Structural changes at microtubule ends accompanying GTP hydrolysis: Information from a slowly hydrolyzable analogue of GTP, guanylyl (α,β)methylenediphosphonate

Proceedings of the National Academy of Sciences of the United States of America

Volumn 95, Issue 7, 1998, Pages 3661-3666

  Müller Reichert, Thomas ^a   Chrétien, Denis ^a   Severin, Fedor ^a   Hyman, Anthony A ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; GUANOSINE TRIPHOSPHATE DERIVATIVE; GUANYLYL ALPHA METHYLENEDIPHOSPHONATE; GUANYLYL BETA METHYLENEDIPHOSPHONATE; NUCLEOTIDE; OLIGOMER; TUBULIN; UNCLASSIFIED DRUG;

ANIMAL TISSUE; ARTICLE; CATTLE; CRYOELECTRON MICROSCOPY; DEPOLYMERIZATION; HYDROLYSIS; MICROSCOPY; MICROTUBULE; NONHUMAN; PRIORITY JOURNAL;

ANIMALS; CATTLE; DIMERIZATION; GUANOSINE TRIPHOSPHATE; HYDROLYSIS; MICROTUBULES;

ANIMALIA; BOS TAURUS;

EID: 0032584067     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.95.7.3661     Document Type: Article

References (29)

1. Avila, J. (1990) Microtubule Proteins (CRC, Boca Raton, FL).
2. Amos, L. & Klug, A. (1974) J. Cell. Sci. 14, 523-549.
3. Mitchison, T. & Kirschner, M. (1984) Nature (London) 312, 237-242.
4. Horio, T. & Hotani, H. (1986) Nature (London) 321, 605-607.
5. Walker, R. A., O'Brien, E. T., Pryer, N. K., Sobeiro, M. F., Voter, W. A., Erickson, H. P. & Salmon, E. D. (1988) J. Cell Biol. 107, 1437-1448.
6. Cassimeris, L., Pryer, N. K. & Salmon, E. D. (1988) J. Cell Biol. 107, 2223-2231.
7. Sammak, P. J. & Borisy, G. G. (1988) Nature (London) 332, 724-726.
8. Carlier, M.-F., Didry, D., Simon, C. & Pantaloni, D. (1989) Biochemistry 28, 1783-1791.
9. Purich, D. L. & Kristoffersen, D. (1984) Adv. Protein Chem. 36, 133-212.
10. Kirschner, M. W. (1978) Int. Rev. Cytol. 54, 1-71.
11. Caplow, M., Kuhlen, R. L. & Shanks, J. (1994) J. Cell Biol. 127, 779-788.
12. Hyman, A. A., Salser, S., Drechsel, D. N., Unwin, N. & Mitchison, T. J. (1992) Mol. Biol. Cell 3, 1155-1167.
13. Audenaert, R., Heremans, L., Heremans, K. & Engelborghs, Y. (1989) Biochim. Biophys. Acta 996, 110-115.
14. Hyman, A. A., Chrétien, D., Arnal, I. & Wade, R. H. (1995) J. Cell Biol. 128, 117-125.
15. Erickson, H. P. (1974) J. Cell Biol. 60, 153-167.
16. Simon, J. R. & Salmon, E. D. (1990) J. Cell Sci. 96, 571-582.
17. Chrétien, D., Fuller, S. D. & Karsenti, E. (1995) J. Cell Biol. 129, 1311-1328.
18. Kirschner, M. W., Williams, R. C., Weingarten, M. & Gerhart, J. C. (1974) Proc. Natl. Acad. Sci. USA 71, 1159-1163.
19. Mandelkow, E. M., Mandelkow, E. & Milligan, R. A. (1991) J. Cell Biol. 114, 977-991.
20. Warner, F. D. & Satir, P. (1973) J. Cell Sci. 12, 313-326.
21. Melki, R., Carlier, M.-F., Pantaloni, D. & Timasheff, S. N. (1989) Biochemistry 28, 9143-9152.
22. Ashford, T., Andersen, S. & Hyman, A. A. (1988) in Cell Biology, a Laboratory Handbook, ed. Celis, J. E. (Academic, San Diego), 2nd Ed., Vol. 2, pp. 205-212.
23. Mitchison, T. & Kirschner, M. (1984) Nature (London) 312, 232-237.
24. Porter, M. E. & Johnson, K. A. (1983) J. Biol. Chem. 258, 6575-6581.
25. Field, C. M., Al-Awar, O., Rosenblatt, J., Wong, M. L., Alberts, B. & Mitchison, T. J. (1996) J. Cell Biol. 133, 605-616.
26. Tran, P. T., Joshi, P. & Salmon, E. D. (1997) J. Struct. Biol. 118, 107-118.
27. Howard, W. D. & Timasheff, S. N. (1986) Biochemistry 25, 8292-8300.
28. Mickey, B. & Howard, J. (1995) J. Cell Biol. 130, 909-917.
29. Hyman, A. A. & Karsenti, E. (1996) Cell 84, 401-410.