The intrinsically disordered C terminus of troponin T binds to troponin C to modulate myocardial force generation

Aberrant regulation of myocardial force production represents an early biomechanical defect associated with sarcomeric cardiomyopathies, but the molecular mechanisms remain poorly defined. Here, we evaluated the pathogenicity of a previously unreported sarcomeric gene variant identified in a pediatr...

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Veröffentlicht in:	The Journal of biological chemistry 2019-12, Vol.294 (52), p.20054-20069
Hauptverfasser:	Johnston, Jamie R., Landim-Vieira, Maicon, Marques, Mayra A., de Oliveira, Guilherme A.P., Gonzalez-Martinez, David, Moraes, Adolfo H., He, Huan, Iqbal, Anwar, Wilnai, Yael, Birk, Einat, Zucker, Nili, Silva, Jerson L., Chase, P. Bryant, Pinto, Jose Renato
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites Calcium - metabolism cardiac muscle cardiomyopathy Cardiomyopathy, Dilated - metabolism Cardiomyopathy, Dilated - pathology cardiovascular disease contractile protein cross-bridges Female Humans Male Molecular Bases of Disease Mutagenesis, Site-Directed Myocardial Contraction Myocardium - metabolism Myofibrils - physiology NMR Nuclear Magnetic Resonance, Biomolecular Pedigree Protein Binding Protein Domains protein dynamic Protein Structure, Secondary structure–function troponin Troponin C - chemistry Troponin C - metabolism Troponin T - chemistry Troponin T - genetics Troponin T - metabolism
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