The PDZ2 domain of zonula occludens-1 and -2 is a phosphoinositide binding domain - Test2 - elhamkhani - TriplyDB

The PDZ2 domain of zonula occludens-1 and -2 is a phosphoinositide binding domain

The PDZ2 domain of zonula occludens-1 and -2 is a phosphoinositide binding domain

http://www.wikidata.org/entity/Q39794504

about

PDZ domains and their binding partners: structure, specificity, and modification Membrane Binding and Modulation of the PDZ Domain of PICK1 A ZO-1/α5β1-integrin complex regulates cytokinesis downstream of PKCε in NCI-H460 cells plated on fibronectin 1H, 13C, and 15N resonance assignment of the first PDZ domain of mouse ZO-1 TRAF4 Is a Novel Phosphoinositide-Binding Protein Modulating Tight Junctions and Favoring Cell Migration Frizzled 7 and PIP2 binding by syntenin PDZ2 domain supports Frizzled 7 trafficking and signalling Comprehensive analysis of yeast surface displayed cDNA library selection outputs by exon microarray to identify novel protein-ligand interactions.Prevalence, specificity and determinants of lipid-interacting PDZ domains from an in-cell screen and in vitro binding experiments Architecture of tight junctions and principles of molecular composition.The phosphoinositide-binding protein TRAF4 modulates tight junction stability and migration of cancer cells.Cooperative phosphoinositide and peptide binding by PSD-95/discs large/ZO-1 (PDZ) domain of polychaetoid, Drosophila zonulin Utilizing Yeast Surface Human Proteome Display Libraries to Identify Small Molecule-Protein Interactions.Genome-wide functional annotation of dual-specificity protein- and lipid-binding modules that regulate protein interactions.Cholesterol modulates cell signaling and protein networking by specifically interacting with PDZ domain-containing scaffold proteins.New aspects of the molecular constituents of tissue barriers.Nuclear phosphoinositides and their roles in cell biology and disease.Plasticity of PDZ domains in ligand recognition and signaling.ZO-2, a tight junction scaffold protein involved in the regulation of cell proliferation and apoptosis.Beyond cell-cell adhesion: Emerging roles of the tight junction scaffold ZO-2.The mucosal barrier at a glance.ZO-2, a tight junction protein involved in gene expression, proliferation, apoptosis, and cell size regulation.Functional complexes between YAP2 and ZO-2 are PDZ domain-dependent, and regulate YAP2 nuclear localization and signalling.Nuclear speckles: molecular organization, biological function and role in disease.Localization and projected role of phosphatidylinositol 4-kinases IIα and IIβ in inositol 1,4,5-trisphosphate-sensitive nucleoplasmic Ca²⁺ store vesicles.[TRAF4, a multifaceted protein involved in carcinoma progression].

P2860

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P2860

The PDZ2 domain of zonula occludens-1 and -2 is a phosphoinositide binding domain

http://www.wikidata.org/entity/Q39794504

description

2009 nî lūn-bûn

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2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

2009年论文

@zh

2009年论文

@zh-cn

name

The PDZ2 domain of zonula occludens-1 and -2 is a phosphoinositide binding domain

@en

The PDZ2 domain of zonula occludens-1 and -2 is a phosphoinositide binding domain.

@nl

type

label

The PDZ2 domain of zonula occludens-1 and -2 is a phosphoinositide binding domain

@en

The PDZ2 domain of zonula occludens-1 and -2 is a phosphoinositide binding domain.

@nl

prefLabel

The PDZ2 domain of zonula occludens-1 and -2 is a phosphoinositide binding domain

@en

The PDZ2 domain of zonula occludens-1 and -2 is a phosphoinositide binding domain.

@nl

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P1433

Cellular and Molecular Life Sciences

P1476

The PDZ2 domain of zonula occludens-1 and -2 is a phosphoinositide binding domain

@en

P2093

Ariane De Ganck

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

Berlinda Vanloo

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

Ciska Boucherie

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

Eline Remue

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

Hui Lu

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

Jan Gettemans

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

Joël Vandekerckhove

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

Kris Meerschaert

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

Moe Phyu Tun

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

Nitin Bhardwaj

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

P2860

Mechanistic basis of differential cellular responses of phosphatidylinositol 3,4-bisphosphate- and phosphatidylinositol 3,4,5-trisphosphate-binding pleckstrin homology domains

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Structure determination and ligand interactions of the PDZ2b domain of PTP-Bas (hPTP1E): splicing-induced modulation of ligand specificity

Domain Swapping within PDZ2 Is Responsible for Dimerization of ZO Proteins

PDZ domains of Par-3 as potential phosphoinositide signaling integrators

Domain-swapped dimerization of ZO-1 PDZ2 generates specific and regulatory connexin43-binding sites

Mechanism and role of PDZ domains in signaling complex assembly

The tight junction protein ZO-2 localizes to the nucleus and interacts with the heterogeneous nuclear ribonucleoprotein scaffold attachment factor-B

Nuclear PI(4,5)P(2): a new place for an old signal

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s00018-009-0156-6

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3951-3966

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scholarly article

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10.1007/S00018-009-0156-6

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24

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66

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Gisèle Degeest

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2009-09-22T00:00:00Z

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19784548

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