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Volumn 27, Issue 2, 2006, Pages 161-171

Back on track - On the role of the microtubule for kinesin motility and cellular function

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; KINESIN; MICROTUBULE PROTEIN;

EID: 33746102907     PISSN: 01424319     EISSN: 15732657     Source Type: Journal    
DOI: 10.1007/s10974-005-9052-3     Document Type: Review
Times cited : (16)

References (120)
  • 1
    • 0032481381 scopus 로고    scopus 로고
    • Proteolytic mapping of kinesin/ncd-microtubule interface: Nucleotide-dependent conformational changes in the loops L8 and L12
    • Alonso MC, Vanderkerckhove J and Cross RA (1998) Proteolytic mapping of kinesin/ncd-microtubule interface: nucleotide-dependent conformational changes in the loops L8 and L12. EMBO J 17: 945-951.
    • (1998) EMBO J , vol.17 , pp. 945-951
    • Alonso, M.C.1    Vanderkerckhove, J.2    Cross, R.A.3
  • 2
    • 0016438632 scopus 로고
    • Tentative identification of the amino acid that binds tyrosine as a single unit into a soluble brain protein
    • Arce CA, Barra HS, Rodriguez JA and Caputto R (1975) Tentative identification of the amino acid that binds tyrosine as a single unit into a soluble brain protein. FEBS Lett 50: 5-7.
    • (1975) FEBS Lett , vol.50 , pp. 5-7
    • Arce, C.A.1    Barra, H.S.2    Rodriguez, J.A.3    Caputto, R.4
  • 3
    • 0017903434 scopus 로고
    • Release of [14C]tyrosine from tubulinyl-[14C]tyrosine by brain extract. Separation of a carboxypeptidase from tubulin-tyrosine ligase
    • Argarana CE, Barra HS and Caputto R (1978) Release of [14C]tyrosine from tubulinyl-[14C]tyrosine by brain extract. Separation of a carboxypeptidase from tubulin-tyrosine ligase. Mol Cell Biochem 19: 17-21.
    • (1978) Mol Cell Biochem , vol.19 , pp. 17-21
    • Argarana, C.E.1    Barra, H.S.2    Caputto, R.3
  • 4
    • 0018841905 scopus 로고
    • Tubulinyl-tyrosine carboxypeptidase from chicken brain: Properties and partial purification
    • Argarana CE, Barra HS and Caputto R (1980) Tubulinyl-tyrosine carboxypeptidase from chicken brain: properties and partial purification. J Neurochem 34: 114-118.
    • (1980) J Neurochem , vol.34 , pp. 114-118
    • Argarana, C.E.1    Barra, H.S.2    Caputto, R.3
  • 5
    • 0347623370 scopus 로고    scopus 로고
    • Kinesin moves by an asymmetric hand-over-hand mechanism
    • Asbury CL, Fehr AN and Block SM (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
  • 6
    • 23044513072 scopus 로고    scopus 로고
    • The complex interplay between the neck and hinge domains in kinesin-1 dimerization and motor activity
    • Bathe F, Hahlen K, Dombi R, Driller L, Schliwa M and Woehlke G (2005) The complex interplay between the neck and hinge domains in kinesin-1 dimerization and motor activity. Mol Biol Cell 16: 3529-3537.
    • (2005) Mol Biol Cell , vol.16 , pp. 3529-3537
    • Bathe, F.1    Hahlen, K.2    Dombi, R.3    Driller, L.4    Schliwa, M.5    Woehlke, G.6
  • 7
    • 0022385617 scopus 로고
    • Tubulin, hybrid dimers, and tubulin S. Stepwise charge reduction and polymerization
    • Bhattacharyya B, Sackett DL and Wolff J (1985) Tubulin, hybrid dimers, and tubulin S. Stepwise charge reduction and polymerization. J Biol Chem 260: 10208-10216.
    • (1985) J Biol Chem , vol.260 , pp. 10208-10216
    • Bhattacharyya, B.1    Sackett, D.L.2    Wolff, J.3
  • 9
    • 0035918287 scopus 로고    scopus 로고
    • Differential binding regulation of microtubule-associated proteins MAP1A, MAP1B, and MAP2 by tubulin polyglutamylation
    • Bonnet C, Boucher D, Lazereg S, Pedrotti B, Islam K, Denoulet P and Larcher JC (2001) Differential binding regulation of microtubule-associated proteins MAP1A, MAP1B, and MAP2 by tubulin polyglutamylation. J Biol Chem 276: 12839-12848.
    • (2001) J Biol Chem , vol.276 , pp. 12839-12848
    • Bonnet, C.1    Boucher, D.2    Lazereg, S.3    Pedrotti, B.4    Islam, K.5    Denoulet, P.6    Larcher, J.C.7
  • 10
    • 0028110393 scopus 로고
    • Polyglutamylation of tubulin as a progressive regulator of in vitro interactions between the microtubule-associated protein Tau and tubulin
    • Boucher D, Larcher JC, Gros F and Denoulet P (1994) Polyglutamylation of tubulin as a progressive regulator of in vitro interactions between the microtubule-associated protein Tau and tubulin. Biochemistry 33: 12471-12477.
    • (1994) Biochemistry , vol.33 , pp. 12471-12477
    • Boucher, D.1    Larcher, J.C.2    Gros, F.3    Denoulet, P.4
  • 11
    • 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
  • 12
    • 9244261065 scopus 로고    scopus 로고
    • Axonemal tubulin polyglycylation probed with two monoclonal antibodies: Widespread evolutionary distribution, appearance during spermatozoan maturation and possible function in motility
    • Bre MH, Redeker V, Quibell M, Darmanaden-Delorme J, Bressac C, Cosson J, Huitorel P, Schmitter JM, Rossler J, Johnson T and others (1996) Axonemal tubulin polyglycylation probed with two monoclonal antibodies: widespread evolutionary distribution, appearance during spermatozoan maturation and possible function in motility. J Cell Sci 109: 727-738.
