메뉴 건너뛰기




Volumn 60, Issue SUPPL. 1, 2011, Pages

From electron microscopy to molecular cell biology, molecular genetics and structural biology: Intracellular transport and kinesin superfamily proteins, KIFs: Genes, structure, dynamics and functions

Author keywords

kinesin superfamily proteins; molecular cell biology; molecular genetics; molecular motor; quick freeze electron microscopy; structural biology

Indexed keywords

KINESIN; MOLECULAR MOTOR;

EID: 80052075956     PISSN: 00220744     EISSN: 14779986     Source Type: Journal    
DOI: 10.1093/jmicro/dfr051     Document Type: Article
Times cited : (16)

References (170)
  • 1
    • 0024438386 scopus 로고
    • Quick-freeze, deep-etch electron microscopy
    • Hirokawa N (1989) Quick-freeze, deep-etch electron microscopy. J. Electron Microsc. 38(suppl.): s123-s128.
    • (1989) J. Electron Microsc. , vol.38 , Issue.SUPPL.
    • Hirokawa, N.1
  • 2
    • 0029882116 scopus 로고    scopus 로고
    • Organelle transport along microtubules - The role of KIFs
    • DOI 10.1016/0962-8924(96)10003-9
    • Hirokawa N (1996) Organelle transport along microtubule - the role of KIFs (Kinesin superfamily proteins). Trend Cell Biol. 6: 135-141. (Pubitemid 26082830)
    • (1996) Trends in Cell Biology , vol.6 , Issue.4 , pp. 135-141
    • Hirokawa, N.1
  • 3
    • 0032559260 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins and the mechanism of organelle transport
    • DOI 10.1126/science.279.5350.519
    • Hirokawa N (1998) Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science 279: 519-526. (Pubitemid 28067273)
    • (1998) Science , vol.279 , Issue.5350 , pp. 519-526
    • Hirokawa, N.1
  • 4
    • 14844331501 scopus 로고    scopus 로고
    • Molecular motors and mechanisms of directional transport in neurons
    • DOI 10.1038/nrn1624
    • Hirokawa N and Takemura R (2005) Molecular motors and mechanisms of directional transport in neurons. Nat. Rev. Neurosci. 6: 201-214. (Pubitemid 40342415)
    • (2005) Nature Reviews Neuroscience , vol.6 , Issue.3 , pp. 201-214
    • Hirokawa, N.1    Takemura, R.2
  • 5
    • 33646204913 scopus 로고    scopus 로고
    • Nodal flow and the generation of left-right asymmetry
    • Hirokawa N, Tanaka Y, Okada Y, and Takeda S (2006) Nodal flow and the generation of left-right asymmetry. Cell 125: 33-45.
    • (2006) Cell , vol.125 , pp. 33-45
    • Hirokawa, N.1    Tanaka, Y.2    Okada, Y.3    Takeda, S.4
  • 6
    • 50349090965 scopus 로고    scopus 로고
    • Intracellular transport and kinesin superfamily proteins, KIFs: Structure, function, and dynamics
    • Hirokawa N and Noda Y (2008) Intracellular transport and kinesin superfamily proteins, KIFs: structure, function, and dynamics. Physiol. Rev. 88: 1089-1118.
    • (2008) Physiol. Rev. , vol.88 , pp. 1089-1118
    • Hirokawa, N.1    Noda, Y.2
  • 7
    • 70349437416 scopus 로고    scopus 로고
    • Kinesin superfamily motor proteins and intracellular transport
    • Hirokawa N, Noda Y, Tanaka Y, and Niwa S (2009) Kinesin superfamily motor proteins and intracellular transport. Nat. Rev. Mol. Cell Biol. 10: 682-696.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 682-696
    • Hirokawa, N.1    Noda, Y.2    Tanaka, Y.3    Niwa, S.4
  • 8
    • 77957274269 scopus 로고    scopus 로고
    • Left-right determination: Involvement of molecular motor KIF3, cilia, and nodal flow
    • Hirokawa N, Tanaka Y, and Okada Y (2009) Left-right determination: involvement of molecular motor KIF3, cilia, and nodal flow. Cold Spring Harbor Perspect. Biol. 1: a000802.
    • (2009) Cold Spring Harbor Perspect. Biol. , vol.1
    • Hirokawa, N.1    Tanaka, Y.2    Okada, Y.3
  • 9
    • 70450270783 scopus 로고    scopus 로고
    • The mechanisms of kinesin motor motility: Lessons from the monomeric motor KIF1A
    • Hirokawa N, Nitta R, and Okada Y (2009) The mechanisms of kinesin motor motility: lessons from the monomeric motor KIF1A. Nat. Rev. Mol. Cell Biol. 10: 877-884.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 877-884
    • Hirokawa, N.1    Nitta, R.2    Okada, Y.3
  • 10
    • 78449269612 scopus 로고    scopus 로고
    • Molecular motors in neurons: Transport mechanisms and roles in brain function, development and disease
    • Hirokawa N, Niwa S, and Tanaka Y (2010) Molecular motors in neurons: transport mechanisms and roles in brain function, development and disease. Neuron 18: 610-638.
    • (2010) Neuron , vol.18 , pp. 610-638
    • Hirokawa, N.1    Niwa, S.2    Tanaka, Y.3
  • 11
    • 0014378407 scopus 로고
    • Perfusion fixation with glutaraldehyde and post-fixation with osmium tetroxide for electron microscopy
    • Van Harreveld A and Khattab F I (1968) Perfusion fixation with glutaraldehyde and post-fixation with osmium tetroxide for electron microscopy. J. Cell Sci. 3: 579-584.
    • (1968) J. Cell Sci. , vol.3 , pp. 579-584
    • Van Harreveld, A.1    Khattab, F.I.2
  • 12
    • 0014491293 scopus 로고
    • Changes in extracellular space of the mouse cerebral cortex during hydroxyadipaldehyde fixation and osmium tetroxide postfixation
    • Van Harreveld A and Khattab F I (1969) Changes in extracellular space of the mouse cerebral cortex during hydroxyadipaldehyde fixation and osmium tetroxide postfixation. J. Cell Sci. 4: 437-453.
    • (1969) J. Cell Sci. , vol.4 , pp. 437-453
    • Van Harreveld, A.1    Khattab, F.I.2
  • 13
    • 0017445033 scopus 로고
    • Membrane morphology of the vertebrate nervous system
    • Sandri C, Van Buren J M, and Akert K (1977) Membrane morphology of the vertebrate nervous system. Prog. Brain Res. 46: 1-11.
    • (1977) Prog. Brain Res. , vol.46 , pp. 1-11
    • Sandri, C.1    Van Buren, J.M.2    Akert, K.3
  • 14
    • 0344448536 scopus 로고
    • Freeze substitution and supporting techniques
    • Bullivant S (1965) Freeze substitution and supporting techniques. Lab. Invest. 14: 440-457.
    • (1965) Lab. Invest. , vol.14 , pp. 440-457
    • Bullivant, S.1
  • 15
    • 0004948375 scopus 로고
    • Freeze-substitution: Fine structure as a function of water concentration in cells
    • Rebhun L I (1965) Freeze-substitution: fine structure as a function of water concentration in cells. Feder. Proc. 24(Suppl. 15): s217-s236.
    • (1965) Feder. Proc. , vol.24 , Issue.SUPPL. 15
    • Rebhun, L.I.1
  • 16
    • 0017177806 scopus 로고
    • A copper block method for freezing non-cryoprotected tissue to produce ice-crystal-free regions for electron microscopy.I. Evaluation using freezesubstitution
    • Dempsey G P and Bullivant S (1976) A copper block method for freezing non-cryoprotected tissue to produce ice-crystal-free regions for electron microscopy. I. Evaluation using freezesubstitution. J. Microscopy 106: 251-260
    • (1976) J. Microscopy , vol.106 , pp. 251-260
    • Dempsey, G.P.1    Bullivant, S.2
  • 17
    • 0001490234 scopus 로고
    • Low-temperature preparation techniques for electron microscopy of biological specimens based on rapid freezing with liquid helium II
    • Fernandez-Moran H (1960) Low-temperature preparation techniques for electron microscopy of biological specimens based on rapid freezing with liquid helium II. Ann. N. Y. Acad. Sci. 85: 689-713.
    • (1960) Ann. N. Y. Acad. Sci. , vol.85 , pp. 689-713
    • Fernandez-Moran, H.1
  • 18
    • 0017328067 scopus 로고
    • Disappearance of afferent and efferent nerve terminals in the inner ear of the chick embryo after chronic treatment with β bungarotoxin
    • Hirokawa N (1977) Disappearance of afferent and efferent nerve terminals in the inner ear of the chick embryo after chronic treatment with beta-bungarotoxin. J. Cell Biol. 73: 27-46. (Pubitemid 8068591)
    • (1977) Journal of Cell Biology , vol.73 , Issue.1 , pp. 27-46
    • Hirokawa, N.1
  • 19
    • 0018395948 scopus 로고
    • Binding of Clostridium botulinum neurotoxin to the presynaptic membrane in the central nervous system
    • Hirokawa N and Kitamura M (1979) Binding of Clostridium botulinum neurotoxin to the presynaptic membrane in the central nervous system. J. Cell Biol. 81: 43-49. (Pubitemid 9148434)
    • (1979) Journal of Cell Biology , vol.81 , Issue.1 , pp. 43-49
    • Hirokawa, N.1    Kitamura, M.2
  • 20
    • 77954662256 scopus 로고
    • Electron microscopic observation of the central nervous system observed by freeze-substitution method
    • Kirino T and Hirokawa N (1978) Electron microscopic observation of the central nervous system observed by freeze-substitution method. J. Electron Microsc. 27: 339.
