Ezrin and moesin function together to promote T cell activation. - Wikidata - wikimedia - TriplyDB

Ezrin and moesin function together to promote T cell activation.

Ezrin and moesin function together to promote T cell activation.

http://www.wikidata.org/entity/Q36379032

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Advanced glycation end-products induce calpain-mediated degradation of ezrin Ezrin tunes T-cell activation by controlling Dlg1 and microtubule positioning at the immunological synapse.Molecular Mechanisms for cAMP-Mediated Immunoregulation in T cells - Role of Anchored Protein Kinase A Signaling Units Comparative Anatomy of Phagocytic and Immunological Synapses Model membranes to shed light on the biochemical and physical properties of ezrin/radixin/moesin Phosphatidylinositol (4,5) bisphosphate controls T cell activation by regulating T cell rigidity and organization Ezrin and moesin are required for efficient T cell adhesion and homing to lymphoid organs Organizing the cell cortex: the role of ERM proteins Force-dependent calcium signaling and its pathway of human neutrophils on P-selectin in flow Ezrin/Radixin/Moesin proteins and flotillins cooperate to promote uropod formation in T cells Differential involvement of ezrin/radixin/moesin proteins in sphingosine 1-phosphate-induced human pulmonary endothelial cell barrier enhancement Hematopoietic lineage cell-specific protein 1 is recruited to the immunological synapse by IL-2-inducible T cell kinase and regulates phospholipase Cgamma1 Microcluster dynamics during T cell spreading LZTFL1 Upregulated by All-Trans Retinoic Acid during CD4+ T Cell Activation Enhances IL-5 Production.Induction of membrane ceramides: a novel strategy to interfere with T lymphocyte cytoskeletal reorganisation in viral immunosuppression.Ezrin is highly expressed in early thymocytes, but dispensable for T cell development in mice.Ezrin is a component of the HIV-1 virological presynapse and contributes to the inhibition of cell-cell fusion.Binding of moesin and ezrin to membranes containing phosphatidylinositol (4,5) bisphosphate: a comparative study of the affinity constants and conformational changes.Focused examination of the intestinal lamina propria yields greater molecular insight into mechanisms underlying SIV induced immune dysfunction.Characterization of in vivo Dlg1 deletion on T cell development and function CD43 interaction with ezrin-radixin-moesin (ERM) proteins regulates T-cell trafficking and CD43 phosphorylation.Dynamic cortical actin remodeling by ERM proteins controls BCR microcluster organization and integrity.Formation of STIM and Orai complexes: puncta and distal caps.Proteomics analysis of the ezrin interactome in B cells reveals a novel association with Myo18aα.Aniline-induced nitrosative stress in rat spleen: proteomic identification of nitrated proteins.Constitutively active ezrin increases membrane tension, slows migration, and impedes endothelial transmigration of lymphocytes in vivo in mice Ezrin: a regulator of actin microfilaments in cell junctions of the rat testis.From lipid second messengers to molecular motors: microtubule-organizing center reorientation in T cells Spatial coupling of JNK activation to the B cell antigen receptor by tyrosine-phosphorylated ezrin.Loss of TCR-beta F1 and/or EZRIN expression is associated with unfavorable prognosis in nodal peripheral T-cell lymphomas.Ezrin tunes the magnitude of humoral immunity.Coordinate control of cytoskeletal remodeling and calcium mobilization during T-cell activation Engagement of CD81 induces ezrin tyrosine phosphorylation and its cellular redistribution with filamentous actin.FERM domain of moesin desorbs the basic-rich cytoplasmic domain of l-selectin from the anionic membrane surface.The immunological synapse controls local and global calcium signals in T lymphocytes.Modular design of immunological synapses and kinapses.Mechanisms of cellular communication through intercellular protein transfer.Germinal center kinases in immune regulation.Membrane-organizing protein moesin controls Treg differentiation and antitumor immunity via TGF-β signaling Ezrin, Radixin and Moesin: key regulators of membrane-cortex interactions and signaling New insights into the T cell synapse from single molecule techniques.

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Ezrin and moesin function together to promote T cell activation.

http://www.wikidata.org/entity/Q36379032

description

2009 nî lūn-bûn

@nan

2009年の論文

@ja

2009年学术文章

@wuu

2009年学术文章

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2009年学术文章

@zh-hans

2009年学术文章

@zh-my

2009年学术文章

@zh-sg

2009年學術文章

@yue

2009年學術文章

@zh

2009年學術文章

@zh-hant

name

Ezrin and moesin function together to promote T cell activation.

@ast

Ezrin and moesin function together to promote T cell activation.

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type

label

Ezrin and moesin function together to promote T cell activation.

@ast

Ezrin and moesin function together to promote T cell activation.

@en

prefLabel

Ezrin and moesin function together to promote T cell activation.

@ast

Ezrin and moesin function together to promote T cell activation.

@en

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JIMMUNOL.182.2.1021

P1433

Journal of Immunology

P1476

Ezrin and moesin function together to promote T cell activation

@en

P2093

Andrea I McClatchey

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

Bruce D Freedman

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

Ichiko Saotome

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

Meredith H Shaffer

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

Peimin Zhu

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

Renell S Dupree

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

Richard F Schmidt

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

P2860

Inhibition of T cell activation by cyclic adenosine 5'-monophosphate requires lipid raft targeting of protein kinase A type I by the A-kinase anchoring protein ezrin

Ezrin, a plasma membrane-microfilament linker, signals cell survival through the phosphatidylinositol 3-kinase/Akt pathway

Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2

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

Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association

Actin and agonist MHC-peptide complex-dependent T cell receptor microclusters as scaffolds for signaling.

Radixin deficiency causes conjugated hyperbilirubinemia with loss of Mrp2 from bile canalicular membranes

Exclusion of CD43 from the immunological synapse is mediated by phosphorylation-regulated relocation of the cytoskeletal adaptor moesin

Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein

ERM-dependent movement of CD43 defines a novel protein complex distal to the immunological synapse

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1021-1032

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scholarly article

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10.4049/JIMMUNOL.182.2.1021

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2

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182

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Janis K Burkhardt

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2009-01-01T00:00:00Z

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23759787

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19124745

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3491660

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