Distinct VASP tetramers synergize in the processive elongation of individual actin filaments from clustered arrays.

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WH2 and proline-rich domains of WASP-family proteins collaborate to accelerate actin filament elongation.Actin assembly mechanisms at a glance.Computational modeling highlights the role of the disordered Formin Homology 1 domain in profilin-actin transfer.

P2860

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Distinct VASP tetramers synergize in the processive elongation of individual actin filaments from clustered arrays.

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http://www.wikidata.org/entity/Q47969128

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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2017年學術文章

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name

Distinct VASP tetramers synerg ...... laments from clustered arrays.

@en

Distinct VASP tetramers synerg ...... laments from clustered arrays.

@nl

type

Item

label

Distinct VASP tetramers synerg ...... laments from clustered arrays.

@en

Distinct VASP tetramers synerg ...... laments from clustered arrays.

@nl

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Distinct VASP tetramers synerg ...... laments from clustered arrays.

@en

Distinct VASP tetramers synerg ...... laments from clustered arrays.

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P1476

Distinct VASP tetramers synerg ...... laments from clustered arrays.

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P2093

Dmitry S Ushakov

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

Jan Faix

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

Moritz Winterhoff

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

Richard B Dickinson

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

Stefan Brühmann

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

P2860

Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex

Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP.

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

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

Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity

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

Actoclampin (+)-end-tracking motors: How the pursuit of profilin's role(s) in actin-based motility twice led to the discovery of how cells crawl

A de novo peptide hexamer with a mutable channel

A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants

Structure of the profilin-poly-L-proline complex involved in morphogenesis and cytoskeletal regulation

P304

E5815-E5824

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scholarly article

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10.1073/PNAS.1703145114

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English

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P478

114

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P50

Ute Curth

P577

2017-06-30T00:00:00Z

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P698

28667124

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P921

actin filament

P932

5530675

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

Distinct VASP tetramers synergize in the processive elongation of individual actin filaments from clustered arrays.

about

P2860

P2860

Distinct VASP tetramers synergize in the processive elongation of individual actin filaments from clustered arrays.

description

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type

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P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932