ArticleThe EMBO journal1997
Folding of a bacterial outer membrane protein during passage through the periplasm.
Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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
25 citing papers in PubMed, 64 citations in OpenAlex.
- The big BAM theory: An open and closed case?Biochimica et biophysica acta. Biomembranes · 2020Review
- Folding of a bacterial integral outer membrane protein is initiated in the periplasm.Nature communications · 2017Article
- Outer Membrane Biogenesis.Annual review of microbiology · 2017Review
- Membrane integration of an essential β-barrel protein prerequires burial of an extracellular loop.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Associations of microbiota and toll-like receptor signaling pathway in esophageal adenocarcinoma.BMC cancer · 2016Article
- The β-barrel assembly machinery (BAM) is required for the assembly of a primitive S-layer protein in the ancient outer membrane of Thermus thermophilus.Extremophiles : life under extreme conditions · 2012Article
- The bacterial outer membrane β-barrel assembly machinery.Protein science : a publication of the Protein Society · 2012Review
- The Bam machine: a molecular cooper.Biochimica et biophysica acta · 2012Review
- A knowledge-based potential highlights unique features of membrane α-helical and β-barrel protein insertion and folding.Protein science : a publication of the Protein Society · 2012Article
- Assembly of Outer Membrane β-Barrel Proteins: the Bam Complex.EcoSal Plus · 2011Article
- Article
- Conserved properties of polypeptide transport-associated (POTRA) domains derived from cyanobacterial Omp85.The Journal of biological chemistry · 2010Article
- Repetitive architecture of the Haemophilus influenzae Hia trimeric autotransporter.Journal of molecular biology · 2008Article
- Alternative function for the mitochondrial SAM complex in biogenesis of alpha-helical TOM proteins.The Journal of cell biology · 2007Article
- Periplasmic proteins of the extremophile Acidithiobacillus ferrooxidans: a high throughput proteomics analysis.Molecular & cellular proteomics : MCP · 2007Article
- Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli.Genes & development · 2007Article
- Expression, processing, and localization of PmpD of Chlamydia trachomatis Serovar L2 during the chlamydial developmental cycle.PloS one · 2007Article
- Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif.PLoS biology · 2006Article
- Characterizing folding, structure, molecular interactions and ligand gated activation of single sodium/proton antiporters.Naunyn-Schmiedeberg's archives of pharmacology · 2006Review
- Membrane protein insertion: mixing eukaryotic and prokaryotic concepts.EMBO reports · 2005Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The transport of bacterial outer membrane proteins to their destination might be either a one-step process via the contact zones between the inner and outer membrane or a two-step process, implicating a periplasmic intermediate that inserts into the membrane. Furthermore, folding might precede insertion or vice versa. To address these questions, we have made use of the known 3D-structure of the trimeric porin PhoE of Escherichia coli to engineer intramolecular disulfide bridges into this protein at positions that are not exposed to the periplasm once the protein is correctly assembled. The mutations did not interfere with the biogenesis of the protein, and disulfide bond formation appeared to be dependent on the periplasmic enzyme DsbA, which catalyzes disulfide bond formation in the periplasm. This proves that the protein passes through the periplasm on its way to the outer membrane. Furthermore, since the disulfide bonds create elements of tertiary structure within the mutant proteins, it appears that these proteins are at least partially folded before they insert into the outer membrane.
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.