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Volumn 391, Issue 5, 2009, Pages 849-857

Direct Optical Microscopic Observation of the Microtubule Polymerization Intermediate Sheet Structure in the Presence of Gas7

Author keywords

dark field microscopy; Gas7; intermediate sheet; MAPs; microtubule polymerization; Pin1

Indexed keywords

BINDING PROTEIN; GROWTH ARREST SPECIFIC PROTEIN 7; GUANOSINE TRIPHOSPHATASE; TUBULIN; UNCLASSIFIED DRUG;

EID: 68349123588     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.06.081     Document Type: Article
Times cited : (15)

References (20)
  • 1
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison T.J., and Kirschner M.W. Dynamic instability of microtubule growth. Nature 312 (1984) 237-242
    • (1984) Nature , vol.312 , pp. 237-242
    • Mitchison, T.J.1    Kirschner, M.W.2
  • 3
    • 0022492523 scopus 로고
    • Visualization of the dynamic instability of individual microtubules by dark-field microscopy
    • Horio T., and Hotani H. Visualization of the dynamic instability of individual microtubules by dark-field microscopy. Nature 321 (1986) 605-607
    • (1986) Nature , vol.321 , pp. 605-607
    • Horio, T.1    Hotani, H.2
  • 4
    • 0024094432 scopus 로고
    • Dynamic instability of individual microtubules analyzed by video light microscopy: rate constants and transition frequencies
    • Walker R.A., O'Brien E.T., Pryer N.K., Sobeiro M.F., Voter W.A., Erickson H.P., and Salmon E.D. Dynamic instability of individual microtubules analyzed by video light microscopy: rate constants and transition frequencies. J. Cell Biol. 107 (1988) 1437-1448
    • (1988) J. Cell Biol. , vol.107 , pp. 1437-1448
    • Walker, R.A.1    O'Brien, E.T.2    Pryer, N.K.3    Sobeiro, M.F.4    Voter, W.A.5    Erickson, H.P.6    Salmon, E.D.7
  • 5
    • 1642546280 scopus 로고    scopus 로고
    • Microtubule plus-end dynamics in Xenopus egg extract spindles
    • Tirnauer J.S., Salmon E.D., and Mitchison T.J. Microtubule plus-end dynamics in Xenopus egg extract spindles. Mol. Biol. Cell 15 (2004) 1776-1784
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1776-1784
    • Tirnauer, J.S.1    Salmon, E.D.2    Mitchison, T.J.3
  • 7
    • 0025868445 scopus 로고
    • Microtubule dynamics and microtubule caps: a time-resolved cryo-electron microscopy study
    • Mandelkow E.-M., Mandelkow E., and Milligan R.A. Microtubule dynamics and microtubule caps: a time-resolved cryo-electron microscopy study. J. Cell Biol. 114 (1991) 977-999
    • (1991) J. Cell Biol. , vol.114 , pp. 977-999
    • Mandelkow, E.-M.1    Mandelkow, E.2    Milligan, R.A.3
  • 8
    • 20544463212 scopus 로고    scopus 로고
    • Nucleotide-dependent bending flexibility of tubulin regulates microtubule assembly
    • Wang H.W., and Nogales E. Nucleotide-dependent bending flexibility of tubulin regulates microtubule assembly. Nature 435 (2005) 911-915
    • (2005) Nature , vol.435 , pp. 911-915
    • Wang, H.W.1    Nogales, E.2
  • 9
    • 33646494080 scopus 로고    scopus 로고
    • Structural mechanisms underlying nucleotide-dependent self-assembly of tubulin and its relatives
    • Nogales E., and Wang H.W. Structural mechanisms underlying nucleotide-dependent self-assembly of tubulin and its relatives. Curr. Opin. Struct. Biol. 16 (2006) 221-229
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 221-229
    • Nogales, E.1    Wang, H.W.2
  • 10
    • 0016750357 scopus 로고
    • Quantitative electron microscopy of microtubule assembly in vitro
    • Kirschner M.W., Honig L.S., and Williams R.C. Quantitative electron microscopy of microtubule assembly in vitro. J. Mol. Biol. 99 (1975) 263-276
    • (1975) J. Mol. Biol. , vol.99 , pp. 263-276
    • Kirschner, M.W.1    Honig, L.S.2    Williams, R.C.3
  • 11
    • 0029041404 scopus 로고
    • Structure of growing microtubule ends: two-dimensional sheets close into tubes at variable rates
    • Chrétien D., Fuller S.D., and Karsenti E. Structure of growing microtubule ends: two-dimensional sheets close into tubes at variable rates. J. Cell Biol. 129 (1995) 1311-1328
