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387 related items for PubMed ID: 26708479

  • 1. 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.
    Karpicheva OE, Simonyan AO, Kuleva NV, Redwood CS, Borovikov YS.
    Biochim Biophys Acta; 2016 Mar; 1864(3):260-267. PubMed ID: 26708479
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  • 2. Aberrant movement of β-tropomyosin associated with congenital myopathy causes defective response of myosin heads and actin during the ATPase cycle.
    Borovikov YS, Avrova SV, Rysev NA, Sirenko VV, Simonyan AO, Chernev AA, Karpicheva OE, Piers A, Redwood CS.
    Arch Biochem Biophys; 2015 Jul; 577-578():11-23. PubMed ID: 25978979
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  • 3. 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.
    Simonyan AO, Sirenko VV, Karpicheva OE, Robaszkiewicz K, Śliwinska M, Moraczewska J, Krutetskaya ZI, Borovikov YS.
    Arch Biochem Biophys; 2018 Apr 15; 644():17-28. PubMed ID: 29510086
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  • 4. Molecular Mechanisms of Deregulation of Muscle Contractility Caused by the R168H Mutation in TPM3 and Its Attenuation by Therapeutic Agents.
    Karpicheva OE, Avrova SV, Bogdanov AL, Sirenko VV, Redwood CS, Borovikov YS.
    Int J Mol Sci; 2023 Mar 18; 24(6):. PubMed ID: 36982903
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  • 5. 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, Karpicheva OE, Simonyan AO, Avrova SV, Rogozovets EA, Sirenko VV, Redwood CS.
    Int J Mol Sci; 2018 Dec 10; 19(12):. PubMed ID: 30544720
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  • 6. 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.
    Avrova SV, Karpicheva OE, Rysev NA, Simonyan AO, Sirenko VV, Redwood CS, Borovikov YS.
    Biochem Biophys Res Commun; 2018 Jul 12; 502(2):209-214. PubMed ID: 29792862
    [Abstract] [Full Text] [Related]

  • 7. Gly126Arg substitution causes anomalous behaviour of α-skeletal and β-smooth tropomyosins during the ATPase cycle.
    Rysev NA, Nevzorov IA, Avrova SV, Karpicheva OE, Redwood CS, Levitsky DI, Borovikov YS.
    Arch Biochem Biophys; 2014 Feb 01; 543():57-66. PubMed ID: 24374033
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  • 8. 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.
    Borovikov YS, Simonyan AO, Karpicheva OE, Avrova SV, Rysev NA, Sirenko VV, Piers A, Redwood CS.
    Biochem Biophys Res Commun; 2017 Dec 16; 494(3-4):681-686. PubMed ID: 29097206
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  • 11. Hypertrophic cardiomyopathy-causing Asp175asn and Glu180gly Tpm1 mutations shift tropomyosin strands further towards the open position during the ATPase cycle.
    Borovikov YS, Rysev NA, Karpicheva OE, Redwood CS.
    Biochem Biophys Res Commun; 2011 Apr 01; 407(1):197-201. PubMed ID: 21376702
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  • 14. The nemaline myopathy-causing E117K mutation in β-tropomyosin reduces thin filament activation.
    Karpicheva OE, Robinson P, Piers A, Borovikov YS, Redwood CS.
    Arch Biochem Biophys; 2013 Aug 01; 536(1):25-30. PubMed ID: 23689010
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