    • (1996) J Cell Sci , vol.109 , pp. 727-738
    • Bre, M.H.1    Redeker, V.2    Quibell, M.3    Darmanaden-Delorme, J.4    Bressac, C.5    Cosson, J.6    Huitorel, P.7    Schmitter, J.M.8    Rossler, J.9    Johnson, T.10
  • 13
    • 0031665835 scopus 로고    scopus 로고
    • Tubulin polyglycylation: Differential posttranslational modification of dynamic cytoplasmic and stable axonemal microtubules in paramecium
    • Bre MH, Redeker V, Vinh J, Rossier J and Levilliers N (1998) Tubulin polyglycylation: differential posttranslational modification of dynamic cytoplasmic and stable axonemal microtubules in paramecium. Mol Biol Cell 9: 2655-2665.
    • (1998) Mol Biol Cell , vol.9 , pp. 2655-2665
    • Bre, M.H.1    Redeker, V.2    Vinh, J.3    Rossier, J.4    Levilliers, N.5
  • 14
    • 0033491554 scopus 로고    scopus 로고
    • Rotokinesis, a novel phenomenon of cell locomotion-assisted cytokinesis in the ciliate Tetrahymena thermophila
    • Brown JM, Hardin C and Gaertig J (1999) Rotokinesis, a novel phenomenon of cell locomotion-assisted cytokinesis in the ciliate Tetrahymena thermophila. Cell Biol Int 23: 841-848.
    • (1999) Cell Biol Int , vol.23 , pp. 841-848
    • Brown, J.M.1    Hardin, C.2    Gaertig, J.3
  • 15
    • 19644377414 scopus 로고    scopus 로고
    • Mechanics of the kinesin step
    • Carter NJ and Cross RA (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
  • 16
  • 17
    • 0033193864 scopus 로고    scopus 로고
    • Kinesin's tail domain is an inhibitory regulator of the motor domain
    • Coy DL, Hancock WO, Wagenbach M and Howard J (1999) Kinesin's tail domain is an inhibitory regulator of the motor domain. Nat Cell Biol 1: 288-292.
    • (1999) Nat Cell Biol , vol.1 , pp. 288-292
    • Coy, D.L.1    Hancock, W.O.2    Wagenbach, M.3    Howard, J.4
  • 18
    • 0026570397 scopus 로고
    • Evidence that the stalk of Drosophila kinesin heavy chain is an alpha-helical coiled coil
    • de Cuevas M, Tao T and Goldstein LS (1992) Evidence that the stalk of Drosophila kinesin heavy chain is an alpha-helical coiled coil. J Cell Biol 116: 957-965.
    • (1992) J Cell Biol , vol.116 , pp. 957-965
    • De Cuevas, M.1    Tao, T.2    Goldstein, L.S.3
  • 19
    • 0037133046 scopus 로고    scopus 로고
    • Both carboxy-terminal tails of alpha- and beta-tubulin are essential, but either one will suffice
    • Duan J and Gorovsky MA (2002) Both carboxy-terminal tails of alpha- and beta-tubulin are essential, but either one will suffice. Curr Biol 12: 313-316.
    • (2002) Curr Biol , vol.12 , pp. 313-316
    • Duan, J.1    Gorovsky, M.A.2
  • 20
    • 0032476645 scopus 로고    scopus 로고
    • Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: Implications for Alzheimer's disease
    • Ebneth A, Godemann R, Stamer K, Illenberger S, Trinczek B and Mandelkow E (1998) Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: implications for Alzheimer's disease. J Cell Biol 143: 777-794.
    • (1998) J Cell Biol , vol.143 , pp. 777-794
    • Ebneth, A.1    Godemann, R.2    Stamer, K.3    Illenberger, S.4    Trinczek, B.5    Mandelkow, E.6
  • 21
    • 0032992466 scopus 로고    scopus 로고
    • Microtubule dysfunction by posttranslational nitrotyrosination of alpha-tubulin: A nitric oxide-dependent mechanism of cellular injury
    • Eiserich JP, Estevez AG, Bamberg TV, Ye YZ, Chumley PH, Beckman JS and Freeman BA (1999) Microtubule dysfunction by posttranslational nitrotyrosination of alpha-tubulin: a nitric oxide-dependent mechanism of cellular injury. Proc Natl Acad Sci USA 96: 6365-6370.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6365-6370
    • Eiserich, J.P.1    Estevez, A.G.2    Bamberg, T.V.3    Ye, Y.Z.4    Chumley, P.H.5    Beckman, J.S.6    Freeman, B.A.7
  • 23
    • 0029035184 scopus 로고
    • Acetylation of lysine 40 in alpha-tubulin is not essential in Tetrahymena thermophila
    • Gaertig J, Cruz MA, Bowen J, Gu L, Pennock DG and Gorovsky MA (1995) Acetylation of lysine 40 in alpha-tubulin is not essential in Tetrahymena thermophila. J Cell Biol 129: 1301-1310.
    • (1995) J Cell Biol , vol.129 , pp. 1301-1310
    • Gaertig, J.1    Cruz, M.A.2    Bowen, J.3    Gu, L.4    Pennock, D.G.5    Gorovsky, M.A.6
  • 24
    • 0027298836 scopus 로고
    • Perspectives on tubulin isotype function and evolution based on the observation that Tetrahymena thermophila microtubules contain a single alpha- and beta-tubulin
    • Gaertig J, Thatcher TH, McGrath KE, Callahan RC and Gorovsky MA (1993) Perspectives on tubulin isotype function and evolution based on the observation that Tetrahymena thermophila microtubules contain a single alpha- and beta-tubulin. Cell Motil Cytoskeleton 25: 243-253.
