Evidence map›Paper›PMID 40618468›Full record

ReviewCurrent opinion in microbiology2025

Encapsulins: catalysis inside a shell.

Asif Fazal, Tobias W Giessen

Abstract readReview
In one paragraph

Review in Current opinion in microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

2 authors.

Asif FazalDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.
Tobias W GiessenDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: tgiessen@umich.edu.

Funding

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 R35 GM133325
6 · The paper itself

Abstract

Internal cellular organization is a defining feature of life, and encapsulins are an effective, protein-based method for prokaryotic cells to achieve compartmentalization of chemical reactions and metabolic processes. The defining feature of encapsulins is their ability to encapsulate cargo proteins inside a self-assembling protein shell, mediated by cargo-encoded targeting peptides or domains. The biochemical and physiological function of an encapsulin system is dictated by the catalytic activity of encapsulated components, with the protein shell acting as a selectively permeable diffusion barrier. Encapsulating cargo proteins confers multiple advantages, including enhanced stability, increased activity, regulatory control, and sequestration of reactive intermediates or reaction products. Encapsulin-cargo systems have key functions in elemental homeostasis, storage, stress resistance, and varied anabolic pathways. This review will focus on the so far characterized cargo proteins encapsulated within encapsulin shells, specifically their catalytic mechanisms and the particular reasons and benefits for protein encapsulation.

Indexed as

BacteriaBacterial ProteinsCatalysisBacterial Proteins

Identifiers

PMID40618468
PMCPMC12746231

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.