Developing an innovative chimeric multi-epitope subunit vaccine against <i>Staphylococcus intermedius</i> using an immunoinformatics strategy via Multi-omics approaches. [PDF]
Naveed M +11 more
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Identification and evaluation of tumor pyroptosis-associated antigens for design a vaccine candidate against lung cancer. [PDF]
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A gut sense for a microbial pattern regulates feeding. [PDF]
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Comment on "Intratumorally specific microbial-derived lipopolysaccharide contributes to non-small cell lung cancer progression". [PDF]
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Balancing harm and harmony: Evolutionary dynamics between gut microbiota-derived flagellin and TLR5-mediated host immunity and metabolism. [PDF]
Seo B, Lim MY.
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Helicobacter pylori flagellin: TLR5 evasion and fusion-based conversion into a TLR5 agonist
Biochemical and Biophysical Research Communications, 2018Helicobacter pylori is a flagellated bacterium of the Epsilonproteobacteria class that causes peptic ulcers. Flagellin is a primary structural protein that assembles into the flagellar filament. Flagellins from bacteria that belong to the Gammaproteobacteria and Firmicutes groups are detected by Toll-like receptor 5 (TLR5) in the host, triggering the ...
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The human gastrointestinal tract is a dynamic melting pot of commensal bacteria. Although the apical surface of intestinal epithelial cells lining the gut is constantly exposed to proinflammatory bacterial products, this rarely results in an inflammatory response.
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Activation of TLR5 induces podocyte apoptosis
Cell Biochemistry and Function, 2016The apoptosis plays a critical role in a number of inflammatory disorders. Bacterial infection is one of the causes inducing apoptosis. This study aims to investigate the mechanism by which activation of TLR5 induces podocyte apoptosis. In this study, a podocyte cell line was cultured in RPMI1640 medium. The expression of TLR5 was assessed by real‐time
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The flagellin-TLR5 axis: Therapeutic opportunities
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Hayashi et al. characterized the transmembrane Toll-like receptor (TLR) 5 protein and identified a physiologically relevant ligand capable of activating TLR5 signaling. Overexpression of chimeric proteins consisting of the intracellular domain of TLR5 fused to the extracellular domain of CD4 (to promote dimerization)
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