메뉴 건너뛰기




Volumn 435, Issue 7041, 2005, Pages 523-527

Insights into microtubule nucleation from the crystal structure of human γ-tubulin

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CONFORMATIONS; CRYSTAL STRUCTURE; OLIGOMERS; PROTEINS;

EID: 19544384914     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature03586     Document Type: Article
Times cited : (153)

References (15)
  • 1
    • 0028293043 scopus 로고
    • In vitro reconstitution of centrosome assembly and function: The central role of γ-tubulin
    • Stearns, T. & Kirschner, M. In vitro reconstitution of centrosome assembly and function: the central role of γ-tubulin. Cell 76, 623-637 (1994).
    • (1994) Cell , vol.76 , pp. 623-637
    • Stearns, T.1    Kirschner, M.2
  • 2
    • 0028879986 scopus 로고
    • Nucleation of microtubule assembly by a γ-tubulin-containing ring complex
    • Zheng, Y. et al. Nucleation of microtubule assembly by a γ-tubulin-containing ring complex. Nature 378, 578-583 (1995).
    • (1995) Nature , vol.378 , pp. 578-583
    • Zheng, Y.1
  • 3
    • 0031854868 scopus 로고    scopus 로고
    • Recruitment of the γ-tubulin ring complex to Drosophila salt-stripped centrosome scaffolds
    • Moritz, M. et al. Recruitment of the γ-tubulin ring complex to Drosophila salt-stripped centrosome scaffolds. J. Cell Biol. 142, 775-786 (1998).
    • (1998) J. Cell Biol. , vol.142 , pp. 775-786
    • Moritz, M.1
  • 4
    • 1642401199 scopus 로고    scopus 로고
    • Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain
    • Ravelli, R. B. G. et al. Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain. Nature 378, 198-202 (2004).
    • (2004) Nature , vol.378 , pp. 198-202
    • Ravelli, R.B.G.1
  • 5
    • 0036774026 scopus 로고    scopus 로고
    • Microtubule structure at 8 Å resolution
    • Li, H. et al. Microtubule structure at 8 Å resolution. Structure (Camb.) 10, 1317-1328 (2002).
    • (2002) Structure (Camb.) , vol.10 , pp. 1317-1328
    • Li, H.1
  • 6
    • 0035834521 scopus 로고    scopus 로고
    • Refined structure of αβ-tubulin at 3.5 Å resolution
    • Lowe, J. et al. Refined structure of αβ-tubulin at 3.5 Å resolution. J. Mol. Biol. 313, 1045-1057 (2001).
    • (2001) J. Mol. Biol. , vol.313 , pp. 1045-1057
    • Lowe, J.1
  • 7
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the αβ tubulin dimer by electron crystallography
    • Nogales, E., Wolf, S. G. & Downing, K. H. Structure of the αβ tubulin dimer by electron crystallography. Nature 391, 199-203 (1998).
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 8
    • 0031780061 scopus 로고    scopus 로고
    • Tubulin and FtsZ form a distinct class of GTPases
    • Nogales, E. et al. Tubulin and FtsZ form a distinct class of GTPases. Nature Struct. Biol. 5, 451-458 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 451-458
    • Nogales, E.1
  • 9
    • 13444274140 scopus 로고    scopus 로고
    • Structural insights into FtsZ protofilament formation
    • Oliva, M. A., Cordell, S. C. & Lowe, J. Structural insights into FtsZ protofilament formation. Nature Struct. Mol. Biol. 11, 1243-1250 (2004).
    • (2004) Nature Struct. Mol. Biol. , vol.11 , pp. 1243-1250
    • Oliva, M.A.1    Cordell, S.C.2    Lowe, J.3
  • 10
    • 0029041404 scopus 로고
    • Structure of growing microtubule ends: Two-dimensional sheets close into tubes at variable rates
    • Chretien, D., Fuller, S. D. & Karsenti, E. Structure of growing microtubule ends: two-dimensional sheets close into tubes at variable rates. J. Cell Biol. 129, 1311-1328 (1995).
    • (1995) J. Cell Biol. , vol.129 , pp. 1311-1328
    • Chretien, D.1    Fuller, S.D.2    Karsenti, E.3
  • 11
    • 0031010658 scopus 로고    scopus 로고
    • Microtubule release from the centrosome
    • Keating, T. J. et al. Microtubule release from the centrosome. Proc Natl Acad. Sci. USA 94, 5078-5083 (1997).
    • (1997) Proc Natl Acad. Sci. USA , vol.94 , pp. 5078-5083
    • Keating, T.J.1
  • 13
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 14
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A. et al. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.