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How Do Mutations in Contractile Proteins Cause the Primary Familial Cardiomyopathies?

Journal of cardiovascular translational research, 2011-06, Vol.4 (3), p.245-255

Marston, Steven B.

2011

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Atomic model of the human cardiac muscle myosin filament

Proceedings of the National Academy of Sciences - PNAS, 2013-01, Vol.110 (1), p.318-323

2013

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Troponin phosphorylation and regulatory function in human heart muscle: Dephosphorylation of Ser23/24 on troponin I could account for the contractile defect in end-stage heart failure

Journal of molecular and cellular cardiology, 2007-01, Vol.42 (1), p.247-259

2007

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Approaches to High-Throughput Analysis of Cardiomyocyte Contractility

Frontiers in physiology, 2020-07, Vol.11, p.612-612

2020

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Molecular Defects in Cardiac Myofilament Ca2+-Regulation Due to Cardiomyopathy-Linked Mutations Can Be Reversed by Small Molecules Binding to Troponin

Frontiers in physiology, 2018-03, Vol.9, p.243-243

2018

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Modulation of Structure and Dynamics of Cardiac Troponin by Phosphorylation and Mutations Revealed by Molecular Dynamics Simulations

The journal of physical chemistry. B, 2023-10, Vol.127 (41), p.8736-8748

2023

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Author Correction: Abnormal contractility in human heart myofibrils from patients with dilated cardiomyopathy due to mutations in TTN and contractile protein genes

Scientific reports, 2018-09, Vol.8 (1), p.14485-2, Article 14485

2018

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A post-MI power struggle: adaptations in cardiac power occur at the sarcomere level alongside MyBP-C and RLC phosphorylation

American journal of physiology. Heart and circulatory physiology, 2016-08, Vol.311 (2), p.H465-H475

2016

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Modulation of cardiac thin filament structure by phosphorylated troponin-I analyzed by protein-protein docking and molecular dynamics simulation

Archives of biochemistry and biophysics, 2022-08, Vol.725, p.109282-109282, Article 109282

2022

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Investigations into the Sarcomeric Protein and Ca2+-Regulation Abnormalities Underlying Hypertrophic Cardiomyopathy in Cats (Felix catus)

Frontiers in physiology, 2017-06, Vol.8, p.348-348

2017

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Why Is there a Limit to the Changes in Myofilament Ca2+-Sensitivity Associated with Myopathy Causing Mutations?

Frontiers in physiology, 2016-09, Vol.7, p.415-415

Marston, Steven B.

2016

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Distinct hypertrophic cardiomyopathy genotypes result in convergent sarcomeric proteoform profiles revealed by top-down proteomics

Proceedings of the National Academy of Sciences - PNAS, 2020-10, Vol.117 (40), p.24691-24700

2020

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The use of phosphate-affinity SDS-PAGE to measure the cardiac troponin I phosphorylation site distribution in human heart muscle

Proteomics. Clinical applications, 2009-12, Vol.3 (12), p.1371-1382

2009

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The European Muscle Conference 2019 Special Issue

Journal of muscle research and cell motility, 2019-06, Vol.40 (2), p.67-67

2019

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Titin-truncating mutations associated with dilated cardiomyopathy alter length-dependent activation and its modulation via phosphorylation

Cardiovascular research, 2022-01, Vol.118 (1), p.241-253

2022

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Uncoupling of myofilament Ca2+ sensitivity from troponin I phosphorylation by mutations can be reversed by epigallocatechin-3-gallate

Cardiovascular research, 2015-10, Vol.108 (1), p.99-110

2015

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Familial dilated cardiomyopathy mutations uncouple troponin I phosphorylation from changes in myofibrillar Ca²⁺ sensitivity

Cardiovascular research, 2013-07, Vol.99 (1), p.65-73

2013

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Analysis of cardiac myosin binding protein-C phosphorylation in human heart muscle

Journal of molecular and cellular cardiology, 2010-12, Vol.49 (6), p.1003-1011

2010

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Troponin structure: its modulation by Ca2+ and phosphorylation studied by molecular dynamics simulations

Physical chemistry chemical physics : PCCP, 2016-08, Vol.18 (30), p.20691-20707

2016

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Troponin structure: its modulation by Ca(2+) and phosphorylation studied by molecular dynamics simulations

