Results 131 to 140 of about 19,605,718 (146)
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Gene, 2000
Two cDNAs encoding troponin C (TnC) isoforms are isolated from the scallop, Patinopecten yessoensis, striated adductor muscle. The sequential differences between these isoforms, named TnC(long) and TnC(short), are restricted in several residues of the C-terminal region. TnC(long) is commonly expressed in both the striated and the smooth adductor muscle;
Hajime J. Yuasa, Takashi Takagi
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Two cDNAs encoding troponin C (TnC) isoforms are isolated from the scallop, Patinopecten yessoensis, striated adductor muscle. The sequential differences between these isoforms, named TnC(long) and TnC(short), are restricted in several residues of the C-terminal region. TnC(long) is commonly expressed in both the striated and the smooth adductor muscle;
Hajime J. Yuasa, Takashi Takagi
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Calcium-induced flexibility changes in the troponin C–troponin I complex
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000The contraction of vertebrate striated muscle is modulated by Ca(2+) binding to the regulatory protein troponin C (TnC). Ca(2+) binding causes conformational changes in TnC which alter its interaction with the inhibitory protein troponin I (TnI), initiating the regulatory process.
John H. Collins+9 more
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Biochemistry, 2008
NMR spectroscopy has been employed to elucidate the molecular consequences of the DCM G159D mutation on the structure and dynamics of troponin C, and its interaction with troponin I (TnI).
O. Baryshnikova+3 more
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NMR spectroscopy has been employed to elucidate the molecular consequences of the DCM G159D mutation on the structure and dynamics of troponin C, and its interaction with troponin I (TnI).
O. Baryshnikova+3 more
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The Role of Electrostatics in the Interaction of the Inhibitory Region of Troponin I with Troponin C
Biochemistry, 2005We have addressed the electrostatic interactions occurring between the inhibitory region of cardiac troponin I with the C-lobe of troponin C using scanning glycine mutagenesis of the inhibitory region. We report variations in the electric potentials due to mutation of charged residues within this complex based upon the solved NMR structure (1OZS ...
Brian D. Sykes+4 more
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Determination of the complete amino acid sequence of bovine cardiac troponin C.
, 1976: The amino acid sequence of bovine cardiac troponin C has been completely determined. The protein was cleaved by cyanogen bromide and the resulting peptides were isolated.
J. P. Eerd, Kenji Takahashi
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Australian and New Zealand journal of psychiatry (Print), 2015
K. Ronaldson, P. Fitzgerald, J. McNeil
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K. Ronaldson, P. Fitzgerald, J. McNeil
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Troponin C — Troponin I Interactions and Molecular Signalling in Cardiac Myofilaments
1995This chapter describes a current perception of the molecular interactions regulating myofilament activity in heart cells. The focus is on the interaction between troponin-C (TnC), the Ca(2+)-receptor and troponin I (TnI), an inhibitory protein. It is this interaction that appears to form a molecular switch that turns on the thin filament.
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