ArticleJournal of bacteriology1995
Conformational analysis of the Campylobacter jejuni porin.
Article in Journal of bacteriology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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.
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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.
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Who cites it
23 citing papers in PubMed, 67 citations in OpenAlex.
- Antibacterial Mode of Action of theMolecules (Basel, Switzerland) · 2020Article
- The Rho-Independent Transcription Terminator for theInfection and immunity · 2019Article
- In planta expression of nanobody-based designer chicken antibodies targeting Campylobacter.PloS one · 2018Article
- Understanding antibiotic resistance via outer membrane permeability.Infection and drug resistance · 2018Review
- Identification and Characterization of the Major Porin of Desulfovibrio vulgaris Hildenborough.Journal of bacteriology · 2017Article
- Peptide translocation across MOMP, the major outer membrane channel fromBiochemistry and biophysics reports · 2017Article
- MOMP from Campylobacter jejuni Is a Trimer of 18-Stranded β-Barrel Monomers with a CaJournal of molecular biology · 2016Article
- Proteomic and genomic analysis reveals novelEuPA open proteomics · 2014Article
- A novel O-linked glycan modulates Campylobacter jejuni major outer membrane protein-mediated adhesion to human histo-blood group antigens and chicken colonization.Open biology · 2014Article
- Resistance mechanisms in Campylobacter jejuni.Virulence · 2013Review
- Microarray-based method for screening of immunogenic proteins from bacteria.Journal of nanobiotechnology · 2012Article
- Article
- Functional characterization of a lipoprotein-encoding operon in Campylobacter jejuni.PloS one · 2011Article
- Examination of Campylobacter jejuni putative adhesins leads to the identification of a new protein, designated FlpA, required for chicken colonization.Infection and immunity · 2009Article
- Structural and functional analyses of the major outer membrane protein of Chlamydia trachomatis.Journal of bacteriology · 2007Article
- Channel formation by CarO, the carbapenem resistance-associated outer membrane protein of Acinetobacter baumannii.Antimicrobial agents and chemotherapy · 2005Article
- Use of the omp50 gene for identification of Campylobacter species by PCR.Journal of clinical microbiology · 2004Article
- Functional refolding of the Campylobacter jejuni MOMP (major outer membrane protein) porin by GroEL from the same species.The Biochemical journal · 2004Article
- Molecular basis of bacterial outer membrane permeability revisited.Microbiology and molecular biology reviews : MMBR · 2003Review
- Environmental regulation of Campylobacter jejuni major outer membrane protein porin expression in Escherichia coli monitored by using green fluorescent protein.Applied and environmental microbiology · 2002Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The major outer membrane protein (MOMP) of Campylobacter jejuni was purified to homogeneity by selective solubilization and fast protein liquid chromatography. The amino acid composition of the MOMP indicates the presence of cysteine residues. The amino-terminal sequence, determined over 31 residues, shows no significant homology with any other porin from gram-negative bacteria except in a discrete region. Immunocross-reactivity between Escherichia coli OmpC and the MOMP was analyzed, and a common antigenic site between these two porins was identified with an anti-peptide antibody. From circular dichroism and immunological investigations, the existence of a stable folded monomer, containing a high level of beta-sheet secondary structure, is evident. Conformational analyses show the presence of a native trimeric state generated by association of the three folded monomers; the stability of this trimer is reduced compared with that of E. coli porins. This study clearly reveals that the C. jejuni MOMP is related to the family of trimeric bacterial porins.
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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.