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Volumn 58, Issue , 1996, Pages 703-729

The movement of kinesin along microtubules

Author keywords

cell motility; chemomechanical transduction; molecular motor; motor protein

Indexed keywords

KINESIN; MYOSIN; TUBULIN;

EID: 0029960345     PISSN: 00664278     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.ph.58.030196.003415     Document Type: Review
Times cited : (220)

References (79)
  • 2
    • 0016367327 scopus 로고
    • Arrangement of subunits in flagellar microtubules
    • Amos LA, Klug A. 1974. Arrangement of subunits in flagellar microtubules. J. Cell. Sci. 14:523-49
    • (1974) J. Cell. Sci. , vol.14 , pp. 523-549
    • Amos, L.A.1    Klug, A.2
  • 3
    • 0025251665 scopus 로고
    • Force generation of organelle transport measured in vivo by an infrared laser trap
    • Ashkin A, Schütze K, Dziedzic JM, Euteneuer U, Schliwa M. 1990. Force generation of organelle transport measured in vivo by an infrared laser trap. Nature 348:346-48
    • (1990) Nature , vol.348 , pp. 346-348
    • Ashkin, A.1    Schütze, K.2    Dziedzic, J.M.3    Euteneuer, U.4    Schliwa, M.5
  • 5
    • 0028899953 scopus 로고
    • Failure of single-headed kinesin to track parallel to protofilaments
    • Berliner E, Young EC, Anderson K, Mahtani HK, Gelles J. 1995. Failure of single-headed kinesin to track parallel to protofilaments. Nature 373:718-21
    • (1995) Nature , vol.373 , pp. 718-721
    • Berliner, E.1    Young, E.C.2    Anderson, K.3    Mahtani, H.K.4    Gelles, J.5
  • 6
    • 0025222347 scopus 로고
    • Bead movement by single kinesin molecules studied with optical tweezers
    • Block SM, Goldstein LSB, Schnapp BJ. 1990. Bead movement by single kinesin molecules studied with optical tweezers. Nature 348:348-52
    • (1990) Nature , vol.348 , pp. 348-352
    • Block, S.M.1    Goldstein, L.S.B.2    Schnapp, B.J.3
  • 7
    • 0023944514 scopus 로고
    • Native structure and physical properties of bovine brain kinesin and identification of the ATP-binding subunit polypeptide
    • Bloom GS, Wagner MC, Pfister KK, Brady ST. 1988. Native structure and physical properties of bovine brain kinesin and identification of the ATP-binding subunit polypeptide. Biochemistry 27:3409-16
    • (1988) Biochemistry , vol.27 , pp. 3409-3416
    • Bloom, G.S.1    Wagner, M.C.2    Pfister, K.K.3    Brady, S.T.4
  • 8
    • 0021808444 scopus 로고
    • A novel brain ATPase with properties expected for the fast axonal transport motor
    • Brady ST. 1985. A novel brain ATPase with properties expected for the fast axonal transport motor. Nature 317:73-75
    • (1985) Nature , vol.317 , pp. 73-75
    • Brady, S.T.1
  • 9
    • 0008476926 scopus 로고
    • A ratchet diffusion model for directed motion in muscle
    • Abstr.
    • Braxton S, Yount RG. 1989. A ratchet diffusion model for directed motion in muscle. Biophys J. 55:A12 (Abstr.)
    • (1989) Biophys J. , vol.55
    • Braxton, S.1    Yount, R.G.2
  • 11
    • 0003932766 scopus 로고
    • New York: Freeman. 2nd ed.
    • Creighton TE. 1993. Proteins. New York: Freeman. 2nd ed.
    • (1993) Proteins
    • Creighton, T.E.1
  • 12
    • 0000920828 scopus 로고
    • The packing of α-helices: Simple coiled coils
    • Crick FHC. 1953. The packing of α-helices: simple coiled coils. Acta Cryst. 6:689-97
    • (1953) Acta Cryst. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 15
    • 0026570397 scopus 로고
    • Evidence that the stalk of Drosophila kinesin heavy chain is an α-helical coiled coil
    • de Cuevas M, Tao T, Goldstein LSB. 1992. Evidence that the stalk of Drosophila kinesin heavy chain is an α-helical coiled coil. J. Cell Biol. 116:957-65
    • (1992) J. Cell Biol. , vol.116 , pp. 957-965
    • De Cuevas, M.1    Tao, T.2    Goldstein, L.S.B.3
  • 16
    • 9244261674 scopus 로고
    • Minimal strain-dependent model for motor proteins
    • Submitted
    • Duke T, Leibler S. 1995. Minimal strain-dependent model for motor proteins. Biophys. J. Submitted
    • (1995) Biophys. J.
