메뉴 건너뛰기




Volumn 56, Issue 3-4, 1999, Pages 184-199

Three-dimensional structure of motor molecules

Author keywords

Actin; Cryo electron microscopy; Kinesin; Microtubules; Myosin; ncd; Tubulin

Indexed keywords

KINESIN; MICROTUBULE PROTEIN; MYOSIN; TUBULIN;

EID: 0033569597     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050421     Document Type: Review
Times cited : (15)

References (117)
  • 1
    • 0027279053 scopus 로고
    • Direction of microtubule movement is an intrinsic property of the motor domains of kinesin heavy chain and Drosophila ned protein
    • Stewart R. J., Thaler J. P. and Goldstein L. S. B. (1993) Direction of microtubule movement is an intrinsic property of the motor domains of kinesin heavy chain and Drosophila ned protein. Proc. Natl. Acad. Sci. USA 90: 5209-5213
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5209-5213
    • Stewart, R.J.1    Thaler, J.P.2    Goldstein, L.S.B.3
  • 2
    • 0028363764 scopus 로고
    • Drosophila kinesin minimal motor domain expressed in Escherichia-coli purification and kinetic characterization
    • Huang T. G. and Hackney D. D. (1994) Drosophila kinesin minimal motor domain expressed in Escherichia-coli purification and kinetic characterization. J. Biol. Chem. 269: 16493-16501
    • (1994) J. Biol. Chem. , vol.269 , pp. 16493-16501
    • Huang, T.G.1    Hackney, D.D.2
  • 3
    • 0030444538 scopus 로고    scopus 로고
    • Muscle proteins their actions and interetions
    • Holmes K. C. (1996) Muscle proteins their actions and interetions. Curr. Opin. Struct. Biol. 6: 781-789
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 781-789
    • Holmes, K.C.1
  • 4
    • 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. (1990) The Drosophila claret segregation protein is a minus-end directed motor molecule. Nature 347: 780-782
    • (1990) Nature , vol.347 , pp. 780-782
    • Walker, R.A.1    Salmon, E.D.2    Endow, S.A.3
  • 5
    • 0025608711 scopus 로고
    • The kinesin-like ned protein of Drosophila is a minus end-directed microtubule motor
    • McDonald H. B., Stewart R. J. and Goldstein L. S. B. (1990) The kinesin-like ned protein of Drosophila is a minus end-directed microtubule motor. Cell 63: 1159-1165
    • (1990) Cell , vol.63 , pp. 1159-1165
    • McDonald, H.B.1    Stewart, R.J.2    Goldstein, L.S.B.3
  • 6
    • 0028979598 scopus 로고
    • Nucleotide-dependent angular change in kinesin motor domain bound to tubulin
    • Hirose K., Lockhart A., Cross R. A. and Amos L. A. (1995) Nucleotide-dependent angular change in kinesin motor domain bound to tubulin. Nature (London) 376: 277-279
    • (1995) Nature (London) , vol.376 , pp. 277-279
    • Hirose, K.1    Lockhart, A.2    Cross, R.A.3    Amos, L.A.4
  • 8
    • 0028979606 scopus 로고
    • Three-dimensional structure of the kinesin head-microtubule complex
    • Kikkawa M., Ishikawa T., Wakabayashi T. and Hirokawa N. (1995) Three-dimensional structure of the kinesin head-microtubule complex. Nature 376: 274- 279
    • (1995) Nature , vol.376 , pp. 274-279
    • Kikkawa, M.1    Ishikawa, T.2    Wakabayashi, T.3    Hirokawa, N.4
  • 9
    • 0029989974 scopus 로고    scopus 로고
    • Crystal structure of the kinesin motor domain reveals a structural similarity to myosin
    • Kull F. J., Sablin E. P., Lau R., Fletterick R. J. and Vale R. D. (1996) Crystal structure of the kinesin motor domain reveals a structural similarity to myosin. Nature 380; 550-555
    • (1996) Nature , vol.380 , pp. 550-555
    • Kull, F.J.1    Sablin, E.P.2    Lau, R.3    Fletterick, R.J.4    Vale, R.D.5
  • 10
    • 0029878485 scopus 로고    scopus 로고
    • Crystal structure of the motor domain of the kinesin-related motor ned
    • Sablin E. P., Kull F. J., Cooke R., Vale R. D. and Fletterick R. J. (1996) Crystal structure of the motor domain of the kinesin-related motor ned. Nature 380: 555-559
    • (1996) Nature , vol.380 , pp. 555-559
    • Sablin, E.P.1    Kull, F.J.2    Cooke, R.3    Vale, R.D.4    Fletterick, R.J.5
  • 11
    • 0032559260 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins and the mechanism of organelle transport
    • Hirokawa N. (1998) Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science 279: 519-526
    • (1998) Science , vol.279 , pp. 519-526
    • Hirokawa, N.1
  • 12
    • 0027463255 scopus 로고
    • Structural and functional domains of the Drosophila ned microtubule motor protein
    • Chandra R., Salmon E. D., Erickson H. P., Lockhart A. and Endow S. A. (1993) Structural and functional domains of the Drosophila ned microtubule motor protein. J. Biol. Chem. 268: 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
  • 13
    • 0032559690 scopus 로고    scopus 로고
    • Leading the procession: New insights into kinesin motors
    • Block S. M. (1998) Leading the procession: new insights into kinesin motors. J. Cell Biol. 140: 1281- 1284
