Mouse A6/twinfilin is an actin monomer-binding protein that localizes to the regions of rapid actin dynamics
about
Congenital sensorineural deafness in dalmatian dogs associated with quantitative trait lociMammals have two twinfilin isoforms whose subcellular localizations and tissue distributions are differentially regulatedThe two ADF-H domains of twinfilin play functionally distinct roles in interactions with actin monomers.The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamicsCyclase-associated protein 1 (CAP1) promotes cofilin-induced actin dynamics in mammalian nonmuscle cells.The low-affinity receptor for neurotrophins p75NTR plays a key role for satellite cell function in muscle repair acting via RhoAStress fibers are generated by two distinct actin assembly mechanisms in motile cellsPhosphoregDB: the tissue and sub-cellular distribution of mammalian protein kinases and phosphatases.Structural conservation between the actin monomer-binding sites of twinfilin and actin-depolymerizing factor (ADF)/cofilinHigh-speed depolymerization at actin filament ends jointly catalysed by Twinfilin and Srv2/CAP.Twinfilin is an actin-filament-severing protein and promotes rapid turnover of actin structures in vivo.Different localizations and cellular behaviors of leiomodin and tropomodulin in mature cardiomyocyte sarcomeresActin-depolymerizing factor and cofilin-1 play overlapping roles in promoting rapid F-actin depolymerization in mammalian nonmuscle cells.Mouse MIM, a tissue-specific regulator of cytoskeletal dynamics, interacts with ATP-actin monomers through its C-terminal WH2 domainInteractions with PIP2, ADP-actin monomers, and capping protein regulate the activity and localization of yeast twinfilinArginylation regulates intracellular actin polymer level by modulating actin properties and binding of capping and severing proteins.Mammalian twinfilin sequesters ADP-G-actin and caps filament barbed ends: implications in motilityA genomic and proteomic analysis of activation of the human neutrophil by lipopolysaccharide and its mediation by p38 mitogen-activated protein kinase.MyosinVIIa interacts with Twinfilin-2 at the tips of mechanosensory stereocilia in the inner ear.Structural and functional dissection of the Abp1 ADFH actin-binding domain reveals versatile in vivo adapter functions.Twinfilin-2a is dispensable for mouse developmentCofilin-2 controls actin filament length in muscle sarcomeres.Actin and endocytosis in budding yeast.Genomic profiling of microRNA and messenger RNA reveals deregulated microRNA expression in prostate cancer.Actin-depolymerizing factor homology domain: a conserved fold performing diverse roles in cytoskeletal dynamics.Generation of contractile actomyosin bundles depends on mechanosensitive actin filament assembly and disassembly.Missing-in-metastasis and IRSp53 deform PI(4,5)P2-rich membranes by an inverse BAR domain-like mechanism.Biological role and structural mechanism of twinfilin-capping protein interaction.p116Rip is a novel filamentous actin-binding protein.Drebrin-like protein DBN-1 is a sarcomere component that stabilizes actin filaments during muscle contraction.A twinfilin-like protein coordinates karyokinesis by influencing mitotic spindle elongation and DNA replication in Leishmania.Twinfilin is required for actin-dependent developmental processes in Drosophila.Rac1 pathway mediates stretch response in pulmonary alveolar epithelial cells.Defining mechanisms of actin polymerization and depolymerization during dendritic spine morphogenesis.Actin-binding proteins: how to reveal the conformational changes.Molecular mechanism for inhibition of twinfilin by phosphoinositides.Phosphorylation of the LFA-1 Integrin β2-Chain on Thr-758 Leads to Adhesion, Rac-1/Cdc42 Activation, and Stimulation of CD69 Expression in Human T Cells
