메뉴 건너뛰기




Volumn 10, Issue 10, 2002, Pages 1317-1328

Microtubule structure at 8 Å resolution

Author keywords

Dynamic instability; Electron crystallography; Microtubules; Protein structure; Tubulin

Indexed keywords

TUBULIN; ZINC;

EID: 0036774026     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(02)00827-4     Document Type: Article
Times cited : (349)

References (36)
  • 1
    • 0033791649 scopus 로고    scopus 로고
    • Structural insights into microtubule function
    • Nogales E. Structural insights into microtubule function. Annu. Rev. Biochem. 69:2000;277-302
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 277-302
    • Nogales, E.1
  • 2
    • 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. 391:1998;199-203
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 3
    • 0035834521 scopus 로고    scopus 로고
    • Refined structure of alpha beta-tubulin at 3.5 A resolution
    • Löwe J., Li H., Downing K.H., Nogales E. Refined structure of alpha beta-tubulin at 3.5 A resolution. J. Mol. Biol. 313:2001;1045-1057
    • (2001) J. Mol. Biol , vol.313 , pp. 1045-1057
    • Löwe, J.1    Li, H.2    Downing, K.H.3    Nogales, E.4
  • 4
    • 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., Ludueña R.F., Downing K.H. Structure of tubulin at 6.5 Å and location of the taxol-binding site. Nature. 375:1995;424-427
    • (1995) Nature , vol.375 , pp. 424-427
    • Nogales, E.1    Wolf, S.G.2    Khan, I.A.3    Ludueña, R.F.4    Downing, K.H.5
  • 5
    • 0025814877 scopus 로고
    • New data on the microtubule surface lattice
    • Chrétien D., Wade R. New data on the microtubule surface lattice. Biol. Cell. 71:1991;161-174
    • (1991) Biol. Cell , vol.71 , pp. 161-174
    • Chrétien, D.1    Wade, R.2
  • 7
    • 0032550175 scopus 로고    scopus 로고
    • Image reconstructions of microtubules decorated with monomeric and dimeric kinesins: Comparison with x-ray structure and implications for motility
    • Hoenger A., Sack S., Thormahlen M., Marx A., Muller J., Gross H., Mandelkow E. Image reconstructions of microtubules decorated with monomeric and dimeric kinesins. comparison with x-ray structure and implications for motility J. Cell Biol. 4:1998;419-430
    • (1998) J. Cell Biol , vol.4 , pp. 419-430
    • Hoenger, A.1    Sack, S.2    Thormahlen, M.3    Marx, A.4    Muller, J.5    Gross, H.6    Mandelkow, E.7
  • 8
    • 0030266603 scopus 로고    scopus 로고
    • Three-dimensional structure of functional motor proteins on microtubules
    • Arnal I., Metoz F., DeBonis S., Wade R.H. Three-dimensional structure of functional motor proteins on microtubules. Curr. Biol. 6:1996;1265-1270
    • (1996) Curr. Biol , vol.6 , pp. 1265-1270
    • Arnal, I.1    Metoz, F.2    DeBonis, S.3    Wade, R.H.4
  • 9
    • 0030930492 scopus 로고    scopus 로고
    • Three-dimensional cryoelectron microscopy of 16-protofilament microtubules: Structure, polarity and interaction with motor proteins
    • Hirose K., Amos W.B., Lockhart A., Cross R.A., Amos L.A. Three-dimensional cryoelectron microscopy of 16-protofilament microtubules. structure, polarity and interaction with motor proteins J. Struct. Biol. 118:1997;140-148
    • (1997) J. Struct. Biol , vol.118 , pp. 140-148
    • Hirose, K.1    Amos, W.B.2    Lockhart, A.3    Cross, R.A.4    Amos, L.A.5
  • 10
    • 0034695259 scopus 로고    scopus 로고
    • 15 Å resolution model of the monomeric kinesin motor, KIF1A
