Role of Phosphorylation in Moesin Interactions with PIP2-Containing Biomimetic Membranes.

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Sequential binding of ezrin and moesin to L-selectin regulates monocyte protrusive behaviour during transendothelial migration

P2860

Q58195107-45D20BDF-D3F3-43F9-9E33-2459E1426C37

P2860

Role of Phosphorylation in Moesin Interactions with PIP2-Containing Biomimetic Membranes.

Item

http://www.wikidata.org/entity/Q47213612

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2018 nî lūn-bûn

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2018年の論文

@ja

2018年学术文章

@wuu

2018年学术文章

@zh

2018年学术文章

@zh-cn

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2018年学术文章

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@yue

2018年學術文章

@zh-hant

name

Role of Phosphorylation in Moesin Interactions with PIP2-Containing Biomimetic Membranes.

@en

Role of Phosphorylation in Moesin Interactions with PIP2-Containing Biomimetic Membranes.

@nl

type

Item

label

Role of Phosphorylation in Moesin Interactions with PIP2-Containing Biomimetic Membranes.

@en

Role of Phosphorylation in Moesin Interactions with PIP2-Containing Biomimetic Membranes.

@nl

prefLabel

Role of Phosphorylation in Moesin Interactions with PIP2-Containing Biomimetic Membranes.

@en

Role of Phosphorylation in Moesin Interactions with PIP2-Containing Biomimetic Membranes.

@nl

P1476

Role of Phosphorylation in Moesin Interactions with PIP2-Containing Biomimetic Membranes

@en

P2093

Aline Le Roy

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

Catherine Picart

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

Fabien Dalonneau

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

Marianne Weidenhaupt

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

Mathieu Kowalski

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

Morgane Lourdin

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

Quentin Lubart

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

P2860

The actin-binding ERM protein Moesin binds to and stabilizes microtubules at the cell cortex.

Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain

Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway

Phosphoinositide binding and phosphorylation act sequentially in the activation mechanism of ezrin

Morphogenic effects of ezrin require a phosphorylation-induced transition from oligomers to monomers at the plasma membrane

Model membranes to shed light on the biochemical and physical properties of ezrin/radixin/moesin

Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain

Unique DC-SIGN clustering activity of a small glycomimetic: A lesson for ligand design

Sphingolipid regulation of ezrin, radixin, and moesin proteins family: implications for cell dynamics.

Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling

P304

98-112

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

P31

scholarly article

P356

10.1016/J.BPJ.2017.10.041

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P407

English

P433

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

P478

114

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

P50

Christine Ebel

Helene Vitet

P577

2018-01-01T00:00:00Z

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

P698

29320700

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

P921

phosphorylation

P932

5912500

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

Role of Phosphorylation in Moesin Interactions with PIP2-Containing Biomimetic Membranes.

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P2860

P2860

Role of Phosphorylation in Moesin Interactions with PIP2-Containing Biomimetic Membranes.

description

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type

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P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932