Leiomodin-2 is an antagonist of tropomodulin-1 at the pointed end of the thin filaments in cardiac muscle. - Wikidata - wikimedia - TriplyDB

Leiomodin-2 is an antagonist of tropomodulin-1 at the pointed end of the thin filaments in cardiac muscle.

Leiomodin-2 is an antagonist of tropomodulin-1 at the pointed end of the thin filaments in cardiac muscle.

http://www.wikidata.org/entity/Q41874180

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Tropomodulin capping of actin filaments in striated muscle development and physiology Knockout of Lmod2 results in shorter thin filaments followed by dilated cardiomyopathy and juvenile lethality Severe myopathy in mice lacking the MEF2/SRF-dependent gene leiomodin-3 Lmod2 piggyBac mutant mice exhibit dilated cardiomyopathy.Leiomodin-3 dysfunction results in thin filament disorganization and nemaline myopathy.Actin polymerization is stimulated by actin cross-linking protein palladin.Shared genetic basis for migraine and ischemic stroke: A genome-wide analysis of common variants.Regulation of structure and function of sarcomeric actin filaments in striated muscle of the nematode Caenorhabditis elegans.Comparison of muscle transcriptome between pigs with divergent meat quality phenotypes identifies genes related to muscle metabolism and structure Dynamic regulation of sarcomeric actin filaments in striated muscle A comparative proteomic study of sera in paediatric systemic lupus erythematosus patients and in healthy controls using MALDI-TOF-TOF and LC MS-A pilot study.Leiomodin 3 and tropomodulin 4 have overlapping functions during skeletal myofibrillogenesis.DAAM is required for thin filament formation and Sarcomerogenesis during muscle development in Drosophila Loss of Sarcomere-associated Formins Disrupts Z-line Organization, but does not Prevent Thin Filament Assembly in Caenorhabditis elegans Muscle Z-line formins promote contractile lattice growth and maintenance in striated muscles of C. elegans.Mechanisms of leiomodin 2-mediated regulation of actin filament in muscle cells RNA sequencing for global gene expression associated with muscle growth in a single male modern broiler line compared to a foundational Barred Plymouth Rock chicken line Tropomodulin 1 directly controls thin filament length in both wild-type and tropomodulin 4-deficient skeletal muscle.Tropomodulins and tropomyosins: working as a team 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.Tropomodulins: pointed-end capping proteins that regulate actin filament architecture in diverse cell types.A two-segment model for thin filament architecture in skeletal muscle.Cardiac cytoarchitecture - why the "hardware" is important for heart function!The cardiomyopathy-associated K15N mutation in tropomyosin alters actin filament pointed end dynamics.Tropomodulins and Leiomodins: Actin Pointed End Caps and Nucleators in Muscles.Alterations in thin filament length during postnatal skeletal muscle development and aging in mice.Actin in striated muscle: recent insights into assembly and maintenance Overview of the Muscle Cytoskeleton.Influence of Duroc breed inclusion into Polish Landrace maternal line on pork meat quality traits.The Drosophila formin Fhos is a primary mediator of sarcomeric thin-filament array assembly.Increased Hemodynamic Load in Early Embryonic Stages Alters Myofibril and Mitochondrial Organization in the Myocardium.Thin filament length in the cardiac sarcomere varies with sarcomere length but is independent of titin and nebulin.Phosphoproteomics study based on in vivo inhibition reveals sites of calmodulin-dependent protein kinase II regulation in the heart.Cardiac leiomodin2 binds to the sides of actin filaments and regulates the ATPase activity of myosin HSPB7 is indispensable for heart development by modulating actin filament assembly.Characterizing interaction forces between actin and proteins of the tropomodulin family reveals the presence of the N-terminal actin-binding site in leiomodin.Structural destabilization of tropomyosin induced by the cardiomyopathy-linked mutation R21H.Crystal Structure of Leiomodin 2 in Complex with Actin: A Structural and Functional Reexamination.

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P2860

Leiomodin-2 is an antagonist of tropomodulin-1 at the pointed end of the thin filaments in cardiac muscle.

http://www.wikidata.org/entity/Q41874180

description

2010 nî lūn-bûn

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Leiomodin-2 is an antagonist o ...... n filaments in cardiac muscle.

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Alla S Kostyukova

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Carol C Gregorio

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Christopher T Pappas

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Natalia Moroz

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Parker B Antin

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Takehiro Tsukada

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P2860

Tropomodulin caps the pointed ends of actin filaments

Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Leiomodin is an actin filament nucleator in muscle cells.

Aberrant myofibril assembly in tropomodulin1 null mice leads to aborted heart development and embryonic lethality

Spectroscopic determination of tryptophan and tyrosine in proteins

Myofibril degeneration caused by tropomodulin overexpression leads to dilated cardiomyopathy in juvenile mice.

Identification of a novel tropomodulin isoform, skeletal tropomodulin, that caps actin filament pointed ends in fast skeletal muscle.

Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF).

Effects of CapZ, an actin capping protein of muscle, on the polymerization of actin.

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3136-3145

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10.1242/JCS.071837

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Pt 18

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123

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45827661

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20736303

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2931607

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