    • (1978) J. Electron Microsc. , vol.27 , pp. 339
    • Kirino, T.1    Hirokawa, N.2
  • 21
    • 0018884107 scopus 로고
    • An ultrastructural study of nerve and glial cells by freeze-substitution
    • Hirokawa N and Kirino T (1980) An ultrastructural study of nerve and glial cells by freeze-substitution. J. Neurocytol. 9: 243-254. (Pubitemid 10098943)
    • (1980) Journal of Neurocytology , vol.9 , Issue.2 , pp. 243-254
    • Hirokawa, N.1    Kirino, T.2
  • 22
    • 0022987789 scopus 로고
    • Quick freeze, deep etch of the cytoskeleton
    • Hirokawa N (1986) Quick freeze, deep etch of the cytoskeleton. Method Enzymol. 134: 598-612.
    • (1986) Method Enzymol. , vol.134 , pp. 598-612
    • Hirokawa, N.1
  • 23
    • 0018746093 scopus 로고
    • Synaptic vesicle exocytosis captured by quick freezing and correlated with quantal transmitter release
    • DOI 10.1083/jcb.81.2.275
    • Heuser J E, Reese T S, Dennis M J, Jan Y, Jan L, and Evans L (1979) Synaptic vesicle exocytosis captured by quick freezing and correlated with quantal transmitter release. J. Cell Biol. 81: 275-300. (Pubitemid 9162935)
    • (1979) Journal of Cell Biology , vol.81 , Issue.2 , pp. 275-300
    • Heuser, J.E.1    Reese, T.S.2    Dennis, M.J.3
  • 24
    • 0019365667 scopus 로고
    • Structural evidence that botulinum toxin blocks neuromuscular transmission by impairing the calcium influx that normally accompanies nerve depolarization
    • DOI 10.1083/jcb.88.1.160
    • Hirokawa N and Heuser J E (1981) Structural evidence that botulinum toxin blocks neuromuscular transmission by impairing the calcium influx that normally accompanies nerve depolarization. J. Cell Biol. 88: 160-171. (Pubitemid 11174048)
    • (1981) Journal of Cell Biology , vol.88 , Issue.1 , pp. 160-171
    • Hirokawa, N.1    Heuser, J.E.2
  • 25
    • 0018386027 scopus 로고
    • Organization of acetylcholine receptors in quick-frozen, deep-etched, and rotary-replicated Torpedo postsynaptic membrane
    • DOI 10.1083/jcb.82.1.150
    • Heuser J E and Salpeter S R (1979) Organization of acetylcholine receptors in quick-frozen, deep-etched, and rotary-replicated Torpedo postsynaptic membrane. J. Cell Biol. 82: 150-173. (Pubitemid 9224595)
    • (1979) Journal of Cell Biology , vol.82 , Issue.1 , pp. 150-173
    • Heuser, J.E.1    Salpeter, S.R.2
  • 26
    • 0020047631 scopus 로고
    • Internal and external differentiations of the postsynaptic membrane at the neuromuscular junction
    • DOI 10.1007/BF01257990
    • Hirokawa N and Heuser J E (1982) Internal and external differentiations of the postsynaptic membrane at the neuromuscular junction. J. Neurocyt. 11: 487-510. (Pubitemid 12114620)
    • (1982) Journal of Neurocytology , vol.11 , Issue.3 , pp. 487-510
    • Hirokawa, N.1    Heuser, J.E.2
  • 27
    • 0020187462 scopus 로고
    • The inside and outside of gapjunction membranes visualized by deep etching
    • Hirokawa N and Heuser J E (1982) The inside and outside of gapjunction membranes visualized by deep etching. Cell 30: 395-406.
    • (1982) Cell , vol.30 , pp. 395-406
    • Hirokawa, N.1    Heuser, J.E.2
  • 28
    • 0019859146 scopus 로고
    • Quick-freeze, deep etch visualization of the cytoskeleton beneath surface differentiations of intestinal epithelial cells
    • Hirokawa N and Heuser J E (1981) Quick-freeze, deep-etch visualization of the cytoskeleton beneath surface differentiations of intestinal epithelial cells. J. Cell Biol. 91: 399-409. (Pubitemid 12215627)
    • (1981) Journal of Cell Biology , vol.91 , Issue.2 , pp. 399-409
    • Hirokawa, N.1    Heuser, J.E.2
  • 29
    • 0019975040 scopus 로고
    • Organization of actin, myosin, and intermediate filaments in the brush border of intestinal epithelial cells
    • DOI 10.1083/jcb.94.2.425
    • Hirokawa N, Tilney L G, Fujiwara K, and Heuser J E (1982) Organization of actin, myosin, and intermediate filaments in the brush border of intestinal epithelial cells. J. Cell Biol. 94: 425-443. (Pubitemid 12026794)
    • (1982) Journal of Cell Biology , vol.94 , Issue.2 , pp. 425-443
    • Hirokawa, N.1    Tilney, L.G.2    Fujiwara, K.3    Heuser, J.E.4
  • 30
    • 0020728714 scopus 로고
    • Location of a protein of the fodrin-spectrin-TW260/240 family in the mouse intestinal brush border
    • Hirokawa N, Cheney R E, and Willard M (1983) Location of a protein of the fodrin-spectrin-TW260/240 family in the mouse intestinal brush border. Cell 32: 953-965.
    • (1983) Cell , vol.32 , pp. 953-965
    • Hirokawa, N.1    Cheney, R.E.2    Willard, M.3
  • 31
    • 0020352825 scopus 로고
    • Interactions between actin filaments and between actin filaments and membranes in quick-frozen and deeply etched hair cells of the chick ear
    • DOI 10.1083/jcb.95.1.249
    • Hirokawa N and Tilney L G (1982) Interactions between actin filaments and between actin filaments and membranes in quick-frozen and deeply etched hair cells of the chick ear. J. Cell Biol. 95: 249-261. (Pubitemid 13197095)
    • (1982) Journal of Cell Biology , vol.95 , Issue.1 , pp. 249-261
    • Hirokawa, N.1    Tilney, L.G.2
  • 32
    • 0020966680 scopus 로고
    • Mechanism of brush border contractility studied by the quick-freeze, deep-etch method
    • Hirokawa N, Keller T C, III, Chasan R, and Mooseker M S (1983) Mechanism of brush border contractility studied by the quickfreeze, deep-etch method. J. Cell Biol. 96: 1325-1336. (Pubitemid 13029637)
    • (1983) Journal of Cell Biology , vol.96 , Issue.5 , pp. 1325-1336
    • Hirokawa, N.1    Keller III, T.C.S.2    Chasan, R.3    Mooseker, M.S.4
  • 33
    • 0020326774 scopus 로고
    • Cross-linker system between neurofilaments, microtubules, and membranous organelles in frog axons revealed by the quick-freeze, deep-etching method
    • DOI 10.1083/jcb.94.1.129
    • Hirokawa N (1982) Cross-linker system between neurofilaments, microtubules, and membranous organelles in frog axons revealed by the quick-freeze, deep-etching method. J. Cell Biol. 94: 129-142. (Pubitemid 12033673)
    • (1982) Journal of Cell Biology , vol.94 , Issue.1 , pp. 129-142
    • Hirokawa, N.1
  • 34
    • 0021261943 scopus 로고
    • Organization of mammalian neurofilament polypeptides within the neuronal cytoskeleton
    • Hirokawa N, Glicksman M A, and Willard M B (1984) Organization of mammalian neurofilament polypeptides within the neuronal cytoskeleton. J. Cell Biol. 98: 1523-1536. (Pubitemid 14126982)
    • (1984) Journal of Cell Biology , vol.98 , Issue.4 , pp. 1523-1536
    • Hirokawa, N.1    Glicksman, M.A.2    Willard, M.B.3
  • 35
    • 0022652010 scopus 로고
    • Quick-freeze, deep-etch visualization of the axonal cytoskeleton
    • Hirokawa N (1986) Quick-freeze, deep-etch visualization of the axonal cytoskeleton. Trend. Neurosci. 9: 67-70.
    • (1986) Trend. Neurosci. , vol.9 , pp. 67-70
    • Hirokawa, N.1
  • 36
    • 85004989585 scopus 로고
    • Cytoskeletal architecture in reactivated crayfish axons, with special reference to crossbridges among microtubules and between microtubule membrane organelles
    • Hirokawa N and Yorifuji H (1986) Cytoskeletal architecture in reactivated crayfish axons, with special reference to crossbridges among microtubules and between microtubule membrane organelles. Cell Mot. Cytoskel. 6: 458-468.
    • (1986) Cell Mot. Cytoskel. , vol.6 , pp. 458-468
    • Hirokawa, N.1    Yorifuji, H.2
  • 37
    • 0023262970 scopus 로고
    • The molecular structure of microtubule-associated protein 1A (MAP 1A) in vivo and in vitro. An immunoelectron microscopy and quick-freeze, deep-etch study
    • Shiomura Y and Hirokawa N (1987) The molecular structure of microtubule-associated protein 1A (MAP1A) in vivo and in vitro. An immunoelectron microscopy and quick-freeze, deep-etch study. J. Neurosci. 7: 1461-1469. (Pubitemid 17116098)
    • (1987) Journal of Neuroscience , vol.7 , Issue.5 , pp. 1461-1469
    • Shiomura, Y.1    Hirokawa, N.2
  • 38
    • 0023766743 scopus 로고
    • MAP2 is a component of crossbridges between microtubules and neurofilaments in the neuronal cytoskeleton: Quick-freeze, deep-etch immunoelectron microscopy and reconstitution studies
    • Hirokawa N, Hisanaga S, and Shiomura Y (1988) MAP2 is a component of crossbridges between microtubules and neurofilaments in the neuronal cytoskeleton: quick-freeze, deep-etch immunoelectron microscopy and reconstitution studies. J. Neurosci. 8: 2769-2779.
