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Volumn 25, Issue 2, 2014, Pages 257-266

Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; ALPHA TUBULIN; ALPHA TUBULIN ACETYLTRANSFERASE 1; TUBULIN; TUBULIN ACETYLTRANSFERASE; UNCLASSIFIED DRUG;

EID: 84892547110     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E13-07-0387     Document Type: Article
Times cited : (133)

References (62)
  • 2
    • 0026682713 scopus 로고
    • Low resolution structure of microtubules in solution. Synchrotron X-ray scattering and electron microscopy of Taxol-induced microtubules assembled from purified tubulin in comparison with glycerol and MAP-induced microtubules
    • Andreu JM, Bordas J, Diaz JF, García de Ancos J, Gil R, Medrano FJ, Towns-Andrews E (1992). Low resolution structure of microtubules in solution. Synchrotron X-ray scattering and electron microscopy of Taxol-induced microtubules assembled from purified tubulin in comparison with glycerol and MAP-induced microtubules. J Mol Biol 226, 169-184.
    • (1992) J Mol Biol , vol.226 , pp. 169-184
    • Andreu, J.M.1    Bordas, J.2    Diaz, J.F.3    García De Ancos, J.4    Gil, R.5    Medrano, F.J.6    Towns-Andrews, E.7
  • 3
    • 0029347192 scopus 로고
    • How does Taxol stabilize microtubules?
    • Arnal I, Wade RH (1995). How does Taxol stabilize microtubules? Curr Biol 5, 900-908.
    • (1995) Curr Biol , vol.5 , pp. 900-908
    • Arnal, I.1    Wade, R.H.2
  • 5
    • 0023947838 scopus 로고
    • Posttranslational modifications of alpha tubulin: Detyrosination and acetylation differentiate populations of interphase microtubules in cultured cells
    • Bulinski JC, Richards JE, Piperno G (1988). Posttranslational modifications of alpha tubulin: detyrosination and acetylation differentiate populations of interphase microtubules in cultured cells. J Cell Biol 106, 1213-1220.
    • (1988) J Cell Biol , vol.106 , pp. 1213-1220
    • Bulinski, J.C.1    Richards, J.E.2    Piperno, G.3
  • 6
    • 0021235399 scopus 로고
    • Luminal material in microtubules of frog olfactory axons: Structure and distribution
    • Burton PR (1984). Luminal material in microtubules of frog olfactory axons: structure and distribution. J Cell Biol 99, 520-528. (Pubitemid 14065178)
    • (1984) Journal of Cell Biology , vol.99 , Issue.2 , pp. 520-528
    • Burton, P.R.1
  • 7
    • 70350501513 scopus 로고    scopus 로고
    • Single molecule imaging reveals differences in microtubule track selection between kinesin motors
    • Cai D, McEwen DP, Martens JR, Meyhofer E, Verhey KJ (2009). Single molecule imaging reveals differences in microtubule track selection between kinesin motors. PLoS Biol 7, e1000216.
    • (2009) PLoS Biol , vol.7
    • Cai, D.1    McEwen, D.P.2    Martens, J.R.3    Meyhofer, E.4    Verhey, K.J.5
  • 8
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Mann M (2009). Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 325, 834-40.
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3    Nielsen, M.L.4    Rehman, M.5    Walther, T.C.6    Mann, M.7
  • 9
    • 79951819919 scopus 로고    scopus 로고
    • A novel acetylation of β-tubulin by San modulates microtubule polymerization via down-regulating tubulin incorporation
    • Chu CW, Hou F, Zhang J, Phu L, Loktev AV, Kirkpatrick DS, Zou H (2011). A novel acetylation of β-tubulin by San modulates microtubule polymerization via down-regulating tubulin incorporation. Mol Biol Cell 22, 448-456.
    • (2011) Mol Biol Cell , vol.22 , pp. 448-456
    • Chu, C.W.1    Hou, F.2    Zhang, J.3    Phu, L.4    Loktev, A.V.5    Kirkpatrick, D.S.6    Zou, H.7
  • 10
    • 59349089711 scopus 로고    scopus 로고
    • Elongator controls the migration and differentiation of cortical neurons through acetylation of alpha-tubulin
    • Creppe C, Malinouskaya L, Volvert M-L, Gillard M, Close P, Malaise O, Nguyen L (2009). Elongator controls the migration and differentiation of cortical neurons through acetylation of alpha-tubulin. Cell 136, 551-564.
