Phosphorylation of the Arp2/3 complex is necessary to nucleate actin filaments
about
Post-translational modification-regulated leukocyte adhesion and migrationRegulators of Actin Dynamics in Gastrointestinal Tract TumorsIntracellular Theileria annulata promote invasive cell motility through kinase regulation of the host actin cytoskeletonCrystal structure and putative substrate identification for the Entamoeba histolytica low molecular weight tyrosine phosphatase.Phosphorylation of the Arp2 subunit relieves auto-inhibitory interactions for Arp2/3 complex activationCofilin Activation Is Temporally Associated with the Cessation of Growth in the Developing HippocampusRole and structural mechanism of WASP-triggered conformational changes in branched actin filament nucleation by Arp2/3 complexA nucleator arms race: cellular control of actin assemblyStructure and dynamics of an Arp2/3 complex-independent component of the lamellipodial actin network.Protein kinase C activation decreases peripheral actin network density and increases central nonmuscle myosin II contractility in neuronal growth conesThe Nck-interacting kinase NIK increases Arp2/3 complex activity by phosphorylating the Arp2 subunitEndothelial cell-specific chemotaxis receptor (ecscr) promotes angioblast migration during vasculogenesis and enhances VEGF receptor sensitivityThe exocyst complex in exocytosis and cell migration.The Legionella Kinase LegK2 Targets the ARP2/3 Complex To Inhibit Actin Nucleation on Phagosomes and Allow Bacterial Evasion of the Late Endocytic PathwayDrosophila Src regulates anisotropic apical surface growth to control epithelial tube sizePhosphorylation of actin-related protein 2 (Arp2) is required for normal development and cAMP chemotaxis in Dictyostelium.Small molecules CK-666 and CK-869 inhibit actin-related protein 2/3 complex by blocking an activating conformational change.Capping protein increases the rate of actin-based motility by promoting filament nucleation by the Arp2/3 complexWiskott-Aldrich syndrome protein is an effector of Kit signaling.Accelerators, Brakes, and Gears of Actin Dynamics in Dendritic Spines.Quantitative profiling of spreading-coupled protein tyrosine phosphorylation in migratory cells.Purification of native Arp2/3 complex from bovine thymus.Dose-dependent effects of prostaglandin E2 in macrophage adhesion and migration.Arp2/3 phosphorylation kickstarts cells.The Arp2/3 Regulatory System and Its Deregulation in Cancer.Upregulation of Arp2 expression is associated with the prognosis and prediction of lymph node metastasis in bladder urothelial carcinoma.RhoGAP domain-containing fusions and PPAPDC1A fusions are recurrent and prognostic in diffuse gastric cancerPhosphorylation of Arp2 is not essential for Arp2/3 complex activity in fission yeast
P2860
Q26753208-C030B0F1-1AFF-4608-87B8-BEC6D5177557Q26783246-502993EF-4C57-4AA3-B795-B46352B28878Q27329799-6A3D7FAD-5BF2-4153-87BD-7AF4F22A0683Q27681787-ECB852FE-29E8-49BD-A78C-16AECF2BA1B4Q28478076-D88E7386-78B5-4769-8195-B3D0C8E48001Q28575675-1C2330E2-9B83-4B31-9F2E-9D3C4F0FAAF6Q28830519-EBD0D6F4-7A47-4812-AFC5-AD4AA2FF589BQ29616146-8200A7CD-B6B7-49AE-B71C-2C228BECA964Q30495839-24B75182-0F04-4526-8D93-979E0D746029Q30547068-F4B54095-14E0-4F70-9487-493F41A0522BQ30616543-0B75B77D-F403-4D41-B916-BFB05B295327Q33896702-6A083BC6-BD11-4AC7-BC84-992A119E94B1Q34224053-A5ADD599-3160-42F2-9EEA-F2BA38DEB31FQ35620178-2164D644-0A88-4137-90B2-FB2B018EC043Q35931443-953F4CB4-E5AC-4580-9D54-CEC8FEF7DED9Q36561998-793BD11B-292F-4CB0-86A8-0A80846477CAQ36935603-CEECEDFC-05CD-4145-A0FA-FEB44CC92602Q36957162-595ABF89-3E8B-4030-8622-61C934640338Q37373019-D1191BF9-9619-4872-A774-AFF52E40EFCAQ37750482-D56461D6-0CEA-43F7-A75B-09E7D5BA4E99Q38828489-DB2C0C6D-8E7C-431C-9F22-F783DB353B68Q38880738-64FD0219-AE24-4221-AC67-09367D3098BAQ40885179-7FF701AC-D119-45C5-9DE0-D02B31904CFEQ45997324-0F352BA9-50F8-4F20-9A7F-FFB57C5DABD5Q47322418-75AEB7E0-2F23-4543-9F10-3E96127DBAFCQ52338851-23EFA661-67AD-4EF9-833B-45EE9D487D15Q58561130-890F402D-EF4A-43EB-9876-7D1D573DAD99Q59129036-F464FF16-FA12-4F47-8F9E-1B426E7B5B23
P2860
Phosphorylation of the Arp2/3 complex is necessary to nucleate actin filaments
description
2008 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2008
@ast
im August 2008 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2008/08/25)
@sk
vědecký článek publikovaný v roce 2008
@cs
wetenschappelijk artikel (gepubliceerd op 2008/08/25)
@nl
наукова стаття, опублікована в серпні 2008
@uk
مقالة علمية (نشرت في 25-8-2008)
@ar
name
Phosphorylation of the Arp2/3 complex is necessary to nucleate actin filaments
@ast
Phosphorylation of the Arp2/3 complex is necessary to nucleate actin filaments
@en
Phosphorylation of the Arp2/3 complex is necessary to nucleate actin filaments
@nl
type
label
Phosphorylation of the Arp2/3 complex is necessary to nucleate actin filaments
@ast
Phosphorylation of the Arp2/3 complex is necessary to nucleate actin filaments
@en
Phosphorylation of the Arp2/3 complex is necessary to nucleate actin filaments
@nl
prefLabel
Phosphorylation of the Arp2/3 complex is necessary to nucleate actin filaments
@ast
Phosphorylation of the Arp2/3 complex is necessary to nucleate actin filaments
@en
Phosphorylation of the Arp2/3 complex is necessary to nucleate actin filaments
@nl
P2093
P2860
P3181
P356
P1476
Phosphorylation of the Arp2/3 complex is necessary to nucleate actin filaments
@en
P2093
Diane L. Barber
Janet H. Iwasa
Lawrence L. LeClaire
R. Dyche Mullins
P2860
P304
P3181
P356
10.1083/JCB.200802145
P407
P577
2008-08-25T00:00:00Z