Kindlin-2 directly binds actin and regulates integrin outside-in signaling - Wikidata - wikimedia - TriplyDB

Kindlin-2 directly binds actin and regulates integrin outside-in signaling

Kindlin-2 directly binds actin and regulates integrin outside-in signaling

http://www.wikidata.org/entity/Q36789915

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The integrin adhesome network at a glance Of Kindlins and Cancer A proteomics view on integrin-mediated adhesions.Integrin-mediated mechanotransduction.Stretch-induced actomyosin contraction in epithelial tubes: Mechanotransduction pathways for tubular homeostasis.Kindlin-2 interacts with endothelial adherens junctions to support vascular barrier integrity.The extreme C-terminal region of kindlin-2 is critical to its regulation of integrin activation.Optogenetic interrogation of integrin αVβ3 function in endothelial cells.The binding interface of kindlin-2 and ILK involves Asp344/Asp352/Thr356 in kindlin-2 and Arg243/Arg334 in ILK.Low density lipoprotein receptor-related protein 1 couples β1 integrin activation to degradation.Kindlin supports platelet integrin αIIbβ3 activation by interacting with paxillin.Kindlin-2 Association with Rho GDP-Dissociation Inhibitor α Suppresses Rac1 Activation and Podocyte Injury.Structural basis of kindlin-mediated integrin recognition and activation.Kindlin-2 regulates mesenchymal stem cell differentiation through control of YAP1/TAZ.

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Kindlin-2 directly binds actin and regulates integrin outside-in signaling

http://www.wikidata.org/entity/Q36789915

description

2016 nî lūn-bûn

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2016年の論文

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2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

@zh-cn

name

Kindlin-2 directly binds actin and regulates integrin outside-in signaling

@en

type

label

Kindlin-2 directly binds actin and regulates integrin outside-in signaling

@en

prefLabel

Kindlin-2 directly binds actin and regulates integrin outside-in signaling

@en

P1433

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P1433

Journal of Cell Biology

P1476

Kindlin-2 directly binds actin and regulates integrin outside-in signaling

@en

P2093

Edward F Plow

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

Elzbieta Pluskota

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

Julia Vaynberg

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

Jun Qin

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

Kamila Bledzka

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

Katarzyna Bialkowska

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

Khalid Sossey-Alaoui

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

P2860

Kindlin-2 is required for myocyte elongation and is essential for myogenesis

A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading

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

A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans

Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation.

The integrin co-activator Kindlin-3 is expressed and functional in a non-hematopoietic cell, the endothelial cell.

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

A new 82-kD barbed end-capping protein (radixin) localized in the cell-to-cell adherens junction: purification and characterization

Purification of an 80,000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells

P304

97-108

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scholarly article

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10.1083/JCB.201501006

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P433

1

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P478

213

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2016-04-04T00:00:00Z

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P698

27044892

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P932

4828686

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