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Volumn 7, Issue 7, 2012, Pages

Highly dynamic microtubules improve the effectiveness of early stages of human influenza A/NWS/33 virus infection in LLC-MK2 cells

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TUBULIN; MICROTUBULE ASSOCIATED PROTEIN 4;

EID: 84864111699     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0041207     Document Type: Article
Times cited : (15)

References (65)
  • 1
    • 0034518173 scopus 로고    scopus 로고
    • Structural basis for the interaction of tubulin with proteins and drugs that affect microtubule dynamics
    • Downing KH, (2000) Structural basis for the interaction of tubulin with proteins and drugs that affect microtubule dynamics. Annu Rev Cell Dev Biol 16: 89-111.
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 89-111
    • Downing, K.H.1
  • 2
    • 39149121834 scopus 로고    scopus 로고
    • Tubulin modifications and their cellular functions
    • Hammond JW, Cai D, Verhey KJ, (2008) Tubulin modifications and their cellular functions. Curr Opin Cell Biol 20: 71-76.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 71-76
    • Hammond, J.W.1    Cai, D.2    Verhey, K.J.3
  • 3
    • 70350571135 scopus 로고    scopus 로고
    • On and around microtubules: an overview
    • Wade RH, (2009) On and around microtubules: an overview. Mol Biotechnol 43: 177-191.
    • (2009) Mol Biotechnol , vol.43 , pp. 177-191
    • Wade, R.H.1
  • 4
    • 0034237676 scopus 로고    scopus 로고
    • Spindle assembly and the art of regulating microtubule dynamics by MAPs and Stathmin/Op18
    • Andersen SS, (2000) Spindle assembly and the art of regulating microtubule dynamics by MAPs and Stathmin/Op18. Trends Cell Biol 10: 261-267.
    • (2000) Trends Cell Biol , vol.10 , pp. 261-267
    • Andersen, S.S.1
  • 6
    • 79957784767 scopus 로고    scopus 로고
    • Characterization and detection of cellular and proteomic alterations in stable stathmin-overexpressing, taxol-resistant BT549 breast cancer cells using offgel IEF/PAGE difference gel electrophoresis
    • Balasubramani M, Nakao C, Uechi GT, Cardamone J, Kamath K, et al. (2011) Characterization and detection of cellular and proteomic alterations in stable stathmin-overexpressing, taxol-resistant BT549 breast cancer cells using offgel IEF/PAGE difference gel electrophoresis. Mutat Res 722: 154-164.
    • (2011) Mutat Res , vol.722 , pp. 154-164
    • Balasubramani, M.1    Nakao, C.2    Uechi, G.T.3    Cardamone, J.4    Kamath, K.5
  • 7
    • 0032923913 scopus 로고    scopus 로고
    • Dissociation of the tubulin-sequestering and microtubule catastrophe-promoting activities of oncoprotein 18/stathmin
    • Howell B, Larsson N, Gullberg M, Cassimeris L, (1999) Dissociation of the tubulin-sequestering and microtubule catastrophe-promoting activities of oncoprotein 18/stathmin. Mol Biol Cell 10: 105-118.
    • (1999) Mol Biol Cell , vol.10 , pp. 105-118
    • Howell, B.1    Larsson, N.2    Gullberg, M.3    Cassimeris, L.4
  • 8
    • 79951855247 scopus 로고    scopus 로고
    • The ins and outs of tubulin acetylation: more than just a post-translational modification?
    • Perdiz D, Mackeh R, Poüs C, Baillet A, (2011) The ins and outs of tubulin acetylation: more than just a post-translational modification? Cell Signal 23: 763-771.
    • (2011) Cell Signal , vol.23 , pp. 763-771
    • Perdiz, D.1    Mackeh, R.2    Poüs, C.3    Baillet, A.4
  • 9
    • 0345169048 scopus 로고    scopus 로고
    • Post-translational modifications regulate microtubule function
    • Westermann S, 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
  • 10
    • 12244295468 scopus 로고    scopus 로고
    • In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation
    • Matsuyama A, Shimazu T, Sumida Y, Saito A, Yoshimatsu Y, et al. (2002) In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation. EMBO J 21: 6820-6831.
