메뉴 건너뛰기




Volumn 36, Issue 2, 1997, Pages 125-135

How calcium causes microtubule depolymerization

Author keywords

calcium; catastrophe; dynamic instability; GTP cap; GTP hydrolysis; microtubules

Indexed keywords

CALCIUM ION; GUANOSINE TRIPHOSPHATE;

EID: 0031041436     PISSN: 08861544     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0169(1997)36:2<125::AID-CM3>3.0.CO;2-8     Document Type: Article
Times cited : (126)

References (67)
  • 2
    • 0002445059 scopus 로고
    • Microtubule dynamics in vitro
    • Hyams, J.S., and Lloyd C.W. (eds.). New York, Wiley-Liss
    • Bayley, P.M., Sharma, K.K., and Martin, S.R. (1994): Microtubule dynamics in vitro. In Hyams, J.S., and Lloyd C.W. (eds.): "Microtubules." New York, Wiley-Liss, pp. 111-137.
    • (1994) Microtubules , pp. 111-137
    • Bayley, P.M.1    Sharma, K.K.2    Martin, S.R.3
  • 3
    • 0025109181 scopus 로고
    • Real-time visualization of cell cycle-dependent changes in microtubule dynamics in cytoplasmic extracts
    • Belmont, L.D., Hyman, A.A., Sawin, K.E., and Mitchison, T.J. (1990): Real-time visualization of cell cycle-dependent changes in microtubule dynamics in cytoplasmic extracts. Cell 62:579-589.
    • (1990) Cell , vol.62 , pp. 579-589
    • Belmont, L.D.1    Hyman, A.A.2    Sawin, K.E.3    Mitchison, T.J.4
  • 4
    • 0022557176 scopus 로고
    • The calcium sensitivity of MAP-2 and tau microtubules in the presence of calmodulin
    • Bender, P.K., and Rebhun, L.I. (1986): The calcium sensitivity of MAP-2 and tau microtubules in the presence of calmodulin. Ann. NY Acad. Sci. 466:392-409.
    • (1986) Ann. NY Acad. Sci. , vol.466 , pp. 392-409
    • Bender, P.K.1    Rebhun, L.I.2
  • 5
    • 0021723473 scopus 로고
    • A miniature flow cell designed for rapid exchange of media under high-power microscope objectives
    • Berg, H.C., and Block, S.M. (1984): A miniature flow cell designed for rapid exchange of media under high-power microscope objectives. J. Gen. Microbiol. 130:2915-2920.
    • (1984) J. Gen. Microbiol. , vol.130 , pp. 2915-2920
    • Berg, H.C.1    Block, S.M.2
  • 6
    • 0019857119 scopus 로고
    • Intrinsic calcium sensitivity of tubulin polymerization
    • Berkowitz, S.A., and Wolff, J. (1981): Intrinsic calcium sensitivity of tubulin polymerization. J. Biol. Chem. 256:11216-11223.
    • (1981) J. Biol. Chem. , vol.256 , pp. 11216-11223
    • Berkowitz, S.A.1    Wolff, J.2
  • 7
    • 0015528930 scopus 로고
    • Nucleated assembly of microtubules in porcine brain extracts
    • Borisy, G.G., and Olmsted, J.B. (1972): Nucleated assembly of microtubules in porcine brain extracts. Science 177:1196-1197.
    • (1972) Science , vol.177 , pp. 1196-1197
    • Borisy, G.G.1    Olmsted, J.B.2
  • 8
    • 0026812627 scopus 로고
    • Microtubule dynamics
    • Caplow, M. (1992): Microtubule dynamics. [Review] Curr. Opin. Cell. Biol. 4:58-65.
    • (1992) Curr. Opin. Cell. Biol. , vol.4 , pp. 58-65
    • Caplow, M.1
  • 9
    • 0029989442 scopus 로고    scopus 로고
    • Evidence that a single monolayer tubulin-GTP cap is both necessary and sufficient to stabilize microtubules
    • Caplow, M., and Shanks J. (1996): Evidence that a single monolayer tubulin-GTP cap is both necessary and sufficient to stabilize microtubules. Mol. Biol. Cell. 7:663-675.
