S-nitrosylation regulates VE-cadherin phosphorylation and internalization in microvascular permeability.

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2016 nî lūn-bûn

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2016年の論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年论文

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2016年论文

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2016年论文

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name

S-nitrosylation regulates VE-c ...... in microvascular permeability.

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type

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label

S-nitrosylation regulates VE-c ...... in microvascular permeability.

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S-nitrosylation regulates VE-c ...... in microvascular permeability.

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P1476

S-nitrosylation regulates VE-c ...... in microvascular permeability.

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P2093

Adam Korayem

http://www.w3.org/2001/XMLSchema#string

Anita Guequén

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Fabiola A Sánchez

http://www.w3.org/2001/XMLSchema#string

José Sarmiento

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Lorena Rebolledo

http://www.w3.org/2001/XMLSchema#string

Mauricio P Boric

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Patricia Zamorano

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Pia Burboa

http://www.w3.org/2001/XMLSchema#string

Rodrigo Carrasco

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Walter N Durán

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P2860

VEGF controls endothelial-cell permeability by promoting the beta-arrestin-dependent endocytosis of VE-cadherin

Targeted deficiency or cytosolic truncation of the VE-cadherin gene in mice impairs VEGF-mediated endothelial survival and angiogenesis

Src-induced tyrosine phosphorylation of VE-cadherin is not sufficient to decrease barrier function of endothelial monolayers.

The NO cascade, eNOS location, and microvascular permeability.

Functional significance of differential eNOS translocation.

Functional significance of cytosolic endothelial nitric-oxide synthase (eNOS): regulation of hyperpermeability

Nitric oxide synthase generates nitric oxide locally to regulate compartmentalized protein S-nitrosylation and protein trafficking.

Targeted null-mutation in the vascular endothelial-cadherin gene impairs the organization of vascular-like structures in embryoid bodies.

p120-catenin binding masks an endocytic signal conserved in classical cadherins.

Multiple cadherin extracellular repeats mediate homophilic binding and adhesion.

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H1039-44

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scholarly article

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10.1152/AJPHEART.00063.2016

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310

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2016-02-26T00:00:00Z

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26921435

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4867340

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