메뉴 건너뛰기




Volumn 2007, Issue 79, 2007, Pages 437-462

Electron Microscopy of Microtubule-Based Cytoskeletal Machinery

Author keywords

[No Author keywords available]

Indexed keywords

MICROTUBULE ASSOCIATED PROTEIN;

EID: 33847196039     PISSN: 0091679X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0091-679X(06)79017-3     Document Type: Review
Times cited : (8)

References (87)
  • 1
    • 0344198646 scopus 로고    scopus 로고
    • Distinct conformations of the kinesin Unc104 neck regulate a monomer to dimer motor transition
    • Al-Bassam J., Cui Y., Klopfenstein D., Carragher B.O., Vale R.D., and Milligan R.A. Distinct conformations of the kinesin Unc104 neck regulate a monomer to dimer motor transition. J. Cell Biol. 163 (2003) 743-753
    • (2003) J. Cell Biol. , vol.163 , pp. 743-753
    • Al-Bassam, J.1    Cui, Y.2    Klopfenstein, D.3    Carragher, B.O.4    Vale, R.D.5    Milligan, R.A.6
  • 2
    • 0037166943 scopus 로고    scopus 로고
    • MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments
    • Al-Bassam J., Ozer R.S., Safer D., Halpain S., and Milligan R.A. MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments. J. Cell Biol. 157 (2002) 1187-1196
    • (2002) J. Cell Biol. , vol.157 , pp. 1187-1196
    • Al-Bassam, J.1    Ozer, R.S.2    Safer, D.3    Halpain, S.4    Milligan, R.A.5
  • 3
    • 0018399930 scopus 로고
    • The three-dimensional structure of tubulin protofilaments
    • Amos L.A., and Baker T.S. The three-dimensional structure of tubulin protofilaments. Nature 279 (1979) 607-612
    • (1979) Nature , vol.279 , pp. 607-612
    • Amos, L.A.1    Baker, T.S.2
  • 4
    • 0016367327 scopus 로고
    • Arrangement of subunits in flagellar microtubules
    • Amos L.A., and Klug A. Arrangement of subunits in flagellar microtubules. J. Cell Sci. 14 (1974) 523-549
    • (1974) J. Cell Sci. , vol.14 , pp. 523-549
    • Amos, L.A.1    Klug, A.2
  • 5
    • 0030266603 scopus 로고    scopus 로고
    • Three-dimensional structure of functional motor proteins on microtubules
    • Arnal I., Metoz F., DeBonis S., and 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
  • 6
    • 0033082710 scopus 로고    scopus 로고
    • Electron tomography of molecules and cells
    • Baumeister W., Grimm R., and Walz J. Electron tomography of molecules and cells. Trends Cell Biol. 9 (1999) 81-85
    • (1999) Trends Cell Biol. , vol.9 , pp. 81-85
    • Baumeister, W.1    Grimm, R.2    Walz, J.3
  • 8
    • 0024163316 scopus 로고
    • The reconstruction of helical particles with variable pitch
    • Bluemke D.A., Carragher B., and Josephs R. The reconstruction of helical particles with variable pitch. Ultramicroscopy 26 (1988) 255-270
    • (1988) Ultramicroscopy , vol.26 , pp. 255-270
    • Bluemke, D.A.1    Carragher, B.2    Josephs, R.3
  • 11
    • 0027463255 scopus 로고
    • Structural and functional domains of the Drosophila ncd microtubule motor protein
    • Chandra R., Salmon E.D., Erickson H.P., Lockhart A., and Endow S.A. Structural and functional domains of the Drosophila ncd microtubule motor protein. J. Biol. Chem. 268 (1993) 9005-9013
    • (1993) J. Biol. Chem. , vol.268 , pp. 9005-9013
    • Chandra, R.1    Salmon, E.D.2    Erickson, H.P.3    Lockhart, A.4    Endow, S.A.5
  • 12
    • 0025814877 scopus 로고
    • New data on the microtubule surface lattice
    • Chrétien D., and Wade R.H. 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.H.2
  • 13
    • 0030587566 scopus 로고    scopus 로고
