Analysis of absorption enhancers in epithelial cell models. - Test2 - elhamkhani - TriplyDB

Analysis of absorption enhancers in epithelial cell models.

Analysis of absorption enhancers in epithelial cell models.

http://www.wikidata.org/entity/Q38021498

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Paracellular drug absorption enhancement through tight junction modulation JNK1/2-dependent phosphorylation of angulin-1/LSR is required for the exclusive localization of angulin-1/LSR and tricellulin at tricellular contacts in EpH4 epithelial sheet Comparative analysis of theophylline and cholera toxin in rat colon reveals an induction of sealing tight junction proteins.Laurate permeabilizes the paracellular pathway for small molecules in the intestinal epithelial cell model HT-29/B6 via opening the tight junctions by reversible relocation of claudin-5. [Corrected].Human claudin-8 and -14 are receptors capable of conveying the cytotoxic effects of Clostridium perfringens enterotoxin.A role for tricellulin in the regulation of gill epithelium permeability.A novel perspective and approach to intestinal octreotide absorption: sinomenine-mediated reversible tight junction opening and its molecular mechanism.Strategies for enhanced peptide and protein delivery.The role of epithelial tight junctions involved in pathogen infections.Tight junction physiology of pleural mesothelium.Metallic oxide nanoparticle translocation across the human bronchial epithelial barrier.Perspectives on tight junction research.Mechanisms allowing protein delivery in nasal mucosa using NPL nanoparticles.

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P2860

Analysis of absorption enhancers in epithelial cell models.

http://www.wikidata.org/entity/Q38021498

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artigo científico

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artikel ilmiah

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artículo científico

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Analysis of absorption enhancers in epithelial cell models.

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Analysis of absorption enhancers in epithelial cell models.

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Analysis of absorption enhancers in epithelial cell models.

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J.1749-6632.2012.06562.X

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Annals of the New York Academy of Sciences

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Analysis of absorption enhancers in epithelial cell models.

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Maren Amasheh

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Miriam S Heydt

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Rita Rosenthal

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Salah Amasheh

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P2860

Occludin: a novel integral membrane protein localizing at tight junctions

Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells

Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin

Claudin-1 is a hepatitis C virus co-receptor required for a late step in entry

Clostridium perfringens enterotoxin binds to the second extracellular loop of claudin-3, a tight junction integral membrane protein

Size-selective loosening of the blood-brain barrier in claudin-5-deficient mice

Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells

Claudin-2, a component of the tight junction, forms a paracellular water channel

Delta-aminolevulinic acid transport by intestinal and renal peptide transporters and its physiological and clinical implications

Claudin-based tight junctions are crucial for the mammalian epidermal barrier: a lesson from claudin-1-deficient mice

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86-92

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10.1111/J.1749-6632.2012.06562.X

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1258

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Christoph Stein

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2012-07-01T00:00:00Z

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