    • (1996) Mol. Biol. Cell. , vol.7 , pp. 663-675
    • Caplow, M.1    Shanks, J.2
  • 10
    • 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., and Shanks, J. (1994): 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. 127:779-88.
    • (1994) J. Cell Biol. , vol.127 , pp. 779-788
    • Caplow, M.1    Ruhlen, R.L.2    Shanks, J.3
  • 11
    • 0027372852 scopus 로고
    • Regulation of microtubule dynamic instability
    • Cassimeris, L. (1993): Regulation of microtubule dynamic instability. Cell Motil. Cytoskeleton. 26:275-81.
    • (1993) Cell Motil. Cytoskeleton. , vol.26 , pp. 275-281
    • Cassimeris, L.1
  • 12
    • 0028924141 scopus 로고
    • Modulation of microtubule dynamic instability in vivo by brain microtubule associated proteins
    • Dhamodharan, R., and Wadsworth, P. (1995): Modulation of microtubule dynamic instability in vivo by brain microtubule associated proteins. J. Cell Sci. 108:1679-89.
    • (1995) J. Cell Sci. , vol.108 , pp. 1679-1689
    • Dhamodharan, R.1    Wadsworth, P.2
  • 13
    • 0028291130 scopus 로고
    • Solution structure of GDP-tubulin double rings to 3 nm resolution and comparison with microtubules
    • Diaz, J.F., Pantos, E., Bordas, J., and Andreu, J.M. (1994): Solution structure of GDP-tubulin double rings to 3 nm resolution and comparison with microtubules. J. Mol. Biol. 238:214-225.
    • (1994) J. Mol. Biol. , vol.238 , pp. 214-225
    • Diaz, J.F.1    Pantos, E.2    Bordas, J.3    Andreu, J.M.4
  • 14
    • 0028675012 scopus 로고
    • The minimum GTP cap required to stabilize microtubules
    • Drechsel, D.N., and Kirschner, M.W. (1994): The minimum GTP cap required to stabilize microtubules. Curr. Biol. 4:1053-1061.
    • (1994) Curr. Biol. , vol.4 , pp. 1053-1061
    • Drechsel, D.N.1    Kirschner, M.W.2
  • 15
    • 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., and Kirschner, M.W. (1992): Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Mol. Biol. Cell. 3:1141-54.
    • (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
  • 17
    • 0026555596 scopus 로고
    • Intracellular pH modulates cytosolic free magnesium in cultured chicken heart cells
    • Freudenrich, C.C., Murphy, E., Levy, L.A., London, R.E., and Lieberman, M. (1992): Intracellular pH modulates cytosolic free magnesium in cultured chicken heart cells. Am. J. Physiol. 262:C1024-1030.
    • (1992) Am. J. Physiol. , vol.262
    • Freudenrich, C.C.1    Murphy, E.2    Levy, L.A.3    London, R.E.4    Lieberman, M.5
  • 18
    • 0016792383 scopus 로고
    • Magnesium-induced self-association of calf brain tubulin. I. Stoichiometry
    • Frigon, R.P., and Timasheff, S.N. (1975): Magnesium-induced self-association of calf brain tubulin. I. Stoichiometry. Biochemistry 14:4559-4566.
    • (1975) Biochemistry , vol.14 , pp. 4559-4566
    • Frigon, R.P.1    Timasheff, S.N.2
  • 19
    • 0023710729 scopus 로고
    • Fast disassembly of microtubules induced by Mg2+ or Ca2+
    • Gal, V., Martin, S., and Bayley, P. (1988): Fast disassembly of microtubules induced by Mg2+ or Ca2+. Biochem. Biophys. Res. Commun. 155:1464-1470.