    • Determination of microtubule polarity by cryo-electron microscopy
    • Chrétien D., Kenney J.M., Fuller S.D., and Wade R.H. Determination of microtubule polarity by cryo-electron microscopy. Structure 4 (1996) 1031-1040
    • (1996) Structure , vol.4 , pp. 1031-1040
    • Chrétien, D.1    Kenney, J.M.2    Fuller, S.D.3    Wade, R.H.4
  • 14
    • 0026667023 scopus 로고
    • Lattice defects in microtubules: Protofilament numbers vary within individual microtubules
    • Chrétien D., Metoz F., Verde F., Karsenti E., and 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
  • 15
    • 0014945329 scopus 로고
    • Reconstruction of three-dimensional images from electron micrographs of structures with helical symmetry
    • DeRosier D., and Moore P.B. Reconstruction of three-dimensional images from electron micrographs of structures with helical symmetry. J. Mol. Biol. 52 (1970) 355-369
    • (1970) J. Mol. Biol. , vol.52 , pp. 355-369
    • DeRosier, D.1    Moore, P.B.2
  • 16
    • 0344628696 scopus 로고    scopus 로고
    • Motor protein decoration of microtubules grown in high salt conditions reveals the presence of mixed lattices
    • Dias D.P., and Milligan R.A. Motor protein decoration of microtubules grown in high salt conditions reveals the presence of mixed lattices. J. Mol. Biol. 287 (1999) 287-292
    • (1999) J. Mol. Biol. , vol.287 , pp. 287-292
    • Dias, D.P.1    Milligan, R.A.2
  • 17
    • 0034564239 scopus 로고    scopus 로고
    • A robust algorithm for the reconstruction of helical filaments using single-particle methods
    • Egelman E.H. A robust algorithm for the reconstruction of helical filaments using single-particle methods. Ultramicroscopy 85 (2000) 225-234
    • (2000) Ultramicroscopy , vol.85 , pp. 225-234
    • Egelman, E.H.1
  • 18
    • 0036089703 scopus 로고    scopus 로고
    • Single-particle imaging of macromolecules by cryo-electron microscopy
    • Frank J. Single-particle imaging of macromolecules by cryo-electron microscopy. Annu. Rev. Biophys. Biomol. Struct. 31 (2002) 303-319
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 303-319
    • Frank, J.1
  • 19
    • 0020484108 scopus 로고
    • Correspondence analysis of aligned images of biological particles
    • Frank J., and van Heel M. Correspondence analysis of aligned images of biological particles. J. Mol. Biol. 161 (1982) 134-137
    • (1982) J. Mol. Biol. , vol.161 , pp. 134-137
    • Frank, J.1    van Heel, M.2
  • 20
    • 0015372444 scopus 로고
    • Flagellar movement and adenosine triphosphatase activity in sea urchin sperm extracted with triton X-100
    • Gibbons B.H., and Gibbons I.R. Flagellar movement and adenosine triphosphatase activity in sea urchin sperm extracted with triton X-100. J. Cell Biol. 54 (1972) 75-97
    • (1972) J. Cell Biol. , vol.54 , pp. 75-97
    • Gibbons, B.H.1    Gibbons, I.R.2
  • 21
    • 0015840312 scopus 로고
    • The effect of partial extraction of dynein arms on the movement of reactivated sea-urchin sperm
    • Gibbons B.H., and Gibbons I.R. The effect of partial extraction of dynein arms on the movement of reactivated sea-urchin sperm. J. Cell Sci. 13 (1973) 337-357
    • (1973) J. Cell Sci. , vol.13 , pp. 337-357
    • Gibbons, B.H.1    Gibbons, I.R.2
  • 22
    • 0019781934 scopus 로고
    • Cilia and flagella of eukaryotes
    • Gibbons I.R. Cilia and flagella of eukaryotes. J. Cell Biol. 91 (1981) 107s-124s
    • (1981) J. Cell Biol. , vol.91
    • Gibbons, I.R.1
  • 23
    • 0023039056 scopus 로고
