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Volumn 118, Issue 2, 1997, Pages 107-118

How tubulin subunits are lost from the shortening ends of microtubules

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATE; TUBULIN;

EID: 0030978807     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1997.3844     Document Type: Conference Paper
Times cited : (77)

References (62)
  • 3
    • 0028149355 scopus 로고
    • The free energy for hydrolysis of a microtubule-bound nucleotide triphosphate is near zero: All of the free energy for hydrolysis is stored in the microtubule lattice
    • Caplow M., Ruhlen R. L., Shanks J. The free energy for hydrolysis of a microtubule-bound nucleotide triphosphate is near zero: all of the free energy for hydrolysis is stored in the microtubule lattice. J. Cell Biol. 127:1994;779-788.
    • (1994) J. Cell Biol. , vol.127 , pp. 779-788
    • Caplow, M.1    Ruhlen, R.L.2    Shanks, J.3
  • 5
    • 0025058094 scopus 로고
    • Mechanism for oscillatory assembly of microtubules
    • Caplow M., Shanks J. Mechanism for oscillatory assembly of microtubules. J. Biol. Chem. 265:1990;1414-1418.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1414-1418
    • Caplow, M.1    Shanks, J.2
  • 6
    • 0029989442 scopus 로고    scopus 로고
    • Evidence that a single monolayer tubulin-GTP cap is both necessary and sufficient to stabilize microtubules
    • Caplow M., Shanks J. Evidence that a single monolayer tubulin-GTP cap is both necessary and sufficient to stabilize microtubules. Mol. Biol. Cell. 7:1996;633-675.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 633-675
    • Caplow, M.1    Shanks, J.2
  • 8
    • 0019436432 scopus 로고
    • Kinetic analysis of guanosine 5′-triphosphate hydrolysis associated with tubulin polymerization
    • Carlier M.-F., Pantaloni D. Kinetic analysis of guanosine 5′-triphosphate hydrolysis associated with tubulin polymerization. Biochemistry. 20:1981;1918-1924.
    • (1981) Biochemistry , vol.20 , pp. 1918-1924
    • Carlier, M.-F.1    Pantaloni, D.2
  • 9
    • 0023653153 scopus 로고
    • Microtubule elongation and guanosine 5′-triphosphate hydrolysis: Role of guanine nucleotides in microtubule dynamics
    • Carlier M. F., Didry D., Pantaloni D. Microtubule elongation and guanosine 5′-triphosphate hydrolysis: Role of guanine nucleotides in microtubule dynamics. Biochemistry. 26:1987;4428-4437.
    • (1987) Biochemistry , vol.26 , pp. 4428-4437
    • Carlier, M.F.1    Didry, D.2    Pantaloni, D.3
  • 10
    • 0024202112 scopus 로고
    • Real-time observations of microtubule dynamic instability in living cells
    • Cassimeris L., Pryer N. K., Salmon E. D. Real-time observations of microtubule dynamic instability in living cells. J. Cell Biol. 107:1988;2223-2231.
    • (1988) J. Cell Biol. , vol.107 , pp. 2223-2231
    • Cassimeris, L.1    Pryer, N.K.2    Salmon, E.D.3
  • 11
    • 0029041404 scopus 로고
    • Structure of growing microtubule ends: Two-dimensional sheets close into tubes at variable rates
    • Chrétien D., Fuller S. D., Karsenti E. Structure of growing microtubule ends: Two-dimensional sheets close into tubes at variable rates. J. Cell Biol. 129:1995;1311-1328.
    • (1995) J. Cell Biol. , vol.129 , pp. 1311-1328
    • Chrétien, D.1    Fuller, S.D.2    Karsenti, E.3
  • 12
    • 0026073424 scopus 로고
    • Microtubule depolymerization promotes particle and chromosome movement in vitro
    • Coué M., Lombillo V. A., McIntosh J. R. Microtubule depolymerization promotes particle and chromosome movement in vitro. J. Cell Biol. 112:1991;1165-1175.
