The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition
about
Rab13 regulates neurite outgrowth in PC12 cells through its effector protein, JRAB/MICAL-L2Homozygous loss of DIAPH1 is a novel cause of microcephaly in humansMutations in the formin gene INF2 cause focal segmental glomerulosclerosisProtein-tyrosine kinase and GTPase signals cooperate to phosphorylate and activate Wiskott-Aldrich syndrome protein (WASP)/neuronal WASPBiochemical characterization of the Rho GTPase-regulated actin assembly by diaphanous-related formins, mDia1 and Daam1, in plateletsThe mammalian formin FHOD1 is activated through phosphorylation by ROCK and mediates thrombin-induced stress fibre formation in endothelial cellsInteraction of the RAGE cytoplasmic domain with diaphanous-1 is required for ligand-stimulated cellular migration through activation of Rac1 and Cdc42PKD2 interacts and co-localizes with mDia1 to mitotic spindles of dividing cells: role of mDia1 IN PKD2 localization to mitotic spindlesA conserved mechanism for Bni1- and mDia1-induced actin assembly and dual regulation of Bni1 by Bud6 and profilinThe transcriptional activity of Sox9 in chondrocytes is regulated by RhoA signaling and actin polymerizationMechanism of activation of the Formin protein Daam1The yeast actin cytoskeleton: from cellular function to biochemical mechanismThe Rho-mDia1 pathway regulates cell polarity and focal adhesion turnover in migrating cells through mobilizing Apc and c-SrcAutoinhibition regulates cellular localization and actin assembly activity of the diaphanous-related formins FRLalpha and mDia1.Formin homology 2 domains occur in multiple contexts in angiospermsA comparative sequence analysis reveals a common GBD/FH3-FH1-FH2-DAD architecture in formins from Dictyostelium, fungi and metazoaThe final cut: cell polarity meets cytokinesis at the bud neck in S. cerevisiaeCapping protein regulators fine-tune actin assembly dynamicsFormins at a glanceThe Actin Nucleator Cobl Is Controlled by Calcium and CalmodulinDiaphanous-related formin 2 and profilin I are required for gastrulation cell movementsCrystal structure of human DAAM1 formin homology 2 domainSpecificity of Interactions between mDia Isoforms and Rho ProteinsCrystal Structure of a Complex between Amino and Carboxy Terminal Fragments of mDia1: Insights into Autoinhibition of Diaphanous-Related ForminsCrystal Structure of the Formin mDia1 in Autoinhibited ConformationCrystal Structure of a Coiled-Coil Domain from Human ROCK IThe F-BAR protein Hof1 tunes formin activity to sculpt actin cables during polarized growth.Cdc42p regulation of the yeast formin Bni1p mediated by the effector Gic2p.Displacement of formins from growing barbed ends by bud14 is critical for actin cable architecture and function.Stable and dynamic axes of polarity use distinct formin isoforms in budding yeastDifferential activities and regulation of Saccharomyces cerevisiae formin proteins Bni1 and Bnr1 by Bud6.Ligand-induced activation of a formin-NPF pair leads to collaborative actin nucleationControl of Formin Distribution and Actin Cable Assembly by the E3 Ubiquitin Ligases Dma1 and Dma2.Role of RhoA, mDia, and ROCK in cell shape-dependent control of the Skp2-p27kip1 pathway and the G1/S transitionBiochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1Phylogenetic analysis of the formin homology 2 domainOrigins and evolution of the formin multigene family that is involved in the formation of actin filamentsOligomerization of the diaphanous-related formin FHOD1 requires a coiled-coil motif critical for its cytoskeletal and transcriptional activitiesThere is more than one way to model an elephant. Experiment-driven modeling of the actin cytoskeletonMammalian formin-1 participates in adherens junctions and polymerization of linear actin cables