    • Kikkawa M., Okada Y., Hirokawa N. 15 Å resolution model of the monomeric kinesin motor, KIF1A. Cell. 100:2000;241-252
    • (2000) Cell , vol.100 , pp. 241-252
    • Kikkawa, M.1    Okada, Y.2    Hirokawa, N.3
  • 11
    • 0031010401 scopus 로고    scopus 로고
    • Tomography without tilt: Three dimensional imaging of microtubule/motor complexes
    • Metoz F., Arnal I., Wade R. Tomography without tilt. three dimensional imaging of microtubule/motor complexes J. Struct. Biol. 118:1997;159-168
    • (1997) J. Struct. Biol , vol.118 , pp. 159-168
    • Metoz, F.1    Arnal, I.2    Wade, R.3
  • 12
    • 0030927934 scopus 로고    scopus 로고
    • Three different approaches for calculating the three dimensional structure of microtubules decorated with kinesin motor proteins
    • Sosa H., Hoenger A., Milligan R.A. Three different approaches for calculating the three dimensional structure of microtubules decorated with kinesin motor proteins. J. Struct. Biol. 118:1997;149-158
    • (1997) J. Struct. Biol , vol.118 , pp. 149-158
    • Sosa, H.1    Hoenger, A.2    Milligan, R.A.3
  • 14
    • 0035838406 scopus 로고    scopus 로고
    • Microtubule structure at improved resolution
    • Meurer-Grob P., Kasparian J., Wade R.H. Microtubule structure at improved resolution. Biochemistry. 40:2001;8000-8008
    • (2001) Biochemistry , vol.40 , pp. 8000-8008
    • Meurer-Grob, P.1    Kasparian, J.2    Wade, R.H.3
  • 15
    • 0026667023 scopus 로고
    • Lattice defects in microtubules: Protofilament numbers vary within individual microtubules
    • Chrétien D., Metoz F., Verde F., Karsenti E., Wade R.H. Lattice defects in microtubules. protofilament numbers vary within individual microtubules J. Cell Biol. 117:1992;1031-1040
    • (1992) J. Cell Biol , vol.117 , pp. 1031-1040
    • Chrétien, D.1    Metoz, F.2    Verde, F.3    Karsenti, E.4    Wade, R.H.5
  • 16
    • 0022928662 scopus 로고
    • An algorithm for straightening images of curved filamentous structures
    • Egelman E.G. An algorithm for straightening images of curved filamentous structures. Ultramicroscopy. 19:1986;367-373
    • (1986) Ultramicroscopy , vol.19 , pp. 367-373
    • Egelman, E.G.1
  • 17
    • 0028375920 scopus 로고
    • Three-dimensional reconstruction from random projections: Orientational alignment via radon transforms
    • Radermacher M. Three-dimensional reconstruction from random projections. orientational alignment via radon transforms Ultramicroscopy. 53:1994;121-136
    • (1994) Ultramicroscopy , vol.53 , pp. 121-136
    • Radermacher, M.1
  • 18
    • 0033572575 scopus 로고    scopus 로고
    • Fast and accurate three-dimensional reconstruction from projections with random orientations via radon transforms
    • Lanzavecchia S., Bellon P.L., Radermacher M. Fast and accurate three-dimensional reconstruction from projections with random orientations via radon transforms. J. Struct. Biol. 128:1999;152-164
    • (1999) J. Struct. Biol , vol.128 , pp. 152-164
    • Lanzavecchia, S.1    Bellon, P.L.2    Radermacher, M.3
  • 19
    • 0029975088 scopus 로고    scopus 로고
    • Spider and web: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank J., Radermacher M., Penczek P., Zhu J., Li Y.H., Ladjadj M., Leith A. Spider and web. processing and visualization of images in 3D electron microscopy and related fields J. Struct. Biol. 116:1996;190-199
    • (1996) J. Struct. Biol , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.H.5    Ladjadj, M.6    Leith, A.7
