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Volumn 65, Issue 4, 2008, Pages 509-515

Molecular motors: Not quite like clockwork

Author keywords

Dynein; Kinesin; Microtubules; Molecular motors; Myosin

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; DYNEIN ADENOSINE TRIPHOSPHATASE; KINESIN; KINESIN 1; KINESIN 14; MYOSIN; UNCLASSIFIED DRUG;

EID: 39749098459     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-008-7518-3     Document Type: Short Survey
Times cited : (21)

References (61)
  • 1
    • 0032883413 scopus 로고    scopus 로고
    • Structural mechanism of muscle contraction
    • Geeves, M. A. and Holmes, K. C. (1999) Structural mechanism of muscle contraction. Ann. Rev. Biochem. 68, 687-728.
    • (1999) Ann. Rev. Biochem , vol.68 , pp. 687-728
    • Geeves, M.A.1    Holmes, K.C.2
  • 2
    • 10644225267 scopus 로고    scopus 로고
    • Three myosin V structures delineate essential features of chemomechanical transduction
    • Coureux, P. D., Sweeney, H. L. and Houdusse, A. (2004) Three myosin V structures delineate essential features of chemomechanical transduction. EMBO J. 23, 4527-4537.
    • (2004) EMBO J , vol.23 , pp. 4527-4537
    • Coureux, P.D.1    Sweeney, H.L.2    Houdusse, A.3
  • 5
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley, A. F. (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
  • 6
    • 0034602782 scopus 로고    scopus 로고
    • Kinetic equilibrium of forces and molecular events in muscle contraction
    • Becker, E. W. (2000) Kinetic equilibrium of forces and molecular events in muscle contraction. Proc. Natl. Acad. Sci. USA 97, 157-161.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 157-161
    • Becker, E.W.1
  • 7
    • 0026513219 scopus 로고
    • Dynamics of single-motor molecules: The thermal ratchet model
    • Cordova, N. J., Ermentrout, B. and Oster, G.F. (1992) Dynamics of single-motor molecules: The thermal ratchet model. Proc. Natl. Acad. Sci. USA 89, 339-343.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 339-343
    • Cordova, N.J.1    Ermentrout, B.2    Oster, G.F.3
  • 8
    • 33749439041 scopus 로고    scopus 로고
    • Kinesin's biased stepping mechanism: Amplification of neck linker zippering
    • Mather, W. H. and Fox, R. F. (2006) Kinesin's biased stepping mechanism: amplification of neck linker zippering. Biophys. J. 91, 2416-2426.
    • (2006) Biophys. J , vol.91 , pp. 2416-2426
    • Mather, W.H.1    Fox, R.F.2
  • 10
    • 34247237308 scopus 로고    scopus 로고
    • Multivariate analysis of conserved sequence-structure relationships in kinesins: Coupling of the active site and a tubulin-binding sub-domain
    • Grant, B. J., McCammon, J. A., Caves, L. S. and Cross, R. A. (2007) Multivariate analysis of conserved sequence-structure relationships in kinesins: coupling of the active site and a tubulin-binding sub-domain. J. Mol. Biol. 368, 1231-1248.
    • (2007) J. Mol. Biol , vol.368 , pp. 1231-1248
    • Grant, B.J.1    McCammon, J.A.2    Caves, L.S.3    Cross, R.A.4
  • 11
    • 0347623370 scopus 로고    scopus 로고
    • Kinesin moves by an asymmetric hand-over-hand mechanism
    • Asbury, C. L, Fehr, A. N. and Block, S. M. (2003) Kinesin moves by an asymmetric hand-over-hand mechanism. Science 302, 2130-2134.
    • (2003) Science , vol.302 , pp. 2130-2134
    • Asbury, C.L.1    Fehr, A.N.2    Block, S.M.3
  • 12
    • 19644377414 scopus 로고    scopus 로고
    • Mechanics of the kinesin step
    • Carter, N. J. and Cross, R. A. (2005) Mechanics of the kinesin step. Nature 435, 308-312.