    • (1988) J. Neurosci. , vol.8 , pp. 2769-2779
    • Hirokawa, N.1    Hisanaga, S.2    Shiomura, Y.3
  • 39
    • 0024094998 scopus 로고
    • Tau proteins: The molecular structure and mode of binding on microtubules
    • Hirokawa N, Shiomura Y, and Okabe S (1988) Tau proteins: the molecular structure and mode of binding on microtubules. J. Cell Biol. 107: 1449-1459.
    • (1988) J. Cell Biol. , vol.107 , pp. 1449-1459
    • Hirokawa, N.1    Shiomura, Y.2    Okabe, S.3
  • 40
    • 0024709423 scopus 로고
    • Microtubule-associated protein 1B: Molecular structure, localization, and phosphorylation-dependent expression in developing neurons
    • Sato-Yoshitake R, Shiomura Y, Miyasaka H, and Hirokawa N (1989) Microtubule-associated protein 1B: molecular structure, localization, and phosphorylation-dependent expression in developing neurons. Neuron 3: 229-238.
    • (1989) Neuron , vol.3 , pp. 229-238
    • Sato-Yoshitake, R.1    Shiomura, Y.2    Miyasaka, H.3    Hirokawa, N.4
  • 41
    • 0023181166 scopus 로고
    • Colocalization of microtubule-associated protein 1A and microtubule-associated protein 2 on neuronal microtubules in situ revealed with double-label immunoelectron microscopy
    • DOI 10.1083/jcb.104.6.1575
    • Shiomura Y and Hirokawa N (1987) Colocalization of microtubule-associated protein 1A and microtubule-associated protein 2 on neuronal microtubules in situ revealed with doublelabel immunoelectron microscopy. J. Cell Biol. 104: 1575-1578. (Pubitemid 17104526)
    • (1987) Journal of Cell Biology , vol.104 , Issue.6 , pp. 1575-1578
    • Shiomura, Y.1    Hirokawa, N.2
  • 42
    • 0024438227 scopus 로고
    • Expression of multiple tau isoforms and microtubule bundle formation in fibroblasts transfected with a single tau cDNA
    • Kanai Y, Takemura R, Oshima T, Mori H, Ihara Y, Yanagisawa M, Masaki T, and Hirokawa N (1989) Expression of multiple tau isoforms and microtubule bundle formation in fibroblasts transfected with a single tau cDNA. J. Cell Biol. 109: 1173-1184. (Pubitemid 19220099)
    • (1989) Journal of Cell Biology , vol.109 , Issue.3 , pp. 1173-1184
    • Kanai, Y.1    Takemura, R.2    Oshima, T.3    Mori, H.4    Ihara, Y.5    Yanagisawa, M.6    Masaki, T.7    Hirokawa, N.8
  • 43
    • 0026729767 scopus 로고
    • Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons
    • DOI 10.1038/360674a0
    • Chen J, Kanai Y, Cowan N J, and Hirokawa N (1992) Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons. Nature 360: 674-677. (Pubitemid 23007681)
    • (1992) Nature , vol.360 , Issue.6405 , pp. 674-677
    • Chen, J.1    Kanai, Y.2    Cowan, N.J.3    Hirokawa, N.4
  • 45
    • 0036323447 scopus 로고    scopus 로고
    • MAP2 is required for dendrite elongation, PKA anchoring in dendrites, and proper PKA signal transduction
    • DOI 10.1083/jcb.200110134
    • Harada A, Teng J, Takei Y, Oguchi K, and Hirokawa N (2002) MAP2 is required for dendrite elongation, PKA anchoring in dendrites, and proper PKA signal transduction. J. Cell Biol. 158: 541-549. (Pubitemid 34851712)
    • (2002) Journal of Cell Biology , vol.158 , Issue.3 , pp. 541-549
    • Harada, A.1    Teng, J.2    Takei, Y.3    Oguchi, K.4    Hirokawa, N.5
  • 46
    • 0030917033 scopus 로고    scopus 로고
    • Delayed development of nervous system in mice homozygous for disrupted microtubule-associated protein 1B (MAP1B) gene
    • DOI 10.1083/jcb.137.7.1615
    • Takei Y, Kondo S, Harada A, Inomata S, Noda T, and Hirokawa N (1997) Delayed development of nervous system in mice homozygous for disrupted microtubule-associated protein 1B (MAP1B) gene. J. Cell Biol. 137: 1615-1626. (Pubitemid 27282241)
    • (1997) Journal of Cell Biology , vol.137 , Issue.7 , pp. 1615-1626
    • Takei, Y.1    Kondo, S.2    Harada, A.3    Inomata, S.4    Noda, T.5    Hirokawa, N.6
  • 47
    • 0034605045 scopus 로고    scopus 로고
    • Defects in axonal elongation and neuronal migration in mice with disrupted tau and map1b genes
    • Takei Y, Teng J, Harada A, and Hirokawa N (2000) Defects in axonal elongation and neuronal migration in mice with disrupted tau and map1b genes. J. Cell Biol. 150: 989-1000.
    • (2000) J. Cell Biol. , vol.150 , pp. 989-1000
    • Takei, Y.1    Teng, J.2    Harada, A.3    Hirokawa, N.4
  • 48
    • 0035494477 scopus 로고    scopus 로고
    • Synergistic effects of MAP2 and MAP1B knockout in neuronal migration, dendritic outgrowth, and microtubule organization
    • DOI 10.1083/jcb.200106025
    • Teng J, Takei Y, Harada A, Nakata T, Chen J, and Hirokawa N (2001) Synergistic effects of MAP2 and MAP1B knockout in neuronal migration, dendritic outgrowth, and microtubule organization. J. Cell Biol. 155: 65-76. (Pubitemid 34286208)
    • (2001) Journal of Cell Biology , vol.155 , Issue.1 , pp. 65-76
    • Teng, J.1    Takei, Y.2    Harada, A.3    Nakata, T.4    Chen, J.5    Hirokawa, N.6
  • 49
    • 0028900588 scopus 로고
    • Two distinct functions of the carboxyl-terminal tail domain of NF-M upon neurofilament assembly: Cross-bridge formation and longitudinal elongation of filaments
    • Nakagawa T, Chen J, Zhang Z, Kanai Y, and Hirokawa N (1995) Two distinct functions of the carboxyl-terminal tail domain of NF-M upon neurofilament assembly: cross-bridge formation and longitudinal elongation of filaments. J. Cell Biol. 129: 411-429.
    • (1995) J. Cell Biol. , vol.129 , pp. 411-429
    • Nakagawa, T.1    Chen, J.2    Zhang, Z.3    Kanai, Y.4    Hirokawa, N.5
  • 50
    • 0033677861 scopus 로고    scopus 로고
    • The C-terminal tail domain of neurofilament protein-H (NF-H) forms the crossbridges and regulates neurofilament bundle formation
    • Chen J, Nakata T, Zhang Z, and Hirokawa N (2000) The C-terminal tail domain of neurofilament protein-H (NF-H) forms the crossbridges and regulates neurofilament bundle formation. J. Cell Sci. Pt 21: 3861-3869.
    • (2000) J. Cell Sci , Issue.PART 21 , pp. 3861-3869
    • Chen, J.1    Nakata, T.2    Zhang, Z.3    Hirokawa, N.4
  • 51
    • 0024354716 scopus 로고
    • Rapid turnover of microtubule-associated protein MAP2 in the axon revealed by microinjection of biotinylated MAP2 into cultured neurons
    • DOI 10.1073/pnas.86.11.4127
    • Okabe S and Hirokawa N (1989) Rapid turnover of microtubule-associated protein MAP2 in the axon revealed by microinjection of biotinylated MAP2 into cultured neurons. Proc. Natl Acad. Sci. USA 86: 4127-4131. (Pubitemid 19154749)
    • (1989) Proceedings of the National Academy of Sciences of the United States of America , vol.86 , Issue.11 , pp. 4127-4131
    • Okabe, S.1    Hirokawa, N.2
  • 52
    • 0024426297 scopus 로고
    • Incorporation and turnover of biotin-labeled actin microinjected into fibroblastic cells: An immunoelectron microscopic study
    • Okabe S and Hirokawa N (1989) Incorporation and turnover of biotin-labeled actin microinjected into fibroblastic cells: an immunoelectron microscopic study. J. Cell Biol. 109(Pt 1): 1581-1595. (Pubitemid 19251211)
    • (1989) Journal of Cell Biology , vol.109 , Issue.4 , pp. 1581-1595
    • Okabe, S.1    Hirokawa, N.2
  • 53
    • 0025057070 scopus 로고
    • Turnover of fluorescently labelled tubulin and actin in the axon
    • Okabe S and Hirokawa N (1990) Turnover of fluorescently labelled tubulin and actin in the axon. Nature 343: 479-482.
    • (1990) Nature , vol.343 , pp. 479-482
    • Okabe, S.1    Hirokawa, N.2
  • 54
    • 0025998618 scopus 로고
    • Actin dynamics in growth cones
    • Okabe S and Hirokawa N (1991) Actin dynamics in growth cones. J. Neurosci. 11: 1918-1929.