    • Duke, T.1    Leibler, S.2
  • 18
    • 0025852484 scopus 로고
    • A multimember kinesin gene family in Drosophila
    • Endow SA, Hatsumi M. 1991. A multimember kinesin gene family in Drosophila. Proc. Natl. Acad Sci. USA 88: 4424-27
    • (1991) Proc. Natl. Acad Sci. USA , vol.88 , pp. 4424-4427
    • Endow, S.A.1    Hatsumi, M.2
  • 20
    • 0028261701 scopus 로고
    • Single myosin molecule mechanics: Piconewton forces and nanometer steps
    • Finer JT, Simmons RM, Spudich JA. 1994. Single myosin molecule mechanics: piconewton forces and nanometer steps. Nature 368:113-19
    • (1994) Nature , vol.368 , pp. 113-119
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 21
    • 0011364439 scopus 로고
    • Structural studies of myosin: Nucleotide complexes: a revised model for the molecular basis of muscle contraction
    • Fisher AJ, Smith CA, Thoden J, Smith R, Sutoh K, et al. 1995. Structural studies of myosin: nucleotide complexes: a revised model for the molecular basis of muscle contraction. Biophys. J. 68: S19-S28
    • (1995) Biophys. J. , vol.68
    • Fisher, A.J.1    Smith, C.A.2    Thoden, J.3    Smith, R.4    Sutoh, K.5
  • 22
    • 0027425443 scopus 로고
    • The Drosophila kinesin light chain
    • Gauger AK, Goldstein LSB. 1993. The Drosophila kinesin light chain. J. Biol. Chem. 268:13657-66
    • (1993) J. Biol. Chem. , vol.268 , pp. 13657-13666
    • Gauger, A.K.1    Goldstein, L.S.B.2
  • 23
    • 0040781607 scopus 로고
    • A simple piconewton-scale in vitro force assay for kinesin
    • Abstr.
    • Gittes F, Meyhöfer E, Back S, Howard J. 1994. A simple piconewton-scale in vitro force assay for kinesin. Biophys. J. 66:A312 (Abstr.)
    • (1994) Biophys. J. , vol.66
    • Gittes, F.1    Meyhöfer, E.2    Back, S.3    Howard, J.4
  • 24
    • 0030058832 scopus 로고    scopus 로고
    • Directional loading of the kinesin motor molecule as it buckles a microtubule
    • In press
    • Gittes F, Meyhöfer E, Back S, Howard J. 1996. Directional loading of the kinesin motor molecule as it buckles a microtubule. Biophys. J. 70:In press
    • (1996) Biophys. J. , vol.70
    • Gittes, F.1    Meyhöfer, E.2    Back, S.3    Howard, J.4
  • 25
    • 0027533269 scopus 로고
    • Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape
    • Gittes F, Mickey B, Nettleton J, Howard J. 1993. Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape. J. Cell Biol. 120:923-34
    • (1993) J. Cell Biol. , vol.120 , pp. 923-934
    • Gittes, F.1    Mickey, B.2    Nettleton, J.3    Howard, J.4
  • 26
    • 0028000070 scopus 로고
    • Actin compliance: Are you pulling my chain
    • Goldman YE, Huxley AF. 1994. Actin compliance: are you pulling my chain. Biophys. J. 67:2131-36
    • (1994) Biophys. J. , vol.67 , pp. 2131-2136
    • Goldman, Y.E.1    Huxley, A.F.2
  • 27
    • 0027132479 scopus 로고
    • With apologies to Scheherazade: Tails of 1001 kinesin motors
    • Goldstein LSB. 1993. With apologies to Scheherazade: tails of 1001 kinesin motors. Annu. Rev. Genet. 27:319-51
    • (1993) Annu. Rev. Genet. , vol.27 , pp. 319-351
    • Goldstein, L.S.B.1
  • 28
    • 0028363064 scopus 로고
    • Molecular phylogeny of the kinesin family of microtubule motor proteins
    • Goodson HV, Kang SJ, Endow SA. 1994. Molecular phylogeny of the kinesin family of microtubule motor proteins. J. Cell Sci. 107:1875-84
    • (1994) J. Cell Sci. , vol.107 , pp. 1875-1884
    • Goodson, H.V.1    Kang, S.J.2    Endow, S.A.3
  • 29
    • 0004264248 scopus 로고
    • Cambridge: At the Univ. Press
    • Gray J. 1959. How Animals Move. Cambridge: At the Univ. Press
    • (1959) How Animals Move
    • Gray, J.1
  • 30
    • 0028200793 scopus 로고
    • Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis
    • Hackney DD. 1994. Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis. Proc. Natl. Acad Sci. USA 91:6865-69