    • (2009) Cell , vol.136 , pp. 551-564
    • Creppe, C.1    Malinouskaya, L.2    Volvert, M.-L.3    Gillard, M.4    Close, P.5    Malaise, O.6    Nguyen, L.7
  • 11
    • 84862658847 scopus 로고    scopus 로고
    • Posttranslational acetylation of α-tubulin constrains protofilament number in native microtubules
    • Cueva JG, Hsin J, Huang KC, Goodman MB (2012). Posttranslational acetylation of α-tubulin constrains protofilament number in native microtubules. Curr Biol 22, 1066-1074.
    • (2012) Curr Biol , vol.22 , pp. 1066-1074
    • Cueva, J.G.1    Hsin, J.2    Huang, K.C.3    Goodman, M.B.4
  • 12
    • 0032005552 scopus 로고    scopus 로고
    • Requirement for microtubules in new membrane formation during cytokinesis of Xenopus embryos
    • DOI 10.1006/dbio.1997.8815
    • Danilchik MV, Funk WC, Brown EE, Larkin K (1998). Requirement for microtubules in new membrane formation during cytokinesis of Xenopus embryos. Dev Biol 194, 47-60. (Pubitemid 28115258)
    • (1998) Developmental Biology , vol.194 , Issue.1 , pp. 47-60
    • Danilchik, M.V.1    Funk, W.C.2    Brown, E.E.3    Larkin, K.4
  • 13
    • 0017276478 scopus 로고
    • The effects of methyl (5-(2-thienylcarbonyl)-1H-benzimidazol-2-yl) carbamate, (R 17934; NSC 238159), a new synthetic antitumoral drug interfering with microtubules, on mammalian cells cultured in vitro
    • De Brabander MJ, Van de Veire RM, Aerts FE, Borgers M, Janssen PA (1976). The effects of methyl (5-(2-thienylcarbonyl)-1H-benzimidazol-2-yl) carbamate, (R 17934; NSC 238159), a new synthetic antitumoral drug interfering with microtubules, on mammalian cells cultured in vitro. Cancer Res 36, 905-916.
    • (1976) Cancer Res , vol.36 , pp. 905-916
    • De Brabander, M.J.1    Van De Veire, R.M.2    Aerts, F.E.3    Borgers, M.4    Janssen, P.A.5
  • 14
    • 0037424365 scopus 로고    scopus 로고
    • Fast kinetics of Taxol binding to microtubules: Effects of solution variables and microtubule-associated proteins
    • DOI 10.1074/jbc.M211163200
    • Díaz JF, Barasoain I, Andreu JM (2003). Fast kinetics of Taxol binding to microtubules. Effects of solution variables and microtubule- associated proteins. J Biol Chem 278, 8407-8419. (Pubitemid 36800591)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.10 , pp. 8407-8419
    • Diaz, J.F.1    Barasoain, I.2    Andreu, J.M.3
  • 15
    • 82955207160 scopus 로고    scopus 로고
    • Dysferlin interacts with histone deacetylase 6 and increases alpha-tubulin acetylation
    • Di Fulvio S, Azakir BA, Therrien C, Sinnreich M (2011). Dysferlin interacts with histone deacetylase 6 and increases alpha-tubulin acetylation. PloS One 6, e28563.
    • (2011) PloS One , vol.6
    • Di Fulvio, S.1    Azakir, B.A.2    Therrien, C.3    Sinnreich, M.4
  • 18
    • 33845305513 scopus 로고    scopus 로고
    • The iterative helical real space reconstruction method: Surmounting the problems posed by real polymers
    • DOI 10.1016/j.jsb.2006.05.015, PII S1047847706001687, Software Tools for Macromolecular Microscopy
    • Egelman EH (2007). The iterative helical real space reconstruction method: surmounting the problems posed by real polymers. J Struct Biol 157, 83-94. (Pubitemid 44880783)
    • (2007) Journal of Structural Biology , vol.157 , Issue.1 , pp. 83-94
    • Egelman, E.H.1
  • 19
    • 84864578590 scopus 로고    scopus 로고
    • The bromodomain interaction module
    • Filippakopoulos P, Knapp S (2012). The bromodomain interaction module. FEBS Lett 586, 2692-2704.