    • (1995) J. Cell Biol. , vol.129 , pp. 1311-1328
    • Chrétien, D.1    Fuller, S.D.2    Karsenti, E.3
  • 13
    • 0032530461 scopus 로고    scopus 로고
    • gas7: a gene expressed preferentially in growth-arrested fibroblasts and terminally differentiated Purkinje neurons affects neurite formation
    • Ju Y.T., Chang A.C., She B.R., Tsaur M.L., Hwang H.M., Chao C.C., et al. gas7: a gene expressed preferentially in growth-arrested fibroblasts and terminally differentiated Purkinje neurons affects neurite formation. Proc. Natl Acad. Sci. USA 95 (1998) 11423-11428
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 11423-11428
    • Ju, Y.T.1    Chang, A.C.2    She, B.R.3    Tsaur, M.L.4    Hwang, H.M.5    Chao, C.C.6
  • 14
    • 0025034523 scopus 로고
    • The structure of microtubule ends during the elongation and shortening phases of dynamic instability examined by negative-stain electron microscopy
    • Simon J.R., and Salmon E.D. The structure of microtubule ends during the elongation and shortening phases of dynamic instability examined by negative-stain electron microscopy. J. Cell Sci. 96 (1990) 571-582
    • (1990) J. Cell Sci. , vol.96 , pp. 571-582
    • Simon, J.R.1    Salmon, E.D.2
  • 15
    • 0021171445 scopus 로고
    • The purification of tau protein and the occurrence of two phosphorylation states of tau in brain
    • Lindwall G., and Cole R.D. The purification of tau protein and the occurrence of two phosphorylation states of tau in brain. J. Biol. Chem. 259 (1984) 12241-12245
    • (1984) J. Biol. Chem. , vol.259 , pp. 12241-12245
    • Lindwall, G.1    Cole, R.D.2
  • 16
    • 0028132184 scopus 로고
    • Microtubule-stabilizing activity of microtubule-associated proteins (MAPs) is due to increase in frequency of rescue in dynamic instability: shortening length decreases with binding of MAPs onto microtubules
    • Itoh T.J., and Hotani H. Microtubule-stabilizing activity of microtubule-associated proteins (MAPs) is due to increase in frequency of rescue in dynamic instability: shortening length decreases with binding of MAPs onto microtubules. Cell Struct. Funct. 19 (1994) 279-290
    • (1994) Cell Struct. Funct. , vol.19 , pp. 279-290
    • Itoh, T.J.1    Hotani, H.2
  • 17
    • 0345596417 scopus 로고    scopus 로고
    • Modeling elastic properties of microtubule tips and walls
    • J ánosi I.M., Chrétien D., and Flyvbjerg H. Modeling elastic properties of microtubule tips and walls. Eur. Biophys. J. 27 (1998) 501-513
    • (1998) Eur. Biophys. J. , vol.27 , pp. 501-513
    • J ánosi, I.M.1    Chrétien, D.2    Flyvbjerg, H.3
  • 18
    • 0018654410 scopus 로고
    • Characterization of brain microtubule proteins prepared by selective removal of mitochondrial and synaptosomal components
    • Karr T.L., White H.D., and Purich D.L. Characterization of brain microtubule proteins prepared by selective removal of mitochondrial and synaptosomal components. J. Biol. Chem. 254 (1979) 6107-6111
    • (1979) J. Biol. Chem. , vol.254 , pp. 6107-6111
    • Karr, T.L.1    White, H.D.2    Purich, D.L.3
  • 19
    • 0030847540 scopus 로고    scopus 로고
    • Phosphorylation states of microtubule-associated protein 2 (MAP2) determine the regulatory role of MAP2 in microtubule dynamics
    • Itoh T.J., Hisanaga S., Hosoi T., Kishimoto T., and Hotani H. Phosphorylation states of microtubule-associated protein 2 (MAP2) determine the regulatory role of MAP2 in microtubule dynamics. Biochemistry 36 (1997) 12574-12582
    • (1997) Biochemistry , vol.36 , pp. 12574-12582
    • Itoh, T.J.1    Hisanaga, S.2    Hosoi, T.3    Kishimoto, T.4    Hotani, H.5
  • 20
    • 38449109403 scopus 로고    scopus 로고
    • High-resolution structural analysis of the kinesin-microtubule complex by electron cryo-microscopy
    • Hirose K., and Amos L.A. High-resolution structural analysis of the kinesin-microtubule complex by electron cryo-microscopy. Methods Mol. Biol. 392 (2007) 213-230
    • (2007) Methods Mol. Biol. , vol.392 , pp. 213-230
    • Hirose, K.1    Amos, L.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.