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Volumn 140, Issue 1, 1998, Pages 131-141

Regulation of microtubule dynamics by extracellular signals: CAMP- dependent protein kinase switches off the activity of oncoprotein 18 in intact cells

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE RECEPTOR; CYCLIC AMP DEPENDENT PROTEIN KINASE; ONCOPROTEIN; TUBULIN;

EID: 0031941941     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.140.1.131     Document Type: Article
Times cited : (127)

References (50)
  • 1
    • 0027071663 scopus 로고
    • Thrombin, epidermal growth factor, and phorbol myristate acetate stimulate tubulin polymerization in quiescent cells: A potential link to mitogenesis
    • Ball, R.L., T. Albrecht, W.C. Thompson, O. James, and D.H. Carney. 1992. Thrombin, epidermal growth factor, and phorbol myristate acetate stimulate tubulin polymerization in quiescent cells: a potential link to mitogenesis. Cell Motil. Cytoskeleton. 23:265-278.
    • (1992) Cell Motil. Cytoskeleton , vol.23 , pp. 265-278
    • Ball, R.L.1    Albrecht, T.2    Thompson, W.C.3    James, O.4    Carney, D.H.5
  • 2
    • 0030048731 scopus 로고    scopus 로고
    • Identification of a protein that interacts with tubulin dimers and increases the catastrophe rate of microtubules
    • Belmont, L.D, and T.J. Mitchison. 1996. Identification of a protein that interacts with tubulin dimers and increases the catastrophe rate of microtubules. Cell. 84:623-631.
    • (1996) Cell , vol.84 , pp. 623-631
    • Belmont, L.D.1    Mitchison, T.J.2
  • 4
    • 0027292675 scopus 로고
    • Multiple phosphorylalion of stathmin. Identification of four sites phosphorylated in intact cells and in vitro by cyclic AMP-dependent protein kinase and p34cdc2
    • Beretta, L., T. Dobransky, and A. Sobel. 1993. Multiple phosphorylalion of stathmin. Identification of four sites phosphorylated in intact cells and in vitro by cyclic AMP-dependent protein kinase and p34cdc2. J. Biol. Chem. 268:20076-20084.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20076-20084
    • Beretta, L.1    Dobransky, T.2    Sobel, A.3
  • 5
    • 0019470796 scopus 로고
    • Dibutyryl cyclic AMP-induced phosphorylation of specific proteins in adenohypophysial cells
    • Brattin Jr, W.J., and R. Portanova. 1981. Dibutyryl cyclic AMP-induced phosphorylation of specific proteins in adenohypophysial cells. Mol. Cell. Endocrinol. 23:77-90.
    • (1981) Mol. Cell. Endocrinol. , vol.23 , pp. 77-90
    • Brattin Jr., W.J.1    Portanova, R.2
  • 6
    • 0028273487 scopus 로고
    • Cell-cycle-regulated phosphorylation of oncoprotein 18 on Ser16, Ser25, and Ser38
    • Brattsand, G., U. Marklund, K. Nylander, G. Roos, and M. Gullberg. 1994. Cell-cycle-regulated phosphorylation of oncoprotein 18 on Ser16, Ser25, and Ser38. Eur. J. Biochem. 220:359-368.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 359-368
    • Brattsand, G.1    Marklund, U.2    Nylander, K.3    Roos, G.4    Gullberg, M.5
  • 7
    • 0027253551 scopus 로고
    • Quantitative analysis of the expression and regulation of an activation-regulated phosphoprotein (oncoprotein 18) in normal and neoplastic cells
    • Brattsand, G., G. Roos, U. Marklund, H. Ueda, G. Landberg, E. Nanberg, P. Sideras, and M. Gullberg. 1993. Quantitative analysis of the expression and regulation of an activation-regulated phosphoprotein (oncoprotein 18) in normal and neoplastic cells. Leukemia. 7:569-579.
    • (1993) Leukemia , vol.7 , pp. 569-579
    • Brattsand, G.1    Roos, G.2    Marklund, U.3    Ueda, H.4    Landberg, G.5    Nanberg, E.6    Sideras, P.7    Gullberg, M.8
  • 8
    • 0028365578 scopus 로고
    • G proteins in lymphocyte signalling
    • Cantrell, D. 1994. G proteins in lymphocyte signalling. Curr. Opin. Immunol. 6: 380-384.
