Nebulin plays a direct role in promoting strong actin-myosin interactions. - Wikidata - wikimedia - TriplyDB

Nebulin plays a direct role in promoting strong actin-myosin interactions.

Nebulin plays a direct role in promoting strong actin-myosin interactions.

http://www.wikidata.org/entity/Q33613267

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Tropomodulin capping of actin filaments in striated muscle development and physiology The Nebulin family: an actin support group KLHL40 deficiency destabilizes thin filament proteins and promotes nemaline myopathy Identification of 2 Potentially Relevant Gene Mutations Involved in Strabismus Using Whole-Exome Sequencing The nebulin SH3 domain is dispensable for normal skeletal muscle structure but is required for effective active load bearing in mouse.Nebulin binding impedes mutant desmin filament assembly.Pointed-end capping by tropomodulin modulates actomyosin crossbridge formation in skeletal muscle fibers.Altered myofilament function depresses force generation in patients with nebulin-based nemaline myopathy (NEM2).Nebulin regulates actin filament lengths by a stabilization mechanism.Changes in cross-bridge cycling underlie muscle weakness in patients with tropomyosin 3-based myopathy.Alterations at the cross-bridge level are associated with a paradoxical gain of muscle function in vivo in a mouse model of nemaline myopathy Troponin activator augments muscle force in nemaline myopathy patients with nebulin mutations Nemaline myopathy-related skeletal muscle α-actin (ACTA1) mutation, Asp286Gly, prevents proper strong myosin binding and triggers muscle weakness.Nebulin, a major player in muscle health and disease Fast skeletal muscle troponin activation increases force of mouse fast skeletal muscle and ameliorates weakness due to nebulin-deficiency.Combined MRI and ³¹P-MRS investigations of the ACTA1(H40Y) mouse model of nemaline myopathy show impaired muscle function and altered energy metabolism.Multimodal MRI and (31)P-MRS investigations of the ACTA1(Asp286Gly) mouse model of nemaline myopathy provide evidence of impaired in vivo muscle function, altered muscle structure and disturbed energy metabolism Novel mutations in NEB cause abnormal nebulin expression and markedly impaired muscle force generation in severe nemaline myopathy.The desmin coil 1B mutation K190A impairs nebulin Z-disc assembly and destabilizes actin thin filaments.Disrupted myosin cross-bridge cycling kinetics triggers muscle weakness in nebulin-related myopathy.Effect of levosimendan on the contractility of muscle fibers from nemaline myopathy patients with mutations in the nebulin gene.The sarcomeric protein nebulin: another multifunctional giant in charge of muscle strength optimization Differences in gene expression between strabismic and normal human extraocular muscles.Loss of muscle strength during sepsis is in part regulated by glucocorticoids and is associated with reduced muscle fiber stiffness.Deleting exon 55 from the nebulin gene induces severe muscle weakness in a mouse model for nemaline myopathy.Lifting the nebula: novel insights into skeletal muscle contractility.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.Sarcomere Dysfunction in Nemaline Myopathy.Actin in striated muscle: recent insights into assembly and maintenance Overview of the Muscle Cytoskeleton.Thin filament length in the cardiac sarcomere varies with sarcomere length but is independent of titin and nebulin.Effect of fast pH decline during the early postmortem period on calpain activity and cytoskeletal protein degradation of broiler M. pectoralis major.

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P2860

Nebulin plays a direct role in promoting strong actin-myosin interactions.

http://www.wikidata.org/entity/Q33613267

description

2009 nî lūn-bûn

@nan

2009 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի օգոստոսին հրատարակված գիտական հոդված

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2009年の論文

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年學術文章

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name

Nebulin plays a direct role in promoting strong actin-myosin interactions.

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Nebulin plays a direct role in promoting strong actin-myosin interactions.

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type

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Nebulin plays a direct role in promoting strong actin-myosin interactions.

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Nebulin plays a direct role in promoting strong actin-myosin interactions.

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Nebulin plays a direct role in promoting strong actin-myosin interactions.

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Nebulin plays a direct role in promoting strong actin-myosin interactions.

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Nebulin plays a direct role in promoting strong actin-myosin interactions.

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P2093

Elisabetta Brunello

http://www.w3.org/2001/XMLSchema#string

Ju Chen

http://www.w3.org/2001/XMLSchema#string

Marco Caremani

http://www.w3.org/2001/XMLSchema#string

Marco Linari

http://www.w3.org/2001/XMLSchema#string

Marie-Louise Bang

http://www.w3.org/2001/XMLSchema#string

Richard L Lieber

http://www.w3.org/2001/XMLSchema#string

Ryan Littlefield

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Vincenzo Lombardi

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P2860

Myopalladin, a novel 145-kilodalton sarcomeric protein with multiple roles in Z-disc and I-band protein assemblies

Nebulin regulates thin filament length, contractility, and Z-disk structure in vivo.

The complete primary structure of human nebulin and its correlation to muscle structure

Interaction of nebulin SH3 domain with titin PEVK and myopalladin: implications for the signaling and assembly role of titin and nebulin

Nebulin-deficient mice exhibit shorter thin filament lengths and reduced contractile function in skeletal muscle

Calmodulin-sensitive interaction of human nebulin fragments with actin and myosin

Cap Z(36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle

Inhibition of CapZ during myofibrillogenesis alters assembly of actin filaments

Regulation of contraction in striated muscle

A nebulin ruler does not dictate thin filament lengths

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4117-4125

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10.1096/FJ.09-137729

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12

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23

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2009-08-13T00:00:00Z

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26740933

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19679637

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2812046

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