    • (1998) J. Cell Biol. , vol.140 , pp. 1281-1284
    • Block, S.M.1
  • 16
    • 0032558718 scopus 로고    scopus 로고
    • Direction determination in the minus-end-directed kinesin motor ned
    • Sablin L., Case R. B., Dai S. C., Hart C. L., Ruby A., Vale R. D. et al. (1998) Direction determination in the minus-end-directed kinesin motor ned. Nature 395: 813-816
    • (1998) Nature , vol.395 , pp. 813-816
    • Sablin, L.1    Case, R.B.2    Dai, S.C.3    Hart, C.L.4    Ruby, A.5    Vale, R.D.6
  • 17
    • 0030198499 scopus 로고    scopus 로고
    • Myosin and kinesin mother and child reunited
    • Hackney D. D. (1996) Myosin and kinesin mother and child reunited. Chem. Biol. 3: 525-528
    • (1996) Chem. Biol. , vol.3 , pp. 525-528
    • Hackney, D.D.1
  • 18
    • 0030267349 scopus 로고    scopus 로고
    • Switches, latches and amplifiers: Common themes of G proteins and molecular motors
    • Vale R. D. (1996) Switches, latches and amplifiers: common themes of G proteins and molecular motors. J. Cell Biol. 135: 291-302
    • (1996) J. Cell Biol. , vol.135 , pp. 291-302
    • Vale, R.D.1
  • 20
    • 0029960345 scopus 로고    scopus 로고
    • The movement of kinesin along microtubules
    • Howard J. (1996) The movement of kinesin along microtubules. Ann. Rev. Physiol. 58: 703-729
    • (1996) Ann. Rev. Physiol. , vol.58 , pp. 703-729
    • Howard, J.1
  • 21
    • 0030004865 scopus 로고    scopus 로고
    • The active site of myosin
    • Rayment I. and Smith C. (1996) The active site of myosin, Ann. Rev. Physiol. 58: 671-702
    • (1996) Ann. Rev. Physiol. , vol.58 , pp. 671-702
    • Rayment, I.1    Smith, C.2
  • 22
    • 0029873077 scopus 로고    scopus 로고
    • The kinetic cycles of myosin, kinesin and dynein
    • Hackney D. D. (1996) The kinetic cycles of myosin, kinesin and dynein. Ann. Rev. Physiol. 58: 731- 750
    • (1996) Ann. Rev. Physiol. , vol.58 , pp. 731-750
    • Hackney, D.D.1
  • 23
    • 0027405349 scopus 로고
    • Recombinant kinesin motor domain binds to β-tubulin and decorates microtubules with a B surface lattice
    • Song Y.-H. and Mandelkow E. (1993) Recombinant kinesin motor domain binds to β-tubulin and decorates microtubules with a B surface lattice. Proc. Natl. Acad. Sci. USA 90: 1671-1675
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1671-1675
    • Song, Y.-H.1    Mandelkow, E.2
  • 25
    • 0028854634 scopus 로고
    • The anatomy of flagellar microtubules: Polarity, seam, junctions and lattice
    • Song Y.-H. and Mandelkow E. (1995) The anatomy of flagellar microtubules: polarity, seam, junctions and lattice. J. Cell Biol. 128: 81-94
    • (1995) J. Cell Biol. , vol.128 , pp. 81-94
    • Song, Y.-H.1    Mandelkow, E.2
  • 26
    • 0029114947 scopus 로고
    • Re-examination of the polarity of microtubules and sheets decorated with kinesin motor domain
    • Hirose K., Fan J. and Amos L. A. (1995) Re-examination of the polarity of microtubules and sheets decorated with kinesin motor domain. J. Mol. Biol. 251: 329-333
    • (1995) J. Mol. Biol. , vol.251 , pp. 329-333
    • Hirose, K.1    Fan, J.2    Amos, L.A.3
  • 27
    • 0031042321 scopus 로고    scopus 로고
    • The structure of microtubule-motor complexes
    • Amos L. A. and Hirose K. (1997) The structure of microtubule-motor complexes. Curr. Opin. Cell Biol. 9: 4-11
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 4-11
    • Amos, L.A.1    Hirose, K.2
  • 28
    • 0030601776 scopus 로고    scopus 로고
    • Polarity of 2-D and 3-D maps of tubulin sheets and motor decorated sheets
    • Hoenger A. and Milligan R. A. (1996) Polarity of 2-D and 3-D maps of tubulin sheets and motor decorated sheets. J. Mol. Biol. 263: 114-119
    • (1996) J. Mol. Biol. , vol.263 , pp. 114-119
    • Hoenger, A.1    Milligan, R.A.2
  • 30
    • 0030930492 scopus 로고    scopus 로고
    • Three-dimensional cryoelectron microscopy of 16-protofilament microtubules: Structure, polarity and interaction with motor protein
    • Hirose K., Amos W. B., Lockhart A., Cross R. A. and Amos L. A. (1997) Three-dimensional cryoelectron microscopy of 16-protofilament microtubules: structure, polarity and interaction with motor protein. J. Struct. Biol. 118: 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
  • 31
  • 32
    • 0032079618 scopus 로고    scopus 로고
    • Nucleotide-dependent structural changes in dimeric ned molecules complexed to microtubules
    • Hirose K., Cross R. A. and Amos L. A. (1998) Nucleotide-dependent structural changes in dimeric ned molecules complexed to microtubules. J. Mol. Biol. 278: 389-400
    • (1998) J. Mol. Biol. , vol.278 , pp. 389-400
    • Hirose, K.1    Cross, R.A.2    Amos, L.A.3
  • 33
    • 0029795642 scopus 로고    scopus 로고
    • Three-dimensional cryoelectron microscopy of dimeric kinesin and ned motor domains on microtubules
