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<i>Barnesiella intestinihominis</i> improves gut microbiota disruption and intestinal barrier integrity in mice with impaired glucose regulation. [PDF]
Front PharmacolLiu X +5 more
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Insights into the mechanism of reversible blood-brain barrier opening via second near-infrared region excited gold nanorods photothermal effect: Regulation of the tight junction protein occludin. [PDF]
Smart MolLiang K +8 more
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Occludin: One Protein, Many Forms [PDF]
Molecular and Cellular Biology, 2012 Intercellular tight junctions (TJs) exhibit a complex molecular architecture involving the regulated cointeraction of cytoplasmic adaptor proteins (e.g., zonula occludens) and integral membrane linker proteins (e.g., occludin and claudins). They provide structural integrity to epithelial and endothelial tissues and create highly polarized barriers ...
Philip M Cummins
exaly +3 more sources
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Occludin: Structure, function and regulation
Advanced Drug Delivery Reviews, 2005Epithelial and/or endothelial barriers play a critical role in animal, including human, life forms. The tight junction (TJ) is an essential component of these barriers. Occludin is a major component of the TJ. The structure of occludin, including its gene splice variants and protein essential components have been elucidated.
James M Mullin
exaly +3 more sources
Occludin Phosphorylation in Regulation of Epithelial Tight Junctions [PDF]
Annals of the New York Academy of Sciences, 2009 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
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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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Occludin confers adhesiveness when expressed in fibroblasts
Journal of Cell Science, 1997ABSTRACT Occludin is an integral membrane protein specifically associated with tight junctions. Previous studies suggest it is likely to function in forming the intercellular seal. In the present study, we expressed occludin under an inducible promotor in occludin-null fibroblasts to determine whether this protein confers intercellular ...
C M, Van Itallie, J M, Anderson
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Shear stress regulates occludin content and phosphorylation
American Journal of Physiology-Heart and Circulatory Physiology, 2001Previous studies determined that shear stress imposed on bovine aortic endothelial cell (BAEC) monolayers increased the hydraulic conductivity ( LP); however, the mechanism by which shear stress increases LPremains unknown. This study tested the hypothesis that shear stress regulates paracellular transport by altering the expression and phosphorylation
L, DeMaio +4 more
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Occludin Protein Family: Oxidative Stress and Reducing Conditions
Antioxidants & Redox Signaling, 2011The occludin-like proteins belong to a family of tetraspan transmembrane proteins carrying a marvel domain. The intrinsic function of the occludin family is not yet clear. Occludin is a unique marker of any tight junction and is found in polarized endothelial and epithelial tissue barriers, at least in the adult vertebrate organism. Occludin is able to
Ingolf E, Blasig +6 more
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