    • (2012) FEBS Lett , vol.586 , pp. 2692-2704
    • Filippakopoulos, P.1    Knapp, S.2
  • 21
    • 84870342617 scopus 로고    scopus 로고
    • Structure of the α-tubulin acetyltransferase, αtAT1, and implications for tubulin-specific acetylation
    • Friedmann DR, Aguilar A, Fan J, Nachury MV, Marmorstein R (2012). Structure of the α-tubulin acetyltransferase, αTAT1, and implications for tubulin-specific acetylation. Proc Natl Acad Sci USA 109, 19655-19660.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 19655-19660
    • Friedmann, D.R.1    Aguilar, A.2    Fan, J.3    Nachury, M.V.4    Marmorstein, R.5
  • 25
    • 81855196008 scopus 로고    scopus 로고
    • Post-translational regulation of the microtubule cytoskeleton: Mechanisms and functions
    • Janke C, Bulinski JC (2011). Post-translational regulation of the microtubule cytoskeleton: mechanisms and functions. Nat Rev Mol Cell Biol 12, 773-786.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 773-786
    • Janke, C.1    Bulinski, J.C.2
  • 27
    • 67349200776 scopus 로고    scopus 로고
    • Tubulin tyrosination navigates the kinesin-1 motor domain to axons
    • Konishi Y, Setou M (2009). Tubulin tyrosination navigates the kinesin-1 motor domain to axons. Nat Neurosci 12, 559-567.
    • (2009) Nat Neurosci , vol.12 , pp. 559-567
    • Konishi, Y.1    Setou, M.2
  • 28
    • 84871287765 scopus 로고    scopus 로고
    • Crystal structures of tubulin acetyltransferase reveal a conserved catalytic core and the plasticity of the essential N terminus
    • Kormendi V, Szyk A, Piszczek G, Roll-Mecak A (2012). Crystal structures of tubulin acetyltransferase reveal a conserved catalytic core and the plasticity of the essential N terminus. J Biol Chem 287, 41569-41575.
    • (2012) J Biol Chem , vol.287 , pp. 41569-41575
    • Kormendi, V.1    Szyk, A.2    Piszczek, G.3    Roll-Mecak, A.4
  • 29
    • 84864319735 scopus 로고    scopus 로고
    • +TIPs: SxIPping along microtubule ends
    • Kumar P, Wittmann T (2012). +TIPs: SxIPping along microtubule ends. Trends Cell Biol 22, 418-428.
    • (2012) Trends Cell Biol , vol.22 , pp. 418-428
    • Kumar, P.1    Wittmann, T.2
  • 31
    • 0022539766 scopus 로고
    • Cytoplasmic microtubules containing acetylated α-tubulin in Chlamydomonas reinhardtii: Spatial arrangement and properties
    • LeDizet M, Piperno G (1986). Cytoplasmic microtubules containing acetylated alpha-tubulin in Chlamydomonas reinhardtii: spatial arrangement and properties. J Cell Biol 103, 13-22. (Pubitemid 16066987)
    • (1986) Journal of Cell Biology , vol.103 , Issue.1 , pp. 13-22
    • LeDizet, M.1    Piperno, G.2
  • 32
    • 0023389780 scopus 로고
    • Identification of an acetylation site of Chlamydomonas alpha-tubulin
    • LeDizet M, Piperno G (1987). Identification of an acetylation site of Chlamydomonas alpha-tubulin. Proc Natl Acad Sci USA 84, 5720-5724.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5720-5724
    • Ledizet, M.1    Piperno, G.2
  • 33
    • 0020540736 scopus 로고
    • Chlamydomonas α-tubulin is posttranslationally modified in the flagella during flagellar assembly
    • L'Hernault SW, Rosenbaum JL (1983). Chlamydomonas alpha-tubulin is posttranslationally modified in the flagella during flagellar assembly. J Cell Biol 97, 258-263. (Pubitemid 13076539)
    • (1983) Journal of Cell Biology , vol.97 , Issue.1 , pp. 258-263
    • L'Hernault, S.W.1    Rosenbaum, J.L.2
  • 34
    • 0021993649 scopus 로고
    • Chlamydomonas α-tubulin is posttranslationally modified by acetylation on the ε-amino group of a lysine