    • (1994) Curr. Opin. Immunol. , vol.6 , pp. 380-384
    • Cantrell, D.1
  • 9
    • 0019473226 scopus 로고
    • Unpolymerized tubulin modulates the level of tubulin mRNAs
    • Cleveland, D.W., M.A. Lopata, P. Sherline, and M.W. Kirschner. 1981. Unpolymerized tubulin modulates the level of tubulin mRNAs. Cell. 25:537-546.
    • (1981) Cell , vol.25 , pp. 537-546
    • Cleveland, D.W.1    Lopata, M.A.2    Sherline, P.3    Kirschner, M.W.4
  • 10
    • 0028950267 scopus 로고
    • Organization of organelles and membrane traffic by microtubules
    • Cole, N.B., and J. Lippincott-Schwartz. 1995. Organization of organelles and membrane traffic by microtubules. Curr. Opin. Cell. Biol. 7:55-64.
    • (1995) Curr. Opin. Cell. Biol. , vol.7 , pp. 55-64
    • Cole, N.B.1    Lippincott-Schwartz, J.2
  • 12
    • 0027058857 scopus 로고
    • Modulation of the dynamic instability of tubulin assembly by the microtuhule-associated protein tau
    • Drechsel, D.N., A.A. Hyman, M.H. Cobb, and M.W. Kirschner. 1992. Modulation of the dynamic instability of tubulin assembly by the microtuhule-associated protein tau. Mol. Biol. Cell. 3:1141-1154.
    • (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
  • 13
    • 0029072567 scopus 로고
    • Modulation of the phosphorylation state of tau in situ: The roles of calcium and cyclic AMP
    • Fleming, L.M., and G.V. Johnson. 1995. Modulation of the phosphorylation state of tau in situ: the roles of calcium and cyclic AMP. Biochem. J. 309:41-47.
    • (1995) Biochem. J. , vol.309 , pp. 41-47
    • Fleming, L.M.1    Johnson, G.V.2
  • 14
    • 0024436502 scopus 로고
    • Directional antisense and sense cDNA cloning using Epstein-Barr virus episomal expression vectors
    • Groger, R.K., D.M. Morrow, and M.L. Tykocinski. 1989. Directional antisense and sense cDNA cloning using Epstein-Barr virus episomal expression vectors. Gene. 81:285-294.
    • (1989) Gene , vol.81 , pp. 285-294
    • Groger, R.K.1    Morrow, D.M.2    Tykocinski, M.L.3
  • 15
    • 0030968633 scopus 로고    scopus 로고
    • The microtubule-destabilizing activity of metablastin (p19) is controlled by phosphorylation
    • Horwitz, S.B., H.J. Shen, L.F. He, P. Dittmar, R. Neef, J.H. Chen, and U.K. Schubart. 1997. The microtubule-destabilizing activity of metablastin (p19) is controlled by phosphorylation. J. Biol. Chem. 272:8129-8132.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8129-8132
    • Horwitz, S.B.1    Shen, H.J.2    He, L.F.3    Dittmar, P.4    Neef, R.5    Chen, J.H.6    Schubart, U.K.7
  • 16
    • 0026517618 scopus 로고
    • Mitogen-activated-protein-kinase-catalyzed phosphorylation of microtubule-associated proteins, microtubule-associated protein 2 and microtubule-associated protein 4, induces an alteration in their function
    • Hoshi, M., K. Ohta, Y. Gotoh, A. Mori, H. Murofushi, H. Sakai, and E. Nishida. 1992. Mitogen-activated-protein-kinase-catalyzed phosphorylation of microtubule-associated proteins, microtubule-associated protein 2 and microtubule-associated protein 4, induces an alteration in their function. Eur. J. Biochem. 203:43-52.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 43-52
    • Hoshi, M.1    Ohta, K.2    Gotoh, Y.3    Mori, A.4    Murofushi, H.5    Sakai, H.6    Nishida, E.7
  • 17
    • 0030883128 scopus 로고    scopus 로고
    • Kinase and phosphatase inhibitors cause rapid alterations in microtubule dynamic instability in living cells
    • Howell, B., D.J. Odde, and L. Cassimeris. 1997. Kinase and phosphatase inhibitors cause rapid alterations in microtubule dynamic instability in living cells. Cell Motil. Cytoskeleton. 38:201-214.
