Mutations in Drosophila enabled and rescue by human vasodilator-stimulated phosphoprotein (VASP) indicate important functional roles for Ena/VASP homology domain 1 (EVH1) and EVH2 domains (Q36898959)

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scientific article published on August 1998

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English	Mutations in Drosophila enabled and rescue by human vasodilator-stimulated phosphoprotein (VASP) indicate important functional roles for Ena/VASP homology domain 1 (EVH1) and EVH2 domains	scientific article published on August 1998

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13 November 2019

Mutations in Drosophila enabled and rescue by human vasodilator-stimulated phosphoprotein (VASP) indicate important functional roles for Ena/VASP homology domain 1 (EVH1) and EVH2 domains (English)

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13 November 2019

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S M Ahern-Djamali

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A R Comer

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C Bachmann

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A S Kastenmeier

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S K Reddy

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M C Beckerle

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U Walter

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1 August 1998

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Molecular Biology of the Cell

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13 November 2019

2157-2171

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13 November 2019

Phosphorylation of Enabled by the Drosophila Abelson tyrosine kinase regulates the in vivo function and protein-protein interactions of Enabled

1 reference

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A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family

1 reference

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Mena, a relative of VASP and Drosophila Enabled, is implicated in the control of microfilament dynamics

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Molecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP

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1 reference

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The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins

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Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein)

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12 December 2020

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10.1091/MBC.9.8.2157

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13 November 2019

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