    • (1991) J. Neurosci. , vol.11 , pp. 1918-1929
    • Okabe, S.1    Hirokawa, N.2
  • 55
    • 0026575974 scopus 로고
    • Differential behavior of photoactivated microtubules in growing axons of mouse and frog neurons
    • Okabe S and Hirokawa N (1992) Differential behavior of photoactivated microtubules in growing axons of mouse and frog neurons. J. Cell Biol. 117: 105-120.
    • (1992) J. Cell Biol. , vol.117 , pp. 105-120
    • Okabe, S.1    Hirokawa, N.2
  • 56
    • 0027396954 scopus 로고
    • Do photobleached fluorescent microtubules move?: Re-evaluation of fluorescence laser photobleaching both in vitro and in growing Xenopus axon
    • Okabe S and Hirokawa N (1993) Do photobleached fluorescent microtubules move?: re-evaluation of fluorescence laser photobleaching both in vitro and in growing Xenopus axon. J. Cell Biol. 120: 1177-1186. (Pubitemid 23064172)
    • (1993) Journal of Cell Biology , vol.120 , Issue.5 , pp. 1177-1186
    • Okabe, S.1    Hirokawa, N.2
  • 57
    • 0027480379 scopus 로고
    • Dynamics of the neuronal intermediate filaments
    • Okabe S, Miyasaka H, and Hirokawa N (1993) Dynamics of the neuronal intermediate filaments. J. Cell Biol. 121: 375-386. (Pubitemid 23110881)
    • (1993) Journal of Cell Biology , vol.121 , Issue.2 , pp. 375-386
    • Okabe, S.1    Miyasaka, H.2    Hirokawa, N.3
  • 58
    • 0028000952 scopus 로고
    • Differential dynamics of neurofilament-H protein and neurofilament-L protein in neurons
    • DOI 10.1083/jcb.127.1.173
    • Takeda S, Okabe S, Funakoshi T, and Hirokawa N (1994) Differential dynamics of neurofilament-H protein and neurofilament-L protein in neurons. J. Cell Biol. 127: 173-185. (Pubitemid 24307666)
    • (1994) Journal of Cell Biology , vol.127 , Issue.1 , pp. 173-185
    • Takeda, S.1    Okabe, S.2    Funakoshi, T.3    Hirokawa, N.4
  • 59
    • 0029025222 scopus 로고
    • Tubulin dynamics in neuronal axons of living zebrafish embryos
    • Takeda S, Funakoshi T, and Hirokawa N (1995) Tubulin dynamics in neuronal axons of living zebrafish embryos. Neuron 14: 1257-1264.
    • (1995) Neuron , vol.14 , pp. 1257-1264
    • Takeda, S.1    Funakoshi, T.2    Hirokawa, N.3
  • 60
    • 0029898806 scopus 로고    scopus 로고
    • Active transport of photoactivated tubulin molecules in growing axons revealed by a new electron microscopic analysis
    • DOI 10.1083/jcb.133.6.1347
    • Funakoshi T, Takeda S, and Hirokawa N (1996) Active transport of photoactivated tubulin molecules in growing axons revealed by a new electron microscopic analysis. J. Cell Biol. 133: 1347-1353. (Pubitemid 26192334)
    • (1996) Journal of Cell Biology , vol.133 , Issue.6 , pp. 1347-1353
    • Funakoshi, T.1    Takeda, S.2    Hirokawa, N.3
  • 61
    • 0029778167 scopus 로고    scopus 로고
    • Visualization of slow axonal transport in vivo
    • Terada S, Nakata T, Peterson A C, and Hirokawa N (1996) Visualization of slow axonal transport in vivo. Science 273: 784-788. (Pubitemid 26271521)
    • (1996) Science , vol.273 , Issue.5276 , pp. 784-788
    • Terada, S.1    Nakata, T.2    Peterson, A.C.3    Hirokawa, N.4
  • 62
    • 0026094996 scopus 로고
    • Predominant and developmentally regulated expression of dynamin in neurons
    • Nakata T, Iwamoto A, Noda Y, Takemura R, Yoshikura H, and Hirokawa N (1991) Predominant and developmentally regulated expression of dynamin in neurons. Neuron 7: 461-469.
    • (1991) Neuron , vol.7 , pp. 461-469
    • Nakata, T.1    Iwamoto, A.2    Noda, Y.3    Takemura, R.4    Yoshikura, H.5    Hirokawa, N.6
  • 67
    • 0029051298 scopus 로고
    • The neuron-specific kinesin superfamily protein KIF1A is a unique monomeric motor for anterograde axonal transport of synaptic vesicle precursors
    • Okada Y, Yamazaki H, Sekine-Aizawa Y, and Hirokawa N (1995) The neuron-specific kinesin superfamily protein KIF1A is a unique monomeric motor for anterograde axonal transport of synaptic vesicle precursors. Cell 81: 769-780.
    • (1995) Cell , vol.81 , pp. 769-780
    • Okada, Y.1    Yamazaki, H.2    Sekine-Aizawa, Y.3    Hirokawa, N.4
  • 69
    • 55549134618 scopus 로고    scopus 로고
    • KIF1Bbeta- and KIF1A-mediated axonal transport of presynaptic regulator Rab3 occurs in a GTP-dependent manner through DENN/MADD
    • Niwa S, Tanaka Y, and Hirokawa N (2008) KIF1Bbeta- and KIF1A-mediated axonal transport of presynaptic regulator Rab3 occurs in a GTP-dependent manner through DENN/MADD. Nat. Cell Biol. 11: 1270-1276.
    • (2008) Nat. Cell Biol. , vol.11 , pp. 1270-1276
    • Niwa, S.1    Tanaka, Y.2    Hirokawa, N.3
  • 72
    • 0033582814 scopus 로고    scopus 로고
    • A processive single-headed motor: Kinesin superfamily protein KIF1A
    • Okada Y and Hirokawa N (1999) A processive single-headed motor: kinesin superfamily protein KIF1A. Science 283: 1152-1157.
    • (1999) Science , vol.283 , pp. 1152-1157
    • Okada, Y.1    Hirokawa, N.2
  • 73
    • 0034681137 scopus 로고    scopus 로고
    • Mechanism of the single-headed processivity: Diffusional anchoring between the K-loop of kinesin and the C terminus of tubulin
    • DOI 10.1073/pnas.97.2.640
    • Okada Y and Hirokawa N (2000) Mechanism of the single-headed processivity: diffusional anchoring between the K-loop of kinesin and the C terminus of tubulin. Proc. Natl Acad. Sci. USA 97: 640-645. (Pubitemid 30070362)
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , Issue.2 , pp. 640-645
    • Okada, Y.1    Hirokawa, N.2
  • 74
    • 0041522803 scopus 로고    scopus 로고
    • Processivity of the single-headed kinesin KIF1A through binding to tubulin
    • DOI 10.1038/nature01804
    • Okada Y, Higuchi H, and Hirokawa N (2003) Processivity of the single-headed kinesin KIF1A through biased binding to tubulin. Nature 424: 574-577. (Pubitemid 36975781)
    • (2003) Nature , vol.424 , Issue.6948 , pp. 574-577
    • Okada, Y.1    Higuchi, H.2    Hirokawa, N.3
  • 75
    • 0028641560 scopus 로고
    • KIF1B, a novel microtubule plus end-directed monomeric motor protein for transport of mitochondria
    • Nangaku M, Sato-Yoshitake R, Okada Y, Noda Y, Takemura R, Yamazaki H, and Hirokawa N (1994) KIF1B, a novel microtubule plus end-directed monomeric motor protein for transport of mitochondria. Cell 79: 1209-1220.
    • (1994) Cell , vol.79 , pp. 1209-1220
    • Nangaku, M.1    Sato-Yoshitake, R.2    Okada, Y.3    Noda, Y.4    Takemura, R.5    Yamazaki, H.6    Hirokawa, N.7
  • 76
    • 27644441592 scopus 로고    scopus 로고
    • The novel protein KBP regulates mitochondria localization by interaction with a kinesin-like protein
    • Wozniak M J, Melzer M, Dorner C, Haring H-U, and Lammers R (2005) The novel protein KBP regulates mitochondria localization by interaction with a kinesin-like protein. BMC Cell Biol. 6: 35.
