Results 191 to 200 of about 18,693,880 (254)
JDDG: Journal der Deutschen Dermatologischen Gesellschaft, EarlyView.
Yenny Angela +6 more
wiley +1 more source
NMR analysis of cardiac troponin C-troponin I complexes: effects of phosphorylation [PDF]
FEBS Letters, 1999 Phosphorylation of the cardiac specific amino-terminus of troponin I has been demonstrated to reduce the Ca2+ affinity of the cardiac troponin C regulatory site.
Vadim Gaponenko +2 more
exaly +2 more sources
Gene, 2015 In striated muscle, the protein troponin complex turns contraction on and off in a calcium-dependent manner. The calcium-sensing component of the complex is troponin C, which is expressed from the TNNC1 gene in both cardiac muscle and slow-twitch ...
Peter Hwang, Mónica X Li
exaly +2 more sources
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Biochemistry, 1992
We have quantitated the interactions of two rabbit skeletal troponin C fragments with troponin I and the troponin I inhibitory peptide. The calcium binding properties of the fragments and the ability of the fragments to exert control in the regulated actomyosin ATPase assay have also been studied. The N- and C-terminal divalent metal binding domains of
C A, Swenson, R S, Fredricksen
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We have quantitated the interactions of two rabbit skeletal troponin C fragments with troponin I and the troponin I inhibitory peptide. The calcium binding properties of the fragments and the ability of the fragments to exert control in the regulated actomyosin ATPase assay have also been studied. The N- and C-terminal divalent metal binding domains of
C A, Swenson, R S, Fredricksen
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Biochimica et Biophysica Acta (BBA) - Protein Structure, 1980
The stability of the structure of troponin C (calcium-binding components of troponin from rabbit skeletal muscle) has been studied by the scanning microcalorimetry method. It has been shows that: 1. In the presence of divalent ions the protein structure is represented by two practically independent cooperative blocks, one of which contains Ca2 ...
T N, Tsalkova, P L, Privalov
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The stability of the structure of troponin C (calcium-binding components of troponin from rabbit skeletal muscle) has been studied by the scanning microcalorimetry method. It has been shows that: 1. In the presence of divalent ions the protein structure is represented by two practically independent cooperative blocks, one of which contains Ca2 ...
T N, Tsalkova, P L, Privalov
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Nature, 1975
THE tropomyosin–troponin complex renders actomyosin from vertebrate skeletal muscle calcium sensitive. Troponin itself consists of three subunits: troponin I (TNI), troponin C (TNC) and troponin T (TNT)1. Pure TNI (24,000-dalton subunit) inhibits the actin–myosin interaction irrespective of calcium concentration.
R, Fine, W, Lehman, J, Head, A, Blitz
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THE tropomyosin–troponin complex renders actomyosin from vertebrate skeletal muscle calcium sensitive. Troponin itself consists of three subunits: troponin I (TNI), troponin C (TNC) and troponin T (TNT)1. Pure TNI (24,000-dalton subunit) inhibits the actin–myosin interaction irrespective of calcium concentration.
R, Fine, W, Lehman, J, Head, A, Blitz
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The mobility of troponin C and troponin I in muscle
Journal of Molecular Recognition, 1997In vertebrate skeletal muscle, contraction is initiated by the elevation of the intracellular Ca2+ concentration. The binding of Ca2+ to TnC induces a series of conformational changes which ultimately release the inhibition of the actomyosin ATPase activity by Tnl.
H C, Li, K, Hideg, P G, Fajer
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Calmodulin as a model for troponin C
Biochemical and Biophysical Research Communications, 1980Abstract We have investigated the ability of calmodulin to replace troponin-C in the troponin complex. Unlike troponin-C, calmodulin is able to confer Ca 2+ -sensitivity on the actin-activated myosin subfragment-1 ATPase of filaments containing actin, tropomyosin and troponin-I in the absence of troponin-T. Gel electrophoresis of the supernatants and
CASTELLANI, Loriana +2 more
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Defining the Region of Troponin-I that Binds to Troponin-C
Biochemistry, 1999The kinetics and energetics of the binding of three troponin-I peptides, corresponding to regions 96-131 (TnI96-131), 96-139 (TnI96-139), and 96-148 (TnI96-148), to skeletal chicken troponin-C were investigated using multinuclear, multidimensional NMR spectroscopy.
R T, McKay +4 more
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