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Q21559534-E1E34BBA-2F1A-4A17-B6FA-E14D63DFF37BQ24305185-7CDD835E-2012-4E18-AC46-B2494D6001DAQ24537150-A54E6CC1-E60F-4FEF-AE11-3A9E29E83603Q24555040-31CA8BAA-F15A-4197-A28A-8F9D8106A98DQ24564899-2CB297D8-5CCB-4D38-8411-37D6F664E791Q24655928-03969110-48B9-4753-A7A2-C37AE1B93E30Q24683694-EBB71EA3-3C2C-4EC2-9C1D-0D0397A434ABQ25255571-0C6D4EFF-04FE-4E49-901D-A79F2173A030Q27639578-06A6CFDA-A8E7-4DF9-B859-938AE5F5C9A6Q27935278-00097F59-448A-42F9-9884-164D76A3F9A4Q27936623-740DF981-EF55-4BEF-B996-ACEAD0A9C0A6Q28119062-C50AE02A-2F6C-4478-A7A5-4D525354242CQ28506999-9CC5F986-47A7-405B-835E-3DA91F2F236BQ28507602-F4DA1FEE-F177-4496-A3BB-08C4F37D275CQ28589327-26F33CA7-0AD5-4B67-BE9C-7514AD891FA0Q30435749-E06D4DEE-1DA7-4342-9EC5-81228DC3E08DQ30477108-927D1796-3482-48FE-B142-C0825AC99438Q30831317-D8E1C730-CD9A-4B2D-9D9C-4233062CD77CQ33506085-3F1D468C-FD5A-4375-92F5-4428D76FC3B5Q33877002-99B70EEB-F680-4146-8ABF-197E9A6704D9Q34005387-24F2B09E-93B2-4378-8BA8-96C65A5EC6BEQ34469143-D6CE7FC6-1438-4803-8DC0-EB4390360401Q34667847-16FE0B57-DCEC-4D42-A304-A5A04189EAE9Q34803786-BCAD0222-E5CB-4E77-8D64-FDDBB4F4093AQ37919427-E3008B83-73F1-4923-A8AB-3AD62896EA4BQ38813076-5C396E92-C108-46D5-98F0-723049ABE4C0Q39734937-FAD3098F-B692-460B-AE5A-813F7461C8CDQ39958910-248B7C20-AA3B-4849-BBCB-88B74081B70CQ40649738-320A325D-CA88-4DE8-A43C-10EF0EC5CA71Q40767225-DDDA7A04-B927-4AF7-9F2B-F8FFC67CA5E8Q42486828-910CB1CA-DE5C-4EFF-95C6-4776B741208CQ42860122-4BB334DD-69AB-4152-A2F6-C26F7BAFB275Q43069129-84F76E68-5C69-4567-9EF3-CEA4E09D3BF2Q43107811-1C9ED474-A4D0-4F69-B301-01D7E508F4C7Q46396672-C05B0FF1-C15A-4547-B561-2BD79546A7FDQ50099981-2865B596-5E7C-47BE-8AF0-B05F56A5B104Q58199161-7B0DF0CB-EB11-44BC-A335-47BCEBCA5C05
P2860
Mouse A6/twinfilin is an actin monomer-binding protein that localizes to the regions of rapid actin dynamics
description
2000 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի մարտին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2000
@ast
im März 2000 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2000/03/01)
@sk
vědecký článek publikovaný v roce 2000
@cs
wetenschappelijk artikel (gepubliceerd op 2000/03/01)
@nl
наукова стаття, опублікована в березні 2000
@uk
مقالة علمية (نشرت في مارس 2000)
@ar
name
Mouse A6/twinfilin is an actin ...... egions of rapid actin dynamics
@ast
Mouse A6/twinfilin is an actin ...... egions of rapid actin dynamics
@en
Mouse A6/twinfilin is an actin ...... egions of rapid actin dynamics
@nl
type
label
Mouse A6/twinfilin is an actin ...... egions of rapid actin dynamics
@ast
Mouse A6/twinfilin is an actin ...... egions of rapid actin dynamics
@en
Mouse A6/twinfilin is an actin ...... egions of rapid actin dynamics
@nl
prefLabel
Mouse A6/twinfilin is an actin ...... egions of rapid actin dynamics
@ast
Mouse A6/twinfilin is an actin ...... egions of rapid actin dynamics
@en
Mouse A6/twinfilin is an actin ...... egions of rapid actin dynamics
@nl
P2093
P2860
P1476
Mouse A6/twinfilin is an actin ...... egions of rapid actin dynamics
@en
P2093
J. Peränen
M. Vartiainen
P. Auvinen
P. J. Ojala
P. Lappalainen
P2860
P304
P356
10.1128/MCB.20.5.1772-1783.2000
P407
P577
2000-03-01T00:00:00Z