    • Different structural states of a microtubule cross-linking molecule, captured by quick-freezing motile axostyles in protozoa
    • Heuser J.E. Different structural states of a microtubule cross-linking molecule, captured by quick-freezing motile axostyles in protozoa. J. Cell Biol. 103 (1986) 2209-2227
    • (1986) J. Cell Biol. , vol.103 , pp. 2209-2227
    • Heuser, J.E.1
  • 24
    • 0020326774 scopus 로고
    • Cross-linker system between neurofilaments, microtubules, and membranous organelles in frog axons revealed by the quick-freeze, deep-etching method
    • Hirokawa N. Cross-linker system between neurofilaments, microtubules, and membranous organelles in frog axons revealed by the quick-freeze, deep-etching method. J. Cell Biol. 94 (1982) 129-142
    • (1982) J. Cell Biol. , vol.94 , pp. 129-142
    • Hirokawa, N.1
  • 25
    • 0032559260 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins and the mechanism of organelle transport
    • Hirokawa N. Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science 279 (1998) 519-526
    • (1998) Science , vol.279 , pp. 519-526
    • Hirokawa, N.1
  • 26
    • 0032079618 scopus 로고    scopus 로고
    • Nucleotide-dependent structural changes in dimeric NCD molecules complexed to microtubules
    • Hirose K., Cross R.A., and Amos L.A. Nucleotide-dependent structural changes in dimeric NCD molecules complexed to microtubules. J. Mol. Biol. 278 (1998) 389-400
    • (1998) J. Mol. Biol. , vol.278 , pp. 389-400
    • Hirose, K.1    Cross, R.A.2    Amos, L.A.3
  • 27
    • 0034675854 scopus 로고    scopus 로고
    • Structural comparison of dimeric Eg5, Neurospora kinesin (Nkin) and Ncd head-Nkin neck chimera with conventional kinesin
    • Hirose K., Henningsen U., Schliwa M., Toyoshima C., Shimizu T., Alonso M., Cross R.A., and Amos L.A. Structural comparison of dimeric Eg5, Neurospora kinesin (Nkin) and Ncd head-Nkin neck chimera with conventional kinesin. EMBO J. 10 (2000) 5308-5314
    • (2000) EMBO J. , vol.10 , pp. 5308-5314
    • Hirose, K.1    Henningsen, U.2    Schliwa, M.3    Toyoshima, C.4    Shimizu, T.5    Alonso, M.6    Cross, R.A.7    Amos, L.A.8
  • 28
    • 0033783008 scopus 로고    scopus 로고
    • Surface topography of microtubule walls decorated with monomeric and dimeric kinesin constructs
    • Hoenger A., Doerhoefer M., Woehlke G., Tittmann P., Gross H., Song Y.-H., and Mandelkow E. Surface topography of microtubule walls decorated with monomeric and dimeric kinesin constructs. Biol. Chem. 381 (2000) 1001-1011
    • (2000) Biol. Chem. , vol.381 , pp. 1001-1011
    • Hoenger, A.1    Doerhoefer, M.2    Woehlke, G.3    Tittmann, P.4    Gross, H.5    Song, Y.-H.6    Mandelkow, E.7
  • 29
    • 0031556947 scopus 로고    scopus 로고
    • Motor domains of kinesin and ncd interact with microtubule protofilaments with the same binding geometry
    • Hoenger A., and Milligan R.A. Motor domains of kinesin and ncd interact with microtubule protofilaments with the same binding geometry. J. Mol. Biol. 265 (1997) 553-564
    • (1997) J. Mol. Biol. , vol.265 , pp. 553-564
    • Hoenger, A.1    Milligan, R.A.2
  • 31
    • 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., Thormählen M., Marx A., Muller J., Gross H., and Mandelkow E. Image reconstructions of microtubules decorated with monomeric and dimeric kinesins: Comparison with x-ray structure and implications for motility. J. Cell Biol. 141 (1998) 419-430
    • (1998) J. Cell Biol. , vol.141 , pp. 419-430