  • 20
    • 0035782663 scopus 로고    scopus 로고
    • Fourier amplitude decay of electron cryomicroscopic images of single particles and effects on structure determination
    • Saad A., Ludtke S.J., Jakana J., Rixon F.J., Tsuruta H., Chiu W. Fourier amplitude decay of electron cryomicroscopic images of single particles and effects on structure determination. J. Struct. Biol. 133:2001;32-42
    • (2001) J. Struct. Biol , vol.133 , pp. 32-42
    • Saad, A.1    Ludtke, S.J.2    Jakana, J.3    Rixon, F.J.4    Tsuruta, H.5    Chiu, W.6
  • 21
    • 0028393194 scopus 로고
    • The ribosome at improved resolution: New techniques for merging and orientation refinement in 3D cryo-electron microscopy of biological particles
    • Penczek P.A., Grassucci R.A., Frank J. The ribosome at improved resolution. new techniques for merging and orientation refinement in 3D cryo-electron microscopy of biological particles Ultramicroscopy. 53:1994;251-270
    • (1994) Ultramicroscopy , vol.53 , pp. 251-270
    • Penczek, P.A.1    Grassucci, R.A.2    Frank, J.3
  • 23
    • 0019802812 scopus 로고
    • Computer averaging of electron micrographs of 40S ribosomal subunits
    • Frank J., Verschoor A., Boublik M. Computer averaging of electron micrographs of 40S ribosomal subunits. Science. 214:1981;1353-1355
    • (1981) Science , vol.214 , pp. 1353-1355
    • Frank, J.1    Verschoor, A.2    Boublik, M.3
  • 24
    • 0033102385 scopus 로고    scopus 로고
    • How Taxol stabilizes microtubule structure
    • Amos L., Löwe J. How Taxol stabilizes microtubule structure. Chem. Biol. 6:1999;R65-R69
    • (1999) Chem. Biol , vol.6 , pp. R65-R69
    • Amos, L.1    Löwe, J.2
  • 25
    • 0035942226 scopus 로고    scopus 로고
    • The binding conformation of Taxol in beta-tubulin: A model based on electron crystallographic density
    • Snyder J.P., Nettles J.H., Cornett B., Downing K.H., Nogales E. The binding conformation of Taxol in beta-tubulin. a model based on electron crystallographic density Proc. Natl. Acad. Sci. USA. 98:2001;5312-5316
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5312-5316
    • Snyder, J.P.1    Nettles, J.H.2    Cornett, B.3    Downing, K.H.4    Nogales, E.5
  • 26
    • 0036297629 scopus 로고    scopus 로고
    • Multi-resolution contour-based fitting of macromolecular structures
    • Chacon P., Wriggers W. Multi-resolution contour-based fitting of macromolecular structures. J. Mol. Biol. 317:2002;375-384
    • (2002) J. Mol. Biol , vol.317 , pp. 375-384
    • Chacon, P.1    Wriggers, W.2
  • 27
    • 0030709242 scopus 로고    scopus 로고
    • The multiple forms of tubulin: Different gene products and covalent modifications
    • Ludueña R.F. The multiple forms of tubulin. different gene products and covalent modifications Int. Rev. Cytol. 178:1998;207-275
    • (1998) Int. Rev. Cytol , vol.178 , pp. 207-275
    • Ludueña, R.F.1
  • 28
    • 0030940117 scopus 로고    scopus 로고
    • Taxol differentially modulates the dynamics of microtubules assembled from unfractionated and purified β-tubulin isotypes
    • Derry W.B., Wilson L., Khan I.A., Ludueña R.F., Jordan M.A. Taxol differentially modulates the dynamics of microtubules assembled from unfractionated and purified β-tubulin isotypes. Biochemistry. 36:1997;3554-3562
    • (1997) Biochemistry , vol.36 , pp. 3554-3562
    • Derry, W.B.1    Wilson, L.2    Khan, I.A.3    Ludueña, R.F.4    Jordan, M.A.5
