ArticleInfection and immunity1998
Contact-dependent protein secretion in Porphyromonas gingivalis.
Article in Infection and immunity, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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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Who cites it
20 citing papers in PubMed, 44 citations in OpenAlex.
- Illuminating the oral microbiome: cellular microbiology.FEMS microbiology reviews · 2023Article
- A unique bacterial secretion machinery with multiple secretion centers.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Identification and characterization of a UbK family kinase in Porphyromonas gingivalis that phosphorylates the RprY response regulator.Molecular oral microbiology · 2021Article
- Oxidative stress resistance in Porphyromonas gingivalis.Future microbiology · 2012Review
- Pathogen-mediated proteolysis of the cell death regulator RIPK1 and the host defense modulator RIPK2 in human aortic endothelial cells.PLoS pathogens · 2012Article
- Dichotomy of gingipains action as virulence factors: from cleaving substrates with the precision of a surgeon's knife to a meat chopper-like brutal degradation of proteins.Periodontology 2000 · 2010Review
- Bacterial invasion of epithelial cells and spreading in periodontal tissue.Periodontology 2000 · 2010Review
- Role of Porphyromonas gingivalis SerB in gingival epithelial cell cytoskeletal remodeling and cytokine production.Infection and immunity · 2008Article
- Gingipain-dependent interactions with the host are important for survival of Porphyromonas gingivalis.Frontiers in bioscience : a journal and virtual library · 2008Review
- Quantitative proteomics of intracellular Porphyromonas gingivalis.Proteomics · 2007Article
- A Porphyromonas gingivalis haloacid dehalogenase family phosphatase interacts with human phosphoproteins and is important for invasion.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Gene expression in Porphyromonas gingivalis after contact with human epithelial cells.Infection and immunity · 2005Article
- In vitro models of tissue penetration and destruction by Porphyromonas gingivalis.Infection and immunity · 2004Article
- Porphyromonas gingivalis induces receptor activator of NF-kappaB ligand expression in osteoblasts through the activator protein 1 pathway.Infection and immunity · 2004Article
- Reconstructed protein arrays from 3D HPLC/tandem mass spectrometry and 2D gels: complementary approaches to Porphyromonas gingivalis protein expression.The Analyst · 2002Article
- Role for fimbriae and lysine-specific cysteine proteinase gingipain K in expression of interleukin-8 and monocyte chemoattractant protein in Porphyromonas gingivalis-infected endothelial cells.Infection and immunity · 2002Article
- Assessment of internalization and viability of Porphyromonas gingivalis in KB epithelial cells by confocal microscopy.Infection and immunity · 2001Article
- Association of mitogen-activated protein kinase pathways with gingival epithelial cell responses to Porphyromonas gingivalis infection.Infection and immunity · 2001Article
- Regulation of the Porphyromonas gingivalis fimA (Fimbrillin) gene.Infection and immunity · 2000Article
- Life below the gum line: pathogenic mechanisms of Porphyromonas gingivalis.Microbiology and molecular biology reviews : MMBR · 1998Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Porphyromonas gingivalis can induce its uptake by host epithelial cells; however, the nature and role of the P. gingivalis molecules involved in this invasion process have yet to be determined. In this study, modulation of secreted P. gingivalis proteins following association with gingival epithelial cells was investigated. Western immunoblot analysis showed that contact with epithelial cells or epithelial cell growth media induces P. gingivalis 33277 to secrete several proteins with molecular masses between 35 and 95 kDa. Secretion of the Arg-gingipain and Lys-gingipain proteases was repressed under these conditions. The contact-induced secreted protein profile was altered in Arg-gingipain-deficient and Lys-gingipain-deficient mutants, indicating a possible role for these proteases in the secretion pathway. The P. gingivalis contact-dependent protein secretion pathway differs to some extent from type III protein secretion pathways in enteric pathogens, as a gene homologous to the invA family genes was not detected in P. gingivalis. The secreted proteins of P. gingivalis may play a role in the interactions of the organism with host cells.
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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.