    • (1988) Biochem. Biophys. Res. Commun. , vol.155 , pp. 1464-1470
    • Gal, V.1    Martin, S.2    Bayley, P.3
  • 20
    • 0027385963 scopus 로고
    • How the transition frequencies of microtubule dynamic instability (nucleation, catastrophe and rescue) regulate microtubule dynamics in interphase and mitosis: Analysis using a Monte Carlo computer simulation
    • Gliksman, N.R., Skibbens, R.V., and Salmon, E.D. (1993): How the transition frequencies of microtubule dynamic instability (nucleation, catastrophe and rescue) regulate microtubule dynamics in interphase and mitosis: Analysis using a Monte Carlo computer simulation. Mol. Biol. Cell 4:1035-1050.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1035-1050
    • Gliksman, N.R.1    Skibbens, R.V.2    Salmon, E.D.3
  • 21
    • 0027093095 scopus 로고
    • Calcium and mitosis
    • Hepler, P.K. (1992): Calcium and mitosis. Int. Rev. Cyt. 138:239-268.
    • (1992) Int. Rev. Cyt. , vol.138 , pp. 239-268
    • Hepler, P.K.1
  • 22
    • 0022370234 scopus 로고
    • Generation of microtubule stability subclasses by microtubule-associated proteins: Implications for the microtubule "dynamic instability" model
    • Job, D., Pabion, M., and Margolis, R.L. (1985): Generation of microtubule stability subclasses by microtubule-associated proteins: Implications for the microtubule "dynamic instability" model. J. Cell Biol. 101:1680-1689.
    • (1985) J. Cell Biol. , vol.101 , pp. 1680-1689
    • Job, D.1    Pabion, M.2    Margolis, R.L.3
  • 23
    • 0016196938 scopus 로고
    • Microtubules from mammalian brain: Some properties of their depolymerization products and a proposed mechanism of assembly and disassembly
    • Kirschner, M.W., Williams, R.C., Weingarten, M., and Gerhart, J.C. (1974): Microtubules from mammalian brain: Some properties of their depolymerization products and a proposed mechanism of assembly and disassembly. Proc. Natl. Acad. Sci. USA 71:1159-63.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 1159-1163
    • Kirschner, M.W.1    Williams, R.C.2    Weingarten, M.3    Gerhart, J.C.4
  • 24
    • 0027285334 scopus 로고
    • Microtubule-associated protein 2 alters the dynamic properties of microtubule assembly and disassembly
    • Kowalski, R.J., and Williams, R.C., Jr. (1993): Microtubule-associated protein 2 alters the dynamic properties of microtubule assembly and disassembly. J. Biol. Chem. 268:9847-9855.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9847-9855
    • Kowalski, R.J.1    Williams Jr., R.C.2
  • 25
    • 0024298964 scopus 로고
    • How do enzymes work?
    • Kraut, J. (1988): How do enzymes work? Science 242:533-540.
    • (1988) Science , vol.242 , pp. 533-540
    • Kraut, J.1
  • 26
    • 0016154686 scopus 로고
    • Viscometric demonstration of tubulin polymerization
    • Tokyo
    • Kuriyama, R., and Sakai, H. (1974): Viscometric demonstration of tubulin polymerization. J. Biochem. (Tokyo) 75:463-471.
    • (1974) J. Biochem. , vol.75 , pp. 463-471
    • Kuriyama, R.1    Sakai, H.2
  • 27
    • 0028822031 scopus 로고
    • Microtubule-associated proteins and the flexibility of microtubules
    • Kurz, J.C., and Williams, R.C., Jr. (1995): Microtubule-associated proteins and the flexibility of microtubules. Biochemistry 34:13374-80.
    • (1995) Biochemistry , vol.34 , pp. 13374-13380
    • Kurz, J.C.1    Williams Jr., R.C.2
  • 28
    • 0027419444 scopus 로고
    • Specific responses of axons and dendrites to cytoskeleton perturbations: An in vitro study
    • Lafont, F., Rouget, M., Rousselet, A., Valenza, C., and Prochiantz A. (1993): Specific responses of axons and dendrites to cytoskeleton perturbations: An in vitro study. J. Cell. Sci. 104:433-443.
    • (1993) J. Cell. Sci. , vol.104 , pp. 433-443
    • Lafont, F.1    Rouget, M.2    Rousselet, A.3    Valenza, C.4    Prochiantz, A.5
  • 29
    • 0017334810 scopus 로고
    • In vitro reconstitution of calf brain microtubules: Effects of solution variables
    • Lee, J.C., and Timasheff, S.N. (1977): In vitro reconstitution of calf brain microtubules: Effects of solution variables. Biochemistry 16:1754-1764.
