ReviewEcoSal Plus2019
The TAM: A Translocation and Assembly Module of the β-Barrel Assembly Machinery in Bacterial Outer Membranes.
Review in EcoSal Plus, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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
29 citing papers in PubMed, 41 citations in OpenAlex.
- Integration of Membrane Proteins into the Outer Membrane of Diderm Bacteria by the BAM Complex.Chemical reviews · 2026Review
- The Omp85 family protein, TamA, exhibits characteristics of a suitable drug target againstMicrobiology (Reading, England) · 2026Article
- Structural basis of outer membrane biogenesis by the TamAB translocase.Nature communications · 2026Article
- The TamA protein as a subunit vaccine improves immune protection against highly virulentCurrent research in microbial sciences · 2026Article
- Metabolic strategies that enable oral commensal persistence in a lower airway environment.mBio · 2025Article
- Structure-function relationship of the Pseudomonas aeruginosa AsmA-like proteins YhdP and YdbH involved in outer membrane biogenesis.Protein science : a publication of the Protein Society · 2025Article
- Biochemical characterisation supports a central role for Oep80 from Arabidopsis thaliana in chloroplastic β-barrel protein assembly.Communications biology · 2025Article
- TamL is a Key Player of the Outer Membrane Homeostasis in Bacteroidota.Journal of molecular biology · 2025Article
- A historical perspective on the multifunctional outer membrane channel protein TolC in Escherichia coli.npj antimicrobials and resistance · 2025Review
- The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteins in vitro.Nature communications · 2024Article
- POTRA domains of the TamA insertase interact with the outer membrane and modulate membrane properties.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteinsbioRxiv : the preprint server for biology · 2024Article
- The patatin-like protein PlpD forms structurally dynamic homodimers in the Pseudomonas aeruginosa outer membrane.Nature communications · 2024Article
- YdbH and YnbE form an intermembrane bridge to maintain lipid homeostasis in the outer membrane ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Redundant essentiality of AsmA-like proteins inmSphere · 2024Article
- Molecular mechanism of phospholipid transport at the bacterial outer membrane interface.Nature communications · 2023Article
- TamAB is regulated by PhoPQ and functions in outer membrane homeostasis duringJournal of bacteriology · 2023Article
- Characterization of theJournal of bacteriology · 2023Article
- Forward or backward, that is the question: phospholipid trafficking by the Mla system.Emerging topics in life sciences · 2023Review
- Pseudomonas aeruginosa: pathogenesis, virulence factors, antibiotic resistance, interaction with host, technology advances and emerging therapeutics.Signal transduction and targeted therapy · 2022Review
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 at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Assembly of proteins into the outer membrane is an essential process in the cell biology of bacteria. The integration of β-barrel proteins into the outer membrane is mediated by a system referred to as the β-barrel assembly machinery (BAM) that includes two related proteins: BamA in the BAM complex and TamA in the TAM (translocation and assembly module). Here we review what is known about the TAM in terms of its function and the structural architecture of its two subunits, TamA and TamB. By linking the energy transduction possibilities in the inner membrane to TamA in the outer membrane, the TAM provides additional capability to the β-barrel assembly machinery. Conservation of the TAM across evolutionary boundaries, and the presence of hybrid BAM/TAM complexes in some bacterial lineages, adds insight to our growing understanding of how bacterial outer membranes are built.
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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.