    • Hirose K., Lockhart A., Cross R. A. and Amos L. A. (1996) Three-dimensional cryoelectron microscopy of dimeric kinesin and ned motor domains on microtubules. Proc. Natl. Acad. Sci. USA 93: 9539-9544
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9539-9544
    • Hirose, K.1    Lockhart, A.2    Cross, R.A.3    Amos, L.A.4
  • 34
    • 0030266603 scopus 로고    scopus 로고
    • Three-dimensional structure of functional motor proteins on microtubules
    • Arnal I., Metoz F., DeBonis S. and Wade R. H. (1996) Three-dimensional structure of functional motor proteins on microtubules. Curr. Biol. 6: 1265-1270
    • (1996) Curr. Biol. , vol.6 , pp. 1265-1270
    • Arnal, I.1    Metoz, F.2    DeBonis, S.3    Wade, R.H.4
  • 35
    • 0030564927 scopus 로고    scopus 로고
    • Three-dimensional structure of ned-decorated microtubules obtained by a back-projection method
    • Sosa H. and Milligan R. A. (1996) Three-dimensional structure of ned-decorated microtubules obtained by a back-projection method. J. Mol. Biol. 260: 743- 755
    • (1996) J. Mol. Biol. , vol.260 , pp. 743-755
    • Sosa, H.1    Milligan, R.A.2
  • 36
    • 0343811700 scopus 로고    scopus 로고
    • A model for the microtubule-ned motor protein complex obtained by cryo-electron microscopy and image analysis
    • Sosa H., Dias D. P., Hoenger A., Whittaker M., Wilson-Kubalek E., Sablin E. et al. (1997) A model for the microtubule-ned motor protein complex obtained by cryo-electron microscopy and image analysis. Cell 90: 217-224
    • (1997) Cell , vol.90 , pp. 217-224
    • Sosa, H.1    Dias, D.P.2    Hoenger, A.3    Whittaker, M.4    Wilson-Kubalek, E.5    Sablin, E.6
  • 37
    • 0031556947 scopus 로고    scopus 로고
    • Motor domains of kinesin and ned interact with microtubule protofilaments with the same binding geometry
    • Hoenger A. and Milligan R. A. (1997) Motor domains of kinesin and ned interact with microtubule protofilaments with the same binding geometry. J. Mol. Biol. 265: 553-564
    • (1997) J. Mol. Biol. , vol.265 , pp. 553-564
    • Hoenger, A.1    Milligan, R.A.2
  • 38
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the ab tubulin dimer by electron crystallography
    • Nogales E., Wolf S. and Downing K. H. (1998a) Structure of the ab tubulin dimer by electron crystallography. Nature 391: 199-203
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.2    Downing, K.H.3
  • 39
    • 0028897278 scopus 로고
    • Kinesin does not support the motility of zinc-macrotubes
    • Ray S., Wolf S. G., Howard J. and Downing K. H. (1995) Kinesin does not support the motility of zinc-macrotubes. Cell Motil. Cytoskel. 30: 146-152
    • (1995) Cell Motil. Cytoskel. , vol.30 , pp. 146-152
    • Ray, S.1    Wolf, S.G.2    Howard, J.3    Downing, K.H.4
  • 40
    • 0030927934 scopus 로고    scopus 로고
    • Three different apporoaches for calculating the three-dimensional structure of microtubules decorated with kinesin motor domains
    • Sosa H., Hoenger A. and Milligan R. A. (1997) Three different apporoaches for calculating the three-dimensional structure of microtubules decorated with kinesin motor domains. J. Struct. Biol. 118: 149-158
    • (1997) J. Struct. Biol. , vol.118 , pp. 149-158
    • Sosa, H.1    Hoenger, A.2    Milligan, R.A.3
  • 41
    • 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. (1970) Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments. J. Mol. Biol. 50: 279-295
    • (1970) J. Mol. Biol. , vol.50 , pp. 279-295
    • Moore, P.B.1    Huxley, H.E.2    DeRosier, D.J.3
  • 42
    • 0019873176 scopus 로고
    • A new model for the geometry of the binding of myosin crossbridges to muscle thin filaments
    • Taylor K. A. and Amos L. A. (1981) A new model for the geometry of the binding of myosin crossbridges to muscle thin filaments. J. Mol. Biol. 147: 297- 324
    • (1981) J. Mol. Biol. , vol.147 , pp. 297-324
    • Taylor, K.A.1    Amos, L.A.2
  • 43
    • 0021914089 scopus 로고
    • Three-dimensional image analysis of the complex of thin filaments and myosin molecules from skeletal muscle. V. Assignment of actin in the actin-tropomyosin-myosin subfragment-I complex
    • Toyoshima C. and Wakabayashi T. (1985) Three-dimensional image analysis of the complex of thin filaments and myosin molecules from skeletal muscle. V. Assignment of actin in the actin-tropomyosin-myosin subfragment-I complex. J. Biochem. 97: 245-263
    • (1985) J. Biochem. , vol.97 , pp. 245-263
    • Toyoshima, C.1    Wakabayashi, T.2
  • 44
    • 0023374114 scopus 로고
    • Structural relationships of actin, myosin, and tropomyosin revealed by cryoelectron microscopy
    • Milligan R. A. and Flicker P. F. (1987) Structural relationships of actin, myosin, and tropomyosin revealed by cryoelectron microscopy. J. Cell Biol. 105: 29-39