    • (1997) Cell Motil. Cytoskeleton , vol.38 , pp. 201-214
    • Howell, B.1    Odde, D.J.2    Cassimeris, L.3
  • 18
    • 0030059247 scopus 로고    scopus 로고
    • Morphogenetic properties of microtubules and mitotic spindle assembly
    • Hyman, A.A., and E. Karsenti. 1996. Morphogenetic properties of microtubules and mitotic spindle assembly. Cell. 84:401-410.
    • (1996) Cell , vol.84 , pp. 401-410
    • Hyman, A.A.1    Karsenti, E.2
  • 19
    • 0009623452 scopus 로고
    • Modification of microtubule steady-state dynamics by phosphorylation of the microtubule-associated proteins
    • Jameson, L., and M. Caplow. 1981. Modification of microtubule steady-state dynamics by phosphorylation of the microtubule-associated proteins. Proc. Natl. Acad. Sci. USA. 78:3413-3417.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 3413-3417
    • Jameson, L.1    Caplow, M.2
  • 20
    • 0025966261 scopus 로고
    • Phosphorylation of microtubulc-associated protein-2 in GH3 cells. Regulation by cAMP and by calcium
    • Jefferson, A.B., and H. Schulman. 1991. Phosphorylation of microtubulc-associated protein-2 in GH3 cells. Regulation by cAMP and by calcium. J. Biol. Chem. 266:346-354.
    • (1991) J. Biol. Chem. , vol.266 , pp. 346-354
    • Jefferson, A.B.1    Schulman, H.2
  • 21
    • 0026757277 scopus 로고
    • Analysis of phosphoprotein p19 by liquid chromatography/mass spectrometry. Identification of two proline-directed serine phosphorylation sites and a blocked amino terminus
    • Labdon, J.E., E. Nieves, and U.K. Schubart. 1992. Analysis of phosphoprotein p19 by liquid chromatography/mass spectrometry. Identification of two proline-directed serine phosphorylation sites and a blocked amino terminus. J. Biol. Chem. 267:3506-3513.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3506-3513
    • Labdon, J.E.1    Nieves, E.2    Schubart, U.K.3
  • 22
    • 0029062165 scopus 로고
    • G2/M transition requires multisite phosphorylation of oncoprotein 18 by two distinct protein kinase systems
    • Larsson, N., H. Melander, U. Marklund, O. Osterman, and M. Gullberg. 1995. G2/M transition requires multisite phosphorylation of oncoprotein 18 by two distinct protein kinase systems. J. Biol. Chem. 270:14175-14183.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14175-14183
    • Larsson, N.1    Melander, H.2    Marklund, U.3    Osterman, O.4    Gullberg, M.5
  • 23
    • 0030750560 scopus 로고    scopus 로고
    • Control of microtubule dynamics by Oncoprotein 18: Dissection of the regulatory role of multisite phosphorylation during mitosis
    • Larsson, N., U. Marklund, H. Melander Gradin, G. Brattsand, and M. Gullberg. 1997. Control of microtubule dynamics by Oncoprotein 18: Dissection of the regulatory role of multisite phosphorylation during mitosis. Mol. Cell. Biol 17:5530-5539.
    • (1997) Mol. Cell. Biol , vol.17 , pp. 5530-5539
    • Larsson, N.1    Marklund, U.2    Melander Gradin, H.3    Brattsand, G.4    Gullberg, M.5
  • 24
    • 0021338217 scopus 로고
    • Phosphorylation affects the ability of tau protein to promote microtubule assembly
    • Lindwall, G., and R.D. Cole. 1984. Phosphorylation affects the ability of tau protein to promote microtubule assembly. J. Biol. Chem. 259:5301-5305.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5301-5305
    • Lindwall, G.1    Cole, R.D.2
  • 25
    • 0028845388 scopus 로고
    • Role of microtubule-associated proteins in the control of microtubule assembly
    • Maccioni, R.B., and V. Cambiazo. 1995. Role of microtubule-associated proteins in the control of microtubule assembly. Physiol. Rev. 75:835-864.