    • (1993) Cell Motil Cytoskeleton , vol.25 , pp. 243-253
    • Gaertig, J.1    Thatcher, T.H.2    McGrath, K.E.3    Callahan, R.C.4    Gorovsky, M.A.5
  • 26
    • 0032548489 scopus 로고    scopus 로고
    • Alternating site mechanism of the kinesin ATPase
    • Gilbert SP, Moyer ML and Johnson KA (1998) Alternating site mechanism of the kinesin ATPase. Biochemistry 37: 792-799.
    • (1998) Biochemistry , vol.37 , pp. 792-799
    • Gilbert, S.P.1    Moyer, M.L.2    Johnson, K.A.3
  • 27
    • 0027132479 scopus 로고
    • With apologies to scheherazade: Tails of 1001 kinesin motors
    • Goldstein LS (1993) With apologies to scheherazade: tails of 1001 kinesin motors. Annu Rev Genet 27: 319-351.
    • (1993) Annu Rev Genet , vol.27 , pp. 319-351
    • Goldstein, L.S.1
  • 28
    • 0035575469 scopus 로고    scopus 로고
    • Molecular motors: From one motor many tails to one motor many tales
    • Goldstein LS (2001) Molecular motors: from one motor many tails to one motor many tales. Trends Cell Biol 11: 477-482.
    • (2001) Trends Cell Biol , vol.11 , pp. 477-482
    • Goldstein, L.S.1
  • 29
    • 0028883469 scopus 로고
    • Stable, detyrosinated microtubules function to localize vimentin intermediate filaments in fibroblasts
    • Gurland G and Gundersen GG (1995) Stable, detyrosinated microtubules function to localize vimentin intermediate filaments in fibroblasts. J Cell Biol 131: 1275-1290.
    • (1995) J Cell Biol , vol.131 , pp. 1275-1290
    • Gurland, G.1    Gundersen, G.G.2
  • 30
    • 0025743437 scopus 로고
    • Coalignment of vimentin intermediate filaments with microtubules depends on kinesin
    • Gyoeva FK and Gelfand VI (1991) Coalignment of vimentin intermediate filaments with microtubules depends on kinesin. Nature 353: 445-448.
    • (1991) Nature , vol.353 , pp. 445-448
    • Gyoeva, F.K.1    Gelfand, V.I.2
  • 31
    • 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: 6865-6869.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 6865-6869
    • Hackney, D.D.1
  • 32
    • 0028979598 scopus 로고
    • Nucleotide-dependent angular change in kinesin motor domain bound to tubulin
    • Hirose K, Lockhart A, Cross RA and Amos LA (1995) Nucleotide-dependent angular change in kinesin motor domain bound to tubulin. Nature 376: 277-279.
    • (1995) Nature , vol.376 , pp. 277-279
    • Hirose, K.1    Lockhart, A.2    Cross, R.A.3    Amos, L.A.4
  • 33
    • 0345073110 scopus 로고    scopus 로고
    • 3D electron microscopy of the interaction of kinesin with tubulin
    • Hirose K, Lowe J, Alonso M, Cross RA and Amos LA (1999) 3D electron microscopy of the interaction of kinesin with tubulin. Cell Struct Funct. 24: 277-284.
    • (1999) Cell Struct Funct , vol.24 , pp. 277-284
    • Hirose, K.1    Lowe, J.2    Alonso, M.3    Cross, R.A.4    Amos, L.A.5
  • 34
    • 0031556947 scopus 로고    scopus 로고
    • Motor domains of kinesin and ncd interact with microtubule protofilaments with the same binding geometry
    • Hoenger A and Milligan RA (1997) Motor domains of kinesin and ncd interact with microtubule protofilaments with the same binding geometry. J Mol Biol 265: 553-564.
    • (1997) J Mol Biol , vol.265 , pp. 553-564
    • Hoenger, A.1    Milligan, R.A.2
  • 36
    • 0024463944 scopus 로고
    • Movement of microtubules by single kinesin molecules
    • Howard J, Hudspeth AJ and Vale RD (1989) Movement of microtubules by single kinesin molecules. Nature 342: 154-158.
    • (1989) Nature , vol.342 , pp. 154-158
    • Howard, J.1    Hudspeth, A.J.2    Vale, R.D.3
  • 37
    • 0036203332 scopus 로고    scopus 로고
    • Differential distribution of glutamylated tubulin isoforms along the sea urchin sperm axoneme
    • Huitorel P, White D, Fouquet JP, Kann ML, Cosson J and Gagnon C (2002) Differential distribution of glutamylated tubulin isoforms along the sea urchin sperm axoneme. Mol Reprod Dev 62: 139-148.
    • (2002) Mol Reprod Dev , vol.62 , pp. 139-148
    • Huitorel, P.1    White, D.2    Fouquet, J.P.3    Kann, M.L.4    Cosson, J.5    Gagnon, C.6
  • 38
    • 0030893287 scopus 로고    scopus 로고
    • Structurally similar Drosophila alpha-tubulins are functionally distinct in vivo
    • Hutchens JA, Hoyle HD, Turner FR and Raff EC (1997) Structurally similar Drosophila alpha-tubulins are functionally distinct in vivo. Mol Biol Cell 8: 481-500.
    • (1997) Mol Biol Cell , vol.8 , pp. 481-500
    • Hutchens, J.A.1    Hoyle, H.D.2    Turner, F.R.3    Raff, E.C.4
  • 39
    • 0034044449 scopus 로고    scopus 로고
    • Phosphorylation of tubulin tyrosine ligase: A potential mechanism for regulation of alpha-tubulin tyrosination
    • Idriss HT (2000) Phosphorylation of tubulin tyrosine ligase: a potential mechanism for regulation of alpha-tubulin tyrosination. Cell Motil Cytoskeleton 46: 1-5.