    • (2005) BMC Cell Biol. , vol.6 , pp. 35
    • Wozniak, M.J.1    Melzer, M.2    Dorner, C.3    Haring, H.-U.4    Lammers, R.5
  • 77
    • 0021808444 scopus 로고
    • A novel brain ATPase with properties expected for the fast axonal transport motor
    • DOI 10.1038/317073a0
    • Brady S T (1985) A novel brain ATPase with properties expected for the fast axonal transport motor. Nature 317: 73-75. (Pubitemid 15016692)
    • (1985) Nature , vol.317 , Issue.6032 , pp. 73-75
    • Brady, S.T.1
  • 78
    • 0022385727 scopus 로고
    • Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility
    • Vale R, Reese T, and Sheetz M (1985) Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility. Cell 42: 39-50. (Pubitemid 16237554)
    • (1985) Cell , vol.42 , Issue.1 , pp. 39-50
    • Vale, R.D.1    Reese, T.S.2    Sheetz, M.P.3
  • 79
    • 0024591237 scopus 로고
    • Submolecular domains of bovine brain kinesin identified by electron microscopy and monoclonal antibody decoration
    • DOI 10.1016/0092-8674(89)90691-0
    • Hirokawa N, Pfister K K, Yorifuji H, Wagner M C, Brady S T, and Bloom G S (1989) Submolecular domains of bovine brain kinesin identified by electron microscopy and monoclonal antibody decoration. Cell 56: 867-878. (Pubitemid 19082522)
    • (1989) Cell , vol.56 , Issue.5 , 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
  • 81
    • 0032498607 scopus 로고    scopus 로고
    • Visualization of the dynamics of synaptic vesicle and plasma membrane proteins in living axons
    • DOI 10.1083/jcb.140.3.659
    • Nakata T, Terada S, and Hirokawa N (1998) Visualization of the dynamics of synaptic vesicle and plasma membrane proteins in living axons. J. Cell Biol. 140: 659-674. (Pubitemid 28134068)
    • (1998) Journal of Cell Biology , vol.140 , Issue.3 , pp. 659-674
    • Nakata, T.1    Terada, S.2    Hirokawa, N.3
  • 82
    • 0032568790 scopus 로고    scopus 로고
    • Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria
    • DOI 10.1016/S0092-8674(00)81459-2
    • Tanaka Y, Kanai Y, Okada Y, Nonaka S, Takeda S, Harada A, and Hirokawa N (1998) Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria. Cell 93: 1147-1158. (Pubitemid 28307420)
    • (1998) Cell , vol.93 , Issue.7 , pp. 1147-1158
    • Tanaka, Y.1    Kanai, Y.2    Okada, Y.3    Nonaka, S.4    Takeda, S.5    Harada, A.6    Hirokawa, N.7
  • 84
    • 0035818998 scopus 로고    scopus 로고
    • Kinesin-mediated axonal transport of a membrane compartment containing β-secretase and presenilin-1 requires APP
    • DOI 10.1038/414643a
    • Kamal A, Almenar-Queralt A, LeBlanc J, Roberts E, and Goldstein L (2001) Kinesin-mediated axonal transport of a membrane compartment containing beta-secretase and presenilin-1 requires APP. Nature 414: 643-648. (Pubitemid 33151260)
    • (2001) Nature , vol.414 , Issue.6864 , pp. 643-648
    • Kamal, A.1    Almenar-Queralt, A.2    LeBlanc, J.F.3    Roberts, E.A.4    Goldstein, L.S.B.5
  • 85
    • 27944444156 scopus 로고    scopus 로고
    • 2-terminal kinase-interacting protein-1
    • DOI 10.1083/jcb.200502043
    • Muresan Z and Muresan V (2005) Coordinated transport of phosphorylated amyloid-beta precursor protein and c-Jun NH2-terminal kinase-interacting protein-1. J. Cell Biol. 171: 615-625. (Pubitemid 41668721)
    • (2005) Journal of Cell Biology , vol.171 , Issue.4 , pp. 615-625
    • Muresan, Z.1    Muresan, V.2
  • 86
    • 63849105306 scopus 로고    scopus 로고
    • The cleavage products of amyloid-beta precursor protein are sorted to distinct carrier vesicles that are independently transported within neurites
    • Muresan V, Varvel N, Lamb B, and Muresan Z (2009) The cleavage products of amyloid-beta precursor protein are sorted to distinct carrier vesicles that are independently transported within neurites. J. Neurosci. 29: 3565-3578.
    • (2009) J. Neurosci. , vol.29 , pp. 3565-3578
    • Muresan, V.1    Varvel, N.2    Lamb, B.3    Muresan, Z.4
  • 87
    • 24944534881 scopus 로고    scopus 로고
    • Syntabulin-mediated anterograde transport of mitochondria along neuronal processes
    • DOI 10.1083/jcb.200506042
    • Cai Q, Gerwin C, and Sheng Z (2005) Syntabulin-mediated anterograde transport of mitochondria along neuronal processes. J. Cell Biol. 170: 959-969. (Pubitemid 41306295)
    • (2005) Journal of Cell Biology , vol.170 , Issue.6 , pp. 959-969
    • Cai, Q.1    Gerwin, C.2    Sheng, Z.-H.3
  • 88
    • 34447130225 scopus 로고    scopus 로고
    • Syntabulin-kinesin-1 family member 5B-mediated axonal transport contributes to activity-dependent presynaptic assembly
    • DOI 10.1523/JNEUROSCI.0731-07.2007
    • Cai Q, Pan P, and Sheng Z (2007) Syntabulin-kinesin-1 family member 5B-mediated axonal transport contributes to activitydependent presynaptic assembly. J. Neurosci. 27: 7284-7296. (Pubitemid 47037551)
    • (2007) Journal of Neuroscience , vol.27 , Issue.27 , pp. 7284-7296
    • Cai, Q.1    Pan, P.-Y.2    Sheng, Z.-H.3
  • 89
    • 0024997819 scopus 로고
    • Brain dynein (MAP1C) localizes on both anterogradely and retrogradely transported membranous organelles in vivo
    • Hirokawa N, Sato-Yoshitake R, Yoshida T, and Kawashima T (1990) Brain dynein (MAP1C) localizes on both anterogradely and retrogradely transported membranous organelles in vivo. J. Cell Biol. 111: 1027-1037.
    • (1990) J. Cell Biol. , vol.111 , pp. 1027-1037
    • Hirokawa, N.1    Sato-Yoshitake, R.2    Yoshida, T.3    Kawashima, T.4
  • 93
    • 0034730328 scopus 로고    scopus 로고
    • Oligomeric tubulin in large transporting complex is transported via kinesin in squid giant axons
    • Terada S, Kinjo M, and Hirokawa N (2000) Oligomeric tubulin in large transporting complex is transported via kinesin in squid giant axons. Cell 103: 141-155.
    • (2000) Cell , vol.103 , pp. 141-155
    • Terada, S.1    Kinjo, M.2    Hirokawa, N.3
  • 95
    • 45549099576 scopus 로고    scopus 로고
    • Cytoskeletal requirements in axonal transport of slow component-b
    • Roy S, Winton M, Black M, Trojanowski J, and Lee V (2008) Cytoskeletal requirements in axonal transport of slow component-b. J. Neurosci. 28: 5248-5256.
    • (2008) J. Neurosci. , vol.28 , pp. 5248-5256
    • Roy, S.1    Winton, M.2    Black, M.3    Trojanowski, J.4    Lee, V.5
  • 96
    • 77149135259 scopus 로고    scopus 로고
    • Kinesin-1 Hsc/70-dependent mechanism of slow axonal and its relation to fast axonal transport
    • Terada S, Kinjo M, Aihara M, Takei Y, and Hirokawa N (2010) Kinesin-1 Hsc/70-dependent mechanism of slow axonal and its relation to fast axonal transport. EMBO J. 29: 843-854.
    • (2010) EMBO J. , vol.29 , pp. 843-854
    • Terada, S.1    Kinjo, M.2    Aihara, M.3    Takei, Y.4    Hirokawa, N.5
  • 97
    • 0037007668 scopus 로고    scopus 로고
    • Glutamate-receptor-interacting protein GRIP1 directly steers kinesin to dendrites
    • DOI 10.1038/nature743
    • Setou M, Seog D-H, Tanaka Y, Kanai Y, Takei Y, Kawagishi M, and Hirokawa N (2002) Glutamate-receptor-interacting protein GRIP1 directly steers kinesin to dendrites. Nature 417: 83-87. (Pubitemid 34498820)
    • (2002) Nature , vol.417 , Issue.6884 , pp. 83-87
    • Setou, M.1    Seog, D.-H.2    Tanaka, Y.3    Kanai, Y.4    Takei, Y.5    Kawagishi, M.6    Hirokawa, N.7
  • 98
    • 0141656303 scopus 로고    scopus 로고
    • Microtubules provide directional cues for polarized axonal transport through interaction with kinesin motor head
    • DOI 10.1083/jcb.200302175
    • Nakata T and Hirokawa N (2003) Microtubules provide directional cues for polarized axonal transport through interaction with kinesin motor head. J. Cell Biol. 162: 1045-1055. (Pubitemid 37174187)
    • (2003) Journal of Cell Biology , vol.162 , Issue.6 , pp. 1045-1055
    • Nakata, T.1    Hirokawa, N.2
  • 100
    • 4143088149 scopus 로고    scopus 로고
    • Kinesin transports RNA: Isolation and characterization of an RNA-transporting granule
    • DOI 10.1016/j.neuron.2004.07.022, PII S0896627304004635
    • Kanai Y, Dohmae N, and Hirokawa N (2004) Kinesin transports RNA: isolation and characterization of an RNA-transporting granule. Neuron 43: 513-525. (Pubitemid 39094678)
    • (2004) Neuron , vol.43 , Issue.4 , pp. 513-525
    • Kanai, Y.1    Dohmae, N.2    Hirokawa, N.3
  • 101
    • 0034625631 scopus 로고    scopus 로고
    • Kinesin superfamily motor protein KIF17 and mlin-10 in NMDA receptorcontaining vesicle transport
    • Setou M, Nakagawa T, Seog D-H, and Hirokawa N (2000) Kinesin superfamily motor protein KIF17 and mlin-10 in NMDA receptorcontaining vesicle transport. Science 288: 1693-1920.