    • (1995) Physiol. Rev. , vol.75 , pp. 835-864
    • Maccioni, R.B.1    Cambiazo, V.2
  • 26
    • 0028945057 scopus 로고
    • Microtubules and microtubule-associated proteins
    • Mandelkow, E., and E.M. Mandelkow. 1995. Microtubules and microtubule-associated proteins. Curr. Opin. Cell Biol. 7:72-81.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 72-81
    • Mandelkow, E.1    Mandelkow, E.M.2
  • 27
    • 0027493838 scopus 로고
    • Multiple signal transduction pathways induce phosphorylation of serines 16, 25, and 38 of oncoprotein 18 in T lymphocytes
    • Marklund, U., G. Brattsand, O. Osterman, P.I. Ohlsson, and M. Gullberg. 1993a. Multiple signal transduction pathways induce phosphorylation of serines 16, 25, and 38 of oncoprotein 18 in T lymphocytes. J. Biol. Chem. 268: 25671-25680.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25671-25680
    • Marklund, U.1    Brattsand, G.2    Osterman, O.3    Ohlsson, P.I.4    Gullberg, M.5
  • 28
    • 0027236396 scopus 로고
    • Serine 25 of oncoprotein 18 is a major cytosolic target for the mitogen-activated protein kinase
    • Marklund, U., G. Brattsand, V. Shingler, and M. Gullberg. 1993b. Serine 25 of oncoprotein 18 is a major cytosolic target for the mitogen-activated protein kinase. J. Biol. Chem. 268:15039-15047.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15039-15047
    • Marklund, U.1    Brattsand, G.2    Shingler, V.3    Gullberg, M.4
  • 29
    • 0028171913 scopus 로고
    • The phenotype of a "Cdc2 kinase target site-deficient" mutant of oncoprotein 18 reveals a role of this protein in cell cycle control
    • Marklund, U., O. Osterman, H. Melander, A. Bergh, and M. Gullberg. 1994. The phenotype of a "Cdc2 kinase target site-deficient" mutant of oncoprotein 18 reveals a role of this protein in cell cycle control. J. Biol. Chem. 269: 30626-30635.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30626-30635
    • Marklund, U.1    Osterman, O.2    Melander, H.3    Bergh, A.4    Gullberg, M.5
  • 31
    • 0024316714 scopus 로고
    • Modulation of T cell activation by differential regulation of the phosphorylation of two cytosolic proteins. Implication of both Ca2+ and cyclic AMP-dependent protein kinases
    • Mary, D., J.F. Peyron, P. Auberger, C. Aussel, and M. Fehlmann. 1989. Modulation of T cell activation by differential regulation of the phosphorylation of two cytosolic proteins. Implication of both Ca2+ and cyclic AMP-dependent protein kinases. J. Biol. Chem. 264:14498-14502.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14498-14502
    • Mary, D.1    Peyron, J.F.2    Auberger, P.3    Aussel, C.4    Fehlmann, M.5
  • 32
    • 0028824882 scopus 로고
    • Binding of E-MAP-115 to microtubules is regulated by cell cycle-dependent phosphorylation
    • Masson, D., and T.E. Kreis. 1995. Binding of E-MAP-115 to microtubules is regulated by cell cycle-dependent phosphorylation. J. Cell Biol. 131:1015-1024.
    • (1995) J. Cell Biol. , vol.131 , pp. 1015-1024
    • Masson, D.1    Kreis, T.E.2
  • 33
    • 0030060174 scopus 로고    scopus 로고
    • Modulation of microtubule dynamics during the cell cycle
    • McNally, F.J. 1996. Modulation of microtubule dynamics during the cell cycle. Curr. Opin. Cell. Biol. 8:23-29.
    • (1996) Curr. Opin. Cell. Biol. , vol.8 , pp. 23-29
    • McNally, F.J.1
  • 34
    • 1842409000 scopus 로고    scopus 로고
    • Regulation of microtubule dynamics by Ca2+/calmodulin-dependent kinase IV/Gr-dependent phosphorylation of oncoprotein 18
    • Melander Gradin, H., U. Marklund, N. Larsson, T.A. Chatila, and M. Gullberg. 1997. Regulation of microtubule dynamics by Ca2+/calmodulin-dependent kinase IV/Gr-dependent phosphorylation of oncoprotein 18. Mol. Cell. Biol. 17:3459-3467.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3459-3467
    • Melander Gradin, H.1    Marklund, U.2    Larsson, N.3    Chatila, T.A.4    Gullberg, M.5
  • 35
    • 0025872827 scopus 로고
    • Resistance to antimitotic drugs in Chinese hamster ovary cells correlates with changes in the level of polymerized tubulin
    • Minotti, A.M., S.B. Barlow, and F. Cabrai. 1991. Resistance to antimitotic drugs in Chinese hamster ovary cells correlates with changes in the level of polymerized tubulin. J. Biol. Chem. 266:3987-3994.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3987-3994
    • Minotti, A.M.1    Barlow, S.B.2    Cabrai, F.3
  • 36
    • 0027097614 scopus 로고
    • Compare and contrast actin filaments and microtubules
    • Mitchison, T.J. 1992. Compare and contrast actin filaments and microtubules. Mol. Biol. Cell. 3:1309-1315.