    • (1987) J. Cell Biol. , vol.105 , pp. 29-39
    • Milligan, R.A.1    Flicker, P.F.2
  • 45
    • 0029562245 scopus 로고
    • A 32° tail swing in brush border myosin I on ADP release
    • Jontes J. D., Wilson-Kubalek E. M. and Milligan R. A. (1995) A 32° tail swing in brush border myosin I on ADP release. Nature 378: 751-753
    • (1995) Nature , vol.378 , pp. 751-753
    • Jontes, J.D.1    Wilson-Kubalek, E.M.2    Milligan, R.A.3
  • 47
    • 0027164079 scopus 로고
    • Cryoelectron microscopy of microtubules
    • Wade R. H. and Chrétien D. (1993) Cryoelectron microscopy of microtubules. J. Struct. Biol. 110: 1-27
    • (1993) J. Struct. Biol. , vol.110 , pp. 1-27
    • Wade, R.H.1    Chrétien, D.2
  • 48
    • 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. (1994) Direct visualization of the microtubule lattice seam both in vitro and in vivo. J. Cell Biol. 127: 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
  • 49
    • 0028618715 scopus 로고
    • Three dimensional reconstructions of accessory tubules observed in the sperm axonemes of two insect species
    • Lanzavecchia S., Bellon P. L., Dallai R. and Afzelius B. A. (1994) Three dimensional reconstructions of accessory tubules observed in the sperm axonemes of two insect species. J. Struct. Biol. 113: 225-237
    • (1994) J. Struct. Biol. , vol.113 , pp. 225-237
    • Lanzavecchia, S.1    Bellon, P.L.2    Dallai, R.3    Afzelius, B.A.4
  • 50
    • 0029618993 scopus 로고
    • Toward understanding the structure and interactions of microtubules and motor proteins
    • Wade R. H., Horowitz R. and Milligan R. A. (1995) Toward understanding the structure and interactions of microtubules and motor proteins. Proteins Structure Function and Genetics 23: 502-509
    • (1995) Proteins Structure Function and Genetics , vol.23 , pp. 502-509
    • Wade, R.H.1    Horowitz, R.2    Milligan, R.A.3
  • 51
    • 0031010401 scopus 로고    scopus 로고
    • Tomography without tilt: Three-dimensional imaging of microtubule, motor complexes
    • Metoz F., Arnal I. and Wade R. H. (1997) Tomography without tilt: three-dimensional imaging of microtubule, motor complexes. J. Struct. Biol. 118: 159- 168
    • (1997) J. Struct. Biol. , vol.118 , pp. 159-168
    • Metoz, F.1    Arnal, I.2    Wade, R.H.3
  • 52
    • 0027211908 scopus 로고
    • Kinesin follows the microtubule's protofilament axis
    • Ray S., Meyhöfer L., Milligan R. A. and Howard J. (1993) Kinesin follows the microtubule's protofilament axis. J. Cell Biol. 121: 1083-1093
    • (1993) J. Cell Biol. , vol.121 , pp. 1083-1093
    • Ray, S.1    Meyhöfer, L.2    Milligan, R.A.3    Howard, J.4
  • 53
    • 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., Müller J., Gross H. et al. (1998) Image reconstructions of microtubules decorated with monomeric and dimeric kinesins: comparison with x-ray structure and implications for motility. J. Cell Biol. 141: 419-430
    • (1998) J. Cell Biol. , vol.141 , pp. 419-430
    • Hoenger, A.1    Sack, S.2    Thormählen, M.3    Marx, A.4    Müller, J.5    Gross, H.6
  • 54
    • 0029055373 scopus 로고
    • Ned and kinesin motor domains interact with both alpha-tubulin and beta-tubulin
    • Walker R. A. (1995) Ned and kinesin motor domains interact with both alpha-tubulin and beta-tubulin. Proc. Natl. Acad. Sci. USA 92: 5960-5964
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5960-5964
    • Walker, R.A.1
  • 55
    • 0031004776 scopus 로고    scopus 로고
    • Probing the kinesin-microtubule interaction
    • Tucker C. and Goldstein L. S. B. (1997) Probing the kinesin-microtubule interaction. J. Biol. Chem. 272: 9481-9488
    • (1997) J. Biol. Chem. , vol.272 , pp. 9481-9488
    • Tucker, C.1    Goldstein, L.S.B.2
  • 56
    • 0029814394 scopus 로고    scopus 로고
    • Interaction of kinesin motor domains with alpha-and beta-tubulin subunits at a tau-independent binding site. Regulation by polyglutamylation
    • Larcher J. C., Boucher D., Lazereg S., Gros F. and Denoulet P. (1996) Interaction of kinesin motor domains with alpha-and beta-tubulin subunits at a tau-independent binding site. Regulation by polyglutamylation. J. Biol. Chem. 271: 22117-22124
    • (1996) J. Biol. Chem. , vol.271 , pp. 22117-22124
    • Larcher, J.C.1    Boucher, D.2    Lazereg, S.3    Gros, F.4    Denoulet, P.5
  • 57
    • 0031004867 scopus 로고    scopus 로고
    • Influence of the kinesin neck domain on dimerization and ATPase kinetics
    • Jiang W., Stock M. F., Li X. and Hackney D. D. (1997) Influence of the kinesin neck domain on dimerization and ATPase kinetics. J. Biol. Chem. 272: 7626-7632
    • (1997) J. Biol. Chem. , vol.272 , pp. 7626-7632
    • Jiang, W.1    Stock, M.F.2    Li, X.3    Hackney, D.D.4
  • 58
    • 0028363765 scopus 로고