    • (1977) Biochemistry , vol.16 , pp. 1754-1764
    • Lee, J.C.1    Timasheff, S.N.2
  • 30
    • 0028558494 scopus 로고
    • Regulation of growth cone motility by substratum bound molecules and cytoplasmic [Ca2+]
    • Letourneau, P.C., Snow, D.M., and Gomez, T.M. (1994): Regulation of growth cone motility by substratum bound molecules and cytoplasmic [Ca2+]. Prog. Brain Res. 103:85-98.
    • (1994) Prog. Brain Res. , vol.103 , pp. 85-98
    • Letourneau, P.C.1    Snow, D.M.2    Gomez, T.M.3
  • 31
    • 0027467864 scopus 로고
    • Regulation of the cell cycle by calcium and calmodulin
    • Lu, K.P., and Means, A.R. (1993): Regulation of the cell cycle by calcium and calmodulin. Endocrine Rev. 14:40-58.
    • (1993) Endocrine Rev. , vol.14 , pp. 40-58
    • Lu, K.P.1    Means, A.R.2
  • 32
    • 0025868445 scopus 로고
    • Microtubule dynamics and microtubule caps: A time-resolved cryoelectron microscopy study
    • Mandelkow, E.M., Mandelkow, E., and Milligan, R.A. (1991): Microtubule dynamics and microtubule caps: A time-resolved cryoelectron microscopy study. J. Cell Biol. 114:977-991.
    • (1991) J. Cell Biol. , vol.114 , pp. 977-991
    • Mandelkow, E.M.1    Mandelkow, E.2    Milligan, R.A.3
  • 33
    • 0025122019 scopus 로고
    • Transient increases in cytosolic free calcium appear to be required for the migration of adherent human neutrophils
    • Marks, P.W., and Maxfield, F.R. (1990): Transient increases in cytosolic free calcium appear to be required for the migration of adherent human neutrophils. J. Cell Biol. 110:43-52.
    • (1990) J. Cell Biol. , vol.110 , pp. 43-52
    • Marks, P.W.1    Maxfield, F.R.2
  • 34
    • 0027424297 scopus 로고
    • Identification of katanin, an ATPase that severs and disassembles stable microtubules
    • McNally, F.J., and Vale, R.D. (1993): Identification of katanin, an ATPase that severs and disassembles stable microtubules. Cell 75:419-429.
    • (1993) Cell , vol.75 , pp. 419-429
    • McNally, F.J.1    Vale, R.D.2
  • 35
    • 0024425928 scopus 로고
    • Cold depolymerization of microtubules to double rings: Geometric stabilization of assemblies
    • Melki, R., Carlier, M.-F., Pantaloni, D., and Timasheff, S.N. (1989): Cold depolymerization of microtubules to double rings: Geometric stabilization of assemblies. Biochemistry 28:9143-9152.
    • (1989) Biochemistry , vol.28 , pp. 9143-9152
    • Melki, R.1    Carlier, M.-F.2    Pantaloni, D.3    Timasheff, S.N.4
  • 36
    • 0025146397 scopus 로고
    • Direct evidence for GTP and GDP-Pi intermediates in microtubule assembly
    • Melki, R., Carlier, M.F. and Pantaloni, D. (1990): Direct evidence for GTP and GDP-Pi intermediates in microtubule assembly. Biochemistry 29:8921-8932.
    • (1990) Biochemistry , vol.29 , pp. 8921-8932
    • Melki, R.1    Carlier, M.F.2    Pantaloni, D.3
  • 37
    • 0029153356 scopus 로고
    • Rigidity of microtubules is increased by stabilizing agents
    • Mickey, B., and Howard, J. (1995): Rigidity of microtubules is increased by stabilizing agents. J. Cell Biol. 130:909-917.
    • (1995) J. Cell Biol. , vol.130 , pp. 909-917
    • Mickey, B.1    Howard, J.2
  • 38
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison, T. and Kirschner, M. (1984): Dynamic instability of microtubule growth. Nature 312:237-242.