    • (2002) EMBO J , vol.21 , pp. 6820-6831
    • Matsuyama, A.1    Shimazu, T.2    Sumida, Y.3    Saito, A.4    Yoshimatsu, Y.5
  • 11
    • 34250362299 scopus 로고    scopus 로고
    • Cargo transport: two motors are sometimes better than one
    • Gross SP, Vershinin M, Shubeita GT, (2007) Cargo transport: two motors are sometimes better than one. Curr Biol 17: 478-486.
    • (2007) Curr Biol , vol.17 , pp. 478-486
    • Gross, S.P.1    Vershinin, M.2    Shubeita, G.T.3
  • 12
    • 77953140417 scopus 로고    scopus 로고
    • Bidirectional transport: matchmaking for motors
    • Welte MA, (2010) Bidirectional transport: matchmaking for motors. Curr Biol 20: 410-413.
    • (2010) Curr Biol , vol.20 , pp. 410-413
    • Welte, M.A.1
  • 13
    • 21244468590 scopus 로고    scopus 로고
    • Viral stop-and-go along microtubules: taking a ride with dynein and kinesins
    • Döhner K, Nagel CH, Sodeik B, (2005) Viral stop-and-go along microtubules: taking a ride with dynein and kinesins. Trends Microbiol 13: 320-327.
    • (2005) Trends Microbiol , vol.13 , pp. 320-327
    • Döhner, K.1    Nagel, C.H.2    Sodeik, B.3
  • 14
    • 33644822448 scopus 로고    scopus 로고
    • Viral interactions with the cytoskeleton: a hitchhiker's guide to the cell
    • Radtke K, Döhner K, Sodeik B, (2006) Viral interactions with the cytoskeleton: a hitchhiker's guide to the cell. Cell Microbiol 8: 387-400.
    • (2006) Cell Microbiol , vol.8 , pp. 387-400
    • Radtke, K.1    Döhner, K.2    Sodeik, B.3
  • 15
    • 0036437319 scopus 로고    scopus 로고
    • Break ins and break outs: viral interactions with the cytoskeleton of mammalian cells
    • Smith GA, Enquist LW, (2002) Break ins and break outs: viral interactions with the cytoskeleton of mammalian cells. Annu Rev Cell Dev Biol 18: 135-161.
    • (2002) Annu Rev Cell Dev Biol , vol.18 , pp. 135-161
    • Smith, G.A.1    Enquist, L.W.2
  • 16
    • 18744391391 scopus 로고    scopus 로고
    • Plunder and stowaways: incorporation of cellular proteins by enveloped viruses
    • Cantin R, Méthot S, Tremblay MJ, (2005) Plunder and stowaways: incorporation of cellular proteins by enveloped viruses. J Virol 79: 6577-6587.
    • (2005) J Virol , vol.79 , pp. 6577-6587
    • Cantin, R.1    Méthot, S.2    Tremblay, M.J.3
  • 19
    • 35548976680 scopus 로고    scopus 로고
    • Visualization of microtubule-mediated transport of influenza viral progeny ribonucleoprotein
    • Momose F, Kikuchi Y, Komase K, Morikawa Y, (2007) Visualization of microtubule-mediated transport of influenza viral progeny ribonucleoprotein. Microbes Infect 9: 1422-1433.
    • (2007) Microbes Infect , vol.9 , pp. 1422-1433
    • Momose, F.1    Kikuchi, Y.2    Komase, K.3    Morikawa, Y.4
  • 20
    • 77956643301 scopus 로고    scopus 로고
    • Association of the influenza virus RNA polymerase subunit PB2 with the host chaperonin CCT
    • Fislová T, Thomas B, Graef KM, Fodor E, (2010) Association of the influenza virus RNA polymerase subunit PB2 with the host chaperonin CCT. J Virol 84: 8691-8699.
    • (2010) J Virol , vol.84 , pp. 8691-8699
    • Fislová, T.1    Thomas, B.2    Graef, K.M.3    Fodor, E.4
  • 21
    • 79955415241 scopus 로고    scopus 로고
    • A rab11- and microtubule-dependent mechanism for cytoplasmic transport of influenza A virus viral RNA
    • Amorim MJ, Bruce EA, Read EK, Foeglein A, Mahen R, et al. (2011) A rab11- and microtubule-dependent mechanism for cytoplasmic transport of influenza A virus viral RNA. J Virol 85: 4143-4156.