    • Drosophila kinesin motor domain extending to amino-acid position-392 is dimeric when expressed in Escherichia coli
    • Huang T. G., Suhan J. and Hackney D. D. (1994) Drosophila kinesin motor domain extending to amino-acid position-392 is dimeric when expressed in Escherichia coli. J. Biol. Chem. 269: 16502-16507
    • (1994) J. Biol. Chem. , vol.269 , pp. 16502-16507
    • Huang, T.G.1    Suhan, J.2    Hackney, D.D.3
  • 59
    • 0029012977 scopus 로고
    • Kinesin and ned bind through a single head to microtubules and compete for a shared MT binding site
    • Lockhart A., Crevel I. M.-T. C. and Cross R. A. (1995) Kinesin and ned bind through a single head to microtubules and compete for a shared MT binding site. J. Mol. Biol. 249: 763-771
    • (1995) J. Mol. Biol. , vol.249 , pp. 763-771
    • Lockhart, A.1    Crevel, I.M.-T.C.2    Cross, R.A.3
  • 61
    • 0032539526 scopus 로고    scopus 로고
    • X-ray crystal structure of the yeast Kar3 motor domain complexed with Mg-ADP to 2.3 Å resolution
    • Gulick A. M., Song H., Endow S. A. and Rayment T. (1998) X-ray crystal structure of the yeast Kar3 motor domain complexed with Mg-ADP to 2.3 Å resolution. Biochemistry 37: 1769-1776
    • (1998) Biochemistry , vol.37 , pp. 1769-1776
    • Gulick, A.M.1    Song, H.2    Endow, S.A.3    Rayment, T.4
  • 63
    • 0031471243 scopus 로고    scopus 로고
    • The crystal structure of dimeric kinesin and implications for microtubule-dependent motility
    • Kozielski F., Sack S., Marx A., Thormählen M., Schönbrunn E., Biou V. et al. (1997) The crystal structure of dimeric kinesin and implications for microtubule-dependent motility. Cell 91: 985-994
    • (1997) Cell , vol.91 , pp. 985-994
    • Kozielski, F.1    Sack, S.2    Marx, A.3    Thormählen, M.4    Schönbrunn, E.5    Biou, V.6
  • 64
    • 0031016939 scopus 로고    scopus 로고
    • Identification of kinesin neck region as a stable α-helical coiled coil and its thermodynamic characterization
    • Morii H., Takenawa T., Arisaka F. and Shimizu T. (1997) Identification of kinesin neck region as a stable α-helical coiled coil and its thermodynamic characterization. Biochemistry 36: 1933-1942
    • (1997) Biochemistry , vol.36 , pp. 1933-1942
    • Morii, H.1    Takenawa, T.2    Arisaka, F.3    Shimizu, T.4
  • 67
    • 0027251071 scopus 로고
    • Structure of gelsolin segment I-actin complex and the mechanism of filament severing
    • McLaughlin P. J., Gooch J. T., Mannherz H.-G. and Weeds A. G. (1993) Structure of gelsolin segment I-actin complex and the mechanism of filament severing. Nature 364: 685-692
    • (1993) Nature , vol.364 , pp. 685-692
    • McLaughlin, P.J.1    Gooch, J.T.2    Mannherz, H.-G.3    Weeds, A.G.4
  • 69
    • 0030575783 scopus 로고    scopus 로고
    • The structure of an open state of beta-actin at 2.65 angstrom resolution
    • Chik J. K., Lindberg U. and Schutt C. E. (1996) The structure of an open state of beta-actin at 2.65 angstrom resolution. J. Mol. Biol. 263: 607-623
    • (1996) J. Mol. Biol. , vol.263 , pp. 607-623
    • Chik, J.K.1    Lindberg, U.2    Schutt, C.E.3
  • 71
    • 0027131941 scopus 로고
    • Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm
    • Lorenz M., Popp D. and Holmes K. C. (1993) Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234: 826-836
    • (1993) J. Mol. Biol. , vol.234 , pp. 826-836
    • Lorenz, M.1    Popp, D.2    Holmes, K.C.3
  • 72
    • 0027226230 scopus 로고
    • Structure of the actin-myosin complex and its implications for muscle contraction
    • Rayment I., Holden H. M., Whittaker M., Yohn C. B., Lorenz M., Holmes K. C. et al. (1993) Structure of the actin-myosin complex and its implications for muscle contraction. Science 261: 58-65
    • (1993) Science , vol.261 , pp. 58-65
    • Rayment, I.1    Holden, H.M.2    Whittaker, M.3    Yohn, C.B.4    Lorenz, M.5    Holmes, K.C.6
  • 74
    • 0032481381 scopus 로고    scopus 로고
    • Proteolytic mapping of kinesin/ned-microtubule interface: Nucleotide-dependent conformational changes in the loops L8 and L12
    • Alonso M. C., Vanderkerckhove J. and Cross R. A. (1998) Proteolytic mapping of kinesin/ned-microtubule interface: nucleotide-dependent conformational changes in the loops L8 and L12. EMBO J. 17: 945-951
    • (1998) EMBO J. , vol.17 , pp. 945-951
    • Alonso, M.C.1    Vanderkerckhove, J.2    Cross, R.A.3
  • 76
    • 0024550571 scopus 로고
    • A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses
    • Yang J. T., Laymon R. A. and Goldstein L. S. B. (1989) A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses. Cell 56: 879-889
    • (1989) Cell , vol.56 , pp. 879-889
    • Yang, J.T.1    Laymon, R.A.2    Goldstein, L.S.B.3
  • 77
    • 0344867017 scopus 로고    scopus 로고
    • Congruent docking of dimeric kinesin and ned into 3-d electron cryo-microscopy maps of microtubule-motor ADP complexes