    • (2005) Nature , vol.435 , pp. 308-312
    • Carter, N.J.1    Cross, R.A.2
  • 13
    • 0029156511 scopus 로고    scopus 로고
    • Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains
    • Hackney, D. D. (2002) Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains. Nature 377, 448-450.
    • (2002) Nature , vol.377 , pp. 448-450
    • Hackney, D.D.1
  • 14
    • 0842277818 scopus 로고    scopus 로고
    • Inhibition of kinesin motility by ADP and phosphate supports a hand-over-hand mechanism
    • Schief, W. R., Clark, R. H., Crevenna, A. H. and Howard, J. (2004) Inhibition of kinesin motility by ADP and phosphate supports a hand-over-hand mechanism. Proc. Natl. Acad. Sci. USA 101, 1183-1188.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1183-1188
    • Schief, W.R.1    Clark, R.H.2    Crevenna, A.H.3    Howard, J.4
  • 16
    • 0034722373 scopus 로고    scopus 로고
    • Engineering the processive run length of the kinesin motor
    • Thorn, K. S., Ubersax, J. A. and Vale, R. D. (2000) Engineering the processive run length of the kinesin motor. J. Cell Biol. 151, 1093-1100.
    • (2000) J. Cell Biol , vol.151 , pp. 1093-1100
    • Thorn, K.S.1    Ubersax, J.A.2    Vale, R.D.3
  • 17
    • 0034079578 scopus 로고    scopus 로고
    • The C-terminus of tubulin increases cytoplasmic dynein and kinesin processivity
    • Wang Z, Sheetz M. P. (2000) The C-terminus of tubulin increases cytoplasmic dynein and kinesin processivity. Biophys. J. 78, 1955-1964
    • (2000) Biophys. J , vol.78 , pp. 1955-1964
    • Wang, Z.1    Sheetz, M.P.2
  • 19
    • 0035955690 scopus 로고    scopus 로고
    • ATP reorients the neck linker of kinesin in two sequential steps
    • Rosenfeld, S. S., Jefferson, G. M. and King, P. H. (2001) ATP reorients the neck linker of kinesin in two sequential steps. J. Biol. Chem. 276, 40167-40174.
    • (2001) J. Biol. Chem , vol.276 , pp. 40167-40174
    • Rosenfeld, S.S.1    Jefferson, G.M.2    King, P.H.3
  • 20
    • 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
  • 21
    • 0036830220 scopus 로고    scopus 로고
    • Two conformations in the human kinesin power stroke defined by X-ray crystallography and EPR spectroscopy
    • Sindelar, C. V., Budny, M. J., Rice, S., Naber, N., Fletterick, R. and Cooke, R. (2002) Two conformations in the human kinesin power stroke defined by X-ray crystallography and EPR spectroscopy. Nat. Struct. Biol. 9, 844-848.
    • (2002) Nat. Struct. Biol , vol.9 , pp. 844-848
    • Sindelar, C.V.1    Budny, M.J.2    Rice, S.3    Naber, N.4    Fletterick, R.5    Cooke, R.6
  • 23
    • 0343415156 scopus 로고    scopus 로고
    • The way things move: Looking under the hood of molecular motor proteins
    • Vale, R. D. and Milligan, R. A. (2000) The way things move: looking under the hood of molecular motor proteins. Science 288, 88-95.
    • (2000) Science , vol.288 , pp. 88-95
    • Vale, R.D.1    Milligan, R.A.2
  • 24
    • 33749515974 scopus 로고    scopus 로고
    • Single-molecule observations of neck linker conformational changes in the kinesin motor protein
    • Tomishige, M., Stuurman, N. and Vale, R. D. (2006) Single-molecule observations of neck linker conformational changes in the kinesin motor protein. Nat. Struct. Mol. Biol. 13, 887-894.