    • DOI 10.1021/bi00323a034
    • L'Hernault SW, Rosenbaum JL (1985). Chlamydomonas alpha-tubulin is posttranslationally modified by acetylation on the epsilon-amino group of a lysine. Biochemistry 24, 473-478. (Pubitemid 15105622)
    • (1985) Biochemistry , vol.24 , Issue.2 , pp. 473-478
    • L'Hernault, S.W.1    Rosenbaum, J.L.2
  • 37
    • 0022452231 scopus 로고
    • The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules
    • Maruta H, Greer K, Rosenbaum JL (1986). The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules. J Cell Biol 103, 571-579. (Pubitemid 16055052)
    • (1986) Journal of Cell Biology , vol.103 , Issue.2 , pp. 571-579
    • Maruta, H.1    Greer, K.2    Rosenbaum, J.L.3
  • 38
    • 0035838406 scopus 로고    scopus 로고
    • Microtubule structure at improved resolution
    • DOI 10.1021/bi010343p
    • Meurer-Grob P, Kasparian J, Wade RH (2001). Microtubule structure at improved resolution. Biochemistry 40, 8000-8008. (Pubitemid 32641197)
    • (2001) Biochemistry , vol.40 , Issue.27 , pp. 8000-8008
    • Meurer-Grob, P.1    Kasparian, J.2    Wade, R.H.3
  • 39
    • 0034644119 scopus 로고    scopus 로고
    • The dynamic behavior of the APC-binding protein EB1 on the distal ends of microtubules
    • DOI 10.1016/S0960-9822(00)00600-X
    • Mimori-Kiyosue Y, Shiina N, Tsukita S (2000). The dynamic behavior of the APC-binding protein EB1 on the distal ends of microtubules. Curr Biol 10, 865-868. (Pubitemid 30597208)
    • (2000) Current Biology , vol.10 , Issue.14 , pp. 865-868
    • Mimori-Kiyosue, Y.1    Shiina, N.2    Tsukita, S.3
  • 40
    • 0029615473 scopus 로고
    • The effect of temperature on the structure of vinblastine-induced polymers of purified tubulin: Detection of a reversible conformational change
    • DOI 10.1006/jmbi.1995.0628
    • Nogales E, Medrano FJ, Diakun GP, Mant GR, Towns-Andrews E, Bordas J (1995). The effect of temperature on the structure of vinblastine-induced polymers of purified tubulin: detection of a reversible conformational change. J Mol Biol 254, 416-430. (Pubitemid 26001781)
    • (1995) Journal of Molecular Biology , vol.254 , Issue.3 , pp. 416-430
    • Nogales, E.1    Medrano, F.J.2    Diakun, G.P.3    Mant, G.R.4    Towns-Andrews, E.5    Bordas, J.6
  • 41
    • 0033534629 scopus 로고    scopus 로고
    • High-resolution model of the microtubule
    • DOI 10.1016/S0092-8674(00)80961-7
    • Nogales E, Whittaker M, Milligan RA, Downing KH (1999). High-resolution model of the microtubule. Cell 96, 79-88. (Pubitemid 29044155)
    • (1999) Cell , vol.96 , Issue.1 , pp. 79-88
    • Nogales, E.1    Whittaker, M.2    Milligan, R.A.3    Downing, K.H.4
  • 42
    • 0037291214 scopus 로고    scopus 로고
    • +-dependent tubulin deacetylase
    • DOI 10.1016/S1097-2765(03)00038-8
    • North BJ, Marshall BL, Borra MT, Denu JM, Verdin E (2003). The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell 11, 437-444. (Pubitemid 36293837)
    • (2003) Molecular Cell , vol.11 , Issue.2 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 43
    • 0031687778 scopus 로고    scopus 로고
    • Diffusion inside microtubules
    • DOI 10.1007/s002490050161
    • Odde D (1998). Diffusion inside microtubules. Eur Biophys J 27, 514-520. (Pubitemid 28414891)
    • (1998) European Biophysics Journal , vol.27 , Issue.5 , pp. 514-520
    • Odde, D.1
  • 44
    • 0033582659 scopus 로고    scopus 로고
    • CLIP-170 highlights growing microtubule ends in vivo
    • Perez F, Diamantopoulos GS, Stalder R, Kreis TE (1999). CLIP-170 highlights growing microtubule ends in vivo. Cell 96, 517-527. (Pubitemid 29106839)