    • (1984) Nature , vol.312 , pp. 237-242
    • Mitchison, T.1    Kirschner, M.2
  • 39
    • 0017763702 scopus 로고
    • Calcium-sensitivity of the microtubule reassembly system. Difference between crude brain extract and purified microtubular proteins
    • Tokyo
    • Nishida, E., and Sakai, H. (1977): Calcium-sensitivity of the microtubule reassembly system. Difference between crude brain extract and purified microtubular proteins. J. Biochem. (Tokyo) 82:303-306.
    • (1977) J. Biochem. , vol.82 , pp. 303-306
    • Nishida, E.1    Sakai, H.2
  • 40
    • 0023668240 scopus 로고
    • GTP hydrolysis during microtubule assembly
    • O'Brien, E.T., Voter, W.A., and Erickson, H.P. (1987): GTP hydrolysis during microtubule assembly. Biochemistry 26:4148-4156.
    • (1987) Biochemistry , vol.26 , pp. 4148-4156
    • O'Brien, E.T.1    Voter, W.A.2    Erickson, H.P.3
  • 41
    • 0025366035 scopus 로고
    • Effects of magnesium on the dynamic instability of individual microtubules
    • O'Brien, E.T., Salmon, E.D., Walker, R.W., and Erickson, H.P. (1990): Effects of magnesium on the dynamic instability of individual microtubules. Biochemistry 29:6648-6656.
    • (1990) Biochemistry , vol.29 , pp. 6648-6656
    • O'Brien, E.T.1    Salmon, E.D.2    Walker, R.W.3    Erickson, H.P.4
  • 42
    • 0015818589 scopus 로고
    • Characterization of microtubule assembly in porcine brain extracts by viscometry
    • Olmsted, J.B., and Borisy, G.G. (1973): Characterization of microtubule assembly in porcine brain extracts by viscometry. Biochemistry 12:4282-4289.
    • (1973) Biochemistry , vol.12 , pp. 4282-4289
    • Olmsted, J.B.1    Borisy, G.G.2
  • 43
    • 0016813649 scopus 로고
    • Ionic and nucleotide requirements for microtubule polymerization in vitro
    • Olmsted, J.B., and Borisy, G.G. (1975): Ionic and nucleotide requirements for microtubule polymerization in vitro. Biochemistry 4:2996-3005.
    • (1975) Biochemistry , vol.4 , pp. 2996-3005
    • Olmsted, J.B.1    Borisy, G.G.2
  • 44
    • 0021840109 scopus 로고
    • Changes of free calcium levels with stages of the cell cycle
    • Poenie, M., Alderton, J., Tsien, R.Y., and Steinhardt, R. (1985): Changes of free calcium levels with stages of the cell cycle. Nature 315:147-149.
    • (1985) Nature , vol.315 , pp. 147-149
    • Poenie, M.1    Alderton, J.2    Tsien, R.Y.3    Steinhardt, R.4
  • 45
    • 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., and Salmon, E.D. (1992): Brain microtubule-associated proteins modulate microtubule dynamic instability in vitro. Real-time observations using video microscopy. J. Cell Sci. 103:965-976.
    • (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
  • 46
    • 0025930735 scopus 로고
    • Microtubule polymer assembly and transport during axonal elongation
    • Reinsch, S.S., Mitchison, T.J., and Kirschner M. (1991): Microtubule polymer assembly and transport during axonal elongation. J. Cell Biol. 115:365-367.
    • (1991) J. Cell Biol. , vol.115 , pp. 365-367
    • Reinsch, S.S.1    Mitchison, T.J.2    Kirschner, M.3
  • 47
    • 0010466626 scopus 로고
    • Free calcium increases explosively in activating medaka eggs
    • Ridgway, E.B., Gilkey, J.C., and Jaffe, L.F. (1977): Free calcium increases explosively in activating medaka eggs. Proc. Natl. Acad. Sci. USA 74:623-627.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 623-627
    • Ridgway, E.B.1    Gilkey, J.C.2    Jaffe, L.F.3
  • 48
    • 0002430201 scopus 로고
    • ++ ion concentration by metal chelators
    • A. Schwartz, (ed.). Plenum Pub. Corp.