    • (1992) Mol. Biol. Cell. , vol.3 , pp. 1309-1315
    • Mitchison, T.J.1
  • 37
    • 0028927505 scopus 로고
    • Cyclin B interaction with microtubule-associated protein 4 (MAP4) targets p34cdc2 kinase to microtubules and is a potential regulator of M-phase microtubule dynamics
    • Ookata, K., S. Hisanaga, J.C. Bulinski, H. Murofushi, H. Aizawa, T.J. Itoh, H. Hotani, E. Okumura, K. Tachibana, and T. Kishimoto. 1995. Cyclin B interaction with microtubule-associated protein 4 (MAP4) targets p34cdc2 kinase to microtubules and is a potential regulator of M-phase microtubule dynamics. J. Cell Biol. 128:849-862.
    • (1995) J. Cell Biol. , vol.128 , pp. 849-862
    • Ookata, K.1    Hisanaga, S.2    Bulinski, J.C.3    Murofushi, H.4    Aizawa, H.5    Itoh, T.J.6    Hotani, H.7    Okumura, E.8    Tachibana, K.9    Kishimoto, T.10
  • 38
    • 0026590175 scopus 로고
    • Mutations in the catalytic subunit of cAMP-dependent protein kinase result in unregulated biological activity
    • Orellana, S.A, and G.S. McKnight. 1992. Mutations in the catalytic subunit of cAMP-dependent protein kinase result in unregulated biological activity. Proc. Natl. Acad. Sci. USA. 89:4726-4730.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4726-4730
    • Orellana, S.A.1    McKnight, G.S.2
  • 39
    • 0023634247 scopus 로고
    • Autoregulation of tubulin expression is achieved through specific degradation of polysomal tubulin mRNAs
    • Pachter, J.S., T.J. Yen, and D.W. Cleveland. 1987. Autoregulation of tubulin expression is achieved through specific degradation of polysomal tubulin mRNAs. Cell. 51:283-292.
    • (1987) Cell , vol.51 , pp. 283-292
    • Pachter, J.S.1    Yen, T.J.2    Cleveland, D.W.3
  • 40
    • 0028900380 scopus 로고
    • Stimulus-dependent alterations in macrophage microtubules: Increased tubulin polymerization and detyrosination
    • Robinson, J.M., and D.D. Vandre. 1995. Stimulus-dependent alterations in macrophage microtubules: increased tubulin polymerization and detyrosination. J. Cell Sci. 108:645-655.
    • (1995) J. Cell Sci. , vol.108 , pp. 645-655
    • Robinson, J.M.1    Vandre, D.D.2
  • 41
    • 0027377259 scopus 로고
    • Expression of oncoprotcin 18 in human leukemias and lymphomas
    • Roos, G., G. Brattsand, G. Landberg, U. Marklund, and M. Gullberg. 1993. Expression of oncoprotcin 18 in human leukemias and lymphomas. Leukemia. 7:1538-1546.
    • (1993) Leukemia , vol.7 , pp. 1538-1546
    • Roos, G.1    Brattsand, G.2    Landberg, G.3    Marklund, U.4    Gullberg, M.5
  • 42
    • 0020366092 scopus 로고
    • Regulation of protein phosphorylation in hamster insulinoma cells. Identification of Ca2+-regulated cytoskeletal and cAMP-regulated cytosolic phosphoproteins by two-dimensional electrophoresis
    • Schubart, U.K. 1982. Regulation of protein phosphorylation in hamster insulinoma cells. Identification of Ca2+-regulated cytoskeletal and cAMP-regulated cytosolic phosphoproteins by two-dimensional electrophoresis. J. Biol. Chem. 257:12231-12238.