    • (1994) Proc. Natl. Acad Sci. USA , vol.91 , pp. 6865-6869
    • Hackney, D.D.1
  • 31
    • 0028946849 scopus 로고
    • Implications of diffusion-controlled limit for processivity of dimeric kinesin head domains
    • Hackney DD. 1995. Implications of diffusion-controlled limit for processivity of dimeric kinesin head domains. Biophys. J. 68:8267-70
    • (1995) Biophys. J. , vol.68 , pp. 8267-8270
    • Hackney, D.D.1
  • 34
    • 0023803940 scopus 로고
    • The stiffness under isotonic releases during a twitch of a frog muscle fiber
    • ed. H Sugi, GH Pollack, New York: Plenum
    • Haugen P. 1988. The stiffness under isotonic releases during a twitch of a frog muscle fiber. In Molecular Mechanism of Muscle Contraction, ed. H Sugi, GH Pollack, pp. 461-69. New York: Plenum
    • (1988) Molecular Mechanism of Muscle Contraction , pp. 461-469
    • Haugen, P.1
  • 35
    • 0000682154 scopus 로고
    • The heat of shortening and the dynamic constants of muscle
    • Hill AV. 1938. The heat of shortening and the dynamic constants of muscle. Proc. R. Soc. London 126:136-95
    • (1938) Proc. R. Soc. London , vol.126 , pp. 136-195
    • Hill, A.V.1
  • 36
    • 0024591237 scopus 로고
    • Submolecular domains of bovine brain kinesin identified by electron microscopy and monoclonal antibody decoration
    • Hirokawa N, Pfister KK, Yorifuji H, Wagner MC, Brady ST, Bloom GS. 1989. Submolecular domains of bovine brain kinesin identified by electron microscopy and monoclonal antibody decoration. Cell 56:867-78
    • (1989) Cell , vol.56 , pp. 867-878
    • Hirokawa, N.1    Pfister, K.K.2    Yorifuji, H.3    Wagner, M.C.4    Brady, S.T.5    Bloom, G.S.6
  • 37
    • 0028979598 scopus 로고
    • Nucleotide-dependent angular change in kinesin motor domain bound to kinesin
    • Hirose K, Lockhart A, Cross RA, Amos LA. 1995. Nucleotide-dependent angular change in kinesin motor domain bound to kinesin. Nature 376:277-79
    • (1995) Nature , vol.376 , pp. 277-279
    • Hirose, K.1    Lockhart, A.2    Cross, R.A.3    Amos, L.A.4
  • 38
    • 0028954281 scopus 로고
    • The actomyosin interaction and its control by tropomyosin
    • Holmes KC. 1995. The actomyosin interaction and its control by tropomyosin. Biophys. J. 68:S2-S7
    • (1995) Biophys. J. , vol.68
    • Holmes, K.C.1
  • 39
    • 0028969429 scopus 로고
    • The mechanics of force generation by kinesin
    • Howard J. 1995. The mechanics of force generation by kinesin. Biophys. J. 68: S245-S55
    • (1995) Biophys. J. , vol.68
    • Howard, J.1
  • 40
    • 0024463944 scopus 로고
    • Movement of microtubules by single kinesin molecules
    • Howard J, Hudspeth AJ, Vale RD. 1989. Movement of microtubules by single kinesin molecules. Nature 342:154-58
    • (1989) Nature , vol.342 , pp. 154-158
    • Howard, J.1    Hudspeth, A.J.2    Vale, R.D.3
  • 41
    • 0028363764 scopus 로고
    • Drosophila kinesin minimal motor domain expressed in Escherichia coli
    • Huang T-G, Hackney DD. 1994. Drosophila kinesin minimal motor domain expressed in Escherichia coli. J. Biol. Chem. 269:16493-501
    • (1994) J. Biol. Chem. , vol.269 , pp. 16493-16501
    • Huang, T.-G.1    Hackney, D.D.2
  • 42
    • 0028579468 scopus 로고
    • Drosophila kinesin motor domain extending to amino acid position 392 is dimeric when expressed in Escherichia coli
    • Huang T-G, Suhan J, Hackney DD. 1994. Drosophila kinesin motor domain extending to amino acid position 392 is dimeric when expressed in Escherichia coli. J. Biol. Chem. 269:16502-7
    • (1994) J. Biol. Chem. , vol.269 , pp. 16502-16507
    • Huang, T.-G.1    Suhan, J.2    Hackney, D.D.3
  • 43
    • 0028145209 scopus 로고
    • The force exerted by a single kinesin molecule against a viscous load
    • Hunt AJ, Gittes F, Howard J. 1994. The force exerted by a single kinesin molecule against a viscous load. Biophys. J. 67:766-81
