Structural basis for the autoinhibition of talin in regulating integrin activation. - Wikidata - awgldk - TriplyDB

Structural basis for the autoinhibition of talin in regulating integrin activation.

Structural basis for the autoinhibition of talin in regulating integrin activation.

http://www.wikidata.org/entity/Q42410877

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Kindlin-2 regulates podocyte adhesion and fibronectin matrix deposition through interactions with phosphoinositides and integrins Structural basis of phosphoinositide binding to kindlin-2 protein pleckstrin homology domain in regulating integrin activation Integrins β1 and β3 exhibit distinct dynamic nanoscale organizations inside focal adhesions Pseudopodium-enriched atypical kinase 1 regulates the cytoskeleton and cancer progression [corrected].Kindlin-1 and -2 directly bind the C-terminal region of beta integrin cytoplasmic tails and exert integrin-specific activation effects Integrin cytoplasmic tail interactions Structural Determinants of Integrin Binding to the Talin Rod The Structure of an Interdomain Complex That Regulates Talin Activity Structure of an integrin IIb 3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activation Central Region of Talin Has a Unique Fold That Binds Vinculin and Actin The Structure of the Talin Head Reveals a Novel Extended Conformation of the FERM Domain Rap1-interacting adapter molecule (RIAM) associates with the plasma membrane via a proximity detector Membrane Binding of the N-Terminal Ubiquitin-Like Domain of kindlin-2 Is Crucial for Its Regulation of Integrin Activation RIAM and Vinculin Binding to Talin Are Mutually Exclusive and Regulate Adhesion Assembly and Turnover Solution structure and peptide binding of the PTB domain from the AIDA1 postsynaptic signaling scaffolding protein The structure of Rap1 in complex with RIAM reveals specificity determinants and recruitment mechanism A novel membrane-dependent on/off switch mechanism of talin FERM domain at sites of cell adhesion Phosphatidylinositol 4,5-bisphosphate triggers activation of focal adhesion kinase by inducing clustering and conformational changes PIP kinases define PI4,5P₂signaling specificity by association with effectors Extracellular rigidity sensing by talin isoform-specific mechanical linkages A computational analysis of the dynamic roles of talin, Dok1, and PIPKI for integrin activation Skap2 is required for β2 integrin-mediated neutrophil recruitment and functions.RSK2 protein suppresses integrin activation and fibronectin matrix assembly and promotes cell migration Talin couples the actomyosin cortex to the plasma membrane during rear retraction and cytokinesis.Two modes of integrin activation form a binary molecular switch in adhesion maturation A directional switch of integrin signalling and a new anti-thrombotic strategy.Integrin alphaIIbbeta3 activation in Chinese hamster ovary cells and platelets increases clustering rather than affinity New PI(4,5)P2- and membrane proximal integrin-binding motifs in the talin head control beta3-integrin clustering.Structural and mechanical functions of integrins.Talin regulates moesin-NHE-1 recruitment to invadopodia and promotes mammary tumor metastasis.Significance of talin in cancer progression and metastasis.Mechanical stability of talin rod controls cell migration and substrate sensing.Talins and kindlins: partners in integrin-mediated adhesion.The switchable integrin adhesome.Direct interaction of kindlin-3 with integrin αIIbβ3 in platelets is required for supporting arterial thrombosis in mice.Kindlins, integrin activation and the regulation of talin recruitment to αIIbβ3.Studies on the morphology and spreading of human endothelial cells define key inter- and intramolecular interactions for talin1.Cdk5: A regulator of epithelial cell adhesion and migration.Filamin A regulates focal adhesion disassembly and suppresses breast cancer cell migration and invasion.New isoform-specific monoclonal antibodies reveal different sub-cellular localisations for talin1 and talin2.

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P2860

Structural basis for the autoinhibition of talin in regulating integrin activation.

http://www.wikidata.org/entity/Q42410877

description

2008 nî lūn-bûn

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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2008年论文

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2008年论文

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name

Structural basis for the autoinhibition of talin in regulating integrin activation.

@en

Structural basis for the autoinhibition of talin in regulating integrin activation.

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type

label

Structural basis for the autoinhibition of talin in regulating integrin activation.

@en

Structural basis for the autoinhibition of talin in regulating integrin activation.

@nl

prefLabel

Structural basis for the autoinhibition of talin in regulating integrin activation.

@en

Structural basis for the autoinhibition of talin in regulating integrin activation.

@nl

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J.MOLCEL.2008.06.011

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Structural basis for the autoinhibition of talin in regulating integrin activation.

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P2093

Dhanuja Perera

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Edward F Plow

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Esen Goksoy

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Jun Qin

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Xiangming Kong

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

Xiaoxia Wang

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

Yan-Qing Ma

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

P2860

Conformation, localization, and integrin binding of talin depend on its interaction with phosphoinositides

Structural determinants of integrin recognition by talin

Structural basis of integrin activation by talin

Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle

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

Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

Structural basis for the autoinhibition of focal adhesion kinase

Protein structure prediction servers at University College London

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

A structural mechanism of integrin alpha(IIb)beta(3) "inside-out" activation as regulated by its cytoplasmic face

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124-133

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