Tropomodulin binds two tropomyosins: a novel model for actin filament capping.
about
Integration of troponin I phosphorylation with cardiac regulatory networksTropomodulin capping of actin filaments in striated muscle development and physiologyMechanism of actin filament pointed-end capping by tropomodulinHow Leiomodin and Tropomodulin use a common fold for different actin assembly functions.Knockout of Lmod2 results in shorter thin filaments followed by dilated cardiomyopathy and juvenile lethalityTropomodulin isoforms regulate thin filament pointed-end capping and skeletal muscle physiologyDifferential actin-regulatory activities of Tropomodulin1 and Tropomodulin3 with diverse tropomyosin and actin isoforms.Functional effects of mutations in the tropomyosin-binding sites of tropomodulin1 and tropomodulin3.Role of tropomodulin's leucine rich repeat domain in the formation of neurite-like processesPhosphorylation of tropomodulin1 contributes to the regulation of actin filament architecture in cardiac muscle.Mammalian tropomodulins nucleate actin polymerization via their actin monomer binding and filament pointed end-capping activities.Identification of residues within tropomodulin-1 responsible for its localization at the pointed ends of the actin filaments in cardiac myocytes.Interior decoration: tropomyosin in actin dynamics and cell migration.Leiomodin 3 and tropomodulin 4 have overlapping functions during skeletal myofibrillogenesis.Molecular basis of tropomyosin binding to tropomodulin, an actin-capping protein.Alteration of tropomyosin-binding properties of tropomodulin-1 affects its capping ability and localization in skeletal myocytes.Tropomodulins and tropomyosins: working as a teamTropomodulin isoforms utilize specific binding functions to modulate dendrite development.The N-terminal tropomyosin- and actin-binding sites are important for leiomodin 2's function.Localization of the binding interface between leiomodin-2 and α-tropomyosin.Tropomyosin-binding properties modulate competition between tropomodulin isoforms.Tropomodulins: pointed-end capping proteins that regulate actin filament architecture in diverse cell types.The cardiomyopathy-associated K15N mutation in tropomyosin alters actin filament pointed end dynamics.Actin regulation by tropomodulin and tropomyosin in neuronal morphogenesis and function.Tropomodulins and Leiomodins: Actin Pointed End Caps and Nucleators in Muscles.Tropomyosin Structure, Function, and Interactions: A Dynamic Regulator.Mutations changing tropomodulin affinity for tropomyosin alter neurite formation and extension.Leiomodin-2 is an antagonist of tropomodulin-1 at the pointed end of the thin filaments in cardiac muscle.Stabilization of F-actin by tropomyosin isoforms regulates the morphology and mechanical behavior of red blood cells.Characterizing interaction forces between actin and proteins of the tropomodulin family reveals the presence of the N-terminal actin-binding site in leiomodin.Tropomodulin's Actin-Binding Abilities Are Required to Modulate Dendrite Development
P2860
Q26852120-B947431A-8565-4C96-A93A-DB487FF72080Q26852179-2626BEE7-4281-4666-9BF5-CC6BD5864EFFQ27684814-49DDC4FC-F277-4C84-A6AA-C9649DA671FDQ28119066-9F58A841-ACC2-41C8-8865-1B3CC50A74BFQ28513164-AD96C0E5-10A2-4BF2-8BA9-6052AA1E47FCQ28589016-A2FB5C45-A25A-46AE-895C-61404DB94E0DQ30405662-FE04B30E-7D93-4477-8DB0-50D304EA0090Q30407577-0999DA9E-8E84-4BF1-8C2B-9143726C0456Q33598667-81DCCDD6-1EE7-41D0-9813-E9AE4FDDB567Q34072663-C6C34D0D-BDAA-4631-8CEE-115053B8E108Q34236824-03770CFF-0D73-4F25-8FE4-37D3F628CAC1Q34503247-9AD9BD1C-4336-482F-BD51-0B44C3025285Q34891285-C9121942-D613-41C8-BC8A-2FC62020D0C6Q34961638-E510DD48-622D-4840-91F8-AE8D28911338Q36259368-F5175BB8-538D-40A2-A134-9D894EDB4541Q36620808-42EA92E3-521B-4B68-8A25-8CFBAB278EFBQ36640510-E9A4BFEE-0C9D-4C49-9520-16CA55B26EFFQ37026817-31333CA1-6C04-4C77-82A5-442168337F09Q37175795-A42BAAC2-3931-412D-8295-4D6ECBA37CEDQ37365592-EDE1FE37-1796-44A7-ACEF-6D804474C3ABQ37365595-37861B3E-FA33-40F6-B19A-92069465D13FQ38001405-93594BD7-5C7C-4791-BBCC-EA64CFDB7A69Q38667667-803A4A15-13B1-44AD-84B6-16ADF1DB6F5AQ38692012-A4E05A64-77DF-43C8-AE6B-4FE993B7D8CEQ38791519-EF637386-4E90-4398-994A-ABCD616B0BE8Q39094600-20F6DF61-DD90-44A8-B938-C5FC1D3A1998Q39895735-F13AD4B1-62AE-4A63-A9FE-ED6EFA224144Q41874180-1C57D541-D9C2-4681-948A-1B00CD0134A6Q47137512-BFC00179-ABBE-4ABA-BE81-09707F7D9BDEQ47265042-2C0BDADA-0AF5-462B-98CE-05D30F1407DAQ57816805-4EF26C64-3676-463A-BB9E-995E8BDB0D5E
P2860
Tropomodulin binds two tropomyosins: a novel model for actin filament capping.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on October 2006
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Tropomodulin binds two tropomyosins: a novel model for actin filament capping.
@en
Tropomodulin binds two tropomyosins: a novel model for actin filament capping.
@nl
type
label
Tropomodulin binds two tropomyosins: a novel model for actin filament capping.
@en
Tropomodulin binds two tropomyosins: a novel model for actin filament capping.
@nl
prefLabel
Tropomodulin binds two tropomyosins: a novel model for actin filament capping.
@en
Tropomodulin binds two tropomyosins: a novel model for actin filament capping.
@nl
P2093
P2860
P356
P1433
P1476
Tropomodulin binds two tropomyosins: a novel model for actin filament capping.
@en
P2093
Alla S Kostyukova
Brian A Rapp
P2860
P304
12068-12075
P356
10.1021/BI060899I
P407
P577
2006-10-01T00:00:00Z