The interaction of proline-rich ligands with profilin probed with an enzyme-linked immunosorbent assay.

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Differential remodeling of actin cytoskeleton architecture by profilin isoforms leads to distinct effects on cell migration and invasion

P2860

Q24303907-9D758BB6-F0F4-406F-BC7A-14E3C8A35695

P2860

The interaction of proline-rich ligands with profilin probed with an enzyme-linked immunosorbent assay.

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http://www.wikidata.org/entity/Q39858641

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2009 nî lūn-bûn

@nan

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 interaction of proline-ric ...... me-linked immunosorbent assay.

@en

The interaction of proline-ric ...... me-linked immunosorbent assay.

@nl

type

Item

label

The interaction of proline-ric ...... me-linked immunosorbent assay.

@en

The interaction of proline-ric ...... me-linked immunosorbent assay.

@nl

prefLabel

The interaction of proline-ric ...... me-linked immunosorbent assay.

@en

The interaction of proline-ric ...... me-linked immunosorbent assay.

@nl

P1476

The interaction of proline-ric ...... me-linked immunosorbent assay.

@en

P2093

Anja Lambrechts

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

Christophe Ampe

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

Joël Vandekerckhove

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

Sylvie Veniere

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

P2860

In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly

Profilin II is alternatively spliced, resulting in profilin isoforms that are differentially expressed and have distinct biochemical properties

The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat

Clustering of VASP actively drives processive, WH2 domain-mediated actin filament elongation.

RhoA/ROCK regulation of neuritogenesis via profilin IIa-mediated control of actin stability

Profilin binds proline-rich ligands in two distinct amide backbone orientations

High-resolution structural analysis of mammalian profilin 2a complex formation with two physiological ligands: the formin homology 1 domain of mDia1 and the proline-rich domain of VASP

Bni1p and Bnr1p: downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae.

Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin

cAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP relative, regulates its interaction with actin and SH3 domains

P304

350-359

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P31

scholarly article

P356

10.1177/1087057109332594

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P478

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

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2009-04-01T00:00:00Z

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24378763

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P698

19403918

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

The interaction of proline-rich ligands with profilin probed with an enzyme-linked immunosorbent assay.

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P2860

P2860

The interaction of proline-rich ligands with profilin probed with an enzyme-linked immunosorbent assay.

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P1433

P1476

P2093

P2860

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P356

P433

P478

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P5875

P698

P356

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P2860

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P433

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P5875

P698