ReviewFEMS microbiology reviews2008
Protein secretion and outer membrane assembly in Alphaproteobacteria.
Review in FEMS microbiology reviews, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 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
48 citing papers in PubMed, 88 citations in OpenAlex.
- Targeting Bacterial Cell Wall Synthesis: Structural Insights and Emerging Therapeutic Strategies.Pharmaceutics · 2026Review
- TamL is a Key Player of the Outer Membrane Homeostasis in Bacteroidota.Journal of molecular biology · 2025Article
- Review
- Structural characterization of the Sel1-like repeat protein LceB from Legionella pneumophila.Protein science : a publication of the Protein Society · 2024Article
- Similarly slow diffusion of BAM and SecYEG complexes in live E. coli cells observed with 3D spt-PALM.Biophysical journal · 2023Article
- β-Barrel Assembly Machinery (BAM) Complex as Novel Antibacterial Drug Target.Molecules (Basel, Switzerland) · 2023Review
- The big BAM theory: An open and closed case?Biochimica et biophysica acta. Biomembranes · 2020Review
- MapB, the Brucella suis TamB homologue, is involved in cell envelope biogenesis, cell division and virulence.Scientific reports · 2019Article
- Article
- The Structure of a BamA-BamD Fusion Illuminates the Architecture of the β-Barrel Assembly Machine Core.Structure (London, England : 1993) · 2016Article
- Complete genome and gene expression analyses of Asaia bogorensis reveal unique responses to culture with mammalian cells as a potential opportunistic human pathogen.DNA research : an international journal for rapid publication of reports on genes and genomes · 2015Article
- Characterization of the β-barrel assembly machine accessory lipoproteins from Borrelia burgdorferi.BMC microbiology · 2015Article
- Analyzing the molecular mechanism of lipoprotein localization in Brucella.Frontiers in microbiology · 2015Review
- Proteomic and genomic analysis reveals novelEuPA open proteomics · 2014Article
- Structure, Function and Regulation of Outer Membrane Proteins Involved in Drug Transport in Enterobactericeae: the OmpF/C - TolC Case.The open microbiology journal · 2013Article
- Dynamic association of BAM complex modules includes surface exposure of the lipoprotein BamC.Journal of molecular biology · 2012Article
- Implication of proteins containing tetratricopeptide repeats in conditional virulence phenotypes of Legionella pneumophila.Journal of bacteriology · 2012Article
- The evolution of new lipoprotein subunits of the bacterial outer membrane BAM complex.Molecular microbiology · 2012Article
- The bacterial outer membrane β-barrel assembly machinery.Protein science : a publication of the Protein Society · 2012Review
- BB0324 and BB0028 are constituents of the Borrelia burgdorferi β-barrel assembly machine (BAM) complex.BMC microbiology · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
The assembly of beta-barrel proteins into membranes is a fundamental process that is essential in Gram-negative bacteria, mitochondria and plastids. Our understanding of the mechanism of beta-barrel assembly is progressing from studies carried out in Escherichia coli and Neisseria meningitidis. Comparative sequence analysis suggests that while many components mediating beta-barrel protein assembly are conserved in all groups of bacteria with outer membranes, some components are notably absent. The Alphaproteobacteria in particular seem prone to gene loss and show the presence or absence of specific components mediating the assembly of beta-barrels: some components of the pathway appear to be missing from whole groups of bacteria (e.g. Skp, YfgL and NlpB), other proteins are conserved but are missing characteristic domains (e.g. SurA). This comparative analysis is also revealing important structural signatures that are vague unless multiple members from a protein family are considered as a group (e.g. tetratricopeptide repeat (TPR) motifs in YfiO, beta-propeller signatures in YfgL). Given that the process of the beta-barrel assembly is conserved, analysis of outer membrane biogenesis in Alphaproteobacteria, the bacterial group that gave rise to mitochondria, also promises insight into the assembly of beta-barrel proteins in eukaryotes.
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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.