Detalhe da pesquisa
1.
Molecular Mechanisms of Deregulation of Muscle Contractility Caused by the R168H Mutation in TPM3 and Its Attenuation by Therapeutic Agents.
Int J Mol Sci
; 24(6)2023 Mar 18.
Artigo
em Inglês
| MEDLINE | ID: mdl-36982903
2.
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.
Int J Mol Sci
; 22(12)2021 Jun 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-34204776
3.
The molecular mechanism of muscle dysfunction associated with the R133W mutation in Tpm2.2.
Biochem Biophys Res Commun
; 523(1): 258-262, 2020 02 26.
Artigo
em Inglês
| MEDLINE | ID: mdl-31864708
4.
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.
Int J Mol Sci
; 21(12)2020 Jun 22.
Artigo
em Inglês
| MEDLINE | ID: mdl-32580284
5.
The molecular mechanisms of a high Ca2+-sensitivity and muscle weakness associated with the Ala155Thr substitution in Tpm3.12.
Biochem Biophys Res Commun
; 515(2): 372-377, 2019 07 23.
Artigo
em Inglês
| MEDLINE | ID: mdl-31155291
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.
Biochem Biophys Res Commun
; 502(2): 209-214, 2018 07 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-29792862
7.
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.
Arch Biochem Biophys
; 644: 17-28, 2018 04 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-29510086
8.
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.
Int J Mol Sci
; 19(12)2018 Dec 10.
Artigo
em Inglês
| MEDLINE | ID: mdl-30544720
9.
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.
Biochem Biophys Res Commun
; 494(3-4): 681-686, 2017 12 16.
Artigo
em Inglês
| MEDLINE | ID: mdl-29097206
10.
Deviations in conformational rearrangements of thin filaments and myosin caused by the Ala155Thr substitution in hydrophobic core of tropomyosin.
Biochim Biophys Acta Proteins Proteom
; 1865(12): 1790-1799, 2017 Dec.
Artigo
em Inglês
| MEDLINE | ID: mdl-28939420
11.
Aberrant movement of ß-tropomyosin associated with congenital myopathy causes defective response of myosin heads and actin during the ATPase cycle.
Arch Biochem Biophys
; 577-578: 11-23, 2015 Jul.
Artigo
em Inglês
| MEDLINE | ID: mdl-25978979
12.
Molecular mechanisms of dysfunction of muscle fibres associated with Glu139 deletion in TPM2 gene.
Sci Rep
; 7(1): 16797, 2017 12 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-29196649