Výsledky vyhledávání - "Olga E, Karpicheva"

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

Autor: Stanislava V. Avrova, Vladimir V. Sirenko, Olga E. Karpicheva, Yurii S. Borovikov, Charles Redwood, Armen O. Simonyan

Publikováno v: Biochemical and Biophysical Research Communications. 523:258-262

Ghost muscle fibres reconstituted with myosin heads labeled with the fluorescent probe 1,5-IAEDANS were used for analysis of muscle fibre dysfunction associated with the R133W mutation in β-tropomyosin (Tpm2.2). By using polarized microscopy, we sho

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a0b285e67cd493deae360e9c8e56b82
https://doi.org/10.1016/j.bbrc.2019.12.061

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

Autor: Olga E. Karpicheva, Stanislava V. Avrova, Andrey L. Bogdanov, Vladimir V. Sirenko, Charles S. Redwood, Yurii S. Borovikov

Publikováno v: International Journal of Molecular Sciences; Volume 24; Issue 6; Pages: 5829

The substitution for Arg168His (R168H) in γ-tropomyosin (TPM3 gene, Tpm3.12 isoform) is associated with congenital muscle fiber type disproportion (CFTD) and muscle weakness. It is still unclear what molecular mechanisms underlie the muscle dysfunct

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e602661343926ab19a3aee0c2710c4df
https://doi.org/10.3390/ijms24065829

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

Autor: Armen O. Simonyan, Stanislava V. Avrova, Yurii S. Borovikov, Vladimir V. Sirenko, Olga E. Karpicheva, Charles Redwood

Publikováno v: Biochemical and Biophysical Research Communications. 515:372-377

Substitution of Ala for Thr residue in 155th position in γ-tropomyosin (Tpm3.12) is associated with muscle weakness. To understand the mechanisms of this defect, we studied the Ca2+-sensitivity of thin filaments in solution and multistep changes in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e228b715a36811e239315ab031a63c36
https://doi.org/10.1016/j.bbrc.2019.05.146

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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

Autor: Vladimir V. Sirenko, Olga E. Karpicheva, Stanislava V. Avrova, Charles Redwood, Armen O. Simonyan, Daria D. Andreeva, Yurii S. Borovikov

Publikováno v: International Journal of Molecular Sciences
Volume 22
Issue 12
International Journal of Molecular Sciences, Vol 22, Iss 6318, p 6318 (2021)

Point mutations in the genes encoding the skeletal muscle isoforms of tropomyosin can cause a range of muscle diseases. The amino acid substitution of Arg for Pro residue in the 90th position (R90P) in γ-tropomyosin (Tpm3.12) is associated with cong

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcf31b3fc73deac77bcbc0a1af185c8a
http://europepmc.org/articles/PMC8231546

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

Autor: Charles Redwood, Nikita A. Rysev, Olga E. Karpicheva, Yurii S. Borovikov, Armen O. Simonyan

Publikováno v: International Journal of Molecular Sciences, Vol 21, Iss 7590, p 7590 (2020)
International Journal of Molecular Sciences
Volume 21
Issue 20

We have used the technique of polarized microfluorimetry to obtain new insight into the pathogenesis of skeletal muscle disease caused by the Gln147Pro substitution in &beta
tropomyosin (Tpm2.2). The spatial rearrangements of actin, myosin and t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8cd6b7738d8a7ec5b6c6e13144c872a6
https://www.mdpi.com/1422-0067/21/20/7590

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

Autor: Olga E, Karpicheva, Armen O, Simonyan, Nikita A, Rysev, Charles S, Redwood, Yurii S, Borovikov

Publikováno v: International Journal of Molecular Sciences

We have used the technique of polarized microfluorimetry to obtain new insight into the pathogenesis of skeletal muscle disease caused by the Gln147Pro substitution in β-tropomyosin (Tpm2.2). The spatial rearrangements of actin, myosin and tropomyos

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e0fe044e21d801edc7f9b6e716f83665
https://pubmed.ncbi.nlm.nih.gov/33066566

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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

Autor: Vladimir V. Sirenko, Olga E. Karpicheva, Stanislava V. Avrova, Armen O. Simonyan, Yurii S. Borovikov, Charles Redwood

Publikováno v: International Journal of Molecular Sciences
Volume 21
Issue 12
International Journal of Molecular Sciences, Vol 21, Iss 4421, p 4421 (2020)

Substitution of Ala for Glu residue in position 173 of &gamma
tropomyosin (Tpm3.12) is associated with muscle weakness. Here we observe that this mutation increases myofilament Ca2+-sensitivity and inhibits in vitro actin-activated ATPase activi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ecb8a0679e9fd3dfb0169fe846e3d81

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The Effect of Gly126Arg Substitution in Alpha-Tropomyosin on Interaction of Myosin with Actin in the ATP Hydrolysis Cycle

Autor: Nikita A. Rysev, S.V. Avrova, Olga E. Karpicheva, Dmitrii I. Levitsky, Yu. S. Borovikov, I. A. Nevzorov

Publikováno v: Cell and Tissue Biology. 12:510-516

It is known that the regulation of muscle contraction is carried out by tropomyosin and calcium-sensitive protein troponin, which form thin filament with the F-actin. The noncanonical glycine residue at position 126 of the central part of the skeleta

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ee08747452ed5a0ca2d090616e13e32d
https://doi.org/10.1134/s1990519x1806010x

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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

Autor: Charles Redwood, Stanislava V. Avrova, Nikita A. Rysev, Vladimir V. Sirenko, Olga E. Karpicheva, Yurii S. Borovikov, Armen O. Simonyan

Publikováno v: Biochemical and Biophysical Research Communications. 502:209-214

The E41K mutation in TPM2 gene encoding muscle regulatory protein beta-tropomyosin is associated with nemaline myopathy and cap disease. The mutation results in a reduced Ca2+-sensitivity of the thin filaments and in muscle weakness. To elucidate the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2df56d00063cb0cdf1b1bdfbf5b32110
https://doi.org/10.1016/j.bbrc.2018.05.145

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The Effect of the Arg91Gly and Glu139del Mutations in β-Tropomyosin Associated with Congenital Myopathy of Human Skeletal Muscles on Actin–Myosin Interaction

Autor: Armen O. Simonyan, Nikita A. Rysev, Vladimir V. Sirenko, Olga E. Karpicheva, Yu. S. Borovikov, Charles Redwood

Publikováno v: Cell and Tissue Biology. 12:238-246

The structural changes in proteins of the contractile apparatus of muscle fiber and the violation of their function due to point mutations in these proteins can be a cause of many hereditary diseases of human muscular tissue. Some such diseases are c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::318ed41cf4cd1e79e965ee5aa85464a1
https://doi.org/10.1134/s1990519x18030112

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