Physical chemistry chemical physics : PCCP, 2016-07, Vol.18 (30), p.20691-20707

2016

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The Importance of Intrinsically Disordered Segments of Cardiac Troponin in Modulating Function by Phosphorylation and Disease-Causing Mutations

Frontiers in physiology, 2016-11, Vol.7, p.508-508

2016

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Mutations in troponin T associated with Hypertrophic Cardiomyopathy increase Ca(2+)-sensitivity and suppress the modulation of Ca(2+)-sensitivity by troponin I phosphorylation

Archives of biochemistry and biophysics, 2016-07, Vol.601, p.113

2016

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The homozygous K280N troponin T mutation alters cross-bridge kinetics and energetics in human HCM

The Journal of general physiology, 2019-01, Vol.151 (1), p.18-29

2019

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The flexibility of two tropomyosin mutants, D175N and E180G, that cause hypertrophic cardiomyopathy

Biochemical and biophysical research communications, 2012-08, Vol.424 (3), p.493-496

2012

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Troponin phosphorylation and myofilament Ca2+ -sensitivity in heart failure: Increased or decreased?

Journal of molecular and cellular cardiology, 2008-11, Vol.45 (5), p.603-607

2008

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How Do Mutations in Contractile Proteins Cause the Primary Familial Cardiomyopathies?

Atomic model of the human cardiac muscle myosin filament

Troponin phosphorylation and regulatory function in human heart muscle: Dephosphorylation of Ser23/24 on troponin I could account for the contractile defect in end-stage heart failure

Approaches to High-Throughput Analysis of Cardiomyocyte Contractility

Molecular Defects in Cardiac Myofilament Ca2+-Regulation Due to Cardiomyopathy-Linked Mutations Can Be Reversed by Small Molecules Binding to Troponin

Modulation of Structure and Dynamics of Cardiac Troponin by Phosphorylation and Mutations Revealed by Molecular Dynamics Simulations

Author Correction: Abnormal contractility in human heart myofibrils from patients with dilated cardiomyopathy due to mutations in TTN and contractile protein genes

A post-MI power struggle: adaptations in cardiac power occur at the sarcomere level alongside MyBP-C and RLC phosphorylation

Modulation of cardiac thin filament structure by phosphorylated troponin-I analyzed by protein-protein docking and molecular dynamics simulation

Investigations into the Sarcomeric Protein and Ca2+-Regulation Abnormalities Underlying Hypertrophic Cardiomyopathy in Cats (Felix catus)

Why Is there a Limit to the Changes in Myofilament Ca2+-Sensitivity Associated with Myopathy Causing Mutations?

Distinct hypertrophic cardiomyopathy genotypes result in convergent sarcomeric proteoform profiles revealed by top-down proteomics

The use of phosphate-affinity SDS-PAGE to measure the cardiac troponin I phosphorylation site distribution in human heart muscle

The European Muscle Conference 2019 Special Issue

Titin-truncating mutations associated with dilated cardiomyopathy alter length-dependent activation and its modulation via phosphorylation

Uncoupling of myofilament Ca2+ sensitivity from troponin I phosphorylation by mutations can be reversed by epigallocatechin-3-gallate

Familial dilated cardiomyopathy mutations uncouple troponin I phosphorylation from changes in myofibrillar Ca²⁺ sensitivity

Analysis of cardiac myosin binding protein-C phosphorylation in human heart muscle

Troponin structure: its modulation by Ca2+ and phosphorylation studied by molecular dynamics simulations

Troponin structure: its modulation by Ca(2+) and phosphorylation studied by molecular dynamics simulations

The Importance of Intrinsically Disordered Segments of Cardiac Troponin in Modulating Function by Phosphorylation and Disease-Causing Mutations

Mutations in troponin T associated with Hypertrophic Cardiomyopathy increase Ca(2+)-sensitivity and suppress the modulation of Ca(2+)-sensitivity by troponin I phosphorylation

The homozygous K280N troponin T mutation alters cross-bridge kinetics and energetics in human HCM

The flexibility of two tropomyosin mutants, D175N and E180G, that cause hypertrophic cardiomyopathy

Troponin phosphorylation and myofilament Ca2+ -sensitivity in heart failure: Increased or decreased?

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