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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. / Borovikov, Y.S.; Avrova, S.V.; Rysev, N.A.; Sirenko, V.V.; Simonyan, A.O.; Chernev, A.A.; Karpicheva, O.E.; Piers, A.; Redwood, C.S.

In: Archives of Biochemistry and Biophysics, Vol. 577–578, 2015, p. 13-23.

Research output: Contribution to journal › Article › peer-review

Harvard

Borovikov, YS, Avrova, SV, Rysev, NA, Sirenko, VV, Simonyan, AO, Chernev, AA, Karpicheva, OE, Piers, A & Redwood, CS 2015, '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, vol. 577–578, pp. 13-23. https://doi.org/10.1016/j.abb.2015.05.002

APA

Borovikov, Y. S., Avrova, S. V., Rysev, N. A., Sirenko, V. V., Simonyan, A. O., Chernev, A. A., Karpicheva, O. E., Piers, A., & Redwood, C. S. (2015). 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, 577–578, 13-23. https://doi.org/10.1016/j.abb.2015.05.002

Vancouver

Borovikov YS, Avrova SV, Rysev NA, Sirenko VV, Simonyan AO, Chernev AA et al. 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;577–578:13-23. https://doi.org/10.1016/j.abb.2015.05.002

Author

Borovikov, Y.S. ; Avrova, S.V. ; Rysev, N.A. ; Sirenko, V.V. ; Simonyan, A.O. ; Chernev, A.A. ; Karpicheva, O.E. ; Piers, A. ; Redwood, C.S. / Aberrant movement of β-tropomyosin associated with congenital myopathy causes defective response of myosin heads and actin during the ATPase cycle. In: Archives of Biochemistry and Biophysics. 2015 ; Vol. 577–578. pp. 13-23.

BibTeX

@article{aad3e1d96f20408ea6ca88fbcaa6fb99,
title = "Aberrant movement of β-tropomyosin associated with congenital myopathy causes defective response of myosin heads and actin during the ATPase cycle",
abstract = "We have investigated the effect of the E41K, R91G, and E139del beta-tropomyosin (TM) mutations that cause congenital myopathy on the position of TM and orientation of actin monomers and myosin heads at different mimicked stages of the ATPase cycle in troponin-free ghost muscle fibers by polarized fluorimetry. A multi-step shifting of wild-type TM to the filament center accompanied by an increase in the amount of switched on actin monomers and the strongly bound myosin heads was observed during the ATPase cycle. The R91G mutation shifts TM further towards the inner and outer domains of actin at the strong- and weak-binding stages, respectively. The E139del mutation retains TM near the inner domains, while the E41K mutation captures it near the outer domains. The E41K and R91G mutations can induce the strong binding of myosin heads to actin, when TM is located near the outer domains. The E139del mutation inhibits the amount of strongly bound myosin heads throughout the ATPase cycle. (C) 2015 Elsevier Inc. All r",
author = "Y.S. Borovikov and S.V. Avrova and N.A. Rysev and V.V. Sirenko and A.O. Simonyan and A.A. Chernev and O.E. Karpicheva and A. Piers and C.S. Redwood",
year = "2015",
doi = "10.1016/j.abb.2015.05.002",
language = "English",
volume = "577–578",
pages = "13--23",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Aberrant movement of β-tropomyosin associated with congenital myopathy causes defective response of myosin heads and actin during the ATPase cycle

AU - Borovikov, Y.S.

AU - Avrova, S.V.

AU - Rysev, N.A.

AU - Sirenko, V.V.

AU - Simonyan, A.O.

AU - Chernev, A.A.

AU - Karpicheva, O.E.

AU - Piers, A.

AU - Redwood, C.S.

PY - 2015

Y1 - 2015

N2 - We have investigated the effect of the E41K, R91G, and E139del beta-tropomyosin (TM) mutations that cause congenital myopathy on the position of TM and orientation of actin monomers and myosin heads at different mimicked stages of the ATPase cycle in troponin-free ghost muscle fibers by polarized fluorimetry. A multi-step shifting of wild-type TM to the filament center accompanied by an increase in the amount of switched on actin monomers and the strongly bound myosin heads was observed during the ATPase cycle. The R91G mutation shifts TM further towards the inner and outer domains of actin at the strong- and weak-binding stages, respectively. The E139del mutation retains TM near the inner domains, while the E41K mutation captures it near the outer domains. The E41K and R91G mutations can induce the strong binding of myosin heads to actin, when TM is located near the outer domains. The E139del mutation inhibits the amount of strongly bound myosin heads throughout the ATPase cycle. (C) 2015 Elsevier Inc. All r

AB - We have investigated the effect of the E41K, R91G, and E139del beta-tropomyosin (TM) mutations that cause congenital myopathy on the position of TM and orientation of actin monomers and myosin heads at different mimicked stages of the ATPase cycle in troponin-free ghost muscle fibers by polarized fluorimetry. A multi-step shifting of wild-type TM to the filament center accompanied by an increase in the amount of switched on actin monomers and the strongly bound myosin heads was observed during the ATPase cycle. The R91G mutation shifts TM further towards the inner and outer domains of actin at the strong- and weak-binding stages, respectively. The E139del mutation retains TM near the inner domains, while the E41K mutation captures it near the outer domains. The E41K and R91G mutations can induce the strong binding of myosin heads to actin, when TM is located near the outer domains. The E139del mutation inhibits the amount of strongly bound myosin heads throughout the ATPase cycle. (C) 2015 Elsevier Inc. All r

U2 - 10.1016/j.abb.2015.05.002

DO - 10.1016/j.abb.2015.05.002

M3 - Article

VL - 577–578

SP - 13

EP - 23

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

ER -

ID: 3926106