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 887-894
    • Tomishige, M.1    Stuurman, N.2    Vale, R.D.3
  • 25
    • 33745839864 scopus 로고    scopus 로고
    • Nucleotide binding and hydrolysis induces a disorder-order transition in the kinesin neck-linker region
    • Asenjo, A. B., Weinberg, Y. and Sosa, H. (2006) Nucleotide binding and hydrolysis induces a disorder-order transition in the kinesin neck-linker region. Nat. Struct. Mol. Biol. 13, 648-654.
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 648-654
    • Asenjo, A.B.1    Weinberg, Y.2    Sosa, H.3
  • 26
    • 0037342516 scopus 로고    scopus 로고
    • Thermodynamic properties of the kinesin neck-region docking to the catalytic core
    • Rice, S., Cui, Y., Sindelar, C., Naber, N., Matuska, M., Vale, R. and Cooke, R. (2003) Thermodynamic properties of the kinesin neck-region docking to the catalytic core. Biophys. J. 84, 1844-1854.
    • (2003) Biophys. J , vol.84 , pp. 1844-1854
    • Rice, S.1    Cui, Y.2    Sindelar, C.3    Naber, N.4    Matuska, M.5    Vale, R.6    Cooke, R.7
  • 28
    • 32844474892 scopus 로고    scopus 로고
    • Endres, N. F., Yoshioka, C., Milligan, R. A. and Vale, R. D. (2006) A lever-arm rotation drives motility of the minus-end-directed kinesin Ncd. Nature 439, 875-878.
    • Endres, N. F., Yoshioka, C., Milligan, R. A. and Vale, R. D. (2006) A lever-arm rotation drives motility of the minus-end-directed kinesin Ncd. Nature 439, 875-878.
  • 29
  • 30
    • 0142073737 scopus 로고    scopus 로고
    • Rotation of the stalk/neck and one head in a new crystal structure of the kinesin motor protein, Ncd
    • Yun, M., Bronner, C. E., Park, C. G., Cha, S. S., Park, H. W. and Endow, S. A. (2003) Rotation of the stalk/neck and one head in a new crystal structure of the kinesin motor protein, Ncd. EMBO J. 22, 5382-5389.
    • (2003) EMBO J , vol.22 , pp. 5382-5389
    • Yun, M.1    Bronner, C.E.2    Park, C.G.3    Cha, S.S.4    Park, H.W.5    Endow, S.A.6
  • 31
    • 0020410980 scopus 로고
    • Substructure of the outer dynein arm
    • Goodenough, U. W. and Heuser, J. E. (1982) Substructure of the outer dynein arm. J. Cell Biol. 95, 798-815.
    • (1982) J. Cell Biol , vol.95 , pp. 798-815
    • Goodenough, U.W.1    Heuser, J.E.2
  • 33
    • 0030877444 scopus 로고    scopus 로고
    • Identification of a microtubule binding domain in a cytoplasmic dynein heavy chain
    • Koonce, M. P. (1997) Identification of a microtubule binding domain in a cytoplasmic dynein heavy chain. J. Biol. Chem. 272, 19714-19718.
    • (1997) J. Biol. Chem , vol.272 , pp. 19714-19718
    • Koonce, M.P.1
  • 34
    • 0035341592 scopus 로고    scopus 로고
    • The dynein heavy chain: Structure, mechanics and evolution
    • Asai, D. J. and Koonce, M. P. (2001) The dynein heavy chain: structure, mechanics and evolution. Trends Cell Biol. 11, 196-202.
    • (2001) Trends Cell Biol , vol.11 , pp. 196-202
    • Asai, D.J.1    Koonce, M.P.2
  • 35
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald, A. F., Aravind, L., Spouge, J. L., and Koonin, E. V. (1999) AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9, 27 -43
    • (1999) Genome Res , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 36
    • 0035089503 scopus 로고    scopus 로고
    • Model for the motor component of dynein heavy chain based on homology to the AAA family of oligomeric ATPases
    • Mocz, G. and I. R. Gibbons (2001) Model for the motor component of dynein heavy chain based on homology to the AAA family of oligomeric ATPases. Structure 9, 93-103.
