Results 1 to 10 of about 86,589 (350)
Dynamics of a Troponin Chimera Reproduce the Effects of Calcium on the Troponin Complex [PDF]
Biophysical Journal, 2012 In striated muscle, contraction is regulated in a Ca2+-dependent manner by the three subunits of the troponin complex. Troponin I (TnI) inhibits actomyosin ATPase in the absence of calcium; Ca2+ binding to troponin C (TnC) causes conformational changes that alter the interaction between TnI and TnC, removing the inhibition. These conformational changes
Pascal Mercier +5 more
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Phosphorylation of the ‘37000 component’ of the troponin complex (troponin-T) [PDF]
Biochemical Journal, 1973 Most of the phosphorus present in the troponin complex, which on average contains 1 mol of P/80000g, is associated with the ‘37000 component’ (0.6mol of P/mol). The inhibitory protein and particularly the ‘37000 component’, but not the calcium-binding protein, were phosphorylated when incubated with phosphorylase b kinase and [γ-32P]ATP.
H. A. Cole, S. V. Perry
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An in silico analysis of troponin I mutations in hypertrophic cardiomyopathy of Indian origin. [PDF]
PLoS ONE, 2013 Hypertrophic Cardiomyopathy (HCM) is an autosomal dominant disorder of the myocardium which is hypertrophied resulting in arrhythmias and heart failure leading to sudden cardiac death (SCD).
Gayatri Ramachandran +6 more
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Troponin Variants as Markers of Skeletal Muscle Health and Diseases
Frontiers in Physiology, 2021 Ca2+-regulated contractility is a key determinant of the quality of muscles. The sarcomeric myofilament proteins are essential players in the contraction of striated muscles.
Monica Rasmussen +2 more
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Interaction of bepridil with the cardiac troponin C/troponin I complex [PDF]
FEBS Letters, 2001 We have investigated the binding of bepridil to calcium‐saturated cardiac troponin C in a cardiac troponin C/troponin I complex. Nuclear magnetic resonance spectroscopy and [15N,2H]cardiac troponin C permitted the mapping of bepridil‐induced amide proton chemical shifts. A single bepridil‐binding site in the regulatory domain was found with an affinity
Ekram Abusamhadneh +5 more
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Disease-related cardiac troponins alter thin filament Ca2+ association and dissociation rates. [PDF]
PLoS ONE, 2012 The contractile response of the heart can be altered by disease-related protein modifications to numerous contractile proteins. By utilizing an IAANS labeled fluorescent troponin C, [Formula: see text], we examined the effects of ten disease-related ...
Bin Liu +4 more
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Protein kinase C phosphomimetics alter thin filament Ca2+ binding properties. [PDF]
PLoS ONE, 2014 Adrenergic stimulation modulates cardiac function by altering the phosphorylation status of several cardiac proteins. The Troponin complex, which is the Ca(2+) sensor for cardiac contraction, is a hot spot for adrenergic phosphorylation. While the effect
Bin Liu +3 more
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Hypertrophic Cardiomyopathy Mutations of Troponin Reveal Details of Striated Muscle Regulation
Frontiers in Physiology, 2022 Striated muscle contraction is inhibited by the actin associated proteins tropomyosin, troponin T, troponin I and troponin C. Binding of Ca2+ to troponin C relieves this inhibition by changing contacts among the regulatory components and ultimately ...
J. M. Chalovich, L. Zhu, D. Johnson
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Frontiers in Physiology, 2022 Small molecule cardiac troponin activators could potentially enhance cardiac muscle contraction in the treatment of systolic heart failure. We designed a small molecule, RPI-194, to bind cardiac/slow skeletal muscle troponin (Cardiac muscle and slow ...
Zabed Mahmud +13 more
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Monoclonal Antibodies as Probes to Study Ligand-Induced Conformations of Troponin Subunits
Frontiers in Physiology, 2022 Striated muscle contraction and relaxation is regulated by Ca2+ at the myofilament level via conformational modulations of the troponin complex. To understand the structure–function relationship of troponin in normal muscle and in myopathies, it is ...
Monica Rasmussen +2 more
doaj +1 more source