Evidence map›Paper›PMID 30747342›Full record

ArticleNanoscale research letters2019

Self-Assembly Stability and Variability of Bacterial Microcompartment Shell Proteins in Response to the Environmental Change.

Matthew Faulkner, Long-Sheng Zhao, Steve Barrett, Lu-Ning Liu

Open access · goldAbstract read
In one paragraph

Article in Nanoscale research letters, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
4.8field-weighted citation impact, top 5% 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

16 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Interfacing bacterial microcompartment shell proteins with genetically encoded condensates.Protein science : a publication of the Protein Society · 2025
    Article
  6. Studying Biomolecular Protein Complexes via Origami and 3D-Printed Models.International journal of molecular sciences · 2024
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. 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

4 authors at 1 institution in 1 country.

Matthew FaulknerInstitute of Integrative Biology, University of Liverpool, L69 7ZB, Liverpool, UK.
Long-Sheng ZhaoInstitute of Integrative Biology, University of Liverpool, L69 7ZB, Liverpool, UK.
Steve BarrettDepartment of Physics, University of Liverpool, L69 7ZE, Liverpool, UK.
Lu-Ning LiuInstitute of Integrative Biology, University of Liverpool, L69 7ZB, Liverpool, UK. luning.liu@liverpool.ac.uk.ORCID http://orcid.org/0000-0002-8884-4819
University of Liverpool · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M024202/1Biotechnology and Biological Sciences Research Council BB/R003890/1Royal Society RG130442Royal Society RGF\EA\180233Royal Society UF120411Royal Society URF\R\180030
6 · The paper itself

Abstract

Bacterial microcompartments (BMCs) are proteinaceous self-assembling organelles that are widespread among the prokaryotic kingdom. By segmenting key metabolic enzymes and pathways using a polyhedral shell, BMCs play essential roles in carbon assimilation, pathogenesis, and microbial ecology. The BMC shell is composed of multiple protein homologs that self-assemble to form the defined architecture. There is tremendous interest in engineering BMCs to develop new nanobioreactors and molecular scaffolds. Here, we report the quantitative characterization of the formation and self-assembly dynamics of BMC shell proteins under varying pH and salt conditions using high-speed atomic force microscopy (HS-AFM). We show that 400-mM salt concentration is prone to result in larger single-layered shell patches formed by shell hexamers, and a higher dynamic rate of hexamer self-assembly was observed at neutral pH. We also visualize the variability of shell proteins from hexameric assemblies to fiber-like arrays. This study advances our knowledge about the stability and variability of BMC protein self-assemblies in response to microenvironmental changes, which will inform rational design and construction of synthetic BMC structures with the capacity of remodeling their self-assembly and structural robustness. It also offers a powerful toolbox for quantitatively assessing the self-assembly and formation of BMC-based nanostructures in biotechnology applications.

Indexed as

Bacterial microcompartmentHigh-speed atomic force microscopyProtein dynamicsSelf-assemblySynthetic engineering

Identifiers

PMID30747342
PMCPMC6372710
OpenAlexW2912908646

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.