    • (2000) Science , vol.288 , pp. 1693-1920
    • Setou, M.1    Nakagawa, T.2    Seog, D.-H.3    Hirokawa, N.4
  • 102
    • 37749000849 scopus 로고    scopus 로고
    • Disruption of KIF17-Mint1 interation by CamKII-dependent phosphorylation: A molecular model of kinesin-cargo release
    • Guillaud L, Wong R, and Hirokawa N (2008) Disruption of KIF17-Mint1 interation by CamKII-dependent phosphorylation: a molecular model of kinesin-cargo release. Nat. Cell Biol. 10: 19-29.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 19-29
    • Guillaud, L.1    Wong, R.2    Hirokawa, N.3
  • 104
    • 0030939131 scopus 로고    scopus 로고
    • KIFC2 is a novel neuron-specific C-terminal type kinesin superfamily motor for dendritic transport of multivesicular body-like organelles
    • DOI 10.1016/S0896-6273(00)81243-X
    • Saito N, Okada Y, Noda Y, Kinoshita Y, Kondo S, and Hirokawa N (1997) KIFC2 is a novel neuron-specific C-terminal type kinesin superfamily motor for dendritic transport of multivesicular bodylike organelles. Neuron 18: 425-438. (Pubitemid 27138790)
    • (1997) Neuron , vol.18 , Issue.3 , pp. 425-438
    • Saito, N.1    Okada, Y.2    Noda, Y.3    Kinoshita, Y.4    Kondo, S.5    Hirokawa, N.6
  • 105
    • 0030888785 scopus 로고    scopus 로고
    • Characterization of KIFC2, a neuronal kinesin superfamily member in mouse
    • DOI 10.1016/S0896-6273(00)81244-1
    • Hanlon D, Yang Z, and Goldstein L (1997) Characterization of KIFC2, a neuronal kinesin superfamily member in mouse. Neuron 18: 439-451. (Pubitemid 27138791)
    • (1997) Neuron , vol.18 , Issue.3 , pp. 439-451
    • Hanlon, D.W.1    Yang, Z.2    Goldstein, L.S.B.3
  • 106
    • 33644870579 scopus 로고    scopus 로고
    • A change in the selective translocation of the kinesin-1 motor domain marks the initial specification of the axon
    • DOI 10.1016/j.neuron.2006.02.005, PII S089662730600095X
    • Jacobson C, Schnapp B, and Banker G (2006) A change in the selective translocation of the kinesin-1 motor domain marks the initial specification of the axon. Neuron 49: 797-804. (Pubitemid 43376077)
    • (2006) Neuron , vol.49 , Issue.6 , pp. 797-804
    • Jacobson, C.1    Schnapp, B.2    Banker, G.A.3
  • 107
    • 33750618516 scopus 로고    scopus 로고
    • Microtubule acetylation promotes kinesin-1 binding and transport
    • DOI 10.1016/j.cub.2006.09.014, PII S096098220602207X
    • Reed N, Cai D, Blasius T, Jih G, Meyhofer E, Gaertig J, and Verhey K (2006) Microtubule acetylation promotes kinesin-1 binding and transport. Curr. Biol. 16: 2166-2172. (Pubitemid 44692098)
    • (2006) Current Biology , vol.16 , Issue.21 , pp. 2166-2172
    • Reed, N.A.1    Cai, D.2    Blasius, T.L.3    Jih, G.T.4    Meyhofer, E.5    Gaertig, J.6    Verhey, K.J.7
  • 108
    • 67349200776 scopus 로고    scopus 로고
    • Tubulin tyrosination navigates the kinesin-1 motor domain to axons
    • Konishi Y and Setou M (2009) Tubulin tyrosination navigates the kinesin-1 motor domain to axons. Nat. Neurosci. 12: 559-567.
    • (2009) Nat. Neurosci. , vol.12 , pp. 559-567
    • Konishi, Y.1    Setou, M.2
  • 109
    • 0026267223 scopus 로고
    • Intracellular organization of hippocampal neurons during the development of neuronal polarity
    • Dotti C and Banker G (1991) Intracellular organization of hippocampal neurons during the development of neuronal polarity. J. Cell Sci. 15: 75-84.
    • (1991) J. Cell Sci. , vol.15 , pp. 75-84
    • Dotti, C.1    Banker, G.2
  • 110
    • 76649143069 scopus 로고    scopus 로고
    • Posttranslational modifications of tubulin and the polarized transport of kinesin-1 in neurons
    • Hammond J, Huang C, Kaech S, Jacobson C, Banker G, and Verhey K (2010) Posttranslational modifications of tubulin and the polarized transport of kinesin-1 in neurons. Mol. Biol. Cell 21: 572-583.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 572-583
    • Hammond, J.1    Huang, C.2    Kaech, S.3    Jacobson, C.4    Banker, G.5    Verhey, K.6
  • 112
    • 62149146116 scopus 로고    scopus 로고
    • A selective filter for cytoplasmic transport at the axon initial segment
    • Song A, Wang D, Chen G, Li Y, Luo J, Duan S, and Poo M (2009) A selective filter for cytoplasmic transport at the axon initial segment. Cell 136: 1148-1160.
    • (2009) Cell , vol.136 , pp. 1148-1160
    • Song, A.1    Wang, D.2    Chen, G.3    Li, Y.4    Luo, J.5    Duan, S.6    Poo, M.7
  • 113
    • 15144340442 scopus 로고    scopus 로고
    • Defect in synaptic vesicle precursor transport and neuronal cell death in KIF1A motor protein-deficient mice
    • DOI 10.1083/jcb.141.2.431
    • Yonekawa Y, Harada A, Okada Y, Funakoshi T, Kanai Y, Takei Y, Terada S, Noda T, and Hirokawa N (1998) Defect in synaptic vesicle precursor transport and neuronal cell death in KIF1A motor protein-deficient mice. J. Cell Biol. 141: 431-441. (Pubitemid 28237091)
    • (1998) Journal of Cell Biology , vol.141 , Issue.2 , pp. 431-441
    • Yonekawa, V.1    Harada, A.2    Okada, Y.3    Funakoshi, T.4    Kanai, Y.5    Takei, Y.6    Terada, S.7    Noda, T.8    Hirokawa, N.9
  • 116
    • 14244261725 scopus 로고    scopus 로고
    • Axonal transport defects: A common theme in neurodegenerative diseases
    • DOI 10.1007/s00401-004-0952-x
    • Roy S, Zhang B, Lee V M, and Trojanowski J Q (2005) Axonal transport defects: a common theme in neurodegenerative diseases. Acta Neuropathol. 109: 5-13. (Pubitemid 40287785)
    • (2005) Acta Neuropathologica , vol.109 , Issue.1 , pp. 5-13
    • Roy, S.1    Zhang, B.2    Lee, V.M.-Y.3    Trojanowski, J.Q.4
  • 118
    • 79955088142 scopus 로고    scopus 로고
    • Molecular motor KIF17 is fundamental for memory and learning via differential support of synaptic NR2A.2B levels
    • Yin X, Takei Y, Kido M, and Hirokawa N (2011) Molecular motor KIF17 is fundamental for memory and learning via differential support of synaptic NR2A.2B levels. Neuron 70: 310-325.
    • (2011) Neuron , vol.70 , pp. 310-325
    • Yin, X.1    Takei, Y.2    Kido, M.3    Hirokawa, N.4
  • 120
    • 0029155982 scopus 로고
    • KIF3A/B: A heterodimeric kinesin superfamily protein that works as a microtubule plus end-directed motor for membrane organelle transport
    • Yamazaki H, Nakata T, Okada Y, and Hirokawa N (1995) KIF3A/B: a heterodimeric kinesin superfamily protein that works as a microtubule plus end-directed motor for membrane organelle transport. J. Cell Biol. 130: 1387-1399.
    • (1995) J. Cell Biol. , vol.130 , pp. 1387-1399
    • Yamazaki, H.1    Nakata, T.2    Okada, Y.3    Hirokawa, N.4
  • 121
    • 0029781733 scopus 로고    scopus 로고
    • Cloning and characterization of KAP3: A novel kinesin superfamily-associated protein of KIF3A/3B
    • Yamazaki H, Nakata T, Okada Y, and Hirokawa N (1996) Cloning and characterization of KAP3: a novel kinesin superfamily-associated protein of KIF3A/3B. Proc. Natl Acad. Sci. USA 93: 8443-8448.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 8443-8448
    • Yamazaki, H.1    Nakata, T.2    Okada, Y.3    Hirokawa, N.4
  • 123
    • 0034689028 scopus 로고    scopus 로고
    • Kinesin superfamily protein 3 (KIF3) motor transports fodrin-associating vesicles important for neurite building
    • Takeda S, Yamazaki H, Seog D-H, Kanai Y, Terada S, and Hirokawa N (2000) Kinesin superfamily protein 3 (KIF3) motor transports fodrin-associating vesicles important for neurite building. J. Cell Biol. 148: 1255-1265.
