Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution
暂无分享,去创建一个
[1] R. Kretsinger,et al. Carp muscle calcium-binding protein. II. Structure determination and general description. , 1973, The Journal of biological chemistry.
[2] H E Huxley,et al. The Mechanism of Muscular Contraction , 1965, Scientific American.
[3] E. Eisenberg,et al. Regulation and kinetics of the actin-myosin-ATP interaction. , 1980, Annual review of biochemistry.
[4] J. Wilkinson,et al. The amino acid sequence of troponin I from rabbit skeletal muscle. , 1975, The Biochemical journal.
[5] A. Klug,et al. Three-dimensional image reconstruction of actin-tropomyosin complex and actin-tropomyosin-troponin T-troponin I complex. , 1975, Journal of molecular biology.
[6] R. Kretsinger,et al. Calmodulin, S-100, and crayfish sarcoplasmic calcium-binding protein crystals suitable for X-ray diffraction studies. , 1980, The Journal of biological chemistry.
[7] Z. Grabarek,et al. Comparative studies on thermostability of calmodulin, skeletal muscle troponin C and their tryptic fragments , 1983, FEBS letters.
[8] J. H. Collins,et al. The amino acid sequence of rabbit skeletal muscle troponin C: Gene replication and homology with calcium ‐binding proteins from carp and hake muscle , 1973, FEBS letters.
[9] H. Berendsen,et al. The α-helix dipole and the properties of proteins , 1978, Nature.
[10] S. Rosenfeld,et al. Proteolytic fragments of troponin C. Localization of high and low affinity Ca2+ binding sites and interactions with troponin I and troponin T. , 1978, The Journal of biological chemistry.
[11] H. Huxley. Structural Changes in the Actin- and Myosin-eontaining Filaments during Contraction , 1973 .
[12] F. Crick,et al. The treatment of errors in the isomorphous replacement method , 1959 .
[13] C. Klee,et al. Positive cooperative binding of calcium to bovine brain calmodulin. , 1980, Biochemistry.
[14] J. Thornton,et al. Calcium binding by troponin-C. A proton magnetic resonance study. , 1977, Journal of molecular biology.
[15] C. Kay,et al. Calcium-binding properties of cardiac and skeletal troponin C as determined by circular dichroism and ultraviolet difference spectroscopy. , 1978, Canadian journal of biochemistry.
[16] C. Bugg,et al. Crystallization and preliminary X-ray investigation of calmodulin. , 1980, The Journal of biological chemistry.
[17] M. James,et al. Crystallographic data for troponin C from turkey skeletal muscle. , 1984, Journal of molecular biology.
[18] R. Dickerson,et al. A least‐squares refinement method for isomorphous replacement , 1968 .
[19] S. Rosenfeld,et al. Proteolytic fragments of troponin C. Interactions with the other troponin subunits and biological activity. , 1981, The Journal of biological chemistry.
[20] J. Wilkinson. The amino acid sequence of troponin C from chicken skeletal muscle , 1976, FEBS letters.
[21] K. Moffat,et al. Structure of vitamin D-dependent calcium-binding protein from bovine intestine , 1981, Nature.
[22] L. Smillie,et al. Primary structure of rabbit skeletal muscle troponin-T. Sequence determination of the NH2-terminal fragment CB3 and the complete sequence of troponin-T. , 1977, The Journal of biological chemistry.
[23] P. Laszlo,et al. Sodium-23 nuclear magnetic resonance as an indicator of sodium binding to calmodulin and tryptic fragments, in relation to calcium content. , 1980, European journal of biochemistry.
[24] D. Hartshorne,et al. Ca2+ and Mg2+ dependent conformations of troponin C as determined by 1H and 19F nuclear magnetic resonance. , 1977, Biochemistry.
[25] J Gariépy,et al. Localization of a trifluoperazine binding site on troponin C. , 1983, Biochemistry.
[26] R. Kretsinger,et al. Troponin and parvalbumin calcium binding regions predicted in myosin light chain and T4 lysozyme. , 1975, Science.
[27] J. Gergely,et al. Purification and properties of the components from troponin. , 1973, The Journal of biological chemistry.
[28] J. Richardson,et al. The anatomy and taxonomy of protein structure. , 1981, Advances in protein chemistry.
[29] L. Delbaere,et al. Preliminary X-ray data for the calmodulin/trifluoperazine complex. , 1984, Journal of molecular biology.
[30] J. Haselgrove. X-Ray Evidence for a Conformational Change in the Actin-containing Filaments of Vertebrate Striated Muscle , 1973 .
[31] S. Lehrer,et al. Fluorescence and conformational changes caused by proton binding to troponin C. , 1974, Biochemical and biophysical research communications.
[32] Lindsay Sawyer,et al. Carboxyl–carboxylate interactions in proteins , 1982, Nature.
[33] E. Eisenberg,et al. Mechanism of action of troponin . tropomyosin. Inhibition of actomyosin ATPase activity without inhibition of myosin binding to actin. , 1981, The Journal of biological chemistry.
[34] M. James,et al. Conformational flexibility in the active sites of aspartyl proteinases revealed by a pepstatin fragment binding to penicillopepsin. , 1982, Proceedings of the National Academy of Sciences of the United States of America.
[35] G J Williams,et al. The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1977, Journal of molecular biology.
[36] Robert Huber,et al. Conformational flexibility and its functional significance in some protein molecules , 1979 .
[37] C. D. Barry,et al. The predicted structure of the calcium-binding component of troponin. , 1975, Biochimica et biophysica acta.