The Diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia. (Q46503087)

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scientific article published on 22 May 2005

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English	The Diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia.	scientific article published on 22 May 2005

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Europe PubMed Central

PubMed publication ID

15908944

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15908944%20AND%20SRC:MED&resulttype=core&format=json

retrieved

12 January 2020

title

The Diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia (English)

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stated in

Europe PubMed Central

PubMed publication ID

15908944

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15908944%20AND%20SRC:MED&resulttype=core&format=json

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12 January 2020

author

Till Bretschneider

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2

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Europe PubMed Central

PubMed publication ID

15908944

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15908944%20AND%20SRC:MED&resulttype=core&format=json

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12 January 2020

author name string

Antje Schirenbeck

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1

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Europe PubMed Central

PubMed publication ID

15908944

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15908944%20AND%20SRC:MED&resulttype=core&format=json

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12 January 2020

Rajesh Arasada

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3

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Europe PubMed Central

PubMed publication ID

15908944

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15908944%20AND%20SRC:MED&resulttype=core&format=json

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12 January 2020

Michael Schleicher

series ordinal

4

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Europe PubMed Central

PubMed publication ID

15908944

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15908944%20AND%20SRC:MED&resulttype=core&format=json

retrieved

12 January 2020

Jan Faix

series ordinal

5

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stated in

Europe PubMed Central

PubMed publication ID

15908944

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15908944%20AND%20SRC:MED&resulttype=core&format=json

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12 January 2020

publication date

22 May 2005

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Europe PubMed Central

PubMed publication ID

15908944

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15908944%20AND%20SRC:MED&resulttype=core&format=json

retrieved

12 January 2020

published in

Nature Cell Biology

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stated in

Europe PubMed Central

PubMed publication ID

15908944

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15908944%20AND%20SRC:MED&resulttype=core&format=json

retrieved

12 January 2020

volume

7

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Europe PubMed Central

PubMed publication ID

15908944

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15908944%20AND%20SRC:MED&resulttype=core&format=json

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12 January 2020

issue

6

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Europe PubMed Central

PubMed publication ID

15908944

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15908944%20AND%20SRC:MED&resulttype=core&format=json

retrieved

12 January 2020

page(s)

619-625

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Europe PubMed Central

PubMed publication ID

15908944

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15908944%20AND%20SRC:MED&resulttype=core&format=json

retrieved

12 January 2020

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The formins: active scaffolds that remodel the cytoskeleton

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FH3, a domain found in formins, targets the fission yeast formin Fus1 to the projection tip during conjugation

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21 January 2018

Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain

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21 January 2018

The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization

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21 January 2018

Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture

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21 January 2018

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p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin

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The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin

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Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast

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Disruption of the Diaphanous-related formin Drf1 gene encoding mDia1 reveals a role for Drf3 as an effector for Cdc42

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The Rho family GTPase Rif induces filopodia through mDia2.

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Membrane tether formation from blebbing cells

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Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis

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21 January 2018

Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces

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ForC, a novel type of formin family protein lacking an FH1 domain, is involved in multicellular development in Dictyostelium discoideum

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Dictyostelium amoebae that lack G-actin-sequestering profilins show defects in F-actin content, cytokinesis, and development.

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Recruitment of cortexillin into the cleavage furrow is controlled by Rac1 and IQGAP-related proteins

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The lamellipodium: where motility begins

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Requirement of a vasodilator-stimulated phosphoprotein family member for cell adhesion, the formation of filopodia, and chemotaxis in dictyostelium

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Mechanism of filopodia initiation by reorganization of a dendritic network

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Critical role of Ena/VASP proteins for filopodia formation in neurons and in function downstream of netrin-1.

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Capping protein levels influence actin assembly and cell motility in dictyostelium

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A transformation vector for dictyostelium discoideum with a new selectable marker bsr.

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DGAP1, a homologue of rasGTPase activating proteins that controls growth, cytokinesis, and development in Dictyostelium discoideum

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Cytokinesis mediated through the recruitment of cortexillins into the cleavage furrow

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Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains

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An actin nucleation mechanism mediated by Bni1 and profilin

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based on heuristic

inferred from DOI database lookup

Characterization of actin- and lipid-binding domains in severin, a Ca(2+)-dependent F-actin fragmenting protein

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based on heuristic

inferred from DOI database lookup

Identifiers

DOI

10.1038/NCB1266

1 reference

stated in

Europe PubMed Central

PubMed publication ID

15908944

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15908944%20AND%20SRC:MED&resulttype=core&format=json

retrieved

12 January 2020

PubMed publication ID

15908944

1 reference

stated in

Europe PubMed Central

PubMed publication ID

15908944

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15908944%20AND%20SRC:MED&resulttype=core&format=json

retrieved

12 January 2020

ResearchGate publication ID

7832551

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