Micro-mechanical response and power-law exponents from the longitudinal fluctuations of F-actin solutions

Autor: Pablo Domínguez-García, Jose R. Pinto, Ana Akrap, Sylvia Jeney

Publikováno v: Soft Matter. 19:3652-3660

We investigate the local fluctuations of filamentous actin (F-actin), with a focus on the skeletal thin filament, using single-particle optical trapping interferometry.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8a6200e23af420f7ac99a090cf4c774c
https://doi.org/10.1039/d2sm01445a

Amide hydrogens reveal a temperature-dependent structural transition that enhances site-II Ca2+-binding affinity in a C-domain mutant of cardiac troponin C

Autor: Tiago Veltri, Guilherme A. P. de Oliveira, Ewa A. Bienkiewicz, Fernando L. Palhano, Mayra de A. Marques, Adolfo H. Moraes, Jerson L. Silva, Martha M. Sorenson, Jose R. Pinto

Publikováno v: Scientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)

Abstract The hypertrophic cardiomyopathy-associated mutant D145E, in cardiac troponin C (cTnC) C-domain, causes generalised instability at multiple sites in the isolated protein. As a result, structure and function of the mutant are more susceptible

Externí odkaz: https://doaj.org/article/24f869ff88314b1487e847a605d31809

Hypertrophic Cardiomyopathy Cardiac Troponin C Mutations Differentially Affect Slow Skeletal and Cardiac Muscle Regulation

Autor: Jose R. Pinto, Tiago Veltri, Maicon Landim-Vieira, Michelle S. Parvatiyar, David Gonzalez-Martinez, Karissa M. Dieseldorff Jones, Clara A. Michell, David Dweck, Andrew P. Landstrom, P. Bryant Chase

Publikováno v: Frontiers in Physiology, Vol 8 (2017)

Mutations in TNNC1—the gene encoding cardiac troponin C (cTnC)—that have been associated with hypertrophic cardiomyopathy (HCM) and cardiac dysfunction may also affect Ca2+-regulation and function of slow skeletal muscle since the same gene is ex

Externí odkaz: https://doaj.org/article/de0f01d82986440e8a1a28beedc74a76

Mutation location of HCM-causing troponin T mutations defines the degree of myofilament dysfunction in human cardiomyocytes

Autor: Jose R. Pinto, Maike Schuldt, Jiayi Pei, Jamie R. Johnston, Michelle Michels, Huan He, Jolanda van der Velden, Corrado Poggesi, Diederik W. D. Kuster, Magdalena Harakalova, Roy Huurman

Publikováno v: Journal of Molecular and Cellular Cardiology, 150, 77-90. Academic Press Inc.
Schuldt, M, Johnston, J R, He, H, Huurman, R, Pei, J, Harakalova, M, Poggesi, C, Michels, M, Kuster, D W D, Pinto, J R & van der Velden, J 2021, ' Mutation location of HCM-causing troponin T mutations defines the degree of myofilament dysfunction in human cardiomyocytes ', Journal of Molecular and Cellular Cardiology, vol. 150, pp. 77-90 . https://doi.org/10.1016/j.yjmcc.2020.10.006
Journal of Molecular and Cellular Cardiology, 150, 77-90. Academic Press

Background: The clinical outcome of hypertrophic cardiomyopathy patients is not only determined by the disease-causing mutation but influenced by a variety of disease modifiers. Here, we defined the role of the mutation location and the mutant protei

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c4902dc1d40840020e52ff33cf96d21
https://doi.org/10.1016/j.yjmcc.2020.10.006

Fluorescent Protein-Based Ca2+ Sensor Reveals Global, Divalent Cation-Dependent Conformational Changes in Cardiac Troponin C.

Autor: Myriam A Badr, Jose R Pinto, Michael W Davidson, P Bryant Chase

Publikováno v: PLoS ONE, Vol 11, Iss 10, p e0164222 (2016)

Cardiac troponin C (cTnC) is a key effector in cardiac muscle excitation-contraction coupling as the Ca2+ sensing subunit responsible for controlling contraction. In this study, we generated several FRET sensors for divalent cations based on cTnC fla

Externí odkaz: https://doaj.org/article/038d79cc8b144263a843d331a3061fee