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Troponin C type 2

skeletal troponin C
Top mentioned proteins: Tenascin, FasT, ACID, CAN, HAD
Papers on skeletal troponin C
Kinetic mechanism of Ca²⁺-controlled changes of skeletal troponin I in psoas myofibrils.
Stehle et al., Köln, Germany. In Biophys J, 2012
Modeling reveals that the fast conformational change can occur after the first Ca(2+) ion binds to skeletal troponin C (sTnC), whereas the slower change requires Ca(2+) binding to both regulatory sites of sTnC.
Measurement of calcium dissociation rates from troponin C in rigor skeletal myofibrils.
Davis et al., Columbus, United States. In Front Physiol, 2010
Chicken skeletal troponin C fluorescently labeled at Cys 101, troponin C(IAEDANS), reported Ca(2+) dissociation exclusively from the structural domain of troponin C at ∼0.37, 0.06, and 0.07/s in isolation, in the presence of troponin I and in myofibrils at 15°C, respectively.
Molecular characterization, expression profile and polymorphisms of the porcine TNNC2 gene.
Zhong et al., Guangzhou, China. In Hereditas, 2008
Fast skeletal troponin C (TNNC2) plays a key role in the regulation of muscle contraction, and modulates the Ca2+-activation characteristics of muscle fibers.
Fast pressure jumps can perturb calcium and magnesium binding to troponin C F29W.
Geeves et al., Canterbury, United Kingdom. In Biochemistry, 2008
We have used rapid pressure jump and stopped-flow fluorometry to investigate calcium and magnesium binding to F29W chicken skeletal troponin C. Increased pressure perturbed calcium binding to the N-terminal sites in the presence and absence of magnesium and provided an estimate for the volume change upon calcium binding (-12 mL/mol).
Thin filament Ca2+ binding properties and regulatory unit interactions alter kinetics of tension development and relaxation in rabbit skeletal muscle.
Regnier et al., Seattle, United States. In J Physiol, 2008
Native skeletal troponin C (sTnC) was replaced with sTnC mutants having altered Ca(2+) dissociation rates (k(off)) or with mixtures of sTnC and D28A, D64A sTnC, that does not bind Ca(2+) at sites I and II (xxsTnC), to reduce near-neighbour regulatory unit (RU) interactions.
Differential effects of a green tea-derived polyphenol (-)-epigallocatechin-3-gallate on the acidosis-induced decrease in the Ca(2+) sensitivity of cardiac and skeletal muscle.
Hsieh et al., T'ai-chung-shih, Taiwan. In Pflugers Arch, 2008
Studies on recombinant mouse cardiac troponin C (cTnC) and chicken fast skeletal troponin C (sTnC) using circular dichroism and intrinsic and extrinsic fluorescence spectroscopy showed that EGCg bound to cTnC with a dissociation constant of approximately 3-4 muM, but did not bind to sTnC.
NMR studies of the dynamics of a bifunctional rhodamine probe attached to troponin C.
Sykes et al., Edmonton, Canada. In J Am Chem Soc, 2008
We previously determined the structure of the N-domain of chicken skeletal troponin C, BR-labeled on the C helix, in complex with the switch region of troponin I, and demonstrated that the probe does not perturb the structure or dynamics of the protein.
Influence of enhanced troponin C Ca2+-binding affinity on cooperative thin filament activation in rabbit skeletal muscle.
Regnier et al., Seattle, United States. In J Physiol, 2007
We studied how enhanced skeletal troponin C (sTnC) Ca2+-binding affinity affects cooperative thin filament activation and contraction in single demembranated rabbit psoas fibres.
[Cloning and expression of the pig fast skeletal muscle troponin C gene].
Li et al., Guangzhou, China. In Yi Chuan, 2006
In silico cloning obtained a 843 bp sequence which we named pig fast skeletal troponin C gene (TNNC2).
Calcium-dependent changes in the flexibility of the regulatory domain of troponin C in the troponin complex.
Sykes et al., Edmonton, Canada. In J Biol Chem, 2005
We used NMR techniques to study the backbone dynamics of skeletal troponin C (TnC) in the complex.
Using lanthanide ions to align troponin complexes in solution: order of lanthanide occupancy in cardiac troponin C.
Sykes et al., Edmonton, Canada. In Protein Sci, 2004
Two-dimensional [(1)H, (15)N] HSQC NMR spectroscopy has been used to examine the binding order of Ce(3+), Tb(3+), and Yb(3+) to both apo- and holo-forms of human cardiac troponin C (cTnC) and of Ce(3+) to holo-chicken skeletal troponin C (sTnC).
Inhibitory profile of nonapeptide derived from porcine troponin C against angiotensin I-converting enzyme.
Muguruma et al., Takatsuki, Japan. In J Agric Food Chem, 2004
A novel angiotensin I-converting enzyme (ACE) inhibitory peptide (RMLGQTPTK; 9mer) from porcine skeletal troponin C was investigated for its inhibitory profile.
Calcium binding to troponin C as a primary step of the regulation of contraction. A microcalorimetric approach.
Yamada, Ōita, Japan. In Adv Exp Med Biol, 2002
There is a good agreement between the results of the calorimetric and the structural studies in frog and chicken skeletal troponin C. In both species one of the N-terminal low-affinity Ca-sites is the "active" Ca site regulating muscle contraction.
Thermodynamic analyses of calcium binding to troponin C, calmodulin and parvalbumins by using microcalorimetry.
Yamada, Ōita, Japan. In Mol Cell Biochem, 1999
Two high-affinity sites of rabbit skeletal troponin C are distinguishable in terms of their affinity to calcium and associated enthalpy changes.
Molecular basis for the influence of muscle length on myocardial performance.
Gulati et al., United States. In Science, 1988
To seek the molecular explanation of this effect, a study was made of the effects of length on Ca2+ sensitivity during tension development by isolated demembranated cardiac muscle in which the cardiac form of troponin C was substituted with skeletal troponin C. The results of troponin C exchange were compared at sarcomere lengths of 1.9 and 2.4 micrometers.
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