    • (2011) J Virol , vol.85 , pp. 4143-4156
    • Amorim, M.J.1    Bruce, E.A.2    Read, E.K.3    Foeglein, A.4    Mahen, R.5
  • 22
    • 79959439722 scopus 로고    scopus 로고
    • Apical transport of influenza A virus ribonucleoprotein requires Rab11-positive recycling endosome
    • Momose F, Sekimoto T, Ohkura T, Jo S, Kawaguchi A, et al. (2011) Apical transport of influenza A virus ribonucleoprotein requires Rab11-positive recycling endosome. PLoS One 6: e21123.
    • (2011) PLoS One , vol.6
    • Momose, F.1    Sekimoto, T.2    Ohkura, T.3    Jo, S.4    Kawaguchi, A.5
  • 23
    • 78650919694 scopus 로고    scopus 로고
    • Enhanced acetylation of alpha-tubulin in influenza A virus infected epithelial cells
    • Husain M, Harrod KS, (2011) Enhanced acetylation of alpha-tubulin in influenza A virus infected epithelial cells. FEBS Lett 585: 128-132.
    • (2011) FEBS Lett , vol.585 , pp. 128-132
    • Husain, M.1    Harrod, K.S.2
  • 24
    • 80055077509 scopus 로고    scopus 로고
    • Histone deacetylase 8 is required for centrosome cohesion and influenza A virus entry
    • Yamauchi Y, Boukari H, Banerjee I, Sbalzarini IF, Horvath P, et al. (2011) Histone deacetylase 8 is required for centrosome cohesion and influenza A virus entry. PLoS Pathog 7: e1002316.
    • (2011) PLoS Pathog , vol.7
    • Yamauchi, Y.1    Boukari, H.2    Banerjee, I.3    Sbalzarini, I.F.4    Horvath, P.5
  • 25
    • 45849115442 scopus 로고    scopus 로고
    • Host-cell-dependent role of actin cytoskeleton during the replication of a human strain of influenza A virus
    • Arcangeletti MC, De Conto F, Ferraglia F, Pinardi F, Gatti R, et al. (2008) Host-cell-dependent role of actin cytoskeleton during the replication of a human strain of influenza A virus. Arch Virol 153: 1209-1221.
    • (2008) Arch Virol , vol.153 , pp. 1209-1221
    • Arcangeletti, M.C.1    de Conto, F.2    Ferraglia, F.3    Pinardi, F.4    Gatti, R.5
  • 26
    • 78650533541 scopus 로고    scopus 로고
    • Differential infectious entry of human influenza A/NWS/33 virus (H1N1) in mammalian kidney cells
    • De Conto F, Covan S, Arcangeletti MC, Orlandini G, Gatti R, et al. (2011) Differential infectious entry of human influenza A/NWS/33 virus (H1N1) in mammalian kidney cells. Virus Res 155: 221-230.
    • (2011) Virus Res , vol.155 , pp. 221-230
    • de Conto, F.1    Covan, S.2    Arcangeletti, M.C.3    Orlandini, G.4    Gatti, R.5
  • 27
    • 67449089190 scopus 로고    scopus 로고
    • The hepatitis E virus open reading frame 3 product interacts with microtubules and interferes with their dynamics
    • Kannan H, Fan S, Patel D, Bossis I, Zhang YJ, (2009) The hepatitis E virus open reading frame 3 product interacts with microtubules and interferes with their dynamics. J Virol 83: 6375-6382.
    • (2009) J Virol , vol.83 , pp. 6375-6382
    • Kannan, H.1    Fan, S.2    Patel, D.3    Bossis, I.4    Zhang, Y.J.5
  • 28
    • 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
  • 29
    • 0034813059 scopus 로고    scopus 로고
    • African swine fever virus protein p54 interacts with the microtubular motor complex through direct binding to light-chain dynein
    • Alonso C, Miskin J, Hernáez B, Fernandez-Zapatero P, Soto L, et al. (2001) African swine fever virus protein p54 interacts with the microtubular motor complex through direct binding to light-chain dynein. J Virol 75: 9819-9827.
    • (2001) J Virol , vol.75 , pp. 9819-9827
    • Alonso, C.1    Miskin, J.2    Hernáez, B.3    Fernandez-Zapatero, P.4    Soto, L.5
  • 30
    • 0037321752 scopus 로고    scopus 로고
    • Cell penetration and trafficking of polyomavirus
    • Gilbert JM, Goldberg IG, Benjamin TL, (2003) Cell penetration and trafficking of polyomavirus. J Virol 77: 2615-2622.
