Phosphorylation of Tyr-398 and Tyr-402 in Occludin Prevents Its Interaction with ZO-1 and Destabilizes Its Assembly at the Tight Junctions-Reference-Cited by-同舟云学术

Phosphorylation of Tyr-398 and Tyr-402 in Occludin Prevents Its Interaction with ZO-1 and Destabilizes Its Assembly at the Tight Junctions

Published:2009-01 Issue:3 Volume:284 Page:1559-1569
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Elias Bertha C.,Suzuki Takuya,Seth Ankur,Giorgianni Francesco,Kale Gautam,Shen Le,Turner Jerrold R.,Naren Anjaparavanda,Desiderio Dominic M.,Rao Radhakrishna

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference40 articles.

1. Tight junction proteins

2. Role of tight junctions in cell proliferation and cancer

3. Intestinal epithelial responses to enteric pathogens: effects on the tight junction barrier, ion transport, and inflammation

4. Regulation of the intestinal epithelial barrier by the apical junctional complex

5. Regulation of Airway Tight Junctions by Proinflammatory Cytokines

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