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Volumn 118, Issue 2, 1997, Pages 119-127

Visualizing the secondary structure of tubulin: Three-dimensional map at 4 Å

Author keywords

[No Author keywords available]

Indexed keywords

TUBULIN;

EID: 0031010399     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1997.3841     Document Type: Conference Paper
Times cited : (27)

References (18)
  • 1
    • 0023053025 scopus 로고
    • Three-dimensional structure of the regular surface layer (HPI layer) ofDeinococcus radiodurans
    • Baumeister W., Barth M., Hegerl R., Guckenberger R., Hahn M., Saxton W. O. Three-dimensional structure of the regular surface layer (HPI layer) ofDeinococcus radiodurans. J. Mol. Biol. 187:1986;241-253.
    • (1986) J. Mol. Biol. , vol.187 , pp. 241-253
    • Baumeister, W.1    Barth, M.2    Hegerl, R.3    Guckenberger, R.4    Hahn, M.5    Saxton, W.O.6
  • 2
    • 0010570158 scopus 로고
    • Electron crystallography of proteins: State of the art and strategies for the future
    • Baumeister W., Typke D. Electron crystallography of proteins: State of the art and strategies for the future. MSA Bull. 23:1993;11-19.
    • (1993) MSA Bull. , vol.23 , pp. 11-19
    • Baumeister, W.1    Typke, D.2
  • 3
    • 0001879815 scopus 로고
    • Tubulin: Conservation and structure
    • New York: Wiley
    • Burns R. G., Surridge C. D. Tubulin: Conservation and structure. Microtubules. 1993;Wiley, New York.
    • (1993) Microtubules
    • Burns, R.G.1    Surridge, C.D.2
  • 4
    • 0028103275 scopus 로고
    • Acta Crystallogr. D50:1994;760-763.
    • (1994) Acta Crystallogr. , vol.50 , pp. 760-763
  • 5
    • 0028178514 scopus 로고
    • Predominant labeling of β- Over α-tubulin from porcine brain by a photoactivatable taxoid derivative
    • Combeau C., Commerçon A., Mioskowski C., Rousseau B., Aubert F., Goeldner M. Predominant labeling of β- over α-tubulin from porcine brain by a photoactivatable taxoid derivative. Biochemistry. 33:1994;6676-6683.
    • (1994) Biochemistry , vol.33 , pp. 6676-6683
    • Combeau, C.1    Commerçon, A.2    Mioskowski, C.3    Rousseau, B.4    Aubert, F.5    Goeldner, M.6
  • 6
    • 0029852223 scopus 로고    scopus 로고
    • Tubulin secondary structure analysis, limited proteolysis sites and homology to FtsZ
    • de Pereda J. M., Leynadier D., Evangelio J. A., Chacon P., Andreu J. M. Tubulin secondary structure analysis, limited proteolysis sites and homology to FtsZ. Biochemistry. 35:1996;14203-14215.
    • (1996) Biochemistry , vol.35 , pp. 14203-14215
    • De Pereda, J.M.1    Leynadier, D.2    Evangelio, J.A.3    Chacon, P.4    Andreu, J.M.5
  • 7
    • 0026482161 scopus 로고
    • Projection map of tubulin in zinc-induced sheets at 4 Å resolution
    • Downing K. H., Jones J. Projection map of tubulin in zinc-induced sheets at 4 Å resolution. J. Struct. Biol. 109:1992;152-159.
    • (1992) J. Struct. Biol. , vol.109 , pp. 152-159
    • Downing, K.H.1    Jones, J.2
  • 8
    • 0024644887 scopus 로고
    • Three-dimensional reconstructions from incomplete data: Interpretability of density maps at "atomic" resolution
    • Glaeser R. M., Tong L., Kim S. H. Three-dimensional reconstructions from incomplete data: Interpretability of density maps at "atomic" resolution. Ultramicroscopy. 27:1989;307-318.
    • (1989) Ultramicroscopy , vol.27 , pp. 307-318
    • Glaeser, R.M.1    Tong, L.2    Kim, S.H.3
  • 10
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryomicroscopy
    • Henderson R., Baldwin J. M., Ceska T. A., Zemlin F., Beckman E., Downing K. H. Model for the structure of bacteriorhodopsin based on high-resolution electron cryomicroscopy. J. Mol. Biol. 213:1990;899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckman, E.5    Downing, K.H.6
  • 12
    • 0028979606 scopus 로고
    • Three-dimensional structure of the kinesin head-microtubule complex
    • Kikkawa M., Ishikawa T., Wakabayashi T., Hirokawa N. Three-dimensional structure of the kinesin head-microtubule complex. Nature. 376:1995;274-277.
    • (1995) Nature , vol.376 , pp. 274-277
    • Kikkawa, M.1    Ishikawa, T.2    Wakabayashi, T.3    Hirokawa, N.4
  • 13
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • Kuhlbrandt W., Wang D. N., Fujiyoshi Y. Atomic model of plant light-harvesting complex by electron crystallography. Nature. 367:1994;614-621.
    • (1994) Nature , vol.367 , pp. 614-621
    • Kuhlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 15
    • 0029063397 scopus 로고
    • Structure of tubulin at 6.5 Å and location of the taxol-binding site
    • Nogales E., Wolf S. G., Khan I. A., Luduena R. F., Downing K. H. Structure of tubulin at 6.5 Å and location of the taxol-binding site. Nature. 375:1995a;424-427.
    • (1995) Nature , vol.375 , pp. 424-427
    • Nogales, E.1    Wolf, S.G.2    Khan, I.A.3    Luduena, R.F.4    Downing, K.H.5
  • 16
    • 0028856299 scopus 로고
    • Preservation of 2-D crystals of tubulin for electron crystallography
    • Nogales E., Wolf S. G., Zhang S. X., Downing K. H. Preservation of 2-D crystals of tubulin for electron crystallography. J. Struct. Biol. 115:1995b;199-208.
    • (1995) J. Struct. Biol. , vol.115 , pp. 199-208
    • Nogales, E.1    Wolf, S.G.2    Zhang, S.X.3    Downing, K.H.4
  • 17
    • 0026747827 scopus 로고
    • Direct photoaffinity labeling of tubulin with taxol
    • Rao S., Horwitz S. B., Ringel I. Direct photoaffinity labeling of tubulin with taxol. J. Natl. Cancer Inst. 84:1992;785-788.
    • (1992) J. Natl. Cancer Inst. , vol.84 , pp. 785-788
    • Rao, S.1    Horwitz, S.B.2    Ringel, I.3
  • 18
    • 0030569005 scopus 로고    scopus 로고
    • Interpreting a medium-resolution model of tubulin: Comparison of zinc-sheet and microtubule structure
    • Wolf S. G., Nogales E., Kikkawa M., Gratzinger D., Hirokawa N., Downing K. H. Interpreting a medium-resolution model of tubulin: comparison of zinc-sheet and microtubule structure. J. Mol. Biol. 263:1996;485-501.
    • (1996) J. Mol. Biol. , vol.263 , pp. 485-501
    • Wolf, S.G.1    Nogales, E.2    Kikkawa, M.3    Gratzinger, D.4    Hirokawa, N.5    Downing, K.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.