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Molecular Mechanisms of Deregulation of Muscle Contractility Caused by the R168H Mutation in TPM3 and Its Attenuation by Therapeutic Agents

International journal of molecular sciences, 2023-03, Vol.24 (6), p.5829

2023

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Molecular Mechanisms of the Deregulation of Muscle Contraction Induced by the R90P Mutation in Tpm3.12 and the Weakening of This Effect by BDM and W7

International journal of molecular sciences, 2021-06, Vol.22 (12), p.6318

2021

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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

International journal of molecular sciences, 2018-12, Vol.19 (12), p.3975

2018

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Looking for Targets to Restore the Contractile Function in Congenital Myopathy Caused by Gln147Pro Tropomyosin

International journal of molecular sciences, 2020-10, Vol.21 (20), p.7590

2020

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Molecular Mechanisms of Muscle Weakness Associated with E173A Mutation in Tpm3.12. Troponin Ca2+ Sensitivity Inhibitor W7 Can Reduce the Damaging Effect of This Mutation

International journal of molecular sciences, 2020-06, Vol.21 (12), p.4421

2020

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Myosin's powerstroke transitions define atomic scale movement of cardiac thin filament tropomyosin

The Journal of general physiology, 2024-05, Vol.156 (5), p.1

2024

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The molecular mechanism of muscle dysfunction associated with the R133W mutation in Tpm2.2

Biochemical and biophysical research communications, 2020-02, Vol.523 (1), p.258-262

2020

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The molecular mechanisms of a high Ca2+-sensitivity and muscle weakness associated with the Ala155Thr substitution in Tpm3.12

Biochemical and biophysical research communications, 2019-07, Vol.515 (2), p.372-377

2019

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Deviations in conformational rearrangements of thin filaments and myosin caused by the Ala155Thr substitution in hydrophobic core of tropomyosin

Biochimica et biophysica acta. Proteins and proteomics, 2017-12, Vol.1865 (12), p.1790-1799

2017

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Molecular mechanisms of deregulation of the thin filament associated with the R167H and K168E substitutions in tropomyosin Tpm1.1

Archives of biochemistry and biophysics, 2017-01, Vol.614, p.28-40

2017

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Molecular mechanisms of dysfunction of muscle fibres associated with Glu139 deletion in TPM2 gene

Scientific reports, 2017-12, Vol.7 (1), p.16797-10, Article 16797

2017

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The reason for a high Ca2+-sensitivity associated with Arg91Gly substitution in TPM2 gene is the abnormal behavior and high flexibility of tropomyosin during the ATPase cycle

Biochemical and biophysical research communications, 2017-12, Vol.494 (3-4), p.681-686

2017

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Myopathy-causing Q147P TPM2 mutation shifts tropomyosin strands further towards the open position and increases the proportion of strong-binding cross-bridges during the ATPase cycle

Biochimica et biophysica acta, 2016-03, Vol.1864 (3), p.260-267

2016

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The primary cause of muscle disfunction associated with substitutions E240K and R244G in tropomyosin is aberrant behavior of tropomyosin and response of actin and myosin during ATPase cycle

Archives of biochemistry and biophysics, 2018-04, Vol.644, p.17-28

2018

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The E117K mutation in β-tropomyosin disturbs concerted conformational changes of actomyosin in muscle fibers

Archives of biochemistry and biophysics, 2014-05, Vol.549, p.12-16

2014

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The reason for the low Ca2+-sensitivity of thin filaments associated with the Glu41Lys mutation in the TPM2 gene is “freezing” of tropomyosin near the outer domain of actin and inhibition of actin monomer switching off during the ATPase cycle

Biochemical and biophysical research communications, 2018-07, Vol.502 (2), p.209-214

2018

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The reason for the low Ca 2+ -sensitivity of thin filaments associated with the Glu41Lys mutation in the TPM2 gene is "freezing" of tropomyosin near the outer domain of actin and inhibition of actin monomer switching off during the ATPase cycle

Biochemical and biophysical research communications, 2018-07, Vol.502 (2), p.209-214

2018

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Abnormal movement of tropomyosin and response of myosin heads and actin during the ATPase cycle caused by the Arg167His, Arg167Gly and Lys168Glu mutations in TPM1 gene

Archives of biochemistry and biophysics, 2016-09, Vol.606, p.157-166

2016

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Aberrant movement of β-tropomyosin associated with congenital myopathy causes defective response of myosin heads and actin during the ATPase cycle

Archives of biochemistry and biophysics, 2015-07, Vol.577-578, p.11-23

2015

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The nemaline myopathy-causing E117K mutation in β-tropomyosin reduces thin filament activation