    • Hirose K., Löwe J., Alonso M., Cross R. A. and Amos L. A. (1999) Congruent docking of dimeric kinesin and ned into 3-d electron cryo-microscopy maps of microtubule-motor ADP complexes. Mol. Biol. Cell. 10: 2063-2074
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2063-2074
    • Hirose, K.1    Löwe, J.2    Alonso, M.3    Cross, R.A.4    Amos, L.A.5
  • 78
    • 0032509950 scopus 로고    scopus 로고
    • A model of the microtubule-kinesin complex based on electron cryomicroscopy and X-ray crystallography
    • Kozielski F., Arnal I. and Wade R. H. (1998) A model of the microtubule-kinesin complex based on electron cryomicroscopy and X-ray crystallography. Curr. Biol. 8: 191-198
    • (1998) Curr. Biol. , vol.8 , pp. 191-198
    • Kozielski, F.1    Arnal, I.2    Wade, R.H.3
  • 80
    • 0013850715 scopus 로고
    • Induced changes in orientation of the cross-bridge of glycerinated insect flight muscle
    • Reedy M. K., Holmes K. C. and Tregear R. T. (1965) Induced changes in orientation of the cross-bridge of glycerinated insect flight muscle. Nature 207: 1276-1280
    • (1965) Nature , vol.207 , pp. 1276-1280
    • Reedy, M.K.1    Holmes, K.C.2    Tregear, R.T.3
  • 81
    • 0030692707 scopus 로고    scopus 로고
    • Brush border myosin-1 structure and ADP-dependent conformational changes revealed by cryoelectron microscopy and image analysis
    • Joules J. D. and Milligan R. A. (1997) Brush border myosin-1 structure and ADP-dependent conformational changes revealed by cryoelectron microscopy and image analysis. J. Cell Biol. 139: 683-693
    • (1997) J. Cell Biol. , vol.139 , pp. 683-693
    • Joules, J.D.1    Milligan, R.A.2
  • 82
    • 0029745362 scopus 로고    scopus 로고
    • ADP release produces a rotation of the neck region of smooth myosin but not skeletal myosin
    • Golluh J., Cremo C. R. and Cooke R. (1996) ADP release produces a rotation of the neck region of smooth myosin but not skeletal myosin. Nature Struct. Biol. 3: 796-802
    • (1996) Nature Struct. Biol. , vol.3 , pp. 796-802
    • Golluh, J.1    Cremo, C.R.2    Cooke, R.3
  • 84
    • 0029161763 scopus 로고
    • X-ray structure of the magnesium(II)-pyrophosphate complex of the truncated head of dictyostelium discoideum myosin to 2.7 Å resolution
    • Smith C. A. and Rayment I. (1995) X-ray structure of the magnesium(II)-pyrophosphate complex of the truncated head of dictyostelium discoideum myosin to 2.7 Å resolution. Biochemistry 34: 8973-8981
    • (1995) Biochemistry , vol.34 , pp. 8973-8981
    • Smith, C.A.1    Rayment, I.2
  • 85
    • 0029960235 scopus 로고    scopus 로고
    • X-ray structure of the magnesium(II)-ADP-vanadate complex of the dictyostelium discoideum myosin motor domain to 1.9 Å resolution
    • Smith C. A. and Rayment I. (1996) X-ray structure of the magnesium(II)-ADP-vanadate complex of the dictyostelium discoideum myosin motor domain to 1.9 Å resolution. Biochemistry 35: 5404-5417
    • (1996) Biochemistry , vol.35 , pp. 5404-5417
    • Smith, C.A.1    Rayment, I.2
  • 86
    • 0030768794 scopus 로고    scopus 로고
    • X-ray structures of the MgADP, MgATPgS and MgAMPPNP complexes of the Dictyostelium discoideum myosin motor domain
    • Gulick A. M., Bauer C. B., Thoden J. B. and Rayment I.(1997) X-ray structures of the MgADP, MgATPgS and MgAMPPNP complexes of the Dictyostelium discoideum myosin motor domain. Biochemistry 36: 11619-11628
    • (1997) Biochemistry , vol.36 , pp. 11619-11628
    • Gulick, A.M.1    Bauer, C.B.2    Thoden, J.B.3    Rayment, I.4
  • 87
    • 0031079847 scopus 로고    scopus 로고
    • The swinging lever-arm hypothesis of muscle contraction
    • Holmes K. C. (1997) The swinging lever-arm hypothesis of muscle contraction. Curr. Biol. 7: R112-R118
    • (1997) Curr. Biol. , vol.7
    • Holmes, K.C.1
  • 88
    • 0031193924 scopus 로고    scopus 로고
    • Structural studies on myosin II: Communication between distant protein domains
    • Gulick A. M. and Rayment I. (1997) Structural studies on myosin II: communication between distant protein domains. Bioessays 19: 561-569
    • (1997) Bioessays , vol.19 , pp. 561-569
    • Gulick, A.M.1    Rayment, I.2
  • 89
    • 0009469962 scopus 로고    scopus 로고
    • Holmes K. C. (1998) http://lala.mpimf-heidelberg.mpg.de. ~holmes/muscle/muscle2.html
    • (1998)
    • Holmes, K.C.1
  • 90
    • 0032483563 scopus 로고    scopus 로고
    • Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: Visualization of the pre-power stroke state
    • Dominguez R., Freyzon Y., Trybus K. M. and Cohen C.(1998) Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state. Cell 94: 559-571
    • (1998) Cell , vol.94 , pp. 559-571
    • Dominguez, R.1    Freyzon, Y.2    Trybus, K.M.3    Cohen, C.4
  • 92
    • 0017590855 scopus 로고