    • (1991) J. Cell Biol. , vol.112 , pp. 1165-1175
    • Coué, M.1    Lombillo, V.A.2    McIntosh, J.R.3
  • 13
    • 0027058857 scopus 로고
    • Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau
    • Drechsel D. N., Hyman A. A., Cobb M. H., Kirschner M. W. Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Mol. Biol. Cell. 3:1992;1141-1154.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1141-1154
    • Drechsel, D.N.1    Hyman, A.A.2    Cobb, M.H.3    Kirschner, M.W.4
  • 14
    • 0028675012 scopus 로고
    • The minimum GTP cap required to stabilize microtubules
    • Drechsel D. N., Kirschner M. W. The minimum GTP cap required to stabilize microtubules. Curr. Biol. 4:1994;1053-1061.
    • (1994) Curr. Biol. , vol.4 , pp. 1053-1061
    • Drechsel, D.N.1    Kirschner, M.W.2
  • 15
    • 0016373254 scopus 로고
    • Assembly of microtubules from preformed, ring-shaped protofilaments and 6-S tubulin
    • Erickson H. Assembly of microtubules from preformed, ring-shaped protofilaments and 6-S tubulin. J. Supramol. Struct. 2:1974;393-411.
    • (1974) J. Supramol. Struct. , vol.2 , pp. 393-411
    • Erickson, H.1
  • 16
    • 0016587147 scopus 로고
    • The structure and assembly of microtubules
    • Erickson H. P. The structure and assembly of microtubules. Ann. N. Y. Acad. Sci. 253:1975;60-77.
    • (1975) Ann. N. Y. Acad. Sci. , vol.253 , pp. 60-77
    • Erickson, H.P.1
  • 18
    • 0030266954 scopus 로고    scopus 로고
    • Protofilaments and rings, two conformations of the tubulin family conserved from bacterial FtsZ to alpha/beta and gamma tubulin
    • Erickson H. P., Stoffler D. Protofilaments and rings, two conformations of the tubulin family conserved from bacterial FtsZ to alpha/beta and gamma tubulin. J. Cell Biol. 135:1996;5-8.
    • (1996) J. Cell Biol. , vol.135 , pp. 5-8
    • Erickson, H.P.1    Stoffler, D.2
  • 19
    • 0029887264 scopus 로고    scopus 로고
    • Labelling of microtubule minus ends with a phage display antibody to an N-terminal epitope of alpha tubulin
    • Fan J., Lockhart A. D., Cross R. A., Amos L. A. Labelling of microtubule minus ends with a phage display antibody to an N-terminal epitope of alpha tubulin. J. Mol. Biol. 259:1996;325-330.
    • (1996) J. Mol. Biol. , vol.259 , pp. 325-330
    • Fan, J.1    Lockhart, A.D.2    Cross, R.A.3    Amos, L.A.4
  • 21
    • 0025305348 scopus 로고
    • Re-examination of the role of nonhydrolyzable guanosine 5′-triphosphate analogues in tubulin polymerization: Reaction conditions are a critical factor for effective interactions at the exchangeable nucleotide site
    • Hamel E., Lin C. M. Re-examination of the role of nonhydrolyzable guanosine 5′-triphosphate analogues in tubulin polymerization: Reaction conditions are a critical factor for effective interactions at the exchangeable nucleotide site. Biochemistry. 29:1990;2720-2729.
    • (1990) Biochemistry , vol.29 , pp. 2720-2729
    • Hamel, E.1    Lin, C.M.2
  • 22
    • 0029114947 scopus 로고
    • Re-examination of the polarity of microtubules and sheets decorated with kinesin motor domain
    • Hirose K., Fan J., Amos L. A. Re-examination of the polarity of microtubules and sheets decorated with kinesin motor domain. J. Mol. Biol. 251:1995;329-333.
    • (1995) J. Mol. Biol. , vol.251 , pp. 329-333
    • Hirose, K.1    Fan, J.2    Amos, L.A.3
  • 23
    • 0022492523 scopus 로고
    • Visualization of the dynamic instability of individual microtubules by dark-field microscopy
    • Horio T., Hotani H. Visualization of the dynamic instability of individual microtubules by dark-field microscopy. Nature. 321:1986;605-607.