    • (2003) J Virol , vol.77 , pp. 2615-2622
    • Gilbert, J.M.1    Goldberg, I.G.2    Benjamin, T.L.3
  • 31
    • 11144224272 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus modulates microtubule dynamics via RhoA-GTP-diaphanous 2 signaling and utilizes the dynein motors to deliver its DNA to the nucleus
    • Naranatt PP, Krishnan HH, Smith MS, Chandran B, (2005) Kaposi's sarcoma-associated herpesvirus modulates microtubule dynamics via RhoA-GTP-diaphanous 2 signaling and utilizes the dynein motors to deliver its DNA to the nucleus. J Virol 79: 1191-1206.
    • (2005) J Virol , vol.79 , pp. 1191-1206
    • Naranatt, P.P.1    Krishnan, H.H.2    Smith, M.S.3    Chandran, B.4
  • 32
    • 0035009245 scopus 로고    scopus 로고
    • Endocytic traffic in polarized epithelial cells: role of the actin and microtubule cytoskeleton
    • Apodaca G, (2001) Endocytic traffic in polarized epithelial cells: role of the actin and microtubule cytoskeleton. Traffic 2: 149-159.
    • (2001) Traffic , vol.2 , pp. 149-159
    • Apodaca, G.1
  • 33
    • 0025168710 scopus 로고
    • Differential microtubule requirements for transcytosis in MDCK cells
    • Hunziker W, Mâle P, Mellman I, (1990) Differential microtubule requirements for transcytosis in MDCK cells. EMBO J 9: 3515-3525.
    • (1990) EMBO J , vol.9 , pp. 3515-3525
    • Hunziker, W.1    Mâle, P.2    Mellman, I.3
  • 34
    • 0025518412 scopus 로고
    • Microtubule perturbation inhibits intracellular transport of an apical membrane glycoprotein in a substrate-dependent manner in polarized Madin-Darby canine kidney epithelial cells
    • van Zeijl MJ, Matlin KS, (1990) Microtubule perturbation inhibits intracellular transport of an apical membrane glycoprotein in a substrate-dependent manner in polarized Madin-Darby canine kidney epithelial cells. Cell Regul 1: 921-936.
    • (1990) Cell Regul , vol.1 , pp. 921-936
    • van Zeijl, M.J.1    Matlin, K.S.2
  • 35
    • 0035125270 scopus 로고    scopus 로고
    • Microtubule-independent motility and nuclear targeting of adenoviruses with fluorescently labeled genomes
    • Glotzer JB, Michou AI, Baker A, Saltik M, Cotten M, (2001) Microtubule-independent motility and nuclear targeting of adenoviruses with fluorescently labeled genomes. J Virol 75: 2421-2434.
    • (2001) J Virol , vol.75 , pp. 2421-2434
    • Glotzer, J.B.1    Michou, A.I.2    Baker, A.3    Saltik, M.4    Cotten, M.5
  • 36
    • 79952369523 scopus 로고    scopus 로고
    • Effects of microtubule modulators on HIV-1 infection of transformed and resting CD4 T cells
    • Yoder A, Guo J, Yu D, Cui Z, Zhang XE, et al. (2011) Effects of microtubule modulators on HIV-1 infection of transformed and resting CD4 T cells. J Virol 85: 3020-3024.
    • (2011) J Virol , vol.85 , pp. 3020-3024
    • Yoder, A.1    Guo, J.2    Yu, D.3    Cui, Z.4    Zhang, X.E.5
  • 38
    • 75149131559 scopus 로고    scopus 로고
    • Equine herpesvirus type 1 (EHV-1) utilizes microtubules, dynein, and ROCK1 to productively infect cells
    • Frampton AR Jr, Uchida H, von Einem J, Goins WF, Grandi P, et al. (2010) Equine herpesvirus type 1 (EHV-1) utilizes microtubules, dynein, and ROCK1 to productively infect cells. Vet Microbiol 141: 12-21.
    • (2010) Vet Microbiol , vol.141 , pp. 12-21
    • Frampton Jr., A.R.1    Uchida, H.2    von Einem, J.3    Goins, W.F.4    Grandi, P.5
  • 40
    • 0035976603 scopus 로고    scopus 로고
    • Real-time single-molecule imaging of the infection pathway of an adeno-associated virus
    • Seisenberger G, Ried MU, Endress T, Büning H, Hallek M, et al. (2001) Real-time single-molecule imaging of the infection pathway of an adeno-associated virus. Science 294: 1929-1932.