    • ++ ion concentration by metal chelators. In A. Schwartz, (ed.): Methods in Pharmacology 5. Plenum Pub. Corp. pp. 63-75.
    • (1984) Methods in Pharmacology , vol.5 , pp. 63-75
    • Robertson, S.1    Potter, J.D.2
  • 49
    • 0023131037 scopus 로고
    • Microtubule dynamics in vivo: A test of mechanisms of turnover
    • Sammak, P.J., Gorbsky, G.J., and Borisy, G.G. (1987): Microtubule dynamics in vivo: A test of mechanisms of turnover. J. Cell Biol. 104:395-405.
    • (1987) J. Cell Biol. , vol.104 , pp. 395-405
    • Sammak, P.J.1    Gorbsky, G.J.2    Borisy, G.G.3
  • 51
    • 0021929016 scopus 로고
    • Cytosolic free calcium-ion concentration in cleaving embryonic cells of Oryzias latipes measured with calcium-selective microelectrodes
    • Schantz, A.R. (1985): Cytosolic free calcium-ion concentration in cleaving embryonic cells of Oryzias latipes measured with calcium-selective microelectrodes. J. Cell Biol. 100:947-54.
    • (1985) J. Cell Biol. , vol.100 , pp. 947-954
    • Schantz, A.R.1
  • 52
    • 0026630495 scopus 로고
    • Linkage between ligand binding and control of tubulin conformation
    • Shearwin, K.E., and Timasheff, S.N. (1992): Linkage between ligand binding and control of tubulin conformation. Biochemistry 31:8080-8089.
    • (1992) Biochemistry , vol.31 , pp. 8080-8089
    • Shearwin, K.E.1    Timasheff, S.N.2
  • 53
    • 0024561269 scopus 로고
    • Nuclear envelope breakdown and mitosis in sand dollar embryos is inhibited by microinjection of calcium buffers in a calcium-reversible fashion, and by antagonists of intracelular calcium channels
    • Silver, R.B. (1989): Nuclear envelope breakdown and mitosis in sand dollar embryos is inhibited by microinjection of calcium buffers in a calcium-reversible fashion, and by antagonists of intracelular calcium channels. Dev. Biol. 131:11-26.
    • (1989) Dev. Biol. , vol.131 , pp. 11-26
    • Silver, R.B.1
  • 54
    • 0017358347 scopus 로고
    • Binding sites for calcium on tubulin
    • Solomon, F. (1977): Binding sites for calcium on tubulin. Biochemistry 16:358-363.
    • (1977) Biochemistry , vol.16 , pp. 358-363
    • Solomon, F.1
  • 55
    • 0023882072 scopus 로고
    • Intracellular free calcium rise triggers nuclear envelope breakdown in the sea urchin embryo
    • Steinhardt, R., and Alderton, J. (1988): Intracellular free calcium rise triggers nuclear envelope breakdown in the sea urchin embryo. Nature 332:364-366.
    • (1988) Nature , vol.332 , pp. 364-366
    • Steinhardt, R.1    Alderton, J.2
  • 56
    • 0023766191 scopus 로고
    • Calmodulin colocalization with cold stable and nocodozole stable microtubules in living PtK1 cells
    • Sweet, S.C., and Welch, M.J. (1988): Calmodulin colocalization with cold stable and nocodozole stable microtubules in living PtK1 cells. Eur. J. Cell Biol. 47:88-93.
    • (1988) Eur. J. Cell Biol. , vol.47 , pp. 88-93
    • Sweet, S.C.1    Welch, M.J.2
  • 57
    • 0025930998 scopus 로고
    • Microtubule behavior in the growth cones of living neurons during axon elongation
    • Tanaka, E.M., and Kirschner, M.W. (1991): Microtubule behavior in the growth cones of living neurons during axon elongation. J. Cell Biol. 115:345-63.
    • (1991) J. Cell Biol. , vol.115 , pp. 345-363
    • Tanaka, E.M.1    Kirschner, M.W.2
  • 58
    • 0025245420 scopus 로고
    • Calcium channels, stores, and oscillations
    • Tsien, R.W., and Tsien, R.Y. (1990): Calcium channels, stores, and oscillations. Annu. Rev. Cell. Biol. 6:715-760.
