Results 321 to 330 of about 19,667,204 (333)
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Activation of troponin C by Cd2+ and Pb2+

Archives of Toxicology, 1990
Certain heavy metal actions such as Cd2+ and Pb2+ mimic Ca2+ effectively in stimulating calmodulin (CaM). We now show that these cations also activate skeletal muscle troponin C (TnC), a Ca2(+)-binding protein highly homologous to CaM. Like Ca2+, these cations allow TnC to alter its electrophoretic mobility on polyacrylamide gels, and to bind to phenyl-
Sheng-Hao Chao   +3 more
openaire   +3 more sources

Chymotryptic subfragments of troponin T from rabbit skeletal muscle. Interaction with tropomyosin, troponin I and troponin C.

Journal of Biochemistry (Tokyo), 1983
The binding of the chymotryptic troponin T subfragments to tropomyosin, troponin I, and troponin C was semiquantitatively examined by using affinity chromatography, and also by co-sedimentation with F-actin and polyacrylamide gel electrophoresis in 14 mM
M. Tanokura   +3 more
semanticscholar   +1 more source

Binding of lanthanide ions to troponin C

Biochemistry, 1981
Tb3+ and Eu3+ bound to troponin C were detected by (1) changes in the fluorescence of the tyrosine chromophore of the protein or (2) the luminescence of the ions themselves excited by energy transfer from the protein or by direct excitation using a pulsed laser light source [Horrocks, W. DeW., Jr., & Sudnick, D. R. (1979) Science (Washington, D.C.) 206,
John Gergely   +3 more
openaire   +3 more sources

Interaction of a troponin I inhibitory peptide with both domains of troponin C

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1996
Skeletal muscle contraction is regulated by Ca2+ binding to troponin (Tn), a complex of three proteins attached to the actin-tropomyosin filaments. We have been investigating key interactions of the Ca(2+)-binding protein TnC and the inhibitory protein TnI.
John H. Collins   +2 more
openaire   +3 more sources

ASYNCHRONICITY: A JOB FOR TROPONIN C

Journal of Experimental Biology, 2003
![Figure][1] The high wing-beat frequencies of many insect species allows them to fly with remarkable precision, land virtually anywhere (sometimes upside down) and even hover! The key to their flying skills lies in the asynchronous flight muscle, a peculiar type of muscle exclusive to ...
openaire   +2 more sources

Familial hypertrophic cardiomyopathy-related cardiac troponin C mutation L29Q affects Ca2+ binding and myofilament contractility.

Physiological Genomics, 2008
The cardiac troponin C (cTnC) mutation, L29Q, has been found in a patient with familial hypertrophic cardiomyopathy. We previously showed that L29, together with neighboring residues, Asp2, Val28, and Gly30, plays an important role in determining the Ca ...
B. Liang   +7 more
semanticscholar   +1 more source

Comparison of the Kinetic Properties of Troponin-C and Dansylaziridine-Labeled Troponin-C1

The Journal of Biochemistry, 1980
Comparison of the kinetic properties of troponin-C and dansylaziridine-labeled troponin-C revealed that the calcium ion binding and removal reactions with the low affinity Ca2+-binding sites (sites I and II) and the resultant local conformational change are rapid processes, and that the calcium ion binding and removal reactions with the high affinity ...
Hiroshi Kondo, Takayoshi Iio
openaire   +3 more sources

Molecular Dynamics and Docking Studies on Cardiac Troponin C

Journal of Biomolecular Structure and Dynamics, 2011
Jayson F. Varughese, Yumin Li
semanticscholar   +1 more source

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