    • (1986) Nature , vol.321 , pp. 605-607
    • Horio, T.1    Hotani, H.2
  • 24
    • 0023051531 scopus 로고
    • GDP state of tubulin: Stabilization of double rings
    • Howard W. D., Timasheff S. N. GDP state of tubulin: Stabilization of double rings. Biochemistry. 25:1986;8292-8300.
    • (1986) Biochemistry , vol.25 , pp. 8292-8300
    • Howard, W.D.1    Timasheff, S.N.2
  • 25
    • 0028887848 scopus 로고
    • Structural changes accompanying GTP hydrolysis in microtubules: Information from a slowly hydrolyzable analogue guanylyl-(alpha, beta)-methylene-diphosphonate
    • Hyman A. A., Chrétien D., Arnal I., Wade R. H. Structural changes accompanying GTP hydrolysis in microtubules: Information from a slowly hydrolyzable analogue guanylyl-(alpha, beta)-methylene-diphosphonate. J. Cell Biol. 128:1995;117-125.
    • (1995) J. Cell Biol. , vol.128 , pp. 117-125
    • Hyman, A.A.1    Chrétien, D.2    Arnal, I.3    Wade, R.H.4
  • 26
    • 0030059247 scopus 로고    scopus 로고
    • Morphogenetic properties of microtubules and mitotic spindle assembly
    • Hyman A. A., Karsenti E. Morphogenetic properties of microtubules and mitotic spindle assembly. Cell. 84:1996;401-410.
    • (1996) Cell , vol.84 , pp. 401-410
    • Hyman, A.A.1    Karsenti, E.2
  • 27
    • 0027075124 scopus 로고
    • Role of GTP hydrolysis in microtubule dynamics: Information from a slowly hydrolyzable analogue, GMPCPP
    • Hyman A. A., Salser S., Drechsel D. N., Unwin N., Mitchison T. J. Role of GTP hydrolysis in microtubule dynamics: Information from a slowly hydrolyzable analogue, GMPCPP. Mol. Biol. Cell. 3:1992;1155-1167.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1155-1167
    • Hyman, A.A.1    Salser, S.2    Drechsel, D.N.3    Unwin, N.4    Mitchison, T.J.5
  • 28
    • 0028787230 scopus 로고
    • Force generation by microtubule assembly/disassembly in mitosis and related movements
    • Inoué S., Salmon E. D. Force generation by microtubule assembly/disassembly in mitosis and related movements. Mol. Biol. Cell. 6:1995;1619-1640.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1619-1640
    • Inoué, S.1    Salmon, E.D.2
  • 29
    • 0016196938 scopus 로고
    • Microtubules from mammalian brain: Some properties of their depolymerization products and a proposed mechanism of assembly and disassembly
    • Kirschner M., Williams R., Weingarten M., Gerhart J. Microtubules from mammalian brain: Some properties of their depolymerization products and a proposed mechanism of assembly and disassembly. Proc. Natl. Acad. Sci. USA. 71:1974;1159-1163.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 1159-1163
    • Kirschner, M.1    Williams, R.2    Weingarten, M.3    Gerhart, J.4
  • 30
    • 0016750357 scopus 로고
    • Quantitative electron microscopy of microtubule assembly in vitro
    • Kirschner M. W., Honig L. S., Williams R. C. Quantitative electron microscopy of microtubule assembly in vitro. J. Mol. Biol. 99:1975a;263-276.
    • (1975) J. Mol. Biol. , vol.99 , pp. 263-276
    • Kirschner, M.W.1    Honig, L.S.2    Williams, R.C.3
  • 32
    • 0023837441 scopus 로고
    • Polewards chromosome movement driven by microtubule depolymerization in vitro
    • Koshland D. E., Mitchison T. J., Kirschner M. W. Polewards chromosome movement driven by microtubule depolymerization in vitro. Nature. 331:1988;499-504.
    • (1988) Nature , vol.331 , pp. 499-504
    • Koshland, D.E.1    Mitchison, T.J.2    Kirschner, M.W.3
  • 33
    • 0028977966 scopus 로고
    • Minus-end-directed motion of kinesin-coated microspheres driven by microtubule depolymerization
    • Lombillo V. A., Stewart R. J., McIntosh J. R. Minus-end-directed motion of kinesin-coated microspheres driven by microtubule depolymerization. Nature. 373:1995;161-164.
