The C-terminus of troponin T is essential for maintaining the inactive state of regulated actin.
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[1] L. Leinwand,et al. Identification of functional differences between recombinant human α and β cardiac myosin motors , 2012, Cellular and Molecular Life Sciences.
[2] S. Ishiwata,et al. The role of tropomyosin domains in cooperative activation of the actin-myosin interaction. , 2011, Journal of molecular biology.
[3] J. Chalovich,et al. Acrylodan-labeled smooth muscle tropomyosin reports differences in the effects of troponin and caldesmon in the transition from the active state to the inactive state. , 2011, Biochemistry.
[4] J. Tardiff. Thin Filament Mutations: Developing an Integrative Approach to a Complex Disorder , 2011, Circulation research.
[5] R. Solaro,et al. Protein Phosphorylation and Signal Transduction in Cardiac Thin Filaments* , 2011, The Journal of Biological Chemistry.
[6] J. Chalovich,et al. Molecular Dynamics Studies on Troponin (Tnl-TnT-TnC) Complexes: Insight into the Regulation of Muscle Contraction , 2010, Journal of biomolecular structure & dynamics.
[7] J. Jin,et al. Localization of the two tropomyosin-binding sites of troponin T. , 2010, Archives of biochemistry and biophysics.
[8] J. Chalovich,et al. Kinetics of regulated actin transitions measured by probes on tropomyosin. , 2010, Biophysical journal.
[9] J. Chalovich,et al. Some cardiomyopathy-causing troponin I mutations stabilize a functional intermediate actin state. , 2009, Biophysical journal.
[10] J. Chalovich,et al. Negative charges at protein kinase C sites of troponin I stabilize the inactive state of actin. , 2008, Biophysical journal.
[11] Takuo Yasunaga,et al. Structural basis for calcium-regulated relaxation of striated muscles at interaction sites of troponin with actin and tropomyosin. , 2007, Advances in experimental medicine and biology.
[12] R. Solaro,et al. Increased Ca2+ Affinity of Cardiac Thin Filaments Reconstituted with Cardiomyopathy-related Mutant Cardiac Troponin I* , 2006, Journal of Biological Chemistry.
[13] M. Tanokura,et al. Structural basis for Ca2+-regulated muscle relaxation at interaction sites of troponin with actin and tropomyosin. , 2005, Journal of molecular biology.
[14] M. Miki,et al. The Rates of Switching Movement of Troponin T between Three States of Skeletal Muscle Thin Filaments Determined by Fluorescence Resonance Energy Transfer* , 2005, Journal of Biological Chemistry.
[15] P. Chase,et al. The Delta 14 mutation of human cardiac troponin T enhances ATPase activity and alters the cooperative binding of S1-ADP to regulated actin. , 2004, Biochemistry.
[16] L. Leinwand,et al. Expression of cardiac troponin T with COOH-terminal truncation accelerates cross-bridge interaction kinetics in mouse myocardium. , 2004, American journal of physiology. Heart and circulatory physiology.
[17] M. Tyska,et al. A 7-amino-acid insert in the heavy chain nucleotide binding loop alters the kinetics of smooth muscle myosin in the laser trap , 1998, Journal of Muscle Research & Cell Motility.
[18] B. Sykes,et al. Structural based insights into the role of troponin in cardiac muscle pathophysiology , 2004, Journal of Muscle Research & Cell Motility.
[19] Yuichiro Maéda,et al. Structure of the core domain of human cardiac troponin in the Ca2+-saturated form , 2003, Nature.
[20] J. Stephens,et al. Troponin-tropomyosin: an allosteric switch or a steric blocker? , 2002, Biophysical journal.
[21] J. Tardiff,et al. Cardiac troponin T mutations: correlation between the type of mutation and the nature of myofilament dysfunction in transgenic mice , 2001, The Journal of physiology.
[22] H. Watkins,et al. Investigation of a truncated cardiac troponin T that causes familial hypertrophic cardiomyopathy: Ca(2+) regulatory properties of reconstituted thin filaments depend on the ratio of mutant to wild-type protein. , 2000, Circulation research.