    • (2001) Science , vol.294 , pp. 1929-1932
    • Seisenberger, G.1    Ried, M.U.2    Endress, T.3    Büning, H.4    Hallek, M.5
  • 41
    • 0141632830 scopus 로고    scopus 로고
    • Exploitation of microtubule cytoskeleton and dynein during parvoviral traffic toward the nucleus
    • Suikkanen S, Aaltonen T, Nevalainen M, Välilehto O, Lindholm L, et al. (2003) Exploitation of microtubule cytoskeleton and dynein during parvoviral traffic toward the nucleus. J Virol 77: 10270-10279.
    • (2003) J Virol , vol.77 , pp. 10270-10279
    • Suikkanen, S.1    Aaltonen, T.2    Nevalainen, M.3    Välilehto, O.4    Lindholm, L.5
  • 42
    • 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
  • 43
    • 33750618516 scopus 로고    scopus 로고
    • Microtubule acetylation promotes kinesin-1 binding and transport
    • Reed NA, Cai D, Blasius TL, Jih GT, Meyhofer E, et al. (2006) Microtubule acetylation promotes kinesin-1 binding and transport. Curr Biol 16: 2166-2172.
    • (2006) Curr Biol , vol.16 , pp. 2166-2172
    • Reed, N.A.1    Cai, D.2    Blasius, T.L.3    Jih, G.T.4    Meyhofer, E.5
  • 44
    • 77951223432 scopus 로고    scopus 로고
    • The microtubule-associated histone deacetylase 6 (HDAC6) regulates epidermal growth factor receptor (EGFR) endocytic trafficking and degradation
    • Gao YS, Hubbert CC, Yao TP, (2010) The microtubule-associated histone deacetylase 6 (HDAC6) regulates epidermal growth factor receptor (EGFR) endocytic trafficking and degradation. J Biol Chem 285: 11219-11226.
    • (2010) J Biol Chem , vol.285 , pp. 11219-11226
    • Gao, Y.S.1    Hubbert, C.C.2    Yao, T.P.3
  • 45
    • 78549296763 scopus 로고    scopus 로고
    • Acetylated microtubules are required for fusion of autophagosomes with lysosomes
    • Xie R, Nguyen S, McKeehan WL, Liu L, (2010) Acetylated microtubules are required for fusion of autophagosomes with lysosomes. BMC Cell Biol 11: 89.
    • (2010) BMC Cell Biol , vol.11 , pp. 89
    • Xie, R.1    Nguyen, S.2    McKeehan, W.L.3    Liu, L.4
  • 46
    • 43949101050 scopus 로고    scopus 로고
    • Microtubule acetylation and stability may explain alcohol-induced alterations in hepatic protein trafficking
    • Joseph RA, Shepard BD, Kannarkat GT, Rutledge TM, Tuma DJ, et al. (2008) Microtubule acetylation and stability may explain alcohol-induced alterations in hepatic protein trafficking. Hepatology 47: 1745-1753.
    • (2008) Hepatology , vol.47 , pp. 1745-1753
    • Joseph, R.A.1    Shepard, B.D.2    Kannarkat, G.T.3    Rutledge, T.M.4    Tuma, D.J.5
  • 47
    • 0036223620 scopus 로고    scopus 로고
    • Reovirus core protein mu2 determines the filamentous morphology of viral inclusion bodies by interacting with and stabilizing microtubules
    • Parker JS, Broering TJ, Kim J, Higgins DE, Nibert ML, (2002) Reovirus core protein mu2 determines the filamentous morphology of viral inclusion bodies by interacting with and stabilizing microtubules. J Virol 76: 4483-4496.
    • (2002) J Virol , vol.76 , pp. 4483-4496
    • Parker, J.S.1    Broering, T.J.2    Kim, J.3    Higgins, D.E.4    Nibert, M.L.5
  • 48
    • 3242707647 scopus 로고    scopus 로고
    • Transport of African swine fever virus from assembly sites to the plasma membrane is dependent on microtubules and conventional kinesin
    • Jouvenet N, Monaghan P, Way M, Wileman T, (2004) Transport of African swine fever virus from assembly sites to the plasma membrane is dependent on microtubules and conventional kinesin. J Virol 78: 7990-8001.