    • (2001) Structure , vol.9 , pp. 93-103
    • Mocz, G.1    Gibbons, I.R.2
  • 37
    • 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. (2004) 25 Å resolution structure of a cytoplasmic dynein motor reveals a seven-member planar ring. J. Mol. Biol. 340, 1059-1072.
    • (2004) J. Mol. Biol , vol.340 , pp. 1059-1072
    • Samso, M.1    Koonce, M.P.2
  • 38
    • 0023664034 scopus 로고
    • Photosensitized cleavage of dynein heavy chains. Cleavage at the 'V1 site' by irradiation at 365 nm in the presence of ATP and vanadate
    • Gibbons, I. R., Lee-Eiford, A., Mocz, G., Phillipson, C. A., Tang, W.-J. Y. and Gibbons, B. H. (1987) Photosensitized cleavage of dynein heavy chains. Cleavage at the 'V1 site' by irradiation at 365 nm in the presence of ATP and vanadate. J. Biol. Chem. 262, 2780-2786
    • (1987) J. Biol. Chem , vol.262 , pp. 2780-2786
    • Gibbons, I.R.1    Lee-Eiford, A.2    Mocz, G.3    Phillipson, C.A.4    Tang, W.-J.Y.5    Gibbons, B.H.6
  • 39
    • 4444330119 scopus 로고    scopus 로고
    • Distinct functions of nucleotide-binding/hydrolysis sites in the four AAA modules of cytoplasmic dynein
    • Kon, T., Nishiura, M., Ohkura, R., Toyoshima, Y. Y. and Sutoh, K. (2004) Distinct functions of nucleotide-binding/hydrolysis sites in the four AAA modules of cytoplasmic dynein. Biochemistry 43, 11266-11274.
    • (2004) Biochemistry , vol.43 , pp. 11266-11274
    • Kon, T.1    Nishiura, M.2    Ohkura, R.3    Toyoshima, Y.Y.4    Sutoh, K.5
  • 40
    • 21244479076 scopus 로고    scopus 로고
    • The affinity of the dynein microtubule-binding domain is modulated by the conformation of its coiled-coil stalk
    • Gibbons, I. R., Garbarino, J. E., Tan, C. E., Reck-Peterson, S. L., Vale, R. D. and Carter, A. P. (2005) The affinity of the dynein microtubule-binding domain is modulated by the conformation of its coiled-coil stalk. J. Biol. Chem. 280, 23960-23965.
    • (2005) J. Biol. Chem , vol.280 , pp. 23960-23965
    • Gibbons, I.R.1    Garbarino, J.E.2    Tan, C.E.3    Reck-Peterson, S.L.4    Vale, R.D.5    Carter, A.P.6
  • 41
    • 36049016163 scopus 로고    scopus 로고
    • The coordination of cyclic microtubule association/dissociation and tail swing of cytoplasmic dynein
    • Imamula, K., Kon, T., Ohkura, R., Sutoh, K. (2007) The coordination of cyclic microtubule association/dissociation and tail swing of cytoplasmic dynein. Proc. Natl. Acad. Sci. USA 104, 16134-16139.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 16134-16139
    • Imamula, K.1    Kon, T.2    Ohkura, R.3    Sutoh, K.4
  • 42
    • 34547586985 scopus 로고    scopus 로고
    • Kinetic characterization of tail swing steps in the ATPase cycle of Dictyostelium cytoplasmic dynein
    • Mogami, T., Kon, T., Ito, K. and Sutoh, K. (2007) Kinetic characterization of tail swing steps in the ATPase cycle of Dictyostelium cytoplasmic dynein. J. Biol. Chem. 282, 21639-21644.
