三木正雄 研究業績一覧

Publication list(1988-1998)

1. A proposed mechanism for the binding of phalloidin to actin and the relationship between the phalloidin and nucleotide binding sites. Barden, J., Miki, M., Hambly, B. and dos Remedios, C. (1988) Molecular Cell Biol. (Life Sci. Adv.) 7, 19-25.

2. Fluorescence quenching studies of fluorescein attached to Lys-61 or Cys-374 in actin. Miki, M. and dos Remedios, C. (1988) J. Biochem. (Tokyo) 104, 232-235.

3. Characterization of carbethoxylated actin. Miki, M. (1988) J. Biochem. (Tokyo) 104, 312-315.

4. Structure and function of contractile proteins in muscle fibre. Barden, J. A., Bennetts, B., dos Remedios, C. G., Hambly, B. D., Miki, M., and Phillips, L. (1988) Australian Paediatr. Suppl. p. 31-33.

5. The effect of the replacement of ADP with a photoaffinity ATP analogue, 2-azido-ADP, in F-actin on its function. Kuwayama, H., Miki, M. and dos Remedios, C. (1989) FEBS Lett. 250, 328-330.

6. Interaction of Lys-61 labeled actin with myosin subfragment 1 and the regulatory proteins. Miki, M. (1989) J. Biochem. (Tokyo) 106, 651-655.

7. Resonance energy transfer between points in a reconstituted skeletal muscle thin filament. Miki, M. (1990) Eur. J. Biochem. 187, 155-162.

8. Interaction of F-actin-AMPPNP with myosin subfragment 1 and troponin- tropomyosin. Miki, M. (1990) J. Biochem. (Tokyo) 108, 457-461.

9. A detection of the radial coordinate of Tyr-69 in F-actin using fluorescence energy transfer. Miki, M. and dos Remedios, C. (1990) Biochemistry Int. 108, 457-461.

10.Interaction of maleimidobenzoyl actin with myosin subfragment 1 and tropomyosin-troponin. Miki, M. and Hozumi, T. (1991) Biochemistry 30, 5625-5630.

11. Detection of conformational changes in actin by fluorescence resonance energy transfer between Tyrosine-69 and Cysteine-374. Miki, M. (1991) Biochemistry 30, 10878-10884.

12. Removing the two C-terminal residues of actin affects the filament structure. O'Donoghue, S., Miki, M., and dos Remedios, C. (1992) Arch. Biochem. Biophys. 293, 110-116.

13. Structure of actin observed by fluorescence resonance energy transfer spectroscopy. Miki, M., O'Donoghue, S. , and dos Remedios, C. (1992) J. Muscle Res. Cell Motil. 13, 132-145.

14. The mechanism of inhibition of the actin-activated myosin Mg-ATPase by calponin.Miki, M., Walsh, K. P., and Hartshorne, D. J. (1992) Biochem. Biophys. Res. Commun. 187, 867-871

15. Kinetics of Structural Changes of Reconstituted Skeletal Muscle Thin Filaments Observed by Fluorescence Resonance Energy Transfer.Miki, M. and Iio, T. (1993) J. Biol. Chem. 268, 7101-7106

16. Domain motion in Actin Observed by Fluorescence Resonance Energy Transfer Miki, M., and Kouyama, T. (1994) Biochemistry 33, 10171-10177

17. Domain motion in Actin: Determination of Interdomain Distance Distributions by Time-Resolved Fluorescence Energy Transfer Miki, M., and Kouyama, T. (1995) Biophys J. 68, 330s

18.Maleimidobenzoyl Actin: Its Biochemical Properties with Heavy Meromyosin and In Vitro Motility.Hozumi, T., Miki, M., & Higashi-Fujime, S. (1996) J. Biochem.119, 151-156

19. Interhead Distances in Myosin Attached to F-actin Estimated by Fluorescence Energy Transfer Spectroscopy. Ishiwata, S., Miki, M., Shin, I., Funatsu, T., Yasuda, K., & dos Remedios, C. (1997) Biophys. J. 73, 895-904.

20. Ca2+-induced distance change between points on actin and troponin in skeletal muscle thin filaments estimated by fluorescence energy transfer spectroscopy. Miki, M., Kobayashi, T., Kimura, H., Hagiwara, A., Hai, H., and Maeda, Y. J. Biochem. 123, 324-331 (1998)

21. Fluorescence resonance energy transfer between points on tropomyosin and actin in skeletal muscle thin filaments: Does tropomyosin move? Miki, M., Miura, T., Sano, K., Kimura, H., Kondo, H., Ishida, H., and Maeda, Y. J. Biochem. 123, 1104-1111 (1998)

22. Structural changes between regulatory proteins and actin: A regulation model by tropomyosin-troponin based on FRET measurements. Miki, M. in Molecular Interactions of Actin (dos Remedios, C. G. and Thomas, D. D., eds) Springer Verlag, Heidelberg (in press)

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