ReviewBiochimica et biophysica acta. Biomembranes2017
Transmembrane β-barrels: Evolution, folding and energetics.
Review in Biochimica et biophysica acta. Biomembranes, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
What it found
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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
36 citing papers in PubMed.
- Membrane Protein Folding and Biogenesis: Insights from Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- The dynamic lateral gate of the mitochondrial β-barrel biogenesis machinery is blocked by darobactin A.Nature communications · 2025Article
- Barrel expansion of outer membrane protein G nanopore through β-hairpin duplication.Protein science : a publication of the Protein Society · 2025Article
- Article
- Terrabacteria: redefining bacterial envelope diversity, biogenesis and evolution.Nature reviews. Microbiology · 2025Review
- Review
- Host and structure-specific codon usage of G genotype (VP7) among group A rotaviruses.Frontiers in veterinary science · 2024Article
- Photoradical-Mediated Catalyst-Independent Protein Cross-Link with Unusual Fluorescence Properties.Chembiochem : a European journal of chemical biology · 2023Article
- Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets.International journal of molecular sciences · 2023Review
- The Screening of the Protective Antigens ofVaccines · 2023Article
- Generation of unfolded outer membrane protein ensembles defined by hydrodynamic properties.European biophysics journal : EBJ · 2023Article
- Making a chink in their armor: Current and next-generation antimicrobial strategies against the bacterial cell envelope.Advances in microbial physiology · 2023Article
- Structure and Function of Redox-Sensitive Superfolder Green Fluorescent Protein Variant.Antioxidants & redox signaling · 2022Article
- Membrane Proteins and Proteomics of Cronobacter sakazakii Cells: Reliable Method for Identification and Subcellular Localization.Applied and environmental microbiology · 2022Article
- Mitochondrial protein translocation machinery: From TOM structural biogenesis to functional regulation.The Journal of biological chemistry · 2022Review
- Engineering a HyperstableJournal of the American Chemical Society · 2022Article
- A Polyclonal Antibody Raised against theBiomedicines · 2021Article
- β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis.International journal of molecular sciences · 2021Review
- Building Better Barrels - β-barrel Biogenesis and Insertion in Bacteria and Mitochondria.Journal of molecular biology · 2021Review
- Structural Modeling of the Treponema pallidum Outer Membrane Protein Repertoire: a Road Map for Deconvolution of Syphilis Pathogenesis and Development of a Syphilis Vaccine.Journal of bacteriology · 2021Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The biogenesis of transmembrane β-barrels (outer membrane proteins, or OMPs) is an elaborate multistep orchestration of the nascent polypeptide with translocases, barrel assembly machinery, and helper chaperone proteins. Several theories exist that describe the mechanism of chaperone-assisted OMP assembly in vivo and unassisted (spontaneous) folding in vitro. Structurally, OMPs of bacterial origin possess even-numbered strands, while mitochondrial β-barrels are even- and odd-stranded. Several underlying similarities between prokaryotic and eukaryotic β-barrels and their folding machinery are known; yet, the link in their evolutionary origin is unclear. While OMPs exhibit diversity in sequence and function, they share similar biophysical attributes and structure. Similarly, it is important to understand the intricate OMP assembly mechanism, particularly in eukaryotic β-barrels that have evolved to perform more complex functions. Here, we deliberate known facets of β-barrel evolution, folding, and stability, and attempt to highlight outstanding questions in β-barrel biogenesis and proteostasis.
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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.