    • (2007) J. Biol. Chem , vol.282 , pp. 21639-21644
    • Mogami, T.1    Kon, T.2    Ito, K.3    Sutoh, K.4
  • 43
    • 1242319567 scopus 로고    scopus 로고
    • Molecular dissection of the roles of nucleotide binding and hydrolysis in dynein's AAA domains in Saccharomyces cerevisiae
    • Reck-Peterson, S. L. and Vale, R. D. (2004) Molecular dissection of the roles of nucleotide binding and hydrolysis in dynein's AAA domains in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA.101, 1491-1495.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1491-1495
    • Reck-Peterson, S.L.1    Vale, R.D.2
  • 44
    • 4444368230 scopus 로고    scopus 로고
    • Multiple ATP-hydrolyzing sites that potentially function in cytoplasmic dynein
    • Takahashi, Y., Edamatsu, M. and Toyoshima, Y. Y. (2004) Multiple ATP-hydrolyzing sites that potentially function in cytoplasmic dynein. Proc. Natl. Acad. Sci. USA 101, 12865-12869.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 12865-12869
    • Takahashi, Y.1    Edamatsu, M.2    Toyoshima, Y.Y.3
  • 45
    • 0037694982 scopus 로고    scopus 로고
    • The third P-loop domain in cytoplasmic dynein heavy chain is essential for dynein motor function and ATP-sensitive microtubule binding
    • Silvanovich, A., Li, M. G., Serr, M., Mische, S. and Hays, T. S. (2003) The third P-loop domain in cytoplasmic dynein heavy chain is essential for dynein motor function and ATP-sensitive microtubule binding. Mol. Biol. Cell 14, 1355-1365.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1355-1365
    • Silvanovich, A.1    Li, M.G.2    Serr, M.3    Mische, S.4    Hays, T.S.5
  • 46
  • 47
    • 34247211171 scopus 로고    scopus 로고
    • The architecture of outer dynein arms in situ
    • Ishikawa, T., Sakakibara, H. and Oiwa, K. (2007) The architecture of outer dynein arms in situ. J. Mol. Biol. 368, 1249-1258.
    • (2007) J. Mol. Biol , vol.368 , pp. 1249-1258
    • Ishikawa, T.1    Sakakibara, H.2    Oiwa, K.3
  • 48
    • 34247538435 scopus 로고    scopus 로고
    • Three-dimensional structures of the flagellar dynein-microtubule complex by cryoelectron microscopy
    • Oda, T., Hirokawa, N. and Kikkawa, M. (2007) Three-dimensional structures of the flagellar dynein-microtubule complex by cryoelectron microscopy. J. Cell Biol. 177, 243-252.
    • (2007) J. Cell Biol , vol.177 , pp. 243-252
    • Oda, T.1    Hirokawa, N.2    Kikkawa, M.3
  • 49
    • 0024805563 scopus 로고
    • One-dimensional diffusion of microtubules bound to flagellar dynein
    • Vale, R. D., Soll, D. R. and Gibbons, I. R. (1989 One-dimensional diffusion of microtubules bound to flagellar dynein. Cell 59, 915-925.
    • (1989) Cell , vol.59 , pp. 915-925
    • Vale, R.D.1    Soll, D.R.2    Gibbons, I.R.3
  • 50
    • 0032737402 scopus 로고    scopus 로고
    • One-dimensional diffusion on microtubules of particles coated with cytoplasmic dynein and immunoglobulins
    • Wang, Z. and Sheetz, M. P. (1999) One-dimensional diffusion on microtubules of particles coated with cytoplasmic dynein and immunoglobulins. Cell Struct. Funct. 24, 373-383.
    • (1999) Cell Struct. Funct , vol.24 , pp. 373-383
    • Wang, Z.1    Sheetz, M.P.2
  • 51
  • 52
    • 0033527027 scopus 로고    scopus 로고
    • Inner-arm dynein c of Chlamydomonas flagella is a single-headed processive motor
    • Sakakibara, H., Kojima, H., Sakai, Y., Katayama, E. and Oiwa, K. (1999) Inner-arm dynein c of Chlamydomonas flagella is a single-headed processive motor, Nature 400, 586-590.