    • (1994) Biophys. J. , vol.67 , pp. 766-781
    • Hunt, A.J.1    Gittes, F.2    Howard, J.3
  • 44
    • 0027133242 scopus 로고
    • Kinesin swivels to permit microtubule movement in any direction
    • Hunt AJ, Howard J. 1993. Kinesin swivels to permit microtubule movement in any direction. Proc. Natl. Acad Sci. USA 90:11653-57
    • (1993) Proc. Natl. Acad Sci. USA , vol.90 , pp. 11653-11657
    • Hunt, A.J.1    Howard, J.2
  • 45
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley AF. 1957. Muscle structure and theories of contraction. Prog. Biophys. Biophys. Chem. 7:255-318
    • (1957) Prog. Biophys. Biophys. Chem. , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 46
    • 0024251667 scopus 로고
    • Monoclonal antibodies to kinesin heavy chains
    • Ingold AL, Cohn SA, Scholey JM. 1988. Monoclonal antibodies to kinesin heavy chains. J. Cell Biol. 107:2657-67
    • (1988) J. Cell Biol. , vol.107 , pp. 2657-2667
    • Ingold, A.L.1    Cohn, S.A.2    Scholey, J.M.3
  • 48
    • 0028607563 scopus 로고
    • Direct measurement of the stiffness of single actin filaments with and without tropomyosin by in vitro nanomanipulation
    • Kojima H, Ishijima A. Yanagida T. 1994. Direct measurement of the stiffness of single actin filaments with and without tropomyosin by in vitro nanomanipulation. Proc. Natl. Acad. Sci. USA 91:12962-66
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12962-12966
    • Kojima, H.1    Ishijima, A.2    Yanagida, T.3
  • 49
    • 34547275473 scopus 로고
    • Brownian motion in a field of force and the diffusion model of chemical reactions
    • Kramers HA. 1940. Brownian motion in a field of force and the diffusion model of chemical reactions. Physica 7:284-304
    • (1940) Physica , vol.7 , pp. 284-304
    • Kramers, H.A.1
  • 50
    • 0024534133 scopus 로고
    • Isolation of a 45-kDa fragment from the kinesin heavy chain with enhanced ATPase and microtubule-binding activities
    • Kuznetsov SA, Vaisberg YA, Rothwell SW, Murphy DB, Gelfand VI. 1989. Isolation of a 45-kDa fragment from the kinesin heavy chain with enhanced ATPase and microtubule-binding activities. J. Bid. Chem. 264:589-95
    • (1989) J. Bid. Chem. , vol.264 , pp. 589-595
    • Kuznetsov, S.A.1    Vaisberg, Y.A.2    Rothwell, S.W.3    Murphy, D.B.4    Gelfand, V.I.5
  • 51
    • 0022412823 scopus 로고
    • Attachment of transported vesicles to microtubules in axoplasm is facilitated by AMP-PNP
    • Lasek RJ, Brady ST. 1985. Attachment of transported vesicles to microtubules in axoplasm is facilitated by AMP-PNP. Nature 316:645-47
    • (1985) Nature , vol.316 , pp. 645-647
    • Lasek, R.J.1    Brady, S.T.2
  • 52
    • 0027273502 scopus 로고
    • Porters versus rowers: A unified stochastic model of motor proteins
    • Leibler S, Huse D. 1993. Porters versus rowers: a unified stochastic model of motor proteins. J. Cell Biol. 121:1357-68
    • (1993) J. Cell Biol. , vol.121 , pp. 1357-1368
    • Leibler, S.1    Huse, D.2
  • 53
  • 54
    • 0023375957 scopus 로고
    • Hindered diffusion of inert tracer particles in the cytoplasm of mouse 3T3 cells
    • Luby-Phelps K, Castle PE, Taylor DL, Lanni F. 1987. Hindered diffusion of inert tracer particles in the cytoplasm of mouse 3T3 cells. Proc. Natl. Acad. Sci. USA 84:4910-13
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4910-4913
    • Luby-Phelps, K.1    Castle, P.E.2    Taylor, D.L.3    Lanni, F.4
  • 55
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequence
    • Lupas A, van Dyke M, Stock J. 1991. Predicting coiled coils from protein sequence. Science 252:1162-64
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 56
    • 9244236640 scopus 로고
    • Kinetic mechanism of microtubule-kinesin ATPase motor domain K560
    • Abstr.