    • (1995) Nature , vol.373 , pp. 161-164
    • Lombillo, V.A.1    Stewart, R.J.2    McIntosh, J.R.3
  • 34
    • 0022178476 scopus 로고
    • Tubulin domains probed by limited proteolysis and subunit-specific antibodies
    • Mandelkow E.-M., Herrmann M., Ruhl U. Tubulin domains probed by limited proteolysis and subunit-specific antibodies. J. Mol. Biol. 185:1985;311-327.
    • (1985) J. Mol. Biol. , vol.185 , pp. 311-327
    • Mandelkow, E.-M.1    Herrmann, M.2    Ruhl, U.3
  • 36
    • 0025868445 scopus 로고
    • Microtubule dynamics and microtubule caps: A time-resolved cryo-electron microscopy study
    • Mandelkow E. M., Mandelkow E., Milligan R. A. Microtubule dynamics and microtubule caps: A time-resolved cryo-electron microscopy study. J. Cell Biol. 114:1991;977-991.
    • (1991) J. Cell Biol. , vol.114 , pp. 977-991
    • Mandelkow, E.M.1    Mandelkow, E.2    Milligan, R.A.3
  • 37
    • 0025060807 scopus 로고
    • GTP analogues interact with the tubulin exchangeable site during assembly and upon binding
    • Mejillano M. R., Barton J. S., Nath J. P., Himes R. H. GTP analogues interact with the tubulin exchangeable site during assembly and upon binding. Biochemistry. 29:1990;1208-1216.
    • (1990) Biochemistry , vol.29 , pp. 1208-1216
    • Mejillano, M.R.1    Barton, J.S.2    Nath, J.P.3    Himes, R.H.4
  • 38
    • 0024425928 scopus 로고
    • Cold depolymerization of microtubules to double rings: Geometric stabilization of assemblies
    • Melki R., Carlier M.-F., Pantaloni D., Timasheff S. N. Cold depolymerization of microtubules to double rings: Geometric stabilization of assemblies. Biochemistry. 28:1989;9143-9152.
    • (1989) Biochemistry , vol.28 , pp. 9143-9152
    • Melki, R.1    Carlier, M.-F.2    Pantaloni, D.3    Timasheff, S.N.4
  • 39
    • 0025146397 scopus 로고
    • Direct evidence for GTP and GDP-Pi intermediates in microtubule assembly
    • Melki R., Carlier M. F., Pantaloni D. Direct evidence for GTP and GDP-Pi intermediates in microtubule assembly. Biochemistry. 29:1990;8921-8932.
    • (1990) Biochemistry , vol.29 , pp. 8921-8932
    • Melki, R.1    Carlier, M.F.2    Pantaloni, D.3
  • 40
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison T., Kirschner M. Dynamic instability of microtubule growth. Nature. 312:1984;237-242.
    • (1984) Nature , vol.312 , pp. 237-242
    • Mitchison, T.1    Kirschner, M.2
  • 41
    • 0027527453 scopus 로고
    • Localization of an exchangeable GTP binding site at the plus end of microtubules
    • Mitchison T. J. Localization of an exchangeable GTP binding site at the plus end of microtubules. Science. 261:1993;1044-1047.
    • (1993) Science , vol.261 , pp. 1044-1047
    • Mitchison, T.J.1
  • 44
    • 0025366035 scopus 로고
    • Effects of magnesium on the dynamic instability of individual microtubules
    • O'Brien E. T., Salmon E. D., Walker R. A., Erickson H. P. Effects of magnesium on the dynamic instability of individual microtubules. Biochemistry. 29:1990;6648-6656.
    • (1990) Biochemistry , vol.29 , pp. 6648-6656
    • O'Brien, E.T.1    Salmon, E.D.2    Walker, R.A.3    Erickson, H.P.4
  • 45
    • 0028866192 scopus 로고
    • Force production by depolymerizing microtubules: Load-velocity curves and run-pause statistics
    • Peskin C. S., Oster G. F. Force production by depolymerizing microtubules: Load-velocity curves and run-pause statistics. Biophys. J. 69:1995;2268-2276.