    • (1999) Nature , vol.400 , pp. 586-590
    • Sakakibara, H.1    Kojima, H.2    Sakai, Y.3    Katayama, E.4    Oiwa, K.5
  • 53
    • 0041522803 scopus 로고    scopus 로고
    • Processivity of the single-headed kinesin KIF1A through biased binding to tubulin
    • Okada, Y., Higuchi H, and Hirokawa, N. (2003) Processivity of the single-headed kinesin KIF1A through biased binding to tubulin. Nature 424, 574-577.
    • (2003) Nature , vol.424 , pp. 574-577
    • Okada, Y.1    Higuchi, H.2    Hirokawa, N.3
  • 54
  • 55
    • 33749263141 scopus 로고    scopus 로고
    • Head-head coordination is required for the processive motion of cytoplasmic dynein, an AAA+ molecular motor
    • Shima, T., Imamula, K., Kon, T., Ohkura, R. and Sutoh, K. (2006) Head-head coordination is required for the processive motion of cytoplasmic dynein, an AAA+ molecular motor. J. Struct. Biol. 156, 182-189.
    • (2006) J. Struct. Biol , vol.156 , pp. 182-189
    • Shima, T.1    Imamula, K.2    Kon, T.3    Ohkura, R.4    Sutoh, K.5
  • 56
    • 0028859428 scopus 로고
    • Single cytoplasmic dynein molecule movements: Characterization and comparison with kinesin
    • Wang, Z., Khan, S. and Sheetz, M. P. (1995) Single cytoplasmic dynein molecule movements: characterization and comparison with kinesin. Biophys. J. 69, 2011-2023.
    • (1995) Biophys. J , vol.69 , pp. 2011-2023
    • Wang, Z.1    Khan, S.2    Sheetz, M.P.3
  • 57
    • 0033789351 scopus 로고    scopus 로고
    • Dynactin increases the processivity of the cytoplasmic dynein motor
    • King, S. J. and Schroer, T. A. (2000) Dynactin increases the processivity of the cytoplasmic dynein motor. Nat. Cell Biol. 2, 20-24.
    • (2000) Nat. Cell Biol , vol.2 , pp. 20-24
    • King, S.J.1    Schroer, T.A.2
  • 58
    • 33644747344 scopus 로고    scopus 로고
    • A microtubule-binding domain in dynactin increases dynein processivity by skating along microtubules
    • Culver-Hanlon, T. L., Lex, S. A., Stephens, A. D., Quintyne, N. J. and King, S. J. (2006) A microtubule-binding domain in dynactin increases dynein processivity by skating along microtubules. Nat. Cell Biol. 8, 264-270.
    • (2006) Nat. Cell Biol , vol.8 , pp. 264-270
    • Culver-Hanlon, T.L.1    Lex, S.A.2    Stephens, A.D.3    Quintyne, N.J.4    King, S.J.5
  • 59
    • 1342325553 scopus 로고    scopus 로고
    • Cytoplasmic dynein functions as a gear in response to load
    • Mallik, R., Carter, B. C., Lex, S. A., King, S. J. and Gross, S. P. (2004) Cytoplasmic dynein functions as a gear in response to load. Nature 427, 649-652.
    • (2004) Nature , vol.427 , pp. 649-652
    • Mallik, R.1    Carter, B.C.2    Lex, S.A.3    King, S.J.4    Gross, S.P.5
  • 60
    • 20344382542 scopus 로고    scopus 로고
    • Kinesin and dynein move a peroxisome in vivo: A tug-of-war or coordinated movement?
    • Kural, C., Kim, H., Syed, S., Goshima, G., Gelfand, V. I. and Selvin, P. R. (2005) Kinesin and dynein move a peroxisome in vivo: a tug-of-war or coordinated movement? Science 308, 1469-1472.
    • (2005) Science , vol.308 , pp. 1469-1472
    • Kural, C.1    Kim, H.2    Syed, S.3    Goshima, G.4    Gelfand, V.I.5    Selvin, P.R.6


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