    • Hoenger, A.1    Sack, S.2    Thormählen, M.3    Marx, A.4    Muller, J.5    Gross, H.6    Mandelkow, E.7
  • 33
    • 0037413708 scopus 로고    scopus 로고
    • Repeat motifs of tau bind to the insides of microtubules in the absence of taxol
    • Kar S., Fan J., Smith M.J., Goedert M., and Amos L.A. Repeat motifs of tau bind to the insides of microtubules in the absence of taxol. EMBO J. 22 (2003) 70-77
    • (2003) EMBO J. , vol.22 , pp. 70-77
    • Kar, S.1    Fan, J.2    Smith, M.J.3    Goedert, M.4    Amos, L.A.5
  • 34
    • 0028597558 scopus 로고
    • Direct visualization of the microtubule lattice seam both in vitro and in vivo
    • Kikkawa M., Ishikawa T., Nakata T., Wakabayashi T., and Hirokawa N. Direct visualization of the microtubule lattice seam both in vitro and in vivo. J. Cell Biol. 127 (1994) 1965-1971
    • (1994) J. Cell Biol. , vol.127 , pp. 1965-1971
    • Kikkawa, M.1    Ishikawa, T.2    Nakata, T.3    Wakabayashi, T.4    Hirokawa, N.5
  • 35
    • 0028979606 scopus 로고
    • Three-dimensional structure of the kinesin head-microtubule complex
    • Kikkawa M., Ishikawa T., Wakabayashi T., and 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
  • 37
    • 0027050116 scopus 로고
    • Dynein from Dictyostelium: Primary structure comparisons between a cytoplasmic motor enzyme and flagellar dynein
    • Koonce M.P., Grissom P.M., and McIntosh J.R. Dynein from Dictyostelium: Primary structure comparisons between a cytoplasmic motor enzyme and flagellar dynein. J. Cell Biol. 119 (1992) 1597-1604
    • (1992) J. Cell Biol. , vol.119 , pp. 1597-1604
    • Koonce, M.P.1    Grissom, P.M.2    McIntosh, J.R.3
  • 38
    • 0345118121 scopus 로고    scopus 로고
    • Complex formation with kinesin motor domains affects the structure of microtubules
    • Krebs A., Goldie K.N., and Hoenger A. Complex formation with kinesin motor domains affects the structure of microtubules. J. Mol. Biol. 335 (2004) 139-153
    • (2004) J. Mol. Biol. , vol.335 , pp. 139-153
    • Krebs, A.1    Goldie, K.N.2    Hoenger, A.3
  • 42
    • 0035834521 scopus 로고    scopus 로고
    • Refined structure of alpha beta-tubulin at 3.5 A resolution
    • Löwe J., Li H., Downing K.H., and 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
  • 43
    • 0022384496 scopus 로고
    • Unstained microtubules studied by cryo-electron microscopy. Substructure, supertwist and disassembly
    • Mandelkow E.M., and Mandelkow E. Unstained microtubules studied by cryo-electron microscopy. Substructure, supertwist and disassembly. J. Mol. Biol. 181 (1985) 123-135
    • (1985) J. Mol. Biol. , vol.181 , pp. 123-135
    • Mandelkow, E.M.1    Mandelkow, E.2
  • 44
    • 0022483059 scopus 로고
    • On the surface lattice of microtubules: Helix starts, protofilament number, seam and handedness
    • Mandelkow E.M., Schultheiss R., Rapp R., Muller M., and Mandelkow E. On the surface lattice of microtubules: Helix starts, protofilament number, seam and handedness. J. Cell Biol. 102 (1986) 1067-1073
    • (1986) J. Cell Biol. , vol.102 , pp. 1067-1073
    • Mandelkow, E.M.1    Schultheiss, R.2    Rapp, R.3    Muller, M.4    Mandelkow, E.5
  • 45
    • 0025608711 scopus 로고
    • The kinesin-like ncd protein of Drosophila is a minus end-directed microtubule motor
    • McDonald H.B., Stewart R.J., and Goldstein L.S. The kinesin-like ncd protein of Drosophila is a minus end-directed microtubule motor. Cell 63 (1990) 1159-1165
    • (1990) Cell , vol.63 , pp. 1159-1165
    • McDonald, H.B.1    Stewart, R.J.2    Goldstein, L.S.3