    • (2000) Cell Motil Cytoskeleton , vol.46 , pp. 1-5
    • Idriss, H.T.1
  • 42
    • 0031905985 scopus 로고    scopus 로고
    • The axonemal microtubules of the Chlamydomonas flagellum differ in tubulin isoform content
    • Johnson KA (1998) The axonemal microtubules of the Chlamydomonas flagellum differ in tubulin isoform content. J Cell Sci 111: 313-320.
    • (1998) J Cell Sci , vol.111 , pp. 313-320
    • Johnson, K.A.1
  • 43
    • 0025112940 scopus 로고
    • Light chains of sea urchin kinesin identified by immunoadsorption
    • Johnson CS, Buster D and Scholey JM (1990) Light chains of sea urchin kinesin identified by immunoadsorption. Cell Motil Cytoskeleton 16: 204-213.
    • (1990) Cell Motil Cytoskeleton , vol.16 , pp. 204-213
    • Johnson, C.S.1    Buster, D.2    Scholey, J.M.3
  • 44
    • 0034739245 scopus 로고    scopus 로고
    • Incorporation of nitrotyrosine into alpha-tubulin by recombinant mammalian tubulin-tyrosine ligase
    • Kalisz HM, Erck C, Plessmann U and Wehland J (2000) Incorporation of nitrotyrosine into alpha-tubulin by recombinant mammalian tubulin-tyrosine ligase. Biochim Biophys Acta 1481: 131-138.
    • (2000) Biochim Biophys Acta , vol.1481 , pp. 131-138
    • Kalisz, H.M.1    Erck, C.2    Plessmann, U.3    Wehland, J.4
  • 45
    • 0037407651 scopus 로고    scopus 로고
    • Glutamylated tubulin: Diversity of expression and distribution of isoforms
    • Kami ML, Soues S, Levilliers N and Fouquet JP (2003) Glutamylated tubulin: diversity of expression and distribution of isoforms. Cell Motil Cytoskeleton 55: 14-25.
    • (2003) Cell Motil Cytoskeleton , vol.55 , pp. 14-25
    • Kami, M.L.1    Soues, S.2    Levilliers, N.3    Fouquet, J.P.4
  • 46
    • 0037071549 scopus 로고    scopus 로고
    • Searching for the middle ground: Mechanisms of chromosome alignment during mitosis
    • Kapoor TM and Compton DA (2002) Searching for the middle ground: mechanisms of chromosome alignment during mitosis. J Cell Biol 157: 551-556.
    • (2002) J Cell Biol , vol.157 , pp. 551-556
    • Kapoor, T.M.1    Compton, D.A.2
  • 47
    • 0032972965 scopus 로고    scopus 로고
    • Identification of microtubule binding sites in the Ncd tail domain
    • Karabay A and Walker RA (1999a) Identification of microtubule binding sites in the Ncd tail domain. Biochemistry 38: 1838-1849.
    • (1999) Biochemistry , vol.38 , pp. 1838-1849
    • Karabay, A.1    Walker, R.A.2
  • 48
    • 0033614443 scopus 로고    scopus 로고
    • The Ncd tail domain promotes microtubule assembly and stability
    • Karabay A and Walker RA (1999b) The Ncd tail domain promotes microtubule assembly and stability. Biochem Biophys Res Commun 258: 39-43.
    • (1999) Biochem Biophys Res Commun , vol.258 , pp. 39-43
    • Karabay, A.1    Walker, R.A.2
  • 49
    • 0037902489 scopus 로고    scopus 로고
    • Identification of Ncd tail domain-binding sites on the tubulin dimer
    • Karabay A and Walker RA (2003) Identification of Ncd tail domain-binding sites on the tubulin dimer. Biochem Biophys Res Commun 305: 523-528.
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 523-528
    • Karabay, A.1    Walker, R.A.2
  • 51
    • 0033575694 scopus 로고    scopus 로고
    • Functional anatomy of the kinesin molecule in vivo
    • Kirchner J, Seiler S, Fuchs S and Schliwa M (1999) Functional anatomy of the kinesin molecule in vivo. EMBO J 18: 4404-4413.
    • (1999) EMBO J , vol.18 , pp. 4404-4413
    • Kirchner, J.1    Seiler, S.2    Fuchs, S.3    Schliwa, M.4
  • 52
    • 0037013148 scopus 로고    scopus 로고
    • Role of phosphatidylinositol(4,5)bisphosphate organization in membrane transport by the Unc104 kinesin motor
    • Klopfenstein DR, Tomishige M, Stuurman N and Vale RD (2002) Role of phosphatidylinositol(4,5)bisphosphate organization in membrane transport by the Unc104 kinesin motor. Cell 109: 347-358.
    • (2002) Cell , vol.109 , pp. 347-358
    • Klopfenstein, D.R.1    Tomishige, M.2    Stuurman, N.3    Vale, R.D.4
  • 53
    • 0345118121 scopus 로고    scopus 로고
    • Complex formation with kinesin motor domains affects the structure of microtubules
    • Krebs A, Goldie KN and Hoenger A (2004) Complex formation with kinesin motor domains affects the structure of microtubules. J Mol Biol 335: 139-153.
    • (2004) J Mol Biol , vol.335 , pp. 139-153
    • Krebs, A.1    Goldie, K.N.2    Hoenger, A.3
  • 54
    • 0032941748 scopus 로고    scopus 로고
    • Detyrosination of tubulin regulates the interaction of intermediate filaments with microtubules in vivo via a kinesin-dependent mechanism
    • Kreitzer G, Liao G and Gundersen GG (1999) Detyrosination of tubulin regulates the interaction of intermediate filaments with microtubules in vivo via a kinesin-dependent mechanism. Mol Biol Cell 10: 1105-1118.
