ArticleCurrent microbiology2005
The major Aeromonas veronii outer membrane protein: gene cloning and sequence analysis.
Article in Current microbiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed, 7 citations in OpenAlex.
- Genetic cargo and bacterial species set the rate of vesicle-mediated horizontal gene transfer.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The gene encoding the major outer membrane protein (OMP) from Aeromonas veronii, Omp38, was cloned and characterized. Sequence analysis revealed an open reading frame of 1,047 nucleotides coding for a primary protein of 349 amino acids with a 20-amino-acid signal peptide at the N-terminal and the consensus sequence Ala-X-Ala (Ala-Asn-Ala) as the signal peptidase I recognition site. The mature protein is composed of 329 amino acids with a calculated molecular mass of 36,327 Da. The degree of identity of the deduced Omp38 amino acid sequence to porins from enteric bacteria (OmpF, PhoE, and OmpC) was only 30%. Nevertheless, Omp38 possesses typical features of Gram-negative porins, including acidic pI, high glycine and low proline content, no cysteine residues, and a carboxy-terminal Phe. On the basis of PhoE-OmpF three-dimensional structure and the Kyte-Doolittle hydrophobicity analysis, it seems likely that Omp38 secondary structure consists of 16 antiparallel beta-strands and 8 loops. Phylogenetic analyses among Omp38 and related porins from Gram-negative bacteria originate well-defined clusters that agree with the taxonomy of the corresponding organisms.
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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.