Congenital myopathy-causing tropomyosin mutations induce thin filament dysfunction via distinct physiological mechanisms. - Wikidata - wikimedia - TriplyDB

Congenital myopathy-causing tropomyosin mutations induce thin filament dysfunction via distinct physiological mechanisms.

Congenital myopathy-causing tropomyosin mutations induce thin filament dysfunction via distinct physiological mechanisms.

http://www.wikidata.org/entity/Q36283381

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Novel myosin-based therapies for congenital cardiac and skeletal myopathies Poorly understood aspects of striated muscle contraction Energy landscapes reveal the myopathic effects of tropomyosin mutations.Why Is there a Limit to the Changes in Myofilament Ca2+-Sensitivity Associated with Myopathy Causing Mutations?Mutation update and genotype-phenotype correlations of novel and previously described mutations in TPM2 and TPM3 causing congenital myopathies Mutations in repeating structural motifs of tropomyosin cause gain of function in skeletal muscle myopathy patients 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 Mechanistic heterogeneity in contractile properties of α-tropomyosin (TPM1) mutants associated with inherited cardiomyopathies.Muscle weakness in TPM3-myopathy is due to reduced Ca2+-sensitivity and impaired acto-myosin cross-bridge cycling in slow fibres.Tropomodulin 1 directly controls thin filament length in both wild-type and tropomodulin 4-deficient skeletal muscle.TPM3 deletions cause a hypercontractile congenital muscle stiffness phenotype.A two-segment model for thin filament architecture in skeletal muscle.Alterations in thin filament length during postnatal skeletal muscle development and aging in mice.Sarcomere Dysfunction in Nemaline Myopathy.Hypothesis and theory: mechanical instabilities and non-uniformities in hereditary sarcomere myopathies.Skeletal muscle myopathy mutations at the actin tropomyosin interface that cause gain- or loss-of-function.Software-based measurement of thin filament lengths: an open-source GUI for Distributed Deconvolution analysis of fluorescence images.Myofilament lattice structure in presence of a skeletal myopathy-related tropomyosin mutation.Stabilization of F-actin by tropomyosin isoforms regulates the morphology and mechanical behavior of red blood cells.Dysfunctional sarcomere contractility contributes to muscle weakness in ACTA1-related nemaline myopathy (NEM3).

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Congenital myopathy-causing tropomyosin mutations induce thin filament dysfunction via distinct physiological mechanisms.

http://www.wikidata.org/entity/Q36283381

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2012年の論文

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Congenital myopathy-causing tr ...... inct physiological mechanisms.

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Congenital myopathy-causing tr ...... inct physiological mechanisms.

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Human Molecular Genetics

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Congenital myopathy-causing tr ...... tinct physiological mechanisms

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David S Gokhin

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Isabelle Pénisson-Besnier

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Joël Lunardi

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Nicole Monnier

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Norma B Romero

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Susana Quijano-Roy

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P2860

Maximum velocity of shortening in relation to myosin isoform composition in single fibres from human skeletal muscles

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

Structure of the C-domain of human cardiac troponin C in complex with the Ca2+ sensitizing drug EMD 57033

The crystal structure of the C-terminal fragment of striated-muscle alpha-tropomyosin reveals a key troponin T recognition site.

Abnormal actin binding of aberrant β-tropomyosins is a molecular cause of muscle weakness in TPM2-related nemaline and cap myopathy

Molecular and physiological effects of overexpressing striated muscle beta-tropomyosin in the adult murine heart

Beta-tropomyosin overexpression induces severe cardiac abnormalities

The Nebulin family: an actin support group

Effects of a R133W beta-tropomyosin mutation on regulation of muscle contraction in single human muscle fibres

Absence of beta-tropomyosin is a new cause of Escobar syndrome associated with nemaline myopathy

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10.1093/HMG/DDS289

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