    • (1995) Biophys. J. , vol.69 , pp. 2268-2276
    • Peskin, C.S.1    Oster, G.F.2
  • 46
    • 0027048607 scopus 로고
    • Brain microtubule-associated proteins modulate microtubule dynamic instability in vitro: Real-time observations using video microscopy
    • Pryer N. K., Walker R. A., Skeen V. P., Bourns B. D., Soboeiro M. F., Salmon E. D. Brain microtubule-associated proteins modulate microtubule dynamic instability in vitro: Real-time observations using video microscopy. J. Cell Sci. 103:1992;965-976.
    • (1992) J. Cell Sci. , vol.103 , pp. 965-976
    • Pryer, N.K.1    Walker, R.A.2    Skeen, V.P.3    Bourns, B.D.4    Soboeiro, M.F.5    Salmon, E.D.6
  • 47
    • 0028923255 scopus 로고
    • VE-DIC light microscopy and the discovery of kinesin
    • Salmon E. D. VE-DIC light microscopy and the discovery of kinesin. Trends Cell Biol. 5:1995;154-158.
    • (1995) Trends Cell Biol. , vol.5 , pp. 154-158
    • Salmon, E.D.1
  • 48
    • 0024406226 scopus 로고
    • Video-enhanced differential interference contrast light microscopy
    • Salmon E. D., Walker R. A., Pryer N. K. Video-enhanced differential interference contrast light microscopy. BioTechniques. 7:1989;624-633.
    • (1989) BioTechniques , vol.7 , pp. 624-633
    • Salmon, E.D.1    Walker, R.A.2    Pryer, N.K.3
  • 49
    • 0023885426 scopus 로고
    • Direct observation of microtubule dynamics in living cells
    • Sammak P. J., Borisy G. G. Direct observation of microtubule dynamics in living cells. Nature. 332:1988;724-726.
    • (1988) Nature , vol.332 , pp. 724-726
    • Sammak, P.J.1    Borisy, G.G.2
  • 50
    • 0022959708 scopus 로고
    • Viewing single microtubules by video light microscopy
    • Schnapp B. J. Viewing single microtubules by video light microscopy. Methods Enzymol. 134:1986;561-573.
    • (1986) Methods Enzymol. , vol.134 , pp. 561-573
    • Schnapp, B.J.1
  • 51
    • 0023788884 scopus 로고
    • New features of microtubule behavior observed in vivo
    • Schulze E., Kirschner M. New features of microtubule behavior observed in vivo. Nature. 334:1988;356-359.
    • (1988) Nature , vol.334 , pp. 356-359
    • Schulze, E.1    Kirschner, M.2
  • 52
    • 0026630495 scopus 로고
    • Linkage between ligand binding and control of tubulin conformation
    • Shearwin K. E., Timasheff S. N. Linkage between ligand binding and control of tubulin conformation. Biochemistry. 31:1992;8080-8089.
    • (1992) Biochemistry , vol.31 , pp. 8080-8089
    • Shearwin, K.E.1    Timasheff, S.N.2
  • 53
    • 0011918776 scopus 로고
    • Microtubules and tubulin sheet polymers elongate from isolated axonemes in vitro as observed by negative-stain electron microscopy
    • Simon J. R., Adam N. A., Salmon E. D. Microtubules and tubulin sheet polymers elongate from isolated axonemes in vitro as observed by negative-stain electron microscopy. Micron Microsc. Acta. 22:1991;405-412.
    • (1991) Micron Microsc. Acta , vol.22 , pp. 405-412
    • Simon, J.R.1    Adam, N.A.2    Salmon, E.D.3
  • 54
    • 0025034523 scopus 로고
    • The structure of microtubule ends during the elongation and shortening phases of dynamic instability examined by negative-stain electron microscopy
    • Simon J. R., Salmon E. D. The structure of microtubule ends during the elongation and shortening phases of dynamic instability examined by negative-stain electron microscopy. J. Cell Sci. 96:1990;571-582.
