Antioxidant and anti-inflammatory mechanisms of yak-derived Bacillus subtilis against Salmonella Derby-induced enteritis in mice. [PDF]
Ye B +7 more
europepmc +1 more source
<i>Porphyromonas gingivalis</i> drives trimethylamine-N-oxide accumulation via modulation of gut microbial trimethylamine lyase in mice. [PDF]
Xie W +7 more
europepmc +1 more source
<i>Polygonatum cyrtonema</i> Polysaccharides Alleviates Diet-Induced Obesity in Mice by Modulating the Gut Microbiota and Reducing Intestinal Inflammation. [PDF]
Yang R +6 more
europepmc +1 more source
Evodiamine alleviates MPTP-induced Parkinson's disease in mice by regulating gut microbiota and suppressing TLR4/MyD88/NF-kB pathway. [PDF]
Wang S +8 more
europepmc +1 more source
<i>Prevotella intermedia</i> oral infection induces cognitive impairment in C57BL/6 mice via neuroinflammation and barrier damage. [PDF]
Cai Y +8 more
europepmc +1 more source
Proton pump inhibitor increases intestinal epithelial paracellular permeability via the p38-MAPK/NF-κB signaling pathway. [PDF]
Zhang M +8 more
europepmc +1 more source
Occludin Phosphorylation in Regulation of Epithelial Tight Junctions [PDF]
Occludin is the first transmembrane protein of the tight junction to be discovered. While numerous studies emphasized the important role of occludin in assembly and maintenance of tight junctions, occludin knockout studies indicated that it was not required for tight junction assembly in different epithelia.
Radhakrishna Rao
exaly +3 more sources
Occludin Regulates Actin Cytoskeleton in Endothelial Cells.
Occludin is a major membrane component of tight junctions of endothelial cells, though the role of this molecule is not fully understood. RLE cells, derived from rat lung endothelial cells, express a negligible level of occludin with clear expression of E-cadherin and ZO-1 at cell junctions.
Yasuo Kokai +2 more
exaly +4 more sources
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Redox-sensitivity of the dimerization of occludin
Cellular and Molecular Life Sciences, 2009Occludin is a self-associating transmembrane tight junction protein affected in oxidative stress. However, its function is unknown. The cytosolic C-terminal tail contains a coiled coil-domain forming dimers contributing to the self-association. Studying the hypothesis that the self-association is redox-sensitive, we found that the dimerization of the ...
Walter, Juliane K. +6 more
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