[23] T. Hewett,et al. A truncated cardiac troponin T molecule in transgenic mice suggests multiple cellular mechanisms for familial hypertrophic cardiomyopathy. , 1998, The Journal of clinical investigation.
[24] B. Malnic,et al. Regulatory Properties of the NH2- and COOH-terminal Domains of Troponin T , 1998, The Journal of Biological Chemistry.
[25] B. Brenner,et al. Parallel inhibition of active force and relaxed fiber stiffness by caldesmon fragments at physiological ionic strength and temperature conditions: additional evidence that weak cross-bridge binding to actin is an essential intermediate for force generation. , 1995, Biophysical journal.
[26] M. Geeves,et al. Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. , 1993, Biophysical journal.
[27] E. Eisenberg,et al. Cooperative turning on of myosin subfragment 1 adenosinetriphosphatase activity by the troponin-tropomyosin-actin complex. , 1988, Biochemistry.
[28] J. Potter,et al. Calcium-insensitive binding of heavy meromyosin to regulated actin at physiological ionic strength. , 1985, The Journal of biological chemistry.
[29] E. Morris,et al. Troponin-tropomyosin interactions. Fluorescence studies of the binding of troponin, troponin T, and chymotryptic troponin T fragments to specifically labeled tropomyosin. , 1984, Biochemistry.
[30] R. F. Siemankowski,et al. Kinetics of the interaction between actin, ADP, and cardiac myosin-S1. , 1984, The Journal of biological chemistry.
[31] M. Tanokura,et al. Chymotryptic subfragments of troponin T from rabbit skeletal muscle. Interaction with tropomyosin, troponin I and troponin C. , 1983, Journal of biochemistry.
[32] E. Eisenberg,et al. Inhibition of actomyosin ATPase activity by troponin-tropomyosin without blocking the binding of myosin to actin. , 1982, The Journal of biological chemistry.
[33] J. Potter. [22] Preparation of troponin and its subnits , 1982 .
[34] J. Potter. Preparation of troponin and its subunits. , 1982, Methods in enzymology.
[35] L. Smillie. Preparation and identification of alpha- and beta-tropomyosins. , 1982, Methods in enzymology.
[36] T. L. Hill,et al. Theoretical models for cooperative steady-state ATPase activity of myosin subfragment-1 on regulated actin. , 1981, Biophysical journal.
[37] L. Smillie,et al. Identification of a second binding region on rabbit skeletal troponin-T for alpha-tropomyosin. , 1981, FEBS letters.
[38] E. Taylor,et al. Kinetic studies of the cooperative binding of subfragment 1 to regulated actin. , 1980, Proceedings of the National Academy of Sciences of the United States of America.
[39] E. Eisenberg,et al. Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex. , 1980, Proceedings of the National Academy of Sciences of the United States of America.
[40] R. F. Siemankowski,et al. Canine cardiac myosin with special reference to pressure overload cardiac hypertrophy. II. Myosin ATPase. , 1978, The Journal of biological chemistry.
[41] R. F. Siemankowski,et al. Canine cardiac myosin with special referrence to pressure overload cardiac hypertrophy. I. Subunit composition. , 1978, The Journal of biological chemistry.
[42] A. G. WEEDS,et al. Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin , 1975, Nature.
[43] E. Eisenberg,et al. Troponin-tropomyosin complex. Column chromatographic separation and activity of the three, active troponin components with and without tropomyosin present. , 1974, The Journal of biological chemistry.
[44] John M. Murray,et al. Manifestations of Cooperative Behavior in the Regulated Actin Filament during Actin-Activated ATP Hydrolysis in the Presence of Calcium , 1973 .
[45] J. Spudich,et al. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. , 1971, The Journal of biological chemistry.
[46] W. F. Harrington,et al. A model for the myosin molecule. , 1960, Biochimica et biophysica acta.