    • (1990) J. Cell Sci. , vol.96 , pp. 571-582
    • Simon, J.R.1    Salmon, E.D.2
  • 56
    • 0025340139 scopus 로고
    • Role of GTP hydrolysis in microtubule polymerization: Evidence for a coupled hydrolysis mechanism
    • Stewart R. J., Farrell K. W., Wilson L. Role of GTP hydrolysis in microtubule polymerization: Evidence for a coupled hydrolysis mechanism. Biochemistry. 29:1990;6489-6498.
    • (1990) Biochemistry , vol.29 , pp. 6489-6498
    • Stewart, R.J.1    Farrell, K.W.2    Wilson, L.3
  • 57
    • 0021258393 scopus 로고
    • The kinetics of microtubule assembly: Evidence for a two-stage nucleation mechanism
    • Voter W. A., Erickson H. P. The kinetics of microtubule assembly: Evidence for a two-stage nucleation mechanism. J. Bio. Chem. 259:1984;10430-10438.
    • (1984) J. Bio. Chem. , vol.259 , pp. 10430-10438
    • Voter, W.A.1    Erickson, H.P.2
  • 58
    • 0026008120 scopus 로고
    • Dilution-induced disassembly of microtubules: Relation to dynamic instability and the GTP cap
    • Voter W. A., O'Brien E. T., Erickson H. P. Dilution-induced disassembly of microtubules: relation to dynamic instability and the GTP cap. Cell Motil. Cytoskel. 18:1991;55-62.
    • (1991) Cell Motil. Cytoskel. , vol.18 , pp. 55-62
    • Voter, W.A.1    O'Brien, E.T.2    Erickson, H.P.3
  • 59
    • 0024094432 scopus 로고
    • Dynamic instability of individual microtubules analyzed by video light microscopy: Rate constants and transition frequencies
    • Walker R. A., O'Brien E. T., Pryer N. K., Soboeiro M. F., Voter W. A., Erickson H. P., Salmon E. D. Dynamic instability of individual microtubules analyzed by video light microscopy: Rate constants and transition frequencies. J. Cell Biol. 107:1988;1437-1448.
    • (1988) J. Cell Biol. , vol.107 , pp. 1437-1448
    • Walker, R.A.1    O'Brien, E.T.2    Pryer, N.K.3    Soboeiro, M.F.4    Voter, W.A.5    Erickson, H.P.6    Salmon, E.D.7
  • 60
    • 0025946396 scopus 로고
    • Dilution of individual microtubules observed in real time in vitro: Evidence that cap size is small and independent of elongation rate
    • Walker R. A., Pryer N. K., Salmon E. D. Dilution of individual microtubules observed in real time in vitro: Evidence that cap size is small and independent of elongation rate. J. Cell Biol. 114:1991;73-81.
    • (1991) J. Cell Biol. , vol.114 , pp. 73-81
    • Walker, R.A.1    Pryer, N.K.2    Salmon, E.D.3
  • 61
    • 0024544706 scopus 로고
    • Asymmetric behavior of severed microtubule ends after ultra-violet microbeam irradiation of individual microtubule in vitro
    • Walker R. A., Inoue S., Salmon E. D. Asymmetric behavior of severed microtubule ends after ultra-violet microbeam irradiation of individual microtubule in vitro. J. Cell Biol. 108:1989;931-937.
    • (1989) J. Cell Biol. , vol.108 , pp. 931-937
    • Walker, R.A.1    Inoue, S.2    Salmon, E.D.3
  • 62
    • 0029128472 scopus 로고
    • Membrane/microtubule tip attachment complexes (TACs) allow the assembly dynamics of plus ends to push and pull membranes into tubulovesicular networks in interphase Xenopus egg extracts
    • Waterman-Storer C. M., Gregory J., Parsons S. F., Salmon E. D. Membrane/microtubule tip attachment complexes (TACs) allow the assembly dynamics of plus ends to push and pull membranes into tubulovesicular networks in interphase Xenopus egg extracts. J. Cell Biol. 130:1995;1161-1169.
    • (1995) J. Cell Biol. , vol.130 , pp. 1161-1169
    • Waterman-Storer, C.M.1    Gregory, J.2    Parsons, S.F.3    Salmon, E.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.