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Desensitization of the Cardiac Troponin Complex by TnI Phosphorylation and Epigallocatechin-3-Gallate. [PDF]
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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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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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Troponin T fragments: Physical properties and binding to troponin C
Canadian Journal of Biochemistry, 1978Fragments derived from rabbit skeletal troponin T (Tn-T) were tested for binding on a troponin C (Tn-C) – Sepharose affinity column in order to locate the binding site of Tn-C on Tn-T. The COOH-terminal fragments P2 (residues 159–209) and B2 (residues 206–258) were found to bind most strongly, confirming the earlier proposal (Pearlstone, J.
J R, Pearlstone, L B, Smillie
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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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