Evidence map›Paper›PMID 39226211›Full record

ArticleACS nano2024

Pore Engineering as a General Strategy to Improve Protein-Based Enzyme Nanoreactor Performance.

Seokmu Kwon, Michael P Andreas, Tobias W Giessen

Abstract read
In one paragraph

Article in ACS nano, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Buffer and salt dependent reassembly pathways of Myxococcus xanthus encapsulin.Protein science : a publication of the Protein Society · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Characterization of Iron Oxide Nanoparticles Inside theNanomaterials (Basel, Switzerland) · 2025
    Article
  8. Article
  9. Article
  10. Encapsulins: catalysis inside a shell.Current opinion in microbiology · 2025
    Review
  11. Article
  12. Article
  13. The Structural Diversity of Encapsulin Protein Shells.Chembiochem : a European journal of chemical biology · 2024
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Seokmu KwonDepartment of Chemical Engineering, University of Michigan, Ann Arbor, Michigan 48109, United States.
Michael P AndreasDepartment of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48109, United States.ORCID 0000-0001-8871-3053
Tobias W GiessenDepartment of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48109, United States.ORCID 0000-0001-6328-2031

Funding

ChimeraX -- Next Generation Visualization and Analysis Software for Multiscale ModelingR01GM129325 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2018 to 2025
$5.2M
Protein Organelles In Human-Associated BacteriaR35GM133325 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Tobias Wolfgang Giessen · 2019 to 2026
$3.8M
NIGMS NIH HHS R01 GM129325NIGMS NIH HHS R35 GM133325
6 · The paper itself

Abstract

Enzyme nanoreactors are nanoscale compartments consisting of encapsulated enzymes and a selectively permeable barrier. Sequestration and colocalization of enzymes can increase catalytic activity, stability, and longevity, highly desirable features for many biotechnological and biomedical applications of enzyme catalysts. One promising strategy to construct enzyme nanoreactors is to repurpose protein nanocages found in nature. However, protein-based enzyme nanoreactors often exhibit decreased catalytic activity, partially caused by a mismatch of protein shell selectivity and the substrate requirements of encapsulated enzymes. No broadly applicable and modular protein-based nanoreactor platform is currently available. Here, we introduce a pore-engineered universal enzyme nanoreactor platform based on encapsulins-microbial self-assembling protein nanocompartments with programmable and selective enzyme packaging capabilities. We structurally characterize our protein shell designs via cryo-electron microscopy and highlight their polymorphic nature. Through fluorescence polarization assays, we show their improved molecular flux behavior and highlight their expanded substrate range via a number of proof-of-concept enzyme nanoreactor designs. This work lays the foundation for utilizing our encapsulin-based nanoreactor platform for diverse future biotechnological and biomedical applications.

Indexed as

Protein EngineeringBiocatalysisEnzymes, ImmobilizedNanotechnologyParticle SizePorosityEnzymes, Immobilizedbiocatalysisencapsulationencapsulinnanocompartmentnanoreactorporeprotein shell

Identifiers

PMID39226211
PMCPMC11971687

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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.