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

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

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

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

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

Autor: Joanna Moraczewska, Nikita A. Rysev, Armen O. Simonyan, Danuta Borys, Vladimir V. Sirenko, Olga E. Karpicheva, Yurii S. Borovikov

Publikováno v: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1865:1790-1799

Effects of the Ala155Thr substitution in hydrophobic core of tropomyosin Tpm1.1 on conformational rearrangements of the components of the contractile system (Tpm1.1, actin and myosin heads) were studied by polarized fluorimetry technique at different

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c084a2bc70595882f292c2d75e6e2687
https://doi.org/10.1016/j.bbapap.2017.09.008