    • (1999) Mol Biol Cell , vol.10 , pp. 1105-1118
    • Kreitzer, G.1    Liao, G.2    Gundersen, G.G.3
  • 55
    • 0029989974 scopus 로고    scopus 로고
    • Crystal structure of the kinesin motor domain reveals a structural similarity to myosin
    • Kull FJ, Sablin EP, Lau R, Fletterick RJ and Vale RD (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
  • 56
    • 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 and Gelfand VI (1989) Isolation of a 45-kDa fragment from the kinesin heavy chain with enhanced ATPase and microtubule-binding activities. J Biol Chem 264: 589-595.
    • (1989) J Biol 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
  • 59
    • 27744552948 scopus 로고    scopus 로고
    • The E-hook of tubulin interacts with kinesin's head to increase processivity and speed
    • Lakamper S and Meyhofer E (2005) The E-hook of tubulin interacts with kinesin's head to increase processivity and speed. Biophys J 89: 3223-3234.
    • (2005) Biophys J , vol.89 , pp. 3223-3234
    • Lakamper, S.1    Meyhofer, E.2
  • 60
    • 0037340878 scopus 로고    scopus 로고
    • Single fungal kinesin motor molecules move processively along microtubules
    • Lakamper S, Kallipolitou A, Woehlke G, Schliwa M and Meyhofer E (2003) Single fungal kinesin motor molecules move processively along microtubules. Biophys J 84: 1833-1843.
    • (2003) Biophys J , vol.84 , pp. 1833-1843
    • Lakamper, S.1    Kallipolitou, A.2    Woehlke, G.3    Schliwa, M.4    Meyhofer, E.5
  • 61
    • 0029814394 scopus 로고    scopus 로고
    • Interaction of kinesin motor domains with alpha- And beta-tubulin subunits at a tau-independent binding site. Regulation by polyglutamylation
    • Larcher JC, Boucher D, Lazereg S, Gros F and Denoulet P (1996) Interaction of kinesin motor domains with alpha- and beta-tubulin subunits at a tau-independent binding site. Regulation by polyglutamylation. J Biol Chem 271: 22117-22124.
    • (1996) J Biol Chem , vol.271 , pp. 22117-22124
    • Larcher, J.C.1    Boucher, D.2    Lazereg, S.3    Gros, F.4    Denoulet, P.5
  • 63
    • 0029125382 scopus 로고
    • Monoclonal and polyclonal antibodies detect a new type of post-translational modification of axonemal tubulin
    • Levilliers N, Fleury A and Hill AM (1995) Monoclonal and polyclonal antibodies detect a new type of post-translational modification of axonemal tubulin. J Cell Sci 108: 3013-3028.
    • (1995) J Cell Sci , vol.108 , pp. 3013-3028
    • Levilliers, N.1    Fleury, A.2    Hill, A.M.3
  • 64
    • 0032540307 scopus 로고    scopus 로고
    • Kinesin is a candidate for cross-bridging microtubules and intermediate filaments. Selective binding of kinesin to detyrosinated tubulin and vimentin
    • Liao G and Gundersen GG (1998) Kinesin is a candidate for cross-bridging microtubules and intermediate filaments. Selective binding of kinesin to detyrosinated tubulin and vimentin. J Biol Chem 273: 9797-9803.
    • (1998) J Biol Chem , vol.273 , pp. 9797-9803
    • Liao, G.1    Gundersen, G.G.2
  • 65
    • 0030709242 scopus 로고    scopus 로고
    • Multiple forms of tubulin: Different gene products and covalent modifications
    • Luduena RF (1998) Multiple forms of tubulin: different gene products and covalent modifications. Int Rev Cytol 178: 207-275.
    • (1998) Int Rev Cytol , vol.178 , pp. 207-275
    • Luduena, R.F.1
  • 66
    • 0029966076 scopus 로고    scopus 로고
    • Posttranslational modifications in the C-terminal tail of axonemal tubulin from sea urchin sperm
    • Mary J, Redeker V, Le Caer JP, Rossier J and Schmitter JM (1996) Posttranslational modifications in the C-terminal tail of axonemal tubulin from sea urchin sperm. J Biol Chem 271: 9928-9933.
    • (1996) J Biol Chem , vol.271 , pp. 9928-9933
    • Mary, J.1    Redeker, V.2    Le Caer, J.P.3    Rossier, J.4    Schmitter, J.M.5
  • 67
    • 0033807251 scopus 로고    scopus 로고
    • Accessory tubules and axonemal microtubules of Apis mellifera sperm flagellum differ in their tubulin isoform content
    • Mencarelli C, Bre MH, Levilliers N and Dallai R (2000) Accessory tubules and axonemal microtubules of Apis mellifera sperm flagellum differ in their tubulin isoform content. Cell Motil Cytoskeleton 47: 1-12.
    • (2000) Cell Motil Cytoskeleton , vol.47 , pp. 1-12
    • Mencarelli, C.1    Bre, M.H.2    Levilliers, N.3    Dallai, R.4
  • 68
    • 0028843342 scopus 로고
    • The force generated by a single kinesin molecule against an elastic load
    • Meyhofer E and Howard J (1995) The force generated by a single kinesin molecule against an elastic load. Proc Natl Acad Sci USA 92: 574-578.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 574-578
    • Meyhofer, E.1    Howard, J.2
  • 70
    • 0033491915 scopus 로고    scopus 로고
    • Polyglutamylation and polyglycylation of alpha-and beta-tubulins during in vitro ciliated cell differentiation of human respiratory epithelial cells
    • Million K, Larcher J, Laoukili J, Bourguignon D, Marano F and Tournier F (1999) Polyglutamylation and polyglycylation of alpha-and beta-tubulins during in vitro ciliated cell differentiation of human respiratory epithelial cells. J Cell Sci 112: 4357-4366.