    • Ma YZ, Taylor EW. 1995. Kinetic mechanism of microtubule-kinesin ATPase motor domain K560. Biophys. J. 68:A28 (Abstr.)
    • (1995) Biophys. J. , vol.68
    • Ma, Y.Z.1    Taylor, E.W.2
  • 57
    • 0025608711 scopus 로고
    • The kinesin-like ncd protein of Drosophila is a minus end-directed microtubule motor
    • McDonald HB, Stewart RJ, Goldstein LSB. 1990. The kinesin-like ncd protein of Drosophila is a minus end-directed microtubule motor. Cell 63:1159-65
    • (1990) Cell , vol.63 , pp. 1159-1165
    • McDonald, H.B.1    Stewart, R.J.2    Goldstein, L.S.B.3
  • 58
    • 0019463941 scopus 로고
    • Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA
    • McKay DB, Steitz TA. 1981. Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA. Nature 290:744-49
    • (1981) Nature , vol.290 , pp. 744-749
    • McKay, D.B.1    Steitz, T.A.2
  • 59
    • 0028843342 scopus 로고
    • The force generated by a single molecule of kinesin against an elastic load
    • Meyhöfer E, Howard J. 1995. The force generated by a single molecule of kinesin against an elastic load. Proc. Natl. Acad. Sci. USA 92:574-78
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 574-578
    • Meyhöfer, E.1    Howard, J.2
  • 60
    • 0022398557 scopus 로고
    • Cross-bridges mediate anterograde and retrograde vesicle transport along microtubules in squid axoplasm
    • Miller RH, Lasek RJ. 1985. Cross-bridges mediate anterograde and retrograde vesicle transport along microtubules in squid axoplasm. J. Cell Biol. 101:2181-93
    • (1985) J. Cell Biol. , vol.101 , pp. 2181-2193
    • Miller, R.H.1    Lasek, R.J.2
  • 62
    • 0028964579 scopus 로고
    • Single-molecule mechanics of heavy meromyosin and S1 interacting with rabbit or Drosophila actins using optical tweezers
    • Molloy JE, Burns JE, Sparrow JC, Tregear RT, Kendrick-Jones J, White DCS. 1995. Single-molecule mechanics of heavy meromyosin and S1 interacting with rabbit or Drosophila actins using optical tweezers. Biophys. J. 68:5298-305
    • (1995) Biophys. J. , vol.68 , pp. 5298-5305
    • Molloy, J.E.1    Burns, J.E.2    Sparrow, J.C.3    Tregear, R.T.4    Kendrick-Jones, J.5    White, D.C.S.6
  • 63
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea EK, Klemm JD, Kim PS, Alber T. 1991. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 254:539-44
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 64
  • 67
    • 0024597974 scopus 로고
    • Identification of globular mechanochemical heads of kinesin
    • Scholey JM, Heuser J, Yang JT, Goldstein LSB. 1989. Identification of globular mechanochemical heads of kinesin. Nature 338:355-57
    • (1989) Nature , vol.338 , pp. 355-357
    • Scholey, J.M.1    Heuser, J.2    Yang, J.T.3    Goldstein, L.S.B.4
  • 68
    • 0016351193 scopus 로고
    • Flagellar rotation and the mechanism of bacterial motility
    • Silverman M, Simon M. 1974. Flagellar rotation and the mechanism of bacterial motility. Nature 249:73-74
    • (1974) Nature , vol.249 , pp. 73-74
    • Silverman, M.1    Simon, M.2
  • 69
    • 0027279053 scopus 로고
    • Direction of microtubule movement is an intrinsic property of the motor domains of kinesin heavy chain and Drosophila ncd protein
    • Stewart RJ, Thaler JP, Goldstein LSB. 1993. Direction of microtubule movement is an intrinsic property of the motor domains of kinesin heavy chain and Drosophila ncd protein. Proc. Natl. Acad. Sci. USA 90:5209-13
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5209-5213
    • Stewart, R.J.1    Thaler, J.P.2    Goldstein, L.S.B.3
  • 70
    • 0004155427 scopus 로고
    • New York: Freeman. 4th ed.
