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Journal Abstract Search

145 related items for PubMed ID: 20184863

  • 1. A new property of twitchin to restrict the "rolling" of mussel tropomyosin and decrease its affinity for actin during the actomyosin ATPase cycle.
    Avrova SV, Shelud'ko NS, Borovikov YS.
    Biochem Biophys Res Commun; 2010 Mar 26; 394(1):126-9. PubMed ID: 20184863
    [Abstract] [Full Text] [Related]

  • 2. Molluscan twitchin can control actin-myosin interaction during ATPase cycle.
    Borovikov YS, Shelud'ko NS, Avrova SV.
    Arch Biochem Biophys; 2010 Mar 15; 495(2):122-8. PubMed ID: 20060377
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  • 3. Caldesmon restricts the movement of both C- and N-termini of tropomyosin on F-actin in ghost fibers during the actomyosin ATPase cycle.
    Kulikova N, Pronina OE, Dabrowska R, Borovikov YS.
    Biochem Biophys Res Commun; 2006 Jun 23; 345(1):280-6. PubMed ID: 16678131
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  • 4. "Twitchin-actin linkage hypothesis" for the catch mechanism in molluscan muscles: evidence that twitchin interacts with myosin, myorod, and paramyosin core and affects properties of actomyosin.
    Shelud'ko NS, Matusovsky OS, Permyakova TV, Matusovskaya GG.
    Arch Biochem Biophys; 2007 Oct 01; 466(1):125-35. PubMed ID: 17720132
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  • 5. Twitchin can regulate the ATPase cycle of actomyosin in a phosphorylation-dependent manner in skinned mammalian skeletal muscle fibres.
    Avrova SV, Rysev NA, Matusovsky OS, Shelud'ko NS, Borovikov YS.
    Arch Biochem Biophys; 2012 May 01; 521(1-2):1-9. PubMed ID: 22430036
    [Abstract] [Full Text] [Related]

  • 6. Caldesmon inhibits the rotation of smooth actin subdomain-1 and alters its mobility during the ATP hydrolysis cycle.
    Kulikova N, Avrova SV, Borovikov YS.
    Biochem Biophys Res Commun; 2009 Dec 04; 390(1):125-9. PubMed ID: 19782047
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  • 10. Ultrastructure of the contractile system of striated skeletal muscle and the processes of muscular contraction. I. Ultrastructure of the myofibril and source of energy.
    Morel JE, Pinset-Härström I.
    Biomedicine; 1975 Mar 04; 22(2):88-96. PubMed ID: 764891
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  • 13. Caldesmon inhibits the actin-myosin interaction by changing its spatial orientation and mobility during the ATPase activity cycle.
    Kulikova N, Pronina OE, Dabrowska R, Borovikov YS.
    Biochem Biophys Res Commun; 2007 Jun 01; 357(2):461-6. PubMed ID: 17428444
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  • 14. Crossbridge and tropomyosin positions observed in native, interacting thick and thin filaments.
    Craig R, Lehman W.
    J Mol Biol; 2001 Aug 31; 311(5):1027-36. PubMed ID: 11531337
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  • 16. Structural changes in actin-tropomyosin during muscle regulation: computer modelling of low-angle X-ray diffraction data.
    al-Khayat HA, Yagi N, Squire JM.
    J Mol Biol; 1995 Oct 06; 252(5):611-32. PubMed ID: 7563078
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  • 17. 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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  • 18. 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 01; 1864(3):260-267. PubMed ID: 26708479
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  • 19. Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay.
    Harada Y, Sakurada K, Aoki T, Thomas DD, Yanagida T.
    J Mol Biol; 1990 Nov 05; 216(1):49-68. PubMed ID: 2146398
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