    • (1999) J Cell Sci , vol.112 , pp. 4357-4366
    • Million, K.1    Larcher, J.2    Laoukili, J.3    Bourguignon, D.4    Marano, F.5    Tournier, F.6
  • 71
    • 0029757769 scopus 로고    scopus 로고
    • The A and B tubules of the outer doublets of sea urchin sperm axonemes are composed of different tubulin variants
    • Multigner L, Pignot-Paintrand I, Saoudi Y, Job D, Plessmann U, Rudiger M and Weber K (1996) The A and B tubules of the outer doublets of sea urchin sperm axonemes are composed of different tubulin variants. Biochemistry 35: 10862-10871.
    • (1996) Biochemistry , vol.35 , pp. 10862-10871
    • Multigner, L.1    Pignot-Paintrand, I.2    Saoudi, Y.3    Job, D.4    Plessmann, U.5    Rudiger, M.6    Weber, K.7
  • 72
    • 0018991110 scopus 로고
    • Purification and characterization of tubulin-tyrosine ligase from porcine brain
    • Murofushi H (1980) Purification and characterization of tubulin-tyrosine ligase from porcine brain. J Biochem (Tokyo) 87: 979-984.
    • (1980) J Biochem (Tokyo) , vol.87 , pp. 979-984
    • Murofushi, H.1
  • 73
    • 14744280774 scopus 로고    scopus 로고
    • Long-range cooperative binding of kinesin to a microtubule in the presence of ATP
    • Muto E, Sakai H and Kaseda K (2005) Long-range cooperative binding of kinesin to a microtubule in the presence of ATP. J Cell Biol 168: 691-696.
    • (2005) J Cell Biol , vol.168 , pp. 691-696
    • Muto, E.1    Sakai, H.2    Kaseda, K.3
  • 74
    • 0035799299 scopus 로고    scopus 로고
    • Axoneme-specific beta-tubulin specialization: A conserved C-terminal motif specifies the central pair
    • Nielsen MG, Turner FR, Hutchens JA and Raff EC (2001) Axoneme-specific beta-tubulin specialization: a conserved C-terminal motif specifies the central pair. Curr Biol 11: 529-533.
    • (2001) Curr Biol , vol.11 , pp. 529-533
    • Nielsen, M.G.1    Turner, F.R.2    Hutchens, J.A.3    Raff, E.C.4
  • 75
    • 3442876110 scopus 로고    scopus 로고
    • KIF1A alternately uses two loops to bind microtubules
    • Nitta R, Kikkawa M, Okada Y and Hirokawa N (2004) KIF1A alternately uses two loops to bind microtubules. Science 305: 678-683.
    • (2004) Science , vol.305 , pp. 678-683
    • Nitta, R.1    Kikkawa, M.2    Okada, Y.3    Hirokawa, N.4
  • 76
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the alpha beta tubulin dimer by electron crystallography
    • Nogales E, Wolf SG and Downing KH (1998) Structure of the alpha beta tubulin dimer by electron crystallography. Nature 391: 199-203.
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 77
    • 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
  • 78
    • 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
    • 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.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 640-645
    • Okada, Y.1    Hirokawa, N.2
  • 79
    • 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
  • 81
    • 0030849109 scopus 로고    scopus 로고
    • Mammalian sperm tubulin: An exceptionally large number of variants based on several posttranslational modifications
    • Plessmann U and Weber K (1997) Mammalian sperm tubulin: an exceptionally large number of variants based on several posttranslational modifications. J Protein Chem 16: 385-390.
    • (1997) J Protein Chem , vol.16 , pp. 385-390
    • Plessmann, U.1    Weber, K.2
  • 82
    • 0141974953 scopus 로고    scopus 로고
    • Posttranslational incorporation of the antiproliferative agent azatyrosine into the C-terminus of alpha-tubulin
    • Purro SA, Bisig CG, Contin MA, Barra HS and Arce CA (2003) Posttranslational incorporation of the antiproliferative agent azatyrosine into the C-terminus of alpha-tubulin. Biochem J 375: 121-129.
    • (2003) Biochem J , vol.375 , pp. 121-129
    • Purro, S.A.1    Bisig, C.G.2    Contin, M.A.3    Barra, H.S.4    Arce, C.A.5
  • 84
    • 0017406215 scopus 로고
    • Enzyme which specifically adds tyrosine to the alpha chain of tubulin
    • Raybin D and Flavin M (1977a) Enzyme which specifically adds tyrosine to the alpha chain of tubulin. Biochemistry 16: 2189-2194.
    • (1977) Biochemistry , vol.16 , pp. 2189-2194
    • Raybin, D.1    Flavin, M.2
  • 85
    • 0017391714 scopus 로고
    • Modification of tubulin by tyrosylation in cells and extracts and its effect on assembly in vitro
    • Raybin D and Flavin M (1977b) Modification of tubulin by tyrosylation in cells and extracts and its effect on assembly in vitro. J Cell Biol 73: 492-504.
    • (1977) J Cell Biol , vol.73 , pp. 492-504
    • Raybin, D.1    Flavin, M.2
  • 86
    • 4644267074 scopus 로고    scopus 로고
    • Posttranslational modification of brain tubulins from the Antarctic fish Notothenia coriiceps: Reduced C-terminal glutamylation correlates with efficient microtubule assembly at low temperature
    • Redeker V, Frankfurter A, Parker SK, Rossier J, Detrich HW and 3rd (2004) Posttranslational modification of brain tubulins from the Antarctic fish Notothenia coriiceps: reduced C-terminal glutamylation correlates with efficient microtubule assembly at low temperature. Biochemistry 43: 12265-12274.