Archives of biochemistry and biophysics, 2013-08, Vol.536 (1), p.25-30

2013

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The effect of the Asp175Asn and Glu180Gly TPM1 mutations on actin–myosin interaction during the ATPase cycle

Biochimica et biophysica acta, 2012-02, Vol.1824 (2), p.366-373

2012

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The effect of the dilated cardiomyopathy-causing Glu40Lys TPM1 mutation on actin-myosin interactions during the ATPase cycle

Biochemical and biophysical research communications, 2011-08, Vol.411 (3), p.496-500

2011

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Modulation of the effects of tropomyosin on actin and myosin conformational changes by troponin and Ca2

Biochimica et biophysica acta, 2009-07, Vol.1794 (7), p.985-994

2009

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Gly126Arg substitution causes anomalous behaviour of α-skeletal and β-smooth tropomyosins during the ATPase cycle

Archives of biochemistry and biophysics, 2014-02, Vol.543, p.57-66

2014

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Hypertrophic cardiomyopathy-causing Asp175asn and Glu180gly Tpm1 mutations shift tropomyosin strands further towards the open position during the ATPase cycle

Biochemical and biophysical research communications, 2011-04, Vol.407 (1), p.197-201

2011

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Molecular Mechanisms of Deregulation of Muscle Contractility Caused by the R168H Mutation in TPM3 and Its Attenuation by Therapeutic Agents

Molecular Mechanisms of the Deregulation of Muscle Contraction Induced by the R90P Mutation in Tpm3.12 and the Weakening of This Effect by BDM and W7

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

Looking for Targets to Restore the Contractile Function in Congenital Myopathy Caused by Gln147Pro Tropomyosin

Molecular Mechanisms of Muscle Weakness Associated with E173A Mutation in Tpm3.12. Troponin Ca2+ Sensitivity Inhibitor W7 Can Reduce the Damaging Effect of This Mutation

Myosin's powerstroke transitions define atomic scale movement of cardiac thin filament tropomyosin

The molecular mechanism of muscle dysfunction associated with the R133W mutation in Tpm2.2

The molecular mechanisms of a high Ca2+-sensitivity and muscle weakness associated with the Ala155Thr substitution in Tpm3.12

Deviations in conformational rearrangements of thin filaments and myosin caused by the Ala155Thr substitution in hydrophobic core of tropomyosin

Molecular mechanisms of deregulation of the thin filament associated with the R167H and K168E substitutions in tropomyosin Tpm1.1

Molecular mechanisms of dysfunction of muscle fibres associated with Glu139 deletion in TPM2 gene

The reason for a high Ca2+-sensitivity associated with Arg91Gly substitution in TPM2 gene is the abnormal behavior and high flexibility of tropomyosin during the ATPase cycle

Myopathy-causing Q147P TPM2 mutation shifts tropomyosin strands further towards the open position and increases the proportion of strong-binding cross-bridges during the ATPase cycle

The primary cause of muscle disfunction associated with substitutions E240K and R244G in tropomyosin is aberrant behavior of tropomyosin and response of actin and myosin during ATPase cycle

The E117K mutation in β-tropomyosin disturbs concerted conformational changes of actomyosin in muscle fibers

The reason for the low Ca2+-sensitivity of thin filaments associated with the Glu41Lys mutation in the TPM2 gene is “freezing” of tropomyosin near the outer domain of actin and inhibition of actin monomer switching off during the ATPase cycle

The reason for the low Ca 2+ -sensitivity of thin filaments associated with the Glu41Lys mutation in the TPM2 gene is "freezing" of tropomyosin near the outer domain of actin and inhibition of actin monomer switching off during the ATPase cycle

Abnormal movement of tropomyosin and response of myosin heads and actin during the ATPase cycle caused by the Arg167His, Arg167Gly and Lys168Glu mutations in TPM1 gene

Aberrant movement of β-tropomyosin associated with congenital myopathy causes defective response of myosin heads and actin during the ATPase cycle

The nemaline myopathy-causing E117K mutation in β-tropomyosin reduces thin filament activation

The effect of the Asp175Asn and Glu180Gly TPM1 mutations on actin–myosin interaction during the ATPase cycle

The effect of the dilated cardiomyopathy-causing Glu40Lys TPM1 mutation on actin-myosin interactions during the ATPase cycle

Modulation of the effects of tropomyosin on actin and myosin conformational changes by troponin and Ca2

Gly126Arg substitution causes anomalous behaviour of α-skeletal and β-smooth tropomyosins during the ATPase cycle

Hypertrophic cardiomyopathy-causing Asp175asn and Glu180gly Tpm1 mutations shift tropomyosin strands further towards the open position during the ATPase cycle

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