  • 46
    • 11844305068 scopus 로고    scopus 로고
    • New views of cells in 3D: An introduction to electron tomography
    • McIntosh R., Nicastro D., and Mastronarde D. New views of cells in 3D: An introduction to electron tomography. Trends Cell Biol. 15 (2005) 43-51
    • (2005) Trends Cell Biol. , vol.15 , pp. 43-51
    • McIntosh, R.1    Nicastro, D.2    Mastronarde, D.3
  • 47
    • 0031010401 scopus 로고    scopus 로고
    • Tomography without tilt: Three-dimensional imaging of microtubule/motor complexes
    • Metoz F., Arnal I., and Wade R.H. 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.H.3
  • 48
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • Miyazawa A., Fujiyoshi Y., and Unwin N. Structure and gating mechanism of the acetylcholine receptor pore. Nature 423 (2003) 949-955
    • (2003) Nature , vol.423 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 50
    • 0014945041 scopus 로고
    • Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments
    • Moore P.B., Huxley H.E., and DeRosier D.J. Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments. J. Mol. Biol. 50 (1970) 279-295
    • (1970) J. Mol. Biol. , vol.50 , pp. 279-295
    • Moore, P.B.1    Huxley, H.E.2    DeRosier, D.J.3
  • 52
    • 0026931780 scopus 로고
    • Processing images of helical structures: A new twist
    • Morgan D.G., and DeRosier D. Processing images of helical structures: A new twist. Ultramicroscopy 46 (1992) 263-285
    • (1992) Ultramicroscopy , vol.46 , pp. 263-285
    • Morgan, D.G.1    DeRosier, D.2
  • 53
    • 27644477833 scopus 로고    scopus 로고
    • 3D structure of eukaryotic flagella in a quiescent state revealed by cryo-electron tomography
    • Nicastro D., McIntosh J.R., and Baumeister W. 3D structure of eukaryotic flagella in a quiescent state revealed by cryo-electron tomography. Proc. Natl. Acad. Sci. USA 102 (2005) 15889-15894
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15889-15894
    • Nicastro, D.1    McIntosh, J.R.2    Baumeister, W.3
  • 54
    • 33747598723 scopus 로고    scopus 로고
    • Cryo-tomography of axonemes: Insights into the regulation of dynein activity and microtubule stability
    • Nicastro D., Schwartz C., Pierson J., Gaudette R., Porter M.E., and McIntosh J.R. Cryo-tomography of axonemes: Insights into the regulation of dynein activity and microtubule stability. Science 313 (2006) 944-948
    • (2006) Science , vol.313 , pp. 944-948
    • Nicastro, D.1    Schwartz, C.2    Pierson, J.3    Gaudette, R.4    Porter, M.E.5    McIntosh, J.R.6
  • 55
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the alpha beta tubulin dimer by electron crystallography
    • Nogales E., Wolf S.G., and Downing K.H. Structure of the alpha beta 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
  • 62
    • 3242809790 scopus 로고    scopus 로고
    • 25 Å resolution structure of a cytoplasmic dynein motor reveals a seven-member planar ring
    • Samso M., and Koonce M.P. 25 Å resolution structure of a cytoplasmic dynein motor reveals a seven-member planar ring. J. Mol. Biol. 340 (2004) 1059-1072
    • (2004) J. Mol. Biol. , vol.340 , pp. 1059-1072
    • Samso, M.1    Koonce, M.P.2
  • 63
    • 33845683023 scopus 로고    scopus 로고
    • The Schizosaccharomyces pombe EB1 homolog Mal3p localizes preferentially to the Microtubule Lattice Seam
    • in press
    • Sandblad L., Busch K.E., Tittmann P., Gross H., Brunner D., and Hoenger A. The Schizosaccharomyces pombe EB1 homolog Mal3p localizes preferentially to the Microtubule Lattice Seam. Cell (2006) in press
