(Q42198362)

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p38MAPK, Rho/ROCK and PKC pathways are involved in influenza-induced cytoskeletal rearrangement and hyperpermeability in PMVEC via phosphorylating ERM.

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Europe PubMed Central

PubMed publication ID

18 October 2017

p38MAPK, Rho/ROCK and PKC pathways are involved in influenza-induced cytoskeletal rearrangement and hyperpermeability in PMVEC via phosphorylating ERM. (English)

1 reference

Europe PubMed Central

PubMed publication ID

18 October 2017

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phosphorylation

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author name string

Chenyue Zhang

1

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Europe PubMed Central

PubMed publication ID

18 October 2017

Ying Wu

2

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Europe PubMed Central

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18 October 2017

Zinan Xuan

3

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Europe PubMed Central

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18 October 2017

Shujing Zhang

4

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Europe PubMed Central

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18 October 2017

Xudan Wang

5

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Europe PubMed Central

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18 October 2017

Yu Hao

6

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18 October 2017

Jun Wu

7

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Europe PubMed Central

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18 October 2017

Shu Zhang

8

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Europe PubMed Central

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18 October 2017

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19 August 2014

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PubMed publication ID

18 October 2017

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Europe PubMed Central

PubMed publication ID

18 October 2017

192

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PubMed publication ID

18 October 2017

6-15

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Europe PubMed Central

PubMed publication ID

18 October 2017

Ezrin/radixin/moesin proteins differentially regulate endothelial hyperpermeability after thrombin

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The lung microvascular endothelium as a therapeutic target in severe influenza

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Organizing the cell cortex: the role of ERM proteins

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ERM proteins in epithelial cell organization and functions

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The EBP50-moesin interaction involves a binding site regulated by direct masking on the FERM domain

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Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site

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Hantaviruses direct endothelial cell permeability by sensitizing cells to the vascular permeability factor VEGF, while angiopoietin 1 and sphingosine 1-phosphate inhibit hantavirus-directed permeability

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ERM protein moesin is phosphorylated by advanced glycation end products and modulates endothelial permeability

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Rho kinase activates ezrin-radixin-moesin (ERM) proteins and mediates their function in cortical neuron growth, morphology and motility in vitro

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Inhibition of MLC phosphorylation restricts replication of influenza virus--a mechanism of action for anti-influenza agents

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Rho-ROCK-dependent ezrin-radixin-moesin phosphorylation regulates Fas-mediated apoptosis in Jurkat cells

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Specific binding of HIV-1 envelope protein gp120 to the structural membrane proteins ezrin and moesin

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Protein Kinase Cα-Induced p115RhoGEF Phosphorylation Signals Endothelial Cytoskeletal Rearrangement

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Ezrin/radixin/moesin proteins and Rho GTPase signalling in leucocytes

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Ezrin/radixin/moesin proteins are phosphorylated by TNF-alpha and modulate permeability increases in human pulmonary microvascular endothelial cells

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Ezrin, Radixin, and Moesin (ERM) proteins function as pleiotropic regulators of human immunodeficiency virus type 1 infection

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Signaling mechanisms regulating endothelial permeability

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Protein kinase C-alpha signals rho-guanine nucleotide dissociation inhibitor phosphorylation and rho activation and regulates the endothelial cell barrier function

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Ezrin is a downstream effector of trafficking PKC-integrin complexes involved in the control of cell motility

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Ezrin/radixin/moesin: versatile controllers of signaling molecules and of the cortical cytoskeleton

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10.1016/J.VIRUSRES.2014.07.027

1 reference

Europe PubMed Central

PubMed publication ID

18 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

18 October 2017

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