    • (2004) J Virol , vol.78 , pp. 7990-8001
    • Jouvenet, N.1    Monaghan, P.2    Way, M.3    Wileman, T.4
  • 49
    • 16244412942 scopus 로고    scopus 로고
    • Nuclear localizations of the herpes simplex virus type 1 tegument proteins VP13/14, vhs, and VP16 precede VP22-dependent microtubule reorganization and VP22 nuclear import
    • Yedowitz JC, Kotsakis A, Schlegel EF, Blaho JA, (2005) Nuclear localizations of the herpes simplex virus type 1 tegument proteins VP13/14, vhs, and VP16 precede VP22-dependent microtubule reorganization and VP22 nuclear import. J Virol 79: 4730-4743.
    • (2005) J Virol , vol.79 , pp. 4730-4743
    • Yedowitz, J.C.1    Kotsakis, A.2    Schlegel, E.F.3    Blaho, J.A.4
  • 50
    • 35448990549 scopus 로고    scopus 로고
    • The contributions of microtubule stability and dynamic instability to adenovirus nuclear localization efficiency
    • Warren JC, Cassimeris L, (2007) The contributions of microtubule stability and dynamic instability to adenovirus nuclear localization efficiency. Cell Motil Cytoskeleton 64: 675-689.
    • (2007) Cell Motil Cytoskeleton , vol.64 , pp. 675-689
    • Warren, J.C.1    Cassimeris, L.2
  • 51
    • 37549010715 scopus 로고    scopus 로고
    • Histone deacetylase 6 regulates growth factor-induced actin remodeling and endocytosis
    • Gao YS, Hubbert CC, Lu J, Lee YS, Lee JY, et al. (2007) Histone deacetylase 6 regulates growth factor-induced actin remodeling and endocytosis. Mol Cell Biol 27: 8637-8647.
    • (2007) Mol Cell Biol , vol.27 , pp. 8637-8647
    • Gao, Y.S.1    Hubbert, C.C.2    Lu, J.3    Lee, Y.S.4    Lee, J.Y.5
  • 52
    • 48249098842 scopus 로고    scopus 로고
    • GEF-H1 couples nocodazole-induced microtubule disassembly to cell contractility via RhoA
    • Chang YC, Nalbant P, Birkenfeld J, Chang ZF, Bokoch GM, (2008) GEF-H1 couples nocodazole-induced microtubule disassembly to cell contractility via RhoA. Mol Biol Cell 19: 2147-2153.
    • (2008) Mol Biol Cell , vol.19 , pp. 2147-2153
    • Chang, Y.C.1    Nalbant, P.2    Birkenfeld, J.3    Chang, Z.F.4    Bokoch, G.M.5
  • 53
    • 0019292829 scopus 로고
    • Widespread distribution of a 210,000 mol wt microtubule-associated protein in cells and tissues of primates
    • Bulinski JC, Borisy GG, (1980) Widespread distribution of a 210,000 mol wt microtubule-associated protein in cells and tissues of primates. J Cell Biol 87: 802-808.
    • (1980) J Cell Biol , vol.87 , pp. 802-808
    • Bulinski, J.C.1    Borisy, G.G.2
  • 54
    • 0037172666 scopus 로고    scopus 로고
    • MAP4 counteracts microtubule catastrophe promotion but not tubulin-sequestering activity in intact cells
    • Holmfeldt P, Brattsand G, Gullberg M, (2002) MAP4 counteracts microtubule catastrophe promotion but not tubulin-sequestering activity in intact cells. Curr Biol 12: 1034-1039.
    • (2002) Curr Biol , vol.12 , pp. 1034-1039
    • Holmfeldt, P.1    Brattsand, G.2    Gullberg, M.3
  • 55
    • 0021717133 scopus 로고
    • MAP 4: a microtubule-associated protein specific for a subset of tissue microtubules
    • Parysek LM, Wolosewick JJ, Olmsted JB, (1984) MAP 4: a microtubule-associated protein specific for a subset of tissue microtubules. J Cell Biol 99: 2287-2296.
    • (1984) J Cell Biol , vol.99 , pp. 2287-2296
    • Parysek, L.M.1    Wolosewick, J.J.2    Olmsted, J.B.3
  • 56
    • 0028945057 scopus 로고
    • Microtubules and microtubule-associated proteins
    • Mandelkow E, Mandelkow EM, (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
  • 57
    • 0011214518 scopus 로고    scopus 로고
    • Removal of MAP4 from microtubules in vivo produces no observable phenotype at the cellular level
    • Wang XM, Peloquin JG, Zhai Y, Bulinski JC, Borisy GG, (1996) Removal of MAP4 from microtubules in vivo produces no observable phenotype at the cellular level. J Cell Biol 132: 345-357.