    • (1990) Annu. Rev. Cell. Biol. , vol.6 , pp. 715-760
    • Tsien, R.W.1    Tsien, R.Y.2
  • 59
    • 0018557470 scopus 로고
    • Tubulin rings: Curved filaments with limited flexibility and two modes of association
    • Voter, W.A., and Erickson, H.P. (1979): Tubulin rings: Curved filaments with limited flexibility and two modes of association. J. Supramol. Struct. 10:419-431.
    • (1979) J. Supramol. Struct. , vol.10 , pp. 419-431
    • Voter, W.A.1    Erickson, H.P.2
  • 60
    • 0021258393 scopus 로고
    • The kinetics of microtubule assembly. Evidence for a two-stage nucleation mechanism
    • Voter, W.A., and Erickson, H.P. (1984): The kinetics of microtubule assembly. Evidence for a two-stage nucleation mechanism. J. Biol. Chem. 259:10430-10438.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10430-10438
    • Voter, W.A.1    Erickson, H.P.2
  • 61
    • 0026008120 scopus 로고
    • Dilution-induced disassembly of microtubules: Relation to dynamic instability
    • Voter, W.A., O'Brien, E.T., and H.P. Erickson. (1991): Dilution-induced disassembly of microtubules: Relation to dynamic instability. Cell Motil. Cytoskeleton 18:55-62.
    • (1991) Cell Motil. Cytoskeleton , vol.18 , pp. 55-62
    • Voter, W.A.1    O'Brien, E.T.2    Erickson, H.P.3
  • 62
    • 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. and Salmon, E.D. (1988): Dynamic instability of individual microtubules analyzed by video light microscopy: Rate constants and transition frequencies. J. Cell Biol. 107:1437-1448.
    • (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
  • 63
    • 0024544706 scopus 로고
    • Asymmetric behavior of severed microtubule ends after ultraviolet-microbeam irradiation of individual microtubules in vitro
    • Walker, R.A., Inoue, S., and Salmon E.D. (1989): Asymmetric behavior of severed microtubule ends after ultraviolet-microbeam irradiation of individual microtubules in vitro. J. Cell Biol. 108:931-937.
    • (1989) J. Cell Biol. , vol.108 , pp. 931-937
    • Walker, R.A.1    Inoue, S.2    Salmon, E.D.3
  • 64
    • 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., and Salmon, E.D. (1991): Dilution of individual microtubules observed in real time in vitro: Evidence that cap size is small and independent of elongation rate. J. Cell Biol. 114:73-81.
    • (1991) J. Cell Biol. , vol.114 , pp. 73-81
    • Walker, R.A.1    Pryer, N.K.2    Salmon, E.D.3
  • 65
    • 0015520152 scopus 로고
    • Microtubule formation in vitro in solutions containing low calcium concentrations
    • Weisenberg, R.C. (1972): Microtubule formation in vitro in solutions containing low calcium concentrations. Science 177:1104-1105.
    • (1972) Science , vol.177 , pp. 1104-1105
    • Weisenberg, R.C.1
  • 66
    • 0039489189 scopus 로고
    • Calcium-dependent regulator protein: Localization in the mitotic spindle of eukaryotic cells
    • Welsh, M.J., Dedman, J.R., Brinkly, B.R., and Means, A.R. (1978): Calcium-dependent regulator protein: Localization in the mitotic spindle of eukaryotic cells. Proc. Natl. Acad. Sci. USA 75:1867-1871.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 1867-1871
    • Welsh, M.J.1    Dedman, J.R.2    Brinkly, B.R.3    Means, A.R.4
  • 67
    • 0019334765 scopus 로고
    • Exchange of tubulin dimer into rings in microtubule assembly - Disassembly
    • Zeeberg, B., Cheek, J., and Caplow, M. (1980): Exchange of tubulin dimer into rings in microtubule assembly - disassembly. Biochemistry 19:5078-5086.
    • (1980) Biochemistry , vol.19 , pp. 5078-5086
    • Zeeberg, B.1    Cheek, J.2    Caplow, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.