    • (2000) J. Cell Biol. , vol.148 , pp. 1255-1265
    • Takeda, S.1    Yamazaki, H.2    Seog, D.-H.3    Kanai, Y.4    Terada, S.5    Hirokawa, N.6
  • 125
    • 0032428685 scopus 로고    scopus 로고
    • Randomization of left-right asymmetry due to loss of nodal cilia generating leftward flow of extraembryonic fluid in mice lacking KIF3B motor protein
    • DOI 10.1016/S0092-8674(00)81705-5
    • Nonaka S, Tanaka Y, Okada Y, Takeda S, Harada A, Kanai Y, Kido M, and Hirokawa N (1998) Randomization of left-right asymmetry due to loss of nodal cilia generating leftward flow of extraembryonic fluid in mice lacking KIF3B motor protein. Cell 95: 829-837. (Pubitemid 29014462)
    • (1998) Cell , vol.95 , Issue.6 , pp. 829-837
    • Nonaka, S.1    Tanaka, Y.2    Okada, Y.3    Takeda, S.4    Harada, A.5    Kanai, Y.6    Kido, M.7    Hirokawa, N.8
  • 126
    • 0033577894 scopus 로고    scopus 로고
    • Left-right asymmetry and kinesin superfamily protein KIF3a: New insights in determination of laterality and mesoderm induction by KIF3A(-/-) mice analysis
    • DOI 10.1083/jcb.145.4.825
    • Takeda S, Yonekawa Y, Tanaka Y, Okada Y, Nonaka S, and Hirokawa N (1999) Left-right asymmetry and kinesin superfamily protein KIF3A: new insights in determination of laterality and mesoderm induction by kif3a-/- mice analysis. J. Cell Biol. 145: 825-836. (Pubitemid 29240858)
    • (1999) Journal of Cell Biology , vol.145 , Issue.4 , pp. 825-836
    • Takeda, S.1    Yonekawa, Y.2    Tanaka, Y.3    Okada, Y.4    Nonaka, S.5    Hirokawa, N.6
  • 128
    • 19344367605 scopus 로고    scopus 로고
    • Mechanism of nodal flow: A conserved symmetry breaking event in left-right axis determination
    • DOI 10.1016/j.cell.2005.04.008, PII S0092867405003491
    • Okada Y, Takeda S, Tanaka Y, Belmonte J-C I, and Hirokawa N (2005) Mechanism of nodal flow: a conserved symmetry breaking event in left-right axis determination. Cell 121: 633-644. (Pubitemid 40720015)
    • (2005) Cell , vol.121 , Issue.4 , pp. 633-644
    • Okada, Y.1    Takeda, S.2    Tanaka, Y.3    Belmonte, J.-C.I.4    Hirokawa, N.5
  • 129
    • 18744406718 scopus 로고    scopus 로고
    • FGF-induced vesicular release of Sonic hedgehog and retinoic acid in leftward nodal flow is critical for left-right determination
    • DOI 10.1038/nature03494
    • Tanaka Y, Okada Y, and Hirokawa N (2005) FGF-induced vesicular release of Sonic hedgehog and retinoic acid in leftward nodal flow is critical for left-right determination. Nature 435: 172-177. (Pubitemid 40685936)
    • (2005) Nature , vol.435 , Issue.7039 , pp. 172-177
    • Tanaka, Y.1    Okada, Y.2    Hirokawa, N.3
  • 130
    • 0028948491 scopus 로고
    • KIF2 is a new microtubule-based anterograde motor that transports membranous organelles distinct from those carried by kinesin heavy chain or KIF3A/B
    • Noda Y, Sato-Yoshitake R, Kondo S, Nangaku M, and Hirokawa N (1995) KIF2 is a new microtubule-based anterograde motor that transports membranous organelles distinct from those carried by kinesin heavy chain or KIF3A/B. J. Cell Biol. 129: 157-167.
    • (1995) J. Cell Biol. , vol.129 , pp. 157-167
    • Noda, Y.1    Sato-Yoshitake, R.2    Kondo, S.3    Nangaku, M.4    Hirokawa, N.5
  • 131
    • 0043199576 scopus 로고    scopus 로고
    • Kinesin superfamily protein 2A (KIF2A) functions in suppression of collateral branch extension
    • DOI 10.1016/S0092-8674(03)00522-1
    • Homma N, Takei Y, Tanaka Y, Nakata T, Terada S, Kikkawa M, Noda Y, and Hirokawa N (2003) Kinesin superfamily protein 2A (KIF2A) functions in suppression of collateral branch extension. Cell 114: 229-239. (Pubitemid 36936916)
    • (2003) Cell , vol.114 , Issue.2 , pp. 229-239
    • Homma, N.1    Takei, Y.2    Tanaka, Y.3    Nakata, T.4    Terada, S.5    Kikkawa, M.6    Noda, Y.7    Hirokawa, N.8
  • 132
    • 1342296567 scopus 로고    scopus 로고
    • A Common Mechanism for Microtubule Destabilizers - M Type Kinesins Stabilize Curling of the Protofilament Using the Class-Specific Neck and Loops
    • DOI 10.1016/S0092-8674(04)00129-1
    • Ogawa T, Nitta R, Okada Y, and Hirokawa N (2004) A common mechanism for microtubule destabilizers-M-type kinesins stabilize curling of the protofilament using the class-specific neck and loops. Cell 116: 591-602. (Pubitemid 38268103)
    • (2004) Cell , vol.116 , Issue.4 , pp. 591-602
    • Ogawa, T.1    Nitta, R.2    Okada, Y.3    Hirokawa, N.4
  • 133
    • 70350749730 scopus 로고    scopus 로고
    • KIF26A is an unconventional kinesin and regulates GDNF-Ret signaling in enteric neuronal development
    • Zhou R, Niwa S, Homma N, Takei Y, and Hirokawa N (2009) KIF26A is an unconventional kinesin and regulates GDNF-Ret signaling in enteric neuronal development. Cell 139: 802-813.
    • (2009) Cell , vol.139 , pp. 802-813
    • Zhou, R.1    Niwa, S.2    Homma, N.3    Takei, Y.4    Hirokawa, N.5
  • 134
    • 0028031045 scopus 로고
    • A novel microtubule-based motor protein (KIF4) for organelle transports, whose expression is regulated developmentally
    • DOI 10.1083/jcb.127.1.187
    • Sekine Y, Okada Y, Noda Y, Kondo S, Aizawa H, Takemura R, and Hirokawa N (1994) A novel microtubule-based motor protein (KIF4) for organelle transports, whose expression is regulated developmentally. J. Cell Biol. 127: 187-201. (Pubitemid 24307667)
    • (1994) Journal of Cell Biology , vol.127 , Issue.1 , pp. 187-201
    • Sekine, Y.1    Okada, Y.2    Noda, Y.3    Kondo, S.4    Aizawa, H.5    Takemura, R.6    Hirokawa, N.7
  • 135
    • 33646019197 scopus 로고    scopus 로고
    • KIF4 motor regulates activity-dependent neuronal survival by suppressing PARP-1 enzymatic activity
    • Midorikawa R, Takei Y, and Hirokawa N (2006) KIF4 motor regulates activity-dependent neuronal survival by suppressing PARP-1 enzymatic activity. Cell 125: 371-383.
    • (2006) Cell , vol.125 , pp. 371-383
    • Midorikawa, R.1    Takei, Y.2    Hirokawa, N.3
  • 136
    • 0037147176 scopus 로고    scopus 로고
    • CREM-dependent transcription in male germ cells controlled by a kinesin
    • DOI 10.1126/science.1077265
    • Macho B, Brancorsini S, Fimia G M, Setou M, Hirokawa N, and Sassone-Corsi P (2002) CREM-dependent transcription in male germ cells controlled by a kinesin. Science 298: 2388-2390. (Pubitemid 36014211)
    • (2002) Science , vol.298 , Issue.5602 , pp. 2388-2390
    • Macho, B.1    Brancorsini, S.2    Fimia, G.M.3    Setou, M.4    Hirokawa, N.5    Sassone-Corsi, P.6
  • 137
    • 78651456909 scopus 로고    scopus 로고
    • KIF16B/Rab14 molecular motor complex is critical for early embryonic development by transporting FGF receptor
    • Ueno H, Huang X, Tanaka Y, and Hirokawa N (2011) KIF16B/Rab14 molecular motor complex is critical for early embryonic development by transporting FGF receptor. Develop. Cell 20: 60-71.
    • (2011) Develop. Cell , vol.20 , pp. 60-71
    • Ueno, H.1    Huang, X.2    Tanaka, Y.3    Hirokawa, N.4
  • 138
    • 0024463944 scopus 로고
    • Movement of microtubules by single kinesin molecules
    • DOI 10.1038/342154a0
    • Howard J, Hudspeth A J, and Vale R D (1989) Movement of microtubules by single kinesin molecules. Nature 342: 154-158. (Pubitemid 19277017)
    • (1989) Nature , vol.342 , Issue.6246 , pp. 154-158
    • Howard, J.1    Hudspeth, A.J.2    Vale, R.D.3
  • 139
    • 0025222347 scopus 로고
    • Bead movement by single kinesin molecules studied with optical tweezers
    • Block S M, Goldstein L S, and Schnapp B J (1990) Bead movement by single kinesin molecules studied with optical tweezers. Nature 348: 348-352. (Pubitemid 120029107)
    • (1990) Nature , vol.348 , Issue.6299 , pp. 348-352
    • Block, S.M.1    Goldsteint, L.S.B.2    Schnapp, B.J.3
  • 140
    • 0027453868 scopus 로고
    • Direct observation of kinesin stepping by optical trapping interferometry
    • DOI 10.1038/365721a0
    • 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. (Pubitemid 23339876)
    • (1993) Nature , vol.365 , Issue.6448 , pp. 721-727
    • Svoboda, K.1    Schmidt, C.F.2    Schnapp, B.J.3    Block, S.M.4
  • 141
    • 0029156511 scopus 로고
    • Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains
    • Hackney D D (1995) Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains. Nature 377: 448-50.