P2860
Q22001528-E9FED4D3-B78E-4B05-81C8-BD5CCF7845E1Q23778306-D3DE0B83-90BC-4143-B8EB-F9DA79C7ABC3Q24292947-6E7C1EBA-FDD0-4C6B-BA98-1BC19172F587Q24295390-3802BED7-B987-4451-9A26-6558380FE244Q24307657-2132A1BC-B42F-4E7E-B326-CE3EEA516B65Q24309382-73F3C876-C9C6-407F-9AA1-D3D22F0629E0Q24323192-3CBBE25B-7C73-4269-A8C4-68618C5AC083Q24338591-4FA6AF71-DB69-49FC-9741-1C1F2F96E0FAQ24624729-30A588D1-698D-4CB6-B388-29A517209020Q24644717-6F7A118D-AA84-406D-A538-0B839B52BD32Q24657453-3DCF0EDE-5510-4F0A-8A66-1BA785A23F5AQ24669945-5FA42DEB-C279-4815-BEBF-76DC41971522Q24670372-AF4B8B01-E55A-4DD1-B9B6-7F3E1EE4B884Q24682983-61CE0DA5-D88D-4F91-8009-BAB88C4F6A0AQ24797933-33BA18B0-9F7F-4D9E-9B63-3D87E08FDF08Q24806163-28026308-C4ED-4911-AB66-DA7B6A61750AQ26753023-D14C39C1-B7FC-4521-BEFF-8C19A6B15AE4Q27006034-327BBB63-74CF-4E3E-9B43-F6527C43B00AQ27009102-FA8F35D4-7E7A-4A66-897F-A3F6944507D5Q27347223-24D5C2A9-F110-45DF-9A20-D217D3F87DA5Q27438166-450B57A9-5AA5-4B6D-8FA3-F0298F02ACF2Q27648970-4D0B267B-4F89-46D3-9A62-6582747F1DAEQ27652343-AC114544-896A-4899-B35B-4BF7F3DA2648Q27664937-11B49788-CE17-4453-B126-609D7DA9BE60Q27664938-76F1B198-419E-4C82-B2B9-FF13B3A59BBBQ27667345-EE67BFFB-29B9-4A99-BC0C-CDFC128EB91EQ27929842-F3D7327D-4E2B-4EF0-A101-CE888052F45EQ27931032-A20E887F-2158-4129-81B7-E0F3E51750ADQ27932520-3B5AA151-9F6F-46FE-9622-D7B7B6F517B1Q27935764-64D817EB-1C69-4EE9-A075-79AB913D152AQ27937400-F364110D-C809-452E-B1B0-54DBE9895024Q27938894-4B498471-CD17-449B-8FAD-C5E934952696Q27939302-6CE935F0-003C-40DE-8FA5-C2C3230123FCQ28257507-F6D9547E-DA46-4201-9813-18D0C7902274Q28287470-BED525D8-1BF2-4193-87C7-CB350F209433Q28290186-726F281B-0CDA-408E-9DF5-D2F9814D5F41Q28296265-BC0D792E-D380-4B5A-A249-65078ABDF9FCQ28301897-C2551CC0-2F3D-4A3F-AD9C-DC8F3E601D54Q28394155-BE9832E7-5BE7-411D-889E-717B55C2A21CQ28507974-22353E64-68E8-45A8-98DF-3B15BBC8DC64
P2860
The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition
description
2003 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2003
@ast
im August 2003 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2003/08/05)
@sk
vědecký článek publikovaný v roce 2003
@cs
wetenschappelijk artikel (gepubliceerd op 2003/08/05)
@nl
наукова стаття, опублікована в серпні 2003
@uk
مقالة علمية (نشرت في 5-8-2003)
@ar
name
The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition
@ast
The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition
@en
The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition
@nl
type
label
The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition
@ast
The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition
@en
The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition
@nl
prefLabel
The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition
@ast
The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition
@en
The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition
@nl
P3181
P1433
P1476
The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition
@en
P2093
Henry N. Higgs
P304
P3181
P356
10.1016/S0960-9822(03)00540-2
P407
P577
2003-08-05T00:00:00Z