Detalhe da pesquisa
1.
CalTrack: High-Throughput Automated Calcium Transient Analysis in Cardiomyocytes.
Circ Res
; 129(2): 326-341, 2021 07 09.
Artigo
Inglês
| MEDLINE | ID: mdl-34018815
2.
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
Inglês
| MEDLINE | ID: mdl-36982903
3.
Genetics Matters: Voyaging from the Past into the Future of Humanity and Sustainability.
Int J Mol Sci
; 23(7)2022 Apr 02.
Artigo
Inglês
| MEDLINE | ID: mdl-35409335
4.
Myosin Sequestration Regulates Sarcomere Function, Cardiomyocyte Energetics, and Metabolism, Informing the Pathogenesis of Hypertrophic Cardiomyopathy.
Circulation
; 141(10): 828-842, 2020 03 10.
Artigo
Inglês
| MEDLINE | ID: mdl-31983222
5.
Measurement of Myofilament-Localized Calcium Dynamics in Adult Cardiomyocytes and the Effect of Hypertrophic Cardiomyopathy Mutations.
Circ Res
; 124(8): 1228-1239, 2019 04 12.
Artigo
Inglês
| MEDLINE | ID: mdl-30732532
6.
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
Inglês
| MEDLINE | ID: mdl-34204776
7.
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
Inglês
| MEDLINE | ID: mdl-31864708
8.
Looking for Targets to Restore the Contractile Function in Congenital Myopathy Caused by Gln147Pro Tropomyosin.
Int J Mol Sci
; 21(20)2020 Oct 14.
Artigo
Inglês
| MEDLINE | ID: mdl-33066566
9.
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
Inglês
| MEDLINE | ID: mdl-32580284
10.
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
Inglês
| MEDLINE | ID: mdl-31155291
11.
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
Inglês
| MEDLINE | ID: mdl-29792862
12.
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
Inglês
| MEDLINE | ID: mdl-30544720
13.
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.
Biochim Biophys Acta
; 1864(3): 260-267, 2016 Mar.
Artigo
Inglês
| MEDLINE | ID: mdl-26708479
14.
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
Inglês
| MEDLINE | ID: mdl-29097206
15.
Mutations in troponin T associated with Hypertrophic Cardiomyopathy increase Ca(2+)-sensitivity and suppress the modulation of Ca(2+)-sensitivity by troponin I phosphorylation.
Arch Biochem Biophys
; 601: 113-20, 2016 07 01.
Artigo
Inglês
| MEDLINE | ID: mdl-27036851
16.
Does extracellular cardiac troponin I play a pathogenic role independently of autoantibodies?
Clin Sci (Lond)
; 130(24): 2277-2278, 2016 Dec 01.
Artigo
Inglês
| MEDLINE | ID: mdl-30897547
17.
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
Inglês
| MEDLINE | ID: mdl-25978979
18.
The E117K mutation in ß-tropomyosin disturbs concerted conformational changes of actomyosin in muscle fibers.
Arch Biochem Biophys
; 549: 12-6, 2014 May 01.
Artigo
Inglês
| MEDLINE | ID: mdl-24657080
19.
Gly126Arg substitution causes anomalous behaviour of α-skeletal and ß-smooth tropomyosins during the ATPase cycle.
Arch Biochem Biophys
; 543: 57-66, 2014 Feb 01.
Artigo
Inglês
| MEDLINE | ID: mdl-24374033
20.
The effect of the Asp175Asn and Glu180Gly TPM1 mutations on actin-myosin interaction during the ATPase cycle.
Biochim Biophys Acta
; 1824(2): 366-73, 2012 Feb.
Artigo
Inglês
| MEDLINE | ID: mdl-22155441