    • (1999) Cell , vol.96 , Issue.4 , pp. 517-527
    • Perez, F.1    Diamantopoulos, G.S.2    Stalder, R.3    Kreis, T.E.4
  • 47
    • 0022399572 scopus 로고
    • Monoclonal antibodies specific for an acetylated form of α-tubulin recognize the antigen in cilia and flagella from a variety of organisms
    • DOI 10.1083/jcb.101.6.2085
    • Piperno G, Fuller MT (1985). Monoclonal antibodies specific for an acetylated form of alpha-tubulin recognize the antigen in cilia and flagella from a variety of organisms. J Cell Biol 101, 2085-2094. (Pubitemid 16169938)
    • (1985) Journal of Cell Biology , vol.101 , Issue.6 , pp. 2085-2094
    • Piperno, G.1    Fuller, M.T.2
  • 48
    • 0023293040 scopus 로고
    • Microtubules containing acetylated alpha-tubulin in mammalian cells in culture
    • Piperno G, LeDizet M, Chang XJ (1987). Microtubules containing acetylated alpha-tubulin in mammalian cells in culture. J Cell Biol 104, 289-302.
    • (1987) J Cell Biol , vol.104 , pp. 289-302
    • Piperno, G.1    Ledizet, M.2    Chang, X.J.3
  • 49
    • 79953304482 scopus 로고    scopus 로고
    • The posttranslational modification of tubulin undergoes a switch from detyrosination to acetylation as epithelial cells become polarized
    • Quinones GB, Danowski BA, Devaraj A, Singh V, Ligon LA (2011). The posttranslational modification of tubulin undergoes a switch from detyrosination to acetylation as epithelial cells become polarized. Mol Biol Cell 22, 1045-1057.
    • (2011) Mol Biol Cell , vol.22 , pp. 1045-1057
    • Quinones, G.B.1    Danowski, B.A.2    Devaraj, A.3    Singh, V.4    Ligon, L.A.5
  • 50
    • 33750618516 scopus 로고    scopus 로고
    • Microtubule acetylation promotes kinesin-1 binding and transport
    • DOI 10.1016/j.cub.2006.09.014, PII S096098220602207X
    • Reed NA, Cai D, Blasius TL, Jih GT, Meyhofer E, Gaertig J, Verhey KJ (2006). Microtubule acetylation promotes kinesin-1 binding and transport. Curr Biol 16, 2166-2172. (Pubitemid 44692098)
    • (2006) Current Biology , vol.16 , Issue.21 , pp. 2166-2172
    • Reed, N.A.1    Cai, D.2    Blasius, T.L.3    Jih, G.T.4    Meyhofer, E.5    Gaertig, J.6    Verhey, K.J.7
  • 52
    • 1842684989 scopus 로고    scopus 로고
    • HDAC6 deacetylase activity links the tubulin cytoskeleton with immune synapse organization
    • DOI 10.1016/S1074-7613(04)00078-0, PII S1074761304000780
    • Serrador JM, Cabrero JR, Sancho D, Mittelbrunn M, Urzainqui A, Sánchez-Madrid F (2004). HDAC6 deacetylase activity links the tubulin cytoskeleton with immune synapse organization. Immunity 20, 417-428. (Pubitemid 38482120)
    • (2004) Immunity , vol.20 , Issue.4 , pp. 417-428
    • Serrador, J.M.1    Cabrero, J.R.2    Sancho, D.3    Mittelbrunn, M.4    Urzainqui, A.5    Sanchez-Madrid, F.6
  • 53
    • 78650731392 scopus 로고    scopus 로고
    • The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensation
    • Shida T, Cueva JG, Xu Z, Goodman MB, Nachury MV (2010). The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensation. Proc Natl Acad Sci USA 107, 21517-21522.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 21517-21522
    • Shida, T.1    Cueva, J.G.2    Xu, Z.3    Goodman, M.B.4    Nachury, M.V.5
  • 54
    • 0026538495 scopus 로고
    • Tubulin in sea urchin embryonic cilia: Post-translational modifications during regeneration
    • Stephens RE (1992). Tubulin in sea urchin embryonic cilia: post-translational modifications during regeneration. J Cell Sci 101, 837-45.
