HCM and DCM mutations in thin filament proteins have opposite effects on regulation of contractility in vitro

HCM and DCM mutations in thin filament proteins have opposite effects on regulation of contractility in vitro

Номзүйн дэлгэрэнгүй
Үндсэн зохиолчид:	Redwood, C, Robinson, P, Mirza, M, Knott, A, Marston, S, Watkins, H
Формат:	Conference item
Хэвлэсэн:	2003

Ижил төстэй зүйлс

HCM and DCM mutations in cardiac thin filament proteins have opposite effects on the regulation of contractility in vitro
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Effects of DCM mutations in thin filament regulatory proteins on contractile function
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Mutations in tropomyosin that cause DCM, affect cooperativity of cardiac muscle thin filaments
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Two DCM mutations in cardiac tropomyosin alter thin filament function by different mechanisms
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Hypertrophic and dilated cardiomyopathycausing mutations of troponin and alpha-tropomyosin have opposite effects on thin filament calcium binding
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Dilated and hypertrophic cardiomyopathy mutations in troponin and alpha-tropomyosin have opposing effects on the calcium affinity of cardiac thin filaments.
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Dilated cardiomyopathy mutations in thin-filament regulatory proteins reduce contractility, suppress systolic Ca²⁺, and activate NFAT and Akt signaling
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Modulation of thin filament activation by breakdown or isoform switching of thin filament proteins: physiological and pathological implications.
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Dilated cardiomyopathy mutations in three thin filament regulatory proteins result in a common functional phenotype.
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Alterations in thin filament regulation induced by a human cardiac troponin T mutant that causes dilated cardiomyopathy are distinct from those induced by troponin T mutants that cause hypertrophic cardiomyopathy.
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The effect of HCM mutations in troponin T and troponin I on the calcium binding of human cardiac troponin
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Using fluorescence emission spectroscopy to asses the Ca2+ affinity of reconstituted troponin and thin filaments containing cardiomyopathy causing mutations of troponin and alpha-tropomyosin
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Mavacamten rescues increased myofilament calcium sensitivity and dysregulation of Ca2+ flux caused by thin filament hypertrophic cardiomyopathy mutations
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Interaction analyses elucidate the pathophysiology of HCM-causing missense mutations in cardiac myosin binding protein-C.
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Value of MRI derived parameters in the discrimination of familial left ventricular noncompaction (LVNC), DCM and HCM in comparison to healthy volunteers
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Functional investigation of troponin with the homozygous HCM mutation, TNNT2 K280N, obtained from an explanted heart
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Familial Dilated Cardiomyopathy Caused by an Alpha-Tropomyosin Mutation: The Distinctive Natural History of Sarcomeric DCM
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Cardiomyopathy-Causing Mutations in Thin Filament Regulatory Proteins Acutely Affeect Ca2+-Buffering and Ca2+-Dependent Signalling In Situ
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P123The rescue of Ca2+ cycling abnormalities conferred by HCM-causing mutations with analogues of the green tea polyphenol epigallocatechin-3-gallate.
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The HCM-associated cardiac Troponin T mutation K280N causes reduced responsiveness to protein kinase A
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Cardiomyopathy-causing mutations in cardiac thin filament regulatory proteins acutely affect Ca2+ buffering and Ca2+ dependant signalling in situ
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Comparison of the functional effects of mutations in troponin T which cause dilated and hypertrophic cardiomyopathies
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The nemaline myopathy-causing E117K mutation in β-tropomyosin reduces thin filament activation.
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Mutations in fast skeletal troponin I, troponin T and beta-tropomyosin that cause distal arthrogryposis all enhance thin filament activation
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A novel interaction between the C5 and C8 domains of myosin binding protein-C and its modulation by HCM mutations
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Investigation of a truncated cardiac troponin T that causes familial hypertrophic cardiomyopathy: Ca(2+) regulatory properties of reconstituted thin filaments depend on the ratio of mutant to wild-type protein.
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Patients with hypertrophic cardiomyopathy (HCM) and HCM gene carriers have attenuated myocardial oxygenation response to vasodilator stress - a potential mechanism for sudden cardiac death.
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Investigation of troponin I mutations causing familial hypertrophic cardiomyopathy
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