    • (2004) Biochemistry , vol.43 , pp. 12265-12274
    • Redeker, V.1    Frankfurter, A.2    Parker, S.K.3    Rossier, J.4    Detrich III, H.W.5
  • 88
    • 12844266799 scopus 로고    scopus 로고
    • Mutations of tubulin glycylation sites reveal cross-talk between the C termini of alpha- and beta-tubulin and affect the ciliary matrix in Tetrahymena
    • Redeker V, Levilliers N, Vinolo E, Rossier J, Jaillard D, Burnette D, Gaertig J and Bre MH (2005) Mutations of tubulin glycylation sites reveal cross-talk between the C termini of alpha- and beta-tubulin and affect the ciliary matrix in Tetrahymena. J Biol Chem 280: 596-606.
    • (2005) J Biol Chem , vol.280 , pp. 596-606
    • Redeker, V.1    Levilliers, N.2    Vinolo, E.3    Rossier, J.4    Jaillard, D.5    Burnette, D.6    Gaertig, J.7    Bre, M.H.8
  • 91
    • 0021964537 scopus 로고
    • Tubulin subunit carboxyl termini determine polymerization efficiency
    • Sackett DL, Bhattacharyya B and Wolff J (1985) Tubulin subunit carboxyl termini determine polymerization efficiency. J Biol Chem 260: 43-45.
    • (1985) J Biol Chem , vol.260 , pp. 43-45
    • Sackett, D.L.1    Bhattacharyya, B.2    Wolff, J.3
  • 92
    • 0037415729 scopus 로고    scopus 로고
    • A conserved tyrosine in the neck of a fungal kinesin regulates the catalytic motor core
    • Schafer F, Deluca D, Majdic U, Kirchner J, Schliwa M, Moroder L and Woehlke G (2003) A conserved tyrosine in the neck of a fungal kinesin regulates the catalytic motor core. EMBO J 22: 450-458.
    • (2003) EMBO J , vol.22 , pp. 450-458
    • Schafer, F.1    Deluca, D.2    Majdic, U.3    Kirchner, J.4    Schliwa, M.5    Moroder, L.6    Woehlke, G.7
  • 93
    • 0024597974 scopus 로고
    • Identification of globular mechanochemical heads of kinesin
    • Scholey JM, Heuser J, Yang JT and Goldstein LS (1989) Identification of globular mechanochemical heads of kinesin. Nature 338: 355-357.
    • (1989) Nature , vol.338 , pp. 355-357
    • Scholey, J.M.1    Heuser, J.2    Yang, J.T.3    Goldstein, L.S.4
  • 95
    • 0037119947 scopus 로고    scopus 로고
    • Single-molecule investigation of the interference between kinesin, tau and MAP2c
    • Seitz A, Kojima H, Oiwa K, Mandelkow EM, Song YH and Mandelkow E (2002) Single-molecule investigation of the interference between kinesin, tau and MAP2c. EMBO J 21: 4896-4905.
    • (2002) EMBO J , vol.21 , pp. 4896-4905
    • Seitz, A.1    Kojima, H.2    Oiwa, K.3    Mandelkow, E.M.4    Song, Y.H.5    Mandelkow, E.6
  • 96
    • 0038605070 scopus 로고    scopus 로고
    • The second microtubule-binding site of monomeric kid enhances the microtubule affinity
    • Shiroguchi K, Ohsugi M, Edamatsu M, Yamamoto T and Toyoshima YY (2003) The second microtubule-binding site of monomeric kid enhances the microtubule affinity. J Biol Chem 278: 22460-22465.
    • (2003) J Biol Chem , vol.278 , pp. 22460-22465
    • Shiroguchi, K.1    Ohsugi, M.2    Edamatsu, M.3    Yamamoto, T.4    Toyoshima, Y.Y.5
  • 98
    • 0027405349 scopus 로고
    • Recombinant kinesin motor domain binds to beta-tubulin and decorates microtubules with a B surface lattice
    • Song YH and Mandelkow E (1993) Recombinant kinesin motor domain binds to beta-tubulin and decorates microtubules with a B surface lattice. Proc Natl Acad Sci USA 90: 1671-1675.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1671-1675
    • Song, Y.H.1    Mandelkow, E.2
  • 99
    • 0035890161 scopus 로고    scopus 로고
    • Structure of a fast kinesin: Implications for ATPase mechanism and interactions with microtubules
    • Song YH, Marx A, Muller J, Woehlke G, Schliwa M, Krebs A, Hoenger A and Mandelkow E (2001) Structure of a fast kinesin: implications for ATPase mechanism and interactions with microtubules. EMBO J 20: 6213-6225.
    • (2001) EMBO J , vol.20 , pp. 6213-6225
    • Song, Y.H.1    Marx, A.2    Muller, J.3    Woehlke, G.4    Schliwa, M.5    Krebs, A.6    Hoenger, A.7    Mandelkow, E.8
  • 100
    • 0347362829 scopus 로고    scopus 로고
    • The kinesin family member BimC contains a second microtubule binding region attached to the N terminus of the motor domain
    • Stock MF, Chu J and Hackney DD (2003) The kinesin family member BimC contains a second microtubule binding region attached to the N terminus of the motor domain. J Biol Chem 278: 52315-52322.
    • (2003) J Biol Chem , vol.278 , pp. 52315-52322
    • Stock, M.F.1    Chu, J.2    Hackney, D.D.3
  • 101
    • 0011202760 scopus 로고
    • Identification of conserved isotype-defining variable region sequences for four vertebrate beta tubulin polypeptide classes
    • Sullivan KF and Cleveland DW (1986) Identification of conserved isotype-defining variable region sequences for four vertebrate beta tubulin polypeptide classes. Proc Natl Acad Sci USA 83: 4327-4331.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4327-4331
    • Sullivan, K.F.1    Cleveland, D.W.2
  • 102
    • 0027453868 scopus 로고
    • Direct observation of kinesin stepping by optical trapping interferometry
    • Svoboda K, Schmidt CF, Schnapp BJ and Block SM (1993) Direct observation of kinesin stepping by optical trapping interferometry. Nature 365: 721-727.