    • Effect of nucleotide binding on the proximity of the essential sulfhydryl groups of mysin: Chemical probing of movement of residues during conformational transitions
    • Burke M. and Reisler E. (1977) Effect of nucleotide binding on the proximity of the essential sulfhydryl groups of mysin: chemical probing of movement of residues during conformational transitions. Biochemistry 16: 5559-5563
    • (1977) Biochemistry , vol.16 , pp. 5559-5563
    • Burke, M.1    Reisler, E.2
  • 93
    • 0018530414 scopus 로고
    • Active site trapping of nucleotides by crosslinking two sulfhydryls in myosin sub-fragment 1
    • Wells J. A. and Yount R. G. (1979) Active site trapping of nucleotides by crosslinking two sulfhydryls in myosin sub-fragment 1. Proc. Natl. Acad. Sci. USA 75: 4966-4970
    • (1979) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4966-4970
    • Wells, J.A.1    Yount, R.G.2
  • 94
    • 0032569898 scopus 로고    scopus 로고
    • Swing of the lever arm of a myosin motor at the isomerization and phosphate-release steps
    • Suzuki Y., Yasunaga T., Ohkura R., Wakabayashi T. and Sutoh K. (1998) Swing of the lever arm of a myosin motor at the isomerization and phosphate-release steps. Nature 396: 380-383
    • (1998) Nature , vol.396 , pp. 380-383
    • Suzuki, Y.1    Yasunaga, T.2    Ohkura, R.3    Wakabayashi, T.4    Sutoh, K.5
  • 95
    • 0029913456 scopus 로고    scopus 로고
    • The neck region of the myosin motor domain acts as a lever arm to generate movement
    • Uyeda T. Q. P., Abramson P. D. and Spudich J. A. (1996) The neck region of the myosin motor domain acts as a lever arm to generate movement. Pro. Natl. Acad. Sci. USA 93: 4459-4464
    • (1996) Pro. Natl. Acad. Sci. USA , vol.93 , pp. 4459-4464
    • Uyeda, T.Q.P.1    Abramson, P.D.2    Spudich, J.A.3
  • 97
    • 0032559298 scopus 로고    scopus 로고
    • Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin
    • Ishijima A., Kojima H., Funatsu T., Tokunaga M., Higuchi H., Tanaka H. et al. (1998) Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin. Cell 92: 161-171
    • (1998) Cell , vol.92 , pp. 161-171
    • Ishijima, A.1    Kojima, H.2    Funatsu, T.3    Tokunaga, M.4    Higuchi, H.5    Tanaka, H.6
  • 98
    • 0033552942 scopus 로고    scopus 로고
    • A single myosin head moves along an actin filament with regular steps of 5.3 nanometres
    • Kitamura K., Tokunaga M., Iwane A. H. and Yanagida T. (1999) A single myosin head moves along an actin filament with regular steps of 5.3 nanometres. Nature 397: 129-134
    • (1999) Nature , vol.397 , pp. 129-134
    • Kitamura, K.1    Tokunaga, M.2    Iwane, A.H.3    Yanagida, T.4
  • 100
    • 0031041817 scopus 로고    scopus 로고
    • Smooth muscle and skeletal muscle myosin produce similar unitary forces and displacements in the laser trap
    • Guilford W. H., Dupuis D. E., Kennedy G., Wu J., Patlak J. B. and Warshaw D. M. (1997) Smooth muscle and skeletal muscle myosin produce similar unitary forces and displacements in the laser trap. Biophys. J. 72: 1006-1021
    • (1997) Biophys. J. , vol.72 , pp. 1006-1021
    • Guilford, W.H.1    Dupuis, D.E.2    Kennedy, G.3    Wu, J.4    Patlak, J.B.5    Warshaw, D.M.6
  • 101
    • 0345055326 scopus 로고    scopus 로고
    • Conformations of kinesin: Solution vs. crystal structures and interactions with microtubules
    • Marx A., Thormählen M., Müller J., Sack S., Mandelkow E.-M. and Mandelkow E. (1998) Conformations of kinesin: solution vs. crystal structures and interactions with microtubules. Eur. Biophys. J. 27: 455-465
    • (1998) Eur. Biophys. J. , vol.27 , pp. 455-465
    • Marx, A.1    Thormählen, M.2    Müller, J.3    Sack, S.4    Mandelkow, E.-M.5    Mandelkow, E.6
  • 102
    • 0030924142 scopus 로고    scopus 로고
    • Reversal of the direction of movement of a molecular motor
    • Henningsen U. and Schliwa M. (1997) Reversal of the direction of movement of a molecular motor. Nature 389: 93-96
    • (1997) Nature , vol.389 , pp. 93-96
    • Henningsen, U.1    Schliwa, M.2
  • 103
    • 0030874883 scopus 로고    scopus 로고
    • The directional preference of kinesin motors is specified by an element outside of the motor catalytic domain
    • Case R. B., Pierce D. W., Hom-Booher N., Hart C. L. and Vale R. D. (1997) The directional preference of kinesin motors is specified by an element outside of the motor catalytic domain. Cell 90: 959-966
    • (1997) Cell , vol.90 , pp. 959-966
    • Case, R.B.1    Pierce, D.W.2    Hom-Booher, N.3    Hart, C.L.4    Vale, R.D.5
  • 104
    • 0032555532 scopus 로고    scopus 로고
    • Determinants of kinesin motor polarity
    • Endow S. A. and Waligora W. W. (1998) Determinants of kinesin motor polarity. Science 281: 1200-1202
    • (1998) Science , vol.281 , pp. 1200-1202
    • Endow, S.A.1    Waligora, W.W.2
  • 106
    • 0032478540 scopus 로고    scopus 로고
    • Kinesin: What gives?
