ArticleJournal of structural biology: X2022
Recent advances in the structural biology of encapsulin bacterial nanocompartments.
Article in Journal of structural biology: X, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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.
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.
Who cites it
8 citing papers in PubMed.
- Innovation in mRNA Vaccines and RNAi via Protein Nanocages.Vaccines · 2025Review
- The Structural Diversity of Encapsulin Protein Shells.Chembiochem : a European journal of chemical biology · 2024Review
- Encapsulated Ferritin-like Proteins: A Structural Perspective.Biomolecules · 2024Review
- Article
- Structure and heterogeneity of a highly cargo-loaded encapsulin shell.Journal of structural biology · 2023Article
- Structure and heterogeneity of a highly cargo-loaded encapsulin shell.bioRxiv : the preprint server for biology · 2023Article
- Linocin M18 protein from the insect pathogenic bacterium Brevibacillus laterosporus isolates.Applied microbiology and biotechnology · 2023Article
- Encapsulins: Structure, Properties, and Biotechnological Applications.Biochemistry. Biokhimiia · 2023Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Large capsid-like nanocompartments called encapsulins are common in bacteria and archaea and contain cargo proteins with diverse functions. Advances in cryo-electron microscopy have enabled structure determination of many encapsulins in recent years. Here we summarize findings from recent encapsulin structures that have significant implications for their biological roles. We also compare important features such as the E-loop, cargo-peptide binding site, and the fivefold axis channel in different structures. In addition, we describe the discovery of a flavin-binding pocket within the encapsulin shell that may reveal a role for this nanocompartment in iron metabolism.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.