Associated Papers
The Twisting and Untwisting of Actin and Tropomyosin Filaments Are Involved in the Molecular Mechanisms of Muscle Contraction, and Their Disruption Can Result in Muscle Disorders.
Borovikov YS et al.
International Journal of Molecular Sciences, 2025
A recurrent pathogenic variant in TPM2 reveals further phenotypic and genetic heterogeneity in multiple pterygium syndrome-related disorders.
Vogt J et al.
Clinical Genetics, 2020
Estimating dispensable content in the human interactome.
Ghadie M et al.
Nature Communications, 2019
The Primary Causes of Muscle Dysfunction Associated with the Point Mutations in Tpm3.12; Conformational Analysis of Mutant Proteins as a Tool for Classification of Myopathies.
Borovikov YS et al.
International Journal of Molecular Sciences, 2018
Novel mutations in TPM2 and PIEZO2 are responsible for distal arthrogryposis (DA) 2B and mild DA in two Chinese families.
Li S et al.
Bmc Medical Genetics, 2018
Smad4 SUMOylation is essential for memory formation through upregulation of the skeletal myopathy gene TPM2.
Hsu WL et al.
Bmc Biology, 2017
A novel TPM2 gene splice-site mutation causes severe congenital myopathy with arthrogryposis and dysmorphic features.
Mroczek M et al.
Journal of Applied Genetics, 2017
Why Is there a Limit to the Changes in Myofilament Ca2+-Sensitivity Associated with Myopathy Causing Mutations?
Marston SB
Frontiers in Physiology, 2016
Aberrant movement of β-tropomyosin associated with congenital myopathy causes defective response of myosin heads and actin during the ATPase cycle.
Borovikov YS et al.
Archives of Biochemistry and Biophysics, 2015
Pathophysiological concepts in the congenital myopathies: blurring the boundaries, sharpening the focus.
Ravenscroft G et al.
Brain : a Journal of Neurology, 2015
Mutation update and genotype-phenotype correlations of novel and previously described mutations in TPM2 and TPM3 causing congenital myopathies.
Marttila M et al.
Human Mutation, 2014
The E117K mutation in β-tropomyosin disturbs concerted conformational changes of actomyosin in muscle fibers.
Karpicheva OE et al.
Archives of Biochemistry and Biophysics, 2014
Nebulin interactions with actin and tropomyosin are altered by disease-causing mutations.
Marttila M et al.
Skeletal Muscle, 2014
Alterations at the cross-bridge level are associated with a paradoxical gain of muscle function in vivo in a mouse model of nemaline myopathy.
Gineste C et al.
Plos One, 2014
The nemaline myopathy-causing E117K mutation in β-tropomyosin reduces thin filament activation.
Karpicheva OE et al.
Archives of Biochemistry and Biophysics, 2013
Skeletal muscle myopathy mutations at the actin tropomyosin interface that cause gain- or loss-of-function.
Memo M et al.
Journal of Muscle Research and Cell Motility, 2013
K7del is a common TPM2 gene mutation associated with nemaline myopathy and raised myofibre calcium sensitivity.
Mokbel N et al.
Brain : a Journal of Neurology, 2013
Myopathies associated with β-tropomyosin mutations.
Tajsharghi H et al.
Neuromuscular Disorders : Nmd, 2012
Abnormal actin binding of aberrant β-tropomyosins is a molecular cause of muscle weakness in TPM2-related nemaline and cap myopathy.
Marttila M et al.
The Biochemical Journal, 2012
Defective regulation of contractile function in muscle fibres carrying an E41K beta-tropomyosin mutation.
Ochala J et al.
The Journal of Physiology, 2008
Skeletal muscle disease due to mutations in tropomyosin, troponin and cofilin.
Clarke NF
Advances in Experimental Medicine and Biology, 2008
Tropomyosins in skeletal muscle diseases.
Kee AJ et al.
Advances in Experimental Medicine and Biology, 2008
Cap disease caused by heterozygous deletion of the beta-tropomyosin gene TPM2.
Lehtokari VL et al.
Neuromuscular Disorders : Nmd, 2007
Mutations in the beta-tropomyosin (TPM2) gene--a rare cause of nemaline myopathy.
Donner K et al.
Neuromuscular Disorders : Nmd, 2002