    • (2006) Cell
    • Sandblad, L.1    Busch, K.E.2    Tittmann, P.3    Gross, H.4    Brunner, D.5    Hoenger, A.6
  • 66
    • 0029868995 scopus 로고    scopus 로고
    • Kinesin-II, a membrane traffic motor in axons, axonemes, and spindles
    • Scholey J.M. Kinesin-II, a membrane traffic motor in axons, axonemes, and spindles. J. Cell Biol. 133 (1996) 1-4
    • (1996) J. Cell Biol. , vol.133 , pp. 1-4
    • Scholey, J.M.1
  • 67
    • 0029928871 scopus 로고    scopus 로고
    • SUPRIM: Easily modified image-processing software
    • Schroeter J.P., and Bretaudiere J.P. SUPRIM: Easily modified image-processing software. J. Struct. Biol. 116 (1996) 131-137
    • (1996) J. Struct. Biol. , vol.116 , pp. 131-137
    • Schroeter, J.P.1    Bretaudiere, J.P.2
  • 69
    • 0027405349 scopus 로고
    • Recombinant kinesin motor domain binds to αβ-tubulin and decorates microtubules with a B surface lattice
    • Song Y.-H., and Mandelkow E. Recombinant kinesin motor domain binds to αβ-tubulin and decorates microtubules with a B surface lattice. Proc. Natl. Acad. Sci. USA 90 (1993) 1671-1675
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1671-1675
    • Song, Y.-H.1    Mandelkow, E.2
  • 70
    • 0028854634 scopus 로고
    • The anatomy of flagellar microtubules: Polarity, seam, junctions and lattice
    • Song Y.-H., and Mandelkow E. The anatomy of flagellar microtubules: Polarity, seam, junctions and lattice. J. Cell Biol. 128 (1995) 81-94
    • (1995) J. Cell Biol. , vol.128 , pp. 81-94
    • Song, Y.-H.1    Mandelkow, E.2
  • 71
    • 0031596860 scopus 로고    scopus 로고
    • Relationship between moiré patterns, tubulin shape, and microtubule polarity
    • Sosa H., and Chrétien D. Relationship between moiré patterns, tubulin shape, and microtubule polarity. Cell Motil. Cytoskeleton 40 (1998) 38-43
    • (1998) Cell Motil. Cytoskeleton , vol.40 , pp. 38-43
    • Sosa, H.1    Chrétien, D.2
  • 73
    • 0030564927 scopus 로고    scopus 로고
    • Three-dimensional structure of ncd-decorated microtubules obtained by a back-projection method
    • Sosa H., and Milligan R.A. Three-dimensional structure of ncd-decorated microtubules obtained by a back-projection method. J. Mol. Biol. 260 (1996) 743-755
    • (1996) J. Mol. Biol. , vol.260 , pp. 743-755
    • Sosa, H.1    Milligan, R.A.2
  • 74
    • 0018782254 scopus 로고
    • Three-dimensional reconstruction of tubulin in zinc-induced sheets
    • Tamm L.K., Crepeau R.H., and Edelstein S.T. Three-dimensional reconstruction of tubulin in zinc-induced sheets. J. Mol. Biol. 130 (1979) 473-492
    • (1979) J. Mol. Biol. , vol.130 , pp. 473-492
    • Tamm, L.K.1    Crepeau, R.H.2    Edelstein, S.T.3
  • 75
    • 0037459061 scopus 로고    scopus 로고
    • The molecular motor toolbox for intracellular transport
    • Vale R.D. The molecular motor toolbox for intracellular transport. Cell 112 (2003) 467-480
    • (2003) Cell , vol.112 , pp. 467-480
    • Vale, R.D.1
  • 76
    • 0842333851 scopus 로고    scopus 로고
    • Dynein: An ancient motor protein involved in multiple modes of transport
    • Vallee R.B., Williams J.C., Varma D., and Barnhart L.E. Dynein: An ancient motor protein involved in multiple modes of transport. J. Neurobiol. 58 (2004) 189-200
    • (2004) J. Neurobiol. , vol.58 , pp. 189-200
    • Vallee, R.B.1    Williams, J.C.2    Varma, D.3    Barnhart, L.E.4
  • 77
    • 0021645447 scopus 로고