    • (1982) J. Biol. Chem. , vol.257 , pp. 12231-12238
    • Schubart, U.K.1
  • 43
    • 0023664781 scopus 로고
    • Properties of p19, a novel cAMP-dependent protein kinase substrate protein purified from bovine brain
    • Schubart, U.K., W. Alago Jr, and A. Danoff. 1987. Properties of p19, a novel cAMP-dependent protein kinase substrate protein purified from bovine brain. J. Biol. Chem. 262:11871-11877.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11871-11877
    • Schubart, U.K.1    Alago Jr., W.2    Danoff, A.3
  • 44
    • 15844416222 scopus 로고    scopus 로고
    • Normal development of mice lacking metablastin (P19), a phosphoprotein implicated in cell cycle regulation
    • Schubart, U.K., J. Yu, J.A. Amat, Z. Wang, M.K. Hoffmann, and W. Edelmann. 1996. Normal development of mice lacking metablastin (P19), a phosphoprotein implicated in cell cycle regulation. J. Biol. Chem. 271:14062-14066.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14062-14066
    • Schubart, U.K.1    Yu, J.2    Amat, J.A.3    Wang, Z.4    Hoffmann, M.K.5    Edelmann, W.6
  • 45
    • 0026083056 scopus 로고
    • Activation of microtubule-associated protein kinase by microtubule disruption in quiescent rat 3Y1 cells
    • Shinohara-Gotoh, Y., E. Nishida, M. Hoshi, and H. Sakai. 1991. Activation of microtubule-associated protein kinase by microtubule disruption in quiescent rat 3Y1 cells. Exp. Cell Res. 193:161-166.
    • (1991) Exp. Cell Res. , vol.193 , pp. 161-166
    • Shinohara-Gotoh, Y.1    Nishida, E.2    Hoshi, M.3    Sakai, H.4
  • 46
    • 0021077837 scopus 로고
    • Distinct patterns of cytoplasmic protein phosphorylation related to regulation of synthesis and release of prolactin by GH cells
    • Sobel, A., and A.H. Tashjian Jr. 1983. Distinct patterns of cytoplasmic protein phosphorylation related to regulation of synthesis and release of prolactin by GH cells. J. Biol. Chem. 258:10312-10324.
    • (1983) J. Biol. Chem. , vol.258 , pp. 10312-10324
    • Sobel, A.1    Tashjian Jr., A.H.2
  • 48
    • 0028820411 scopus 로고
    • Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules
    • Trinczek, B., J. Biernat, K. Baumann, E.M. Mandelkow, and E. Mandelkow. 1995. Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules. Mol. Biol. Cell. 6:1887-1902.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1887-1902
    • Trinczek, B.1    Biernat, J.2    Baumann, K.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 49
    • 0030031999 scopus 로고    scopus 로고
    • XKCM1: A Xenopus kinesin-related protein that regulates microtubule dynamics during mitotic spindle assembly
    • Walczak, C.E., T.J. Mitchison, and A. Desai. 1996. XKCM1: a Xenopus kinesin-related protein that regulates microtubule dynamics during mitotic spindle assembly. Cell. 84:37-47.
    • (1996) Cell , vol.84 , pp. 37-47
    • Walczak, C.E.1    Mitchison, T.J.2    Desai, A.3
  • 50
    • 0027153595 scopus 로고
    • Phorbol 12-myristate 13-acetate-induced phosphorylation of Op18 in jurkat T cells. Identification of phosphorylation sites by matrix-assisted laser desorption ionization mass spectrometry
    • Wang, Y.K., P.C. Liao, J. Allison, D.A. Gage, P.C. Andrews, D.M. Lubman, S.M. Hanash, and J.R. Strahler. 1993. Phorbol 12-myristate 13-acetate-induced phosphorylation of Op18 in jurkat T cells. Identification of phosphorylation sites by matrix-assisted laser desorption ionization mass spectrometry. J. Biol. Chem. 268:14269-14277.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14269-14277
    • Wang, Y.K.1    Liao, P.C.2    Allison, J.3    Gage, D.A.4    Andrews, P.C.5    Lubman, D.M.6    Hanash, S.M.7    Strahler, J.R.8


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