Ena/VASP Enabled is a highly processive actin polymerase tailored to self-assemble parallel-bundled F-actin networks with Fascin

The Formin Daam1 and Fascin Directly Collaborate to Promote Filopodia Formation

(2013) Richa Jaiswal et al.   CURRENT BIOLOGY

CDC42 switches IRSp53 from inhibition of actin growth to elongation by clustering of VASP

(2013) Andrea Disanza et al.   EMBO JOURNAL

Molecular mechanism of Ena/VASP-mediated actin-filament elongation

(2011) Dennis Breitsprecher et al.   EMBO JOURNAL

Filopodia initiation

(2011) Changsong Yang et al.   Cell Adhesion & Migration

VASP is a processive actin polymerase that requires monomeric actin for barbed end association

(2010) Scott D. Hansen et al.   JOURNAL OF CELL BIOLOGY

A nucleator arms race: cellular control of actin assembly

(2010) Kenneth G. Campellone et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

Actin filament nucleation and elongation factors – structure–function relationships

(2009) Roberto Dominguez   CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY

Actin nucleation and elongation factors: mechanisms and interplay

(2009) Melissa A Chesarone et al.   CURRENT OPINION IN CELL BIOLOGY

Filopodia: Complex models for simple rods

(2009) Jan Faix et al.   INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY

Ena/VASP: towards resolving a pointed controversy at the barbed end

(2009) J. E. Bear et al.   JOURNAL OF CELL SCIENCE

Actin, a Central Player in Cell Shape and Movement

(2009) T. D. Pollard et al.   SCIENCE

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

(2008) Dennis Breitsprecher et al.   EMBO JOURNAL

Ena/VASP Proteins Capture Actin Filament Barbed Ends

(2008) Lejla Pasic et al.   JOURNAL OF BIOLOGICAL CHEMISTRY