    • (1993) Nature , vol.365 , pp. 721-727
    • Svoboda, K.1    Schmidt, C.F.2    Schnapp, B.J.3    Block, S.M.4
  • 103
    • 0036125515 scopus 로고    scopus 로고
    • Polyglycylation domain of beta-tubulin maintains axonemal architecture and affects cytokinesis in Tetrahymena
    • Thazhath R, Liu C and Gaertig J (2002) Polyglycylation domain of beta-tubulin maintains axonemal architecture and affects cytokinesis in Tetrahymena. Nat Cell Biol 4: 256-259.
    • (2002) Nat Cell Biol , vol.4 , pp. 256-259
    • Thazhath, R.1    Liu, C.2    Gaertig, J.3
  • 104
    • 0034722373 scopus 로고    scopus 로고
    • Engineering the processive run length of the kinesin motor
    • Thorn KS, Ubersax JA and Vale RD (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
  • 105
    • 0031004776 scopus 로고    scopus 로고
    • Probing the kinesin-microtubule interaction
    • Tucker C and Goldstein LS (1997) Probing the kinesin-microtubule interaction. J Biol Chem 272: 9481-9488.
    • (1997) J Biol Chem , vol.272 , pp. 9481-9488
    • Tucker, C.1    Goldstein, L.S.2
  • 106
    • 0037459061 scopus 로고    scopus 로고
    • The molecular motor toolbox for intracellular transport
    • Vale RD (2003) The molecular motor toolbox for intracellular transport. Cell 112: 467-480.
    • (2003) Cell , vol.112 , pp. 467-480
    • Vale, R.D.1
  • 107
    • 0028021695 scopus 로고
    • Tubulin GTP hydrolysis influences the structure, mechanical properties, and kinesin-driven transport of microtubules
    • Vale RD, Coppin CM, Malik F, Kull FJ and Milligan RA (1994) Tubulin GTP hydrolysis influences the structure, mechanical properties, and kinesin-driven transport of microtubules. J Biol Chem 269: 23769-23775.
    • (1994) J Biol Chem , vol.269 , pp. 23769-23775
    • Vale, R.D.1    Coppin, C.M.2    Malik, F.3    Kull, F.J.4    Milligan, R.A.5
  • 108
    • 0029879228 scopus 로고    scopus 로고
    • Direct observation of single kinesin molecules moving along microtubules
    • Vale RD, Funatsu T, Pierce DW, Romberg L, Harada Y and Yanagida T (1996) Direct observation of single kinesin molecules moving along microtubules. Nature 380: 451-453.
    • (1996) Nature , vol.380 , pp. 451-453
    • Vale, R.D.1    Funatsu, T.2    Pierce, D.W.3    Romberg, L.4    Harada, Y.5    Yanagida, T.6
  • 109
    • 0022385727 scopus 로고
    • Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility
    • Vale RD, Reese TS and 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
  • 112
    • 0034079578 scopus 로고    scopus 로고
    • The C-terminus of tubulin increases cytoplasmic dynein and kinesin processivity
    • Wang Z and Sheetz MP (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
  • 113
    • 0025294639 scopus 로고
    • Detyrosination of alpha tubulin does not stabilize microtubules in vivo
    • Webster DR, Wehland J, Weber K and Borisy GG (1990) Detyrosination of alpha tubulin does not stabilize microtubules in vivo. J Cell Biol 111: 113-122.
    • (1990) J Cell Biol , vol.111 , pp. 113-122
    • Webster, D.R.1    Wehland, J.2    Weber, K.3    Borisy, G.G.4
  • 114
    • 0141750616 scopus 로고    scopus 로고
    • A structural analysis of the interaction between ncd tail and tubulin protofilaments
    • Wendt T, Karabay A, Krebs A, Gross H, Walker R and Hoenger A (2003) A structural analysis of the interaction between ncd tail and tubulin protofilaments. J Mol Biol 333: 541-552.
    • (2003) J Mol Biol , vol.333 , pp. 541-552
    • Wendt, T.1    Karabay, A.2    Krebs, A.3    Gross, H.4    Walker, R.5    Hoenger, A.6
  • 115
    • 0345169048 scopus 로고    scopus 로고
    • Post-translational modifications regulate microtubule function
    • Westermann S and Weber K (2003) Post-translational modifications regulate microtubule function. Nat Rev Mol Cell Biol 4: 938-947.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 938-947
    • Westermann, S.1    Weber, K.2
  • 116
    • 0035941148 scopus 로고    scopus 로고
    • A look into kinesin's powerhouse
    • Woehlke G (2001) A look into kinesin's powerhouse. FEBS Lett 508: 291-294.
    • (2001) FEBS Lett , vol.508 , pp. 291-294
    • Woehlke, G.1
  • 120
    • 0344874553 scopus 로고    scopus 로고
    • Reduction of detyrosinated microtubules and Golgi fragmentation are linked to tau-induced degeneration in astrocytes
    • Yoshiyama Y, Zhang B, Bruce J, Trojanowski JQ and Lee VM (2003) Reduction of detyrosinated microtubules and Golgi fragmentation are linked to tau-induced degeneration in astrocytes. J Neurosci 23: 10662-10671.
    • (2003) J Neurosci , vol.23 , pp. 10662-10671
    • Yoshiyama, Y.1    Zhang, B.2    Bruce, J.3    Trojanowski, J.Q.4    Lee, V.M.5


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