
Stephen J CrossWolfson Bioimaging Facility, University of Bristol, Bristol, UK.ORCID 0000-0003-3565-0479
Richard ObexerSchool of Chemistry, University of Bristol, Bristol, UK. richard.obexer@manchester.ac.uk.ORCID 0000-0002-4940-3543
Jennifer J McManusHH Wills Physics Laboratory, School of Physics, University of Bristol, Bristol, UK. jennifer.mcmanus@bristol.ac.uk.ORCID 0000-0003-3630-5108
Derek N WoolfsonSchool of Chemistry, University of Bristol, Bristol, UK. D.N.Woolfson@bristol.ac.uk.ORCID 0000-0002-0394-3202

Funding

EC | Horizon 2020 Framework Programme (EU Framework Programme for Research and Innovation H2020) 795867Leverhulme Trust RGP-2021-049RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/L01386X/1RCUK | Engineering and Physical Sciences Research Council (EPSRC) EP/K03927X/1
6 · The paper itself

Abstract

Recent advances in de novo protein design have delivered a diversity of discrete de novo protein structures and complexes. A new challenge for the field is to use these designs directly in cells to intervene in biological processes and augment natural systems. The bottom-up design of self-assembled objects such as microcompartments and membraneless organelles is one such challenge. Here we describe the design of genetically encoded polypeptides that form membraneless organelles in Escherichia coli. To do this, we combine de novo α-helical sequences, intrinsically disordered linkers and client proteins in single-polypeptide constructs. We tailor the properties of the helical regions to shift protein assembly from arrested assemblies to dynamic condensates. The designs are characterized in cells and in vitro using biophysical methods and soft-matter physics. Finally, we use the designed polypeptide to co-compartmentalize a functional enzyme pair in E. coli, improving product formation close to the theoretical limit.

Indexed as

Biomolecular CondensatesEscherichia coliHumansOrganellesPeptidesProtein Conformation, alpha-HelicalProteinsPeptidesProteins

Identifiers

PMID37710047
PMCPMC10774119

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.