    • Multivariate statistical classification of noisy images (randomly oriented biological macromolecules)
    • Van Heel M. Multivariate statistical classification of noisy images (randomly oriented biological macromolecules). Ultramicroscopy 13 (1984) 165-183
    • (1984) Ultramicroscopy , vol.13 , pp. 165-183
    • Van Heel, M.1
  • 78
    • 0019728717 scopus 로고
    • Use of multivariate statistics in analyzing the images of biological macromolecules
    • Van Heel M., and Frank J. Use of multivariate statistics in analyzing the images of biological macromolecules. Ultramicroscopy 6 (1981) 187-194
    • (1981) Ultramicroscopy , vol.6 , pp. 187-194
    • Van Heel, M.1    Frank, J.2
  • 79
    • 0032779888 scopus 로고    scopus 로고
    • Quantitative fitting of atomic models into observed densities derived by electron microscopy
    • Volkmann N., and Hanein D. Quantitative fitting of atomic models into observed densities derived by electron microscopy. J. Struct. Biol. 125 (1999) 176-184
    • (1999) J. Struct. Biol. , vol.125 , pp. 176-184
    • Volkmann, N.1    Hanein, D.2
  • 80
    • 0029618993 scopus 로고
    • Toward understanding the structure and interactions of microtubules and motor proteins
    • Wade R.H., Horowitz R., and Milligan R.A. Toward understanding the structure and interactions of microtubules and motor proteins. Proteins Struct. Funct. Genet. 23 (1995) 502-509
    • (1995) Proteins Struct. Funct. Genet. , vol.23 , pp. 502-509
    • Wade, R.H.1    Horowitz, R.2    Milligan, R.A.3
  • 81
    • 0025186134 scopus 로고
    • The Drosophila claret segregation protein is a minus-end directed motor molecule
    • Walker R.A., Salmon E.D., and Endow S.A. The Drosophila claret segregation protein is a minus-end directed motor molecule. Nature 347 (1990) 780-782
    • (1990) Nature , vol.347 , pp. 780-782
    • Walker, R.A.1    Salmon, E.D.2    Endow, S.A.3
  • 83
    • 0141750616 scopus 로고    scopus 로고
    • A structural analysis of the interaction between ncd tail and tubulin protofilaments
    • Wendt T., Karabay A., Krebs A., Gross H., Walker R.A., and Hoenger A. A structural analysis of the interaction between ncd tail and tubulin protofilaments. J. Mol. Biol. 333 (2003) 541-552
    • (2003) J. Mol. Biol. , vol.333 , pp. 541-552
    • Wendt, T.1    Karabay, A.2    Krebs, A.3    Gross, H.4    Walker, R.A.5    Hoenger, A.6
  • 85
    • 0029311258 scopus 로고
    • PHOELIX: A package for semi-automated helical reconstruction
    • Whittaker M., Carragher B.O., and Milligan R.A. PHOELIX: A package for semi-automated helical reconstruction. Ultramicroscopy 58 (1995) 245-259
    • (1995) Ultramicroscopy , vol.58 , pp. 245-259
    • Whittaker, M.1    Carragher, B.O.2    Milligan, R.A.3
  • 86
    • 0032780181 scopus 로고    scopus 로고
    • Situs: A package for docking crystal structures into low-resolution maps from electron microscopy
    • Wriggers W., Milligan R.A., and McCammon J.A. Situs: A package for docking crystal structures into low-resolution maps from electron microscopy. J. Struct. Biol. 125 (1999) 185-195
    • (1999) J. Struct. Biol. , vol.125 , pp. 185-195
    • Wriggers, W.1    Milligan, R.A.2    McCammon, J.A.3
  • 87
    • 0042238051 scopus 로고    scopus 로고
    • Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy
    • Yonekura K., Maki-Yonekura S., and Namba K. Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy. Nature 424 (2003) 643-650
    • (2003) Nature , vol.424 , pp. 643-650
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.