    • Block S. M. (1998) Kinesin: what gives? Cell 93: 5-8
    • (1998) Cell , vol.93 , pp. 5-8
    • Block, S.M.1
  • 107
    • 0028200793 scopus 로고
    • Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis
    • Hackney D. D. (1994) Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis. Proc. Natl. Acad. Sci. USA 91: 6865-6869
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6865-6869
    • Hackney, D.D.1
  • 108
    • 0032548489 scopus 로고    scopus 로고
    • Alternating site mechanism of the kinesin ATPase
    • Gilbert S. P., Moyer M. L. and Johnson K. A. (1998) Alternating site mechanism of the kinesin ATPase. Biochemistry 37: 792-799
    • (1998) Biochemistry , vol.37 , pp. 792-799
    • Gilbert, S.P.1    Moyer, M.L.2    Johnson, K.A.3
  • 109
    • 0027453868 scopus 로고
    • Direct observation of kinesin stepping by optical trapping interferometry
    • Svoboda K., Schmidt C. F., Schnapp B. J. and Block S. M. (1993) Direct observation of kinesin stepping by optical trapping interferometry. Nature 365: 721-727
    • (1993) Nature , vol.365 , pp. 721-727
    • Svoboda, K.1    Schmidt, C.F.2    Schnapp, B.J.3    Block, S.M.4
  • 110
    • 0030987241 scopus 로고    scopus 로고
    • Demonstration of coiled-coil interactions within the kinesin neck region using synthetic peptides
    • Tripet B., Vale R. D. and Hodges R. S. (1997) Demonstration of coiled-coil interactions within the kinesin neck region using synthetic peptides. J. Biol. Chem. 272: 8946-8956
    • (1997) J. Biol. Chem. , vol.272 , pp. 8946-8956
    • Tripet, B.1    Vale, R.D.2    Hodges, R.S.3
  • 112
    • 0032559824 scopus 로고    scopus 로고
    • Role of the kinesin neck region in processive microtubule-based motility
    • Romberg L., Pierce D. W. and Vale R. D. (1998) Role of the kinesin neck region in processive microtubule-based motility. J. Cell Biol. 140: 1407-1416
    • (1998) J. Cell Biol. , vol.140 , pp. 1407-1416
    • Romberg, L.1    Pierce, D.W.2    Vale, R.D.3
  • 113
    • 0031576329 scopus 로고    scopus 로고
    • Kinetic evidence for low chemical processivity in ned and Eg5
    • Crevel I. M.-T. C., Lockhart A. and Cross R. A. (1997) Kinetic evidence for low chemical processivity in ned and Eg5. J. Mol. Biol. 273: 160-170
    • (1997) J. Mol. Biol. , vol.273 , pp. 160-170
    • Crevel, I.M.-T.C.1    Lockhart, A.2    Cross, R.A.3
  • 114
    • 0032559822 scopus 로고    scopus 로고
    • Processivity of the motor protein kinesin requires two heads
    • Hancock W. O. and Howard J. (1998) Processivity of the motor protein kinesin requires two heads. J. Cell Biol. 140: 1395-1405
    • (1998) J. Cell Biol. , vol.140 , pp. 1395-1405
    • Hancock, W.O.1    Howard, J.2
  • 115
    • 0032502328 scopus 로고    scopus 로고
    • One-headed kinesin derivatives move by a non-processive, low-duty ratio mechanism unlike that of two-headed kinesin
    • Young E. C., Mahtani H. K. and Gelles J. (1998) One-headed kinesin derivatives move by a non-processive, low-duty ratio mechanism unlike that of two-headed kinesin. Biochemistry 37: 3467-3479
    • (1998) Biochemistry , vol.37 , pp. 3467-3479
    • Young, E.C.1    Mahtani, H.K.2    Gelles, J.3
  • 116
    • 0029879228 scopus 로고    scopus 로고
    • Direct observation of single kinesin molecules moving along microtubules
    • Vale R. D., Funatsu T., Pierce D. W., Romberg L., Harada Y. and Yanagida T. (1996) Direct observation of single kinesin molecules moving along microtubules. Nature 380: 451-453
    • (1996) Nature , vol.380 , pp. 451-453
    • Vale, R.D.1    Funatsu, T.2    Pierce, D.W.3    Romberg, L.4    Harada, Y.5    Yanagida, T.6
  • 117
    • 0033582814 scopus 로고    scopus 로고
    • A processive single-headed motor: Kinesin superfamily protein KIF IA
    • Okada Y. and Hirokawa N. (1999) A processive single-headed motor: kinesin superfamily protein KIF IA. Science 283: 1152-1157
    • (1999) Science , vol.283 , pp. 1152-1157
    • Okada, Y.1    Hirokawa, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.