  • 29
    • 0030022120 scopus 로고    scopus 로고
    • Resistance mechanisms in human sarcoma mutants derived by single-step exposure to paclitaxel (Taxol)
    • Dumontet C., Duran G.E., Steger K.A., Beketicoreskovic L., Sikic B.I. Resistance mechanisms in human sarcoma mutants derived by single-step exposure to paclitaxel (Taxol). Cancer Res. 56:1996;1091-1097
    • (1996) Cancer Res , vol.56 , pp. 1091-1097
    • Dumontet, C.1    Duran, G.E.2    Steger, K.A.3    Beketicoreskovic, L.4    Sikic, B.I.5
  • 30
    • 0031914188 scopus 로고    scopus 로고
    • Atomic structures of tubulin and FtsZ
    • Erickson H.P. Atomic structures of tubulin and FtsZ. Trends Cell Biol. 8:1998;133-137
    • (1998) Trends Cell Biol , vol.8 , pp. 133-137
    • Erickson, H.P.1
  • 31
    • 0032509226 scopus 로고    scopus 로고
    • Changes in microtubule protofilament number induced by taxol binding to an easily accessible site - Internal microtubule dynamics
    • Diaz J.F., Valpuesta J.M., Chacon P., Diakun G., Andreu J.M. Changes in microtubule protofilament number induced by taxol binding to an easily accessible site - internal microtubule dynamics. J. Biol. Chem. 273:1998;33803-33810
    • (1998) J. Biol. Chem , vol.273 , pp. 33803-33810
    • Diaz, J.F.1    Valpuesta, J.M.2    Chacon, P.3    Diakun, G.4    Andreu, J.M.5
  • 32
    • 0034714203 scopus 로고    scopus 로고
    • Molecular recognition of Taxol by microtubules - Kinetics and thermodynamics of binding of fluorescent Taxol derivatives to an exposed site
    • Diaz J.F., Strobe R., Engelborghs Y., Souto A.A., Andreu J.M. Molecular recognition of Taxol by microtubules - kinetics and thermodynamics of binding of fluorescent Taxol derivatives to an exposed site. J. Biol. Chem. 275:2000;26265-26276
    • (2000) J. Biol. Chem , vol.275 , pp. 26265-26276
    • Diaz, J.F.1    Strobe, R.2    Engelborghs, Y.3    Souto, A.A.4    Andreu, J.M.5
  • 33
    • 0027891882 scopus 로고
    • Tubulin conformation in zinc-induced sheets and macrotubes
    • Wolf S.G., Mosser G., Downing K.H. Tubulin conformation in zinc-induced sheets and macrotubes. J. Struct. Biol. 111:1993;190-199
    • (1993) J. Struct. Biol , vol.111 , pp. 190-199
    • Wolf, S.G.1    Mosser, G.2    Downing, K.H.3
  • 34
    • 0041156161 scopus 로고    scopus 로고
    • Limited flexibility of the interprotofilament bonds in microtubules assembled from pure tubulin
    • Chrétien D., Flyvbjerg H., Fuller S.F. Limited flexibility of the interprotofilament bonds in microtubules assembled from pure tubulin. Eur. Biophys. J. 27:1998;490-500
    • (1998) Eur. Biophys. J , vol.27 , pp. 490-500
    • Chrétien, D.1    Flyvbjerg, H.2    Fuller, S.F.3
  • 35
    • 0034518173 scopus 로고    scopus 로고
    • Structural basis for the interaction of tubulin with proteins and drugs that affect microtubule dynamics
    • Downing K.H. Structural basis for the interaction of tubulin with proteins and drugs that affect microtubule dynamics. Annu. Rev. Cell Dev. Biol. 16:2000;89-111
    • (2000) Annu. Rev. Cell Dev. Biol , vol.16 , pp. 89-111
    • Downing, K.H.1
  • 36
    • 0026319199 scopus 로고
    • Protein folding and association - Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association - insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11:1991;281-296
    • (1991) Proteins Struct. Funct. Genet , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.