    • Stryer L. 1995. Biochemistry. New York: Freeman. 4th ed.
    • (1995) Biochemistry
    • Stryer, L.1
  • 71
    • 0028362896 scopus 로고
    • Force and velocity measured for single kinesin molecules
    • Svoboda K, Block SM. 1994. Force and velocity measured for single kinesin molecules. Cell 77:773-84
    • (1994) Cell , vol.77 , pp. 773-784
    • Svoboda, K.1    Block, S.M.2
  • 72
    • 0027453868 scopus 로고
    • Direct observation of kinesin stepping by optical trapping interferometry
    • Svoboda K, Schmidt CF, Schnapp BJ, Block SM. 1993. Direct observation of kinesin stepping by optical trapping interferometry. Nature 256:721-27
    • (1993) Nature , vol.256 , pp. 721-727
    • Svoboda, K.1    Schmidt, C.F.2    Schnapp, B.J.3    Block, S.M.4
  • 73
    • 0024991350 scopus 로고
    • Myosin step size. Estimation from slow gliding movement of actin over low densities of heavy meromyosin
    • Uyeda TQP, Kron SJ, Spudich JA. 1990. Myosin step size. Estimation from slow gliding movement of actin over low densities of heavy meromyosin. J. Mol. Biol. 214:699-710
    • (1990) J. Mol. Biol. , vol.214 , pp. 699-710
    • Uyeda, T.Q.P.1    Kron, S.J.2    Spudich, J.A.3
  • 74
    • 0022385727 scopus 로고
    • Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility
    • Vale RD, Reese TS, Sheetz MP. 1985. Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility. Cell 42:39-50
    • (1985) Cell , vol.42 , pp. 39-50
    • Vale, R.D.1    Reese, T.S.2    Sheetz, M.P.3
  • 75
    • 0027164079 scopus 로고
    • Cryoelectron microscopy of microtubules
    • Wade RH, 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
  • 76
    • 0025186134 scopus 로고
    • The Drosophila claret segregation protein is a minus-end directed motor molecule
    • Walker RA, Salmon ED, Endow SA. 1990. The Drosophila claret segregation protein is a minus-end directed motor molecule. Nature 347:780-82
    • (1990) Nature , vol.347 , pp. 780-782
    • Walker, R.A.1    Salmon, E.D.2    Endow, S.A.3
  • 77
    • 0023661228 scopus 로고
    • Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 Å resolution
    • Weber IT, Steitz TA. 1987. Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 Å resolution. J. Mol. Biol. 198:311-26
    • (1987) J. Mol. Biol. , vol.198 , pp. 311-326
    • Weber, I.T.1    Steitz, T.A.2
  • 78
    • 0024550571 scopus 로고
    • A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analysis
    • Yang JT, Laymon RA, Goldstein LSB. 1989. A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analysis. Cell 56:879-89
    • (1989) Cell , vol.56 , pp. 879-889
    • Yang, J.T.1    Laymon, R.A.2    Goldstein, L.S.B.3
  • 79
    • 0025362646 scopus 로고
    • Evidence that the head of kinesin is sufficient for force generation and motility in vitro
    • Yang JT, Saxton WM, Stewart RJ, Raff EC, Goldstein LSB. 1990. Evidence that the head of kinesin is sufficient for force generation and motility in vitro. Science 249:42-47
    • (1990) Science , vol.249 , pp. 42-47
    • Yang, J.T.1    Saxton, W.M.2    Stewart, R.J.3    Raff, E.C.4    Goldstein, L.S.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.