Lamellipodin promotes actin assembly by clustering Ena/VASP proteins and tethering them to actin filaments. - Wikidata - wikimedia - TriplyDB

Lamellipodin promotes actin assembly by clustering Ena/VASP proteins and tethering them to actin filaments.

Lamellipodin promotes actin assembly by clustering Ena/VASP proteins and tethering them to actin filaments.

http://www.wikidata.org/entity/Q35979105

about

A requirement for filopodia extension toward Slit during Robo-mediated axon repulsion PI(3,4)P2 plays critical roles in the regulation of focal adhesion dynamics of MDA-MB-231 breast cancer cells Brain specific Lamellipodin knockout results in hyperactivity and increased anxiety of mice.A proteomic analysis of LRRK2 binding partners reveals interactions with multiple signaling components of the WNT/PCP pathway.Single Filaments to Reveal the Multiple Flavors of Actin.Recent advances in understanding Listeria monocytogenes infection: the importance of subcellular and physiological context.MRL proteins cooperate with activated Ras in glia to drive distinct oncogenic outcomes.Actin Turnover in Lamellipodial Fragments.WH2 and proline-rich domains of WASP-family proteins collaborate to accelerate actin filament elongation.Mind the (sr)GAP - roles of Slit-Robo GAPs in neurons, brains and beyond.Actin assembly mechanisms at a glance.Distinct VASP tetramers synergize in the processive elongation of individual actin filaments from clustered arrays.CRMP-1 enhances EVL-mediated actin elongation to build lamellipodia and the actin cortex.Deconvolution of subcellular protrusion heterogeneity and the underlying actin regulator dynamics from live cell imaging.

P2860

Q30826775-42987971-2C77-49DA-9029-4AD7D275DC43 Q33738762-123BE227-F678-4441-820F-89EFB1EC8AAD Q33905862-2EF0E393-AEDB-480A-990E-0396B4762A9C Q38697548-772AA177-988A-40D3-B98E-C9D979B4F20A Q38844127-493CA4E5-F31F-46D9-BFDF-33E8B890B648 Q40104712-6C98DC83-69B0-4ABE-A363-357E1CF45E1D Q41193891-E26C7FE2-0FBC-4C7E-8D24-5791E93A9A1F Q46168953-56F5DEF6-6481-4C46-827A-FA2A010DDB83 Q47117180-30F360A0-9C15-4E1F-86BA-A27622B8CF17 Q47447885-7C4DFD25-FE4B-4BA2-86D5-CAB0AA1020C5 Q47612448-A8E506EF-A739-4ECC-9AEA-211CDE5A6238 Q47969128-8AD27E96-5A52-485A-B3EA-B8A603FBDD30 Q48255792-15E248AE-69CE-4BE8-BB95-F574D539DEA0 Q54957473-8781D05B-4E47-403D-851B-DFB34201F5A6

P2860

Lamellipodin promotes actin assembly by clustering Ena/VASP proteins and tethering them to actin filaments.

http://www.wikidata.org/entity/Q35979105

description

2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

2015年论文

@zh

2015年论文

@zh-cn

name

Lamellipodin promotes actin as ...... ering them to actin filaments.

@ast

Lamellipodin promotes actin as ...... ering them to actin filaments.

@en

type

label

Lamellipodin promotes actin as ...... ering them to actin filaments.

@ast

Lamellipodin promotes actin as ...... ering them to actin filaments.

@en

prefLabel

Lamellipodin promotes actin as ...... ering them to actin filaments.

@ast

Lamellipodin promotes actin as ...... ering them to actin filaments.

@en

P1433

Q35979105-C2B4952E-DF51-400A-BEC0-B73D1780C879

P1476

Q35979105-F48469D7-72CB-448C-9F5C-3EBB95D62CD3

P2093

Q35979105-4E228DCB-704B-4E4A-8575-48CAD4DE5E32

Q35979105-64AD3334-19B7-4898-9DD0-CDE78441297F

P2860

Q35979105-0786DFCB-19B0-44ED-BB9C-3A41C85FB97C

Q35979105-0843F9E0-D4F9-400C-B14C-D6D2386CB3E9

Q35979105-0D345740-E1C5-4B3B-A3CA-E4C1DA97DA0C

Q35979105-140E7207-E41B-4077-A83B-C83E90595097

Q35979105-16C53C93-D034-4DE1-9950-C580EBF22733

Q35979105-17E4BD36-B472-4BC7-A1C7-355D38356D71

Q35979105-1D74555A-3ED0-4AEA-BD28-5593A6519DAF

Q35979105-1F731C47-D0B3-4825-A7DB-63184D47834C

Q35979105-21281325-FFAF-43E8-9FAB-ED5E237D6FBE

Q35979105-254E28B2-5A75-4DD0-AB5C-328FBA9B95B8

P31

Q35979105-7B1EFBF3-50DF-4DF5-9B30-29BFE3119265

P356

Q35979105-AA691DCD-AF26-41D5-A165-1A9775227657

P407

Q35979105-CBC16B4C-EEAA-4B09-AD3A-923957E8DD31

P478

Q35979105-E4BB38BB-8C70-43A9-ABD6-9DDF6386744A

P577

Q35979105-9F6B117B-DA70-43C5-A0CD-73D0352727AD

P698

Q35979105-1BD0238C-1DA2-40CA-8B35-BFBE3FE3CBF3

P921

Q35979105-E3B89ED9-E22F-408C-BD70-2B7720854A85

P932

Q35979105-F5A43487-B0D1-4B0D-ABD3-492B3F7582BF

P356

P1433

P1476

Lamellipodin promotes actin as ...... ering them to actin filaments.

@en

P2093

R Dyche Mullins

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

Scott D Hansen

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

P2860

Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP), Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2/3 complex link T cell receptor (TCR) signaling to the actin cytoskeleton

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

Endophilin, Lamellipodin, and Mena cooperate to regulate F-actin-dependent EGF-receptor endocytosis.

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.

Profilin1 regulates PI(3,4)P2 and lamellipodin accumulation at the leading edge thus influencing motility of MDA-MB-231 cells

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

Ena/VASP proteins enhance actin polymerization in the presence of barbed end capping proteins

Emergence of large-scale cell morphology and movement from local actin filament growth dynamics

Structure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly

Structural and functional studies of the Ras-associating and pleckstrin-homology domains of Grb10 and Grb14

P31

scholarly article

P356

10.7554/ELIFE.06585

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

P407

P478

4

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

P577

2015-08-21T00:00:00Z

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

P698

26295568

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

P921

P932

4543927

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