    • (1992) J Cell Sci , vol.101 , pp. 837-845
    • Stephens, R.E.1
  • 55
    • 77953046399 scopus 로고    scopus 로고
    • Acetylation of microtubules influences their sensitivity to severing by katanin in neurons and fibroblasts
    • Sudo H, Baas PW (2010). Acetylation of microtubules influences their sensitivity to severing by katanin in neurons and fibroblasts. J Neurosci 30, 7215-7226.
    • (2010) J Neurosci , vol.30 , pp. 7215-7226
    • Sudo, H.1    Baas, P.W.2
  • 56
    • 77955478732 scopus 로고    scopus 로고
    • Structural basis of interprotofilament interaction and lateral deformation of microtubules
    • Sui H, Downing KH (2010). Structural basis of interprotofilament interaction and lateral deformation of microtubules. Structure 18, 1022-1031.
    • (2010) Structure , vol.18 , pp. 1022-1031
    • Sui, H.1    Downing, K.H.2
  • 59
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • DOI 10.1016/j.jsb.2006.05.009, PII S1047847706001894, Software Tools for Macromolecular Microscopy
    • Tang G, Peng L, Baldwin PR, Mann DS, Jiang W, Rees I, Ludtke SJ (2007). EMAN2: an extensible image processing suite for electron microscopy. J Struct Biol 157, 38-46. (Pubitemid 44880785)
    • (2007) Journal of Structural Biology , vol.157 , Issue.1 , pp. 38-46
    • Tang, G.1    Peng, L.2    Baldwin, P.R.3    Mann, D.S.4    Jiang, W.5    Rees, I.6    Ludtke, S.J.7
  • 60
    • 84870316474 scopus 로고    scopus 로고
    • Atomic resolution structure of human α-tubulin acetyltransferase bound to acetyl-CoA
    • Taschner M, Vetter M, Lorentzen E (2012). Atomic resolution structure of human α-tubulin acetyltransferase bound to acetyl-CoA. Proc Natl Acad Sci USA 109, 19649-19654.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 19649-19654
    • Taschner, M.1    Vetter, M.2    Lorentzen, E.3
  • 61
    • 0027248928 scopus 로고
    • Relationship between the Golgi complex and microtubules enriched in detyrosinated or acetylated α-tubulin: Studies on cells recovering from nocodazole and cells in the terminal phase of cytokinesis
    • Thyberg J, Moskalewski S (1993). Relationship between the Golgi complex and microtubules enriched in detyrosinated or acetylated alpha-tubulin: studies on cells recovering from nocodazole and cells in the terminal phase of cytokinesis. Cell Tissue Res 273, 457-466. (Pubitemid 23258493)
    • (1993) Cell and Tissue Research , vol.273 , Issue.3 , pp. 457-466
    • Thyberg, J.1    Moskalewski, S.2
  • 62
    • 84862690126 scopus 로고    scopus 로고
    • Genetically separable functions of the MEC-17 tubulin acetyltransferase affect microtubule organization
    • Topalidou I, Keller C, Kalebic N, Nguyen KCQ, Somhegyi H, Politi KA, Chalfie M (2012). Genetically separable functions of the MEC-17 tubulin acetyltransferase affect microtubule organization. Curr Biol 22, 1057-1065.
    • (2012) Curr Biol , vol.22 , pp. 1057-1065
    • Topalidou, I.1    Keller, C.2    Kalebic, N.3    Nguyen, K.C.Q.4    Somhegyi, H.5    Politi, K.A.6    Chalfie, M.7


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