    • (1995) Nature , vol.377 , pp. 448-50
    • Hackney, D.D.1
  • 142
    • 0029879228 scopus 로고    scopus 로고
    • Direct observation of single kinesin molecules moving along microtubules
    • DOI 10.1038/380451a0
    • 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. (Pubitemid 26102723)
    • (1996) Nature , vol.380 , Issue.6573 , pp. 451-453
    • Vale, R.D.1    Funatsu, T.2    Pierce, D.W.3    Romberg, L.4    Harada, Y.5    Yanagida, T.6
  • 143
    • 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
  • 144
    • 0347623370 scopus 로고    scopus 로고
    • Kinesin Moves by an Asymmetric Hand-Over-Hand Mechanism
    • DOI 10.1126/science.1092985
    • Asbury C L, Fehr A N, and Block S M (2003) Kinesin moves by an asymmetric hand-over-hand mechanism. Science 302: 2130-2134. (Pubitemid 38017947)
    • (2003) Science , vol.302 , Issue.5653 , pp. 2130-2134
    • Asbury, C.L.1    Fehr, A.N.2    Block, S.M.3
  • 145
    • 0345257160 scopus 로고    scopus 로고
    • Alternate fast and slow stepping of a heterodimeric kinesin molecule
    • DOI 10.1038/ncb1067
    • Kaseda K, Higuchi H, and Hirose K (2003) Alternate fast and slow stepping of a heterodimeric kinesin molecule. Nat. Cell Biol. 5: 1079-1082. (Pubitemid 37509114)
    • (2003) Nature Cell Biology , vol.5 , Issue.12 , pp. 1079-1082
    • Kaseda, K.1    Higuchi, H.2    Hirose, K.3
  • 147
    • 33646950699 scopus 로고    scopus 로고
    • The depolymerizing kinesin MCAK uses lattice diffusion to rapidly target microtubule ends
    • Helenius J, Brouhard G, Kalaidzidis Y, Diez S, and Howard J (2002) The depolymerizing kinesin MCAK uses lattice diffusion to rapidly target microtubule ends. Nature 441: 115-119.
    • (2002) Nature , vol.441 , pp. 115-119
    • Helenius, J.1    Brouhard, G.2    Kalaidzidis, Y.3    Diez, S.4    Howard, J.5
  • 148
    • 0037175396 scopus 로고    scopus 로고
    • K-loop insertion restores microtubule depolymerizing activity of a "neckless" MCAK mutant
    • Ovechkina Y, Wagenbach M, and Wordeman L (2002) K-loop insertion restores microtubule depolymerizing activity of a "neckless" MCAK mutant. J. Cell Biol. 159: 557-562.
    • (2002) J. Cell Biol. , vol.159 , pp. 557-562
    • Ovechkina, Y.1    Wagenbach, M.2    Wordeman, L.3
  • 149
    • 0037183926 scopus 로고    scopus 로고
    • Conversion of Unc104/KIF1A kinesin into a processive motor after dimerization
    • Tomishige M, Klopfenstein D R, and Vale R D (2002) Conversion of Unc104/KIF1A kinesin into a processive motor after dimerization. Science 297: 2263-2267.
    • (2002) Science , vol.297 , pp. 2263-2267
    • Tomishige, M.1    Klopfenstein, D.R.2    Vale, R.D.3
  • 150
    • 0029989974 scopus 로고    scopus 로고
    • Crystal structure of the kinesin motor domain reveals a structural similarity to myosin
    • DOI 10.1038/380550a0
    • 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. (Pubitemid 26110647)
    • (1996) Nature , vol.380 , Issue.6574 , pp. 550-555
    • Kull, F.J.1    Sablin, E.P.2    Lau, R.3    Fletterick, R.J.4    Vale, R.D.5
  • 151
    • 0029878485 scopus 로고    scopus 로고
    • Crystal structure of the motor domain of the kinesin-related motor ncd
    • DOI 10.1038/380555a0
    • 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 ncd. Nature 380: 555-559. (Pubitemid 26111333)
    • (1996) Nature , vol.380 , Issue.6574 , pp. 555-559
    • Sablin, E.P.1    Kull, F.J.2    Cooke, R.3    Vale, R.D.4    Fletterick, R.J.5
  • 153
    • 3442876110 scopus 로고    scopus 로고
    • KIF1A alternately uses two loops to bind microtubules
    • DOI 10.1126/science.1096621
    • Nitta R, Kikkawa M, Okada Y, and Hirokawa N (2004) KIF1A alternately uses two loops to bind microtubules. Science 305: 678-683. (Pubitemid 39006759)
    • (2004) Science , vol.305 , Issue.5684 , pp. 678-683
    • Nitta, R.1    Kikkawa, M.2    Okada, Y.3    Hirokawa, N.4
  • 154
    • 53549086926 scopus 로고    scopus 로고
    • Structural model for strain-dependent microtubule activation of Mg-ADP release from kinesin
    • Nitta R, Okada Y, and Hirokawa N (2008) Structural model for strain-dependent microtubule activation of Mg-ADP release from kinesin. Nat. Struct. Mol. Biol. 15: 1067-1075.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1067-1075
    • Nitta, R.1    Okada, Y.2    Hirokawa, N.3
  • 155
    • 0034695259 scopus 로고    scopus 로고
    • 15 Å resolution model of the monomeric kinesin motor, KIF1A
    • Kikkawa M, Okada Y, and Hirokawa N (2000) 15 Angstrom resolution model of the monomeric kinesin motor, KIFIA. Cell 100: 241-252. (Pubitemid 30064912)
    • (2000) Cell , vol.100 , Issue.2 , pp. 241-252
    • Kikkawa, M.1    Okada, Y.2    Hirokawa, N.3
  • 158
    • 33748931452 scopus 로고    scopus 로고
    • High-resolution cryo-EM maps show the nucleotide binding pocket of KIF1A in open and closed conformations
    • DOI 10.1038/sj.emboj.7601299, PII 7601299
    • Kikkawa M and Hirokawa N (2006) High-resolution cryo-EM maps show the nucleotide binding pocket of KIF1A in open and closed conformations. EMBO J. 25: 4187-4194. (Pubitemid 44435216)
    • (2006) EMBO Journal , vol.25 , Issue.18 , pp. 4187-4194
    • Kikkawa, M.1    Hirokawa, N.2
  • 159
    • 0033576727 scopus 로고    scopus 로고
    • A structural change in the kinesin motor protein that drives motility
    • Rice S, et al. (1999) A structural change in the kinesin motor protein that drives motility. Nature 402: 778-784.
    • (1999) Nature , vol.402 , pp. 778-784
    • Rice, S.1
  • 160
    • 0034628619 scopus 로고    scopus 로고
    • Role of the kinesin neck linker and catalytic core in microtubule-based motility
    • DOI 10.1016/S0960-9822(00)00316-X
    • Case R B, Rice S, Hart C L, Ly B, and Vale R D (2000) Role of the kinesin neck linker and catalytic core in microtubule-based motility. Curr. Biol. 10: 157-160. (Pubitemid 30115748)
    • (2000) Current Biology , vol.10 , Issue.3 , pp. 157-160
    • Case, R.B.1    Rice, S.2    Hart, C.L.3    Ly, B.4    Vale, R.D.5
  • 161
    • 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: 1844-1845.
    • (2003) Biophys. J. , vol.84 , pp. 1844-1845
    • Rice, S.1    Cui, Y.2    Sindelar, C.3    Naber, N.4    Matuska, M.5    Vale, R.6    Cooke, R.7
  • 162
    • 0037390461 scopus 로고    scopus 로고
    • Loading direction regulates the affinity of ADP for kinesin
    • DOI 10.1038/nsb911
    • Uemura S and Ishiwata S (2003) Loading direction regulates the affinity of ADP for kinesin. Nat. Struct. Biol. 4: 308-311. (Pubitemid 36418757)
    • (2003) Nature Structural Biology , vol.10 , Issue.4 , pp. 308-311
    • Uemura, S.1    Ishiwata, S.2
  • 164
    • 0033539520 scopus 로고    scopus 로고
    • Kinesins processivity results from mechanical and chemical coordination between the ATP hydrolysis cycles of the two motor domains
    • Hancock W O and Howard J (1999) Kinesins processivity results from mechanical and chemical coordination between the ATP hydrolysis cycles of the two motor domains. Proc. Natl Acad. Sci. USA 96: 13147-13152.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 13147-13152
    • Hancock, W.O.1    Howard, J.2
  • 168
    • 34147188510 scopus 로고    scopus 로고
    • An ATP gate controls tubulin binding by the tethered head of kinesin-1
    • DOI 10.1126/science.1136985
    • Alonso M C, et al. (2007) An ATP gate controls tubulin binding by the tethered head of kinesin-1. Science 316: 120-123. (Pubitemid 46559532)
    • (2007) Science , vol.316 , Issue.5821 , pp. 120-123
    • Alonso, M.C.1    Drummond, D.R.2    Kain, S.3    Hoeng, J.4    Amos, L.5    Cross, R.A.6
  • 169
    • 51549097934 scopus 로고    scopus 로고
    • Intramolecular strain coordinates kinesin stepping behavior along microtubules
    • Yildiz A, Tomishige M, Gennerich A, and Vale R D (2008) Intramolecular strain coordinates kinesin stepping behavior along microtubules. Cell 134: 1030-1041. (Pubitemid 37494968)
    • (2008) Cell , vol.134 , pp. 1030-1041
    • Yildiz, A.1    Tomishige, M.2    Gennerich, A.3    Vale, R.D.4
  • 170
    • 0345118121 scopus 로고    scopus 로고
    • Complex formation with kinesin motor domains affects the structure of microtubules
    • DOI 10.1016/j.jmb.2003.10.039
    • Krebs A, Goldie K N, and Hoenger A (2004) Complex formation with kinesin motor domains affects the structure of microtubules. J. Mol Biol. 335: 139-153.
    • (2004) Journal of Molecular Biology , vol.335 , Issue.1 , pp. 139-153
    • Krebs, A.1    Goldie, K.N.2    Hoenger, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.