    • (1996) J Cell Biol , vol.132 , pp. 345-357
    • Wang, X.M.1    Peloquin, J.G.2    Zhai, Y.3    Bulinski, J.C.4    Borisy, G.G.5
  • 58
    • 0031469160 scopus 로고    scopus 로고
    • Overexpression of MAP4 inhibits organelle motility and trafficking in vivo
    • Bulinski JC, McGraw TE, Gruber D, Nguyen HL, Sheetz MP, (1997) Overexpression of MAP4 inhibits organelle motility and trafficking in vivo. J Cell Sci 110: 3055-3064.
    • (1997) J Cell Sci , vol.110 , pp. 3055-3064
    • Bulinski, J.C.1    McGraw, T.E.2    Gruber, D.3    Nguyen, H.L.4    Sheetz, M.P.5
  • 59
    • 50249139544 scopus 로고    scopus 로고
    • The individualization of cancer therapy: the unexpected role of p53
    • Hait WN, Yang JM, (2006) The individualization of cancer therapy: the unexpected role of p53. Trans Am Clin Climatol Assoc 117: 85-101.
    • (2006) Trans Am Clin Climatol Assoc , vol.117 , pp. 85-101
    • Hait, W.N.1    Yang, J.M.2
  • 60
    • 0029126160 scopus 로고
    • Poliovirus protease 3C mediates cleavage of microtubule-associated protein 4
    • Joachims M, Harris KS, Etchison D, (1995) Poliovirus protease 3C mediates cleavage of microtubule-associated protein 4. Virology 211: 451-461.
    • (1995) Virology , vol.211 , pp. 451-461
    • Joachims, M.1    Harris, K.S.2    Etchison, D.3
  • 61
    • 33646104431 scopus 로고    scopus 로고
    • Tubulin-mediated binding of human immunodeficiency virus-1 Tat to the cytoskeleton causes proteasomal-dependent degradation of microtubule-associated protein 2 and neuronal damage
    • Aprea S, Del Valle L, Mameli G, Sawaya BE, Khalili K, et al. (2006) Tubulin-mediated binding of human immunodeficiency virus-1 Tat to the cytoskeleton causes proteasomal-dependent degradation of microtubule-associated protein 2 and neuronal damage. J Neurosci 26: 4054-4062.
    • (2006) J Neurosci , vol.26 , pp. 4054-4062
    • Aprea, S.1    Del Valle, L.2    Mameli, G.3    Sawaya, B.E.4    Khalili, K.5
  • 62
    • 79953226634 scopus 로고    scopus 로고
    • Microtubule-associated protein 1S (MAP1S) bridges autophagic components with microtubules and mitochondria to affect autophagosomal biogenesis and degradation
    • Xie R, Nguyen S, McKeehan K, Wang F, McKeehan WL, et al. (2011) Microtubule-associated protein 1S (MAP1S) bridges autophagic components with microtubules and mitochondria to affect autophagosomal biogenesis and degradation. J Biol Chem 286: 10367-10377.
    • (2011) J Biol Chem , vol.286 , pp. 10367-10377
    • Xie, R.1    Nguyen, S.2    McKeehan, K.3    Wang, F.4    McKeehan, W.L.5
  • 63
    • 33748154216 scopus 로고    scopus 로고
    • Induction of autophagy in axonal dystrophy and degeneration
    • Wang QJ, Ding Y, Kohtz DS, Mizushima N, Cristea IM, et al. (2006) Induction of autophagy in axonal dystrophy and degeneration. J Neurosci 26: 8057-8068.
    • (2006) J Neurosci , vol.26 , pp. 8057-8068
    • Wang, Q.J.1    Ding, Y.2    Kohtz, D.S.3    Mizushima, N.4    Cristea, I.M.5
  • 64
    • 67549132527 scopus 로고    scopus 로고
    • The late stages of autophagy: how does the end begin?
    • Noda T, Fujita N, Yoshimori T, (2009) The late stages of autophagy: how does the end begin? Cell Death Differ 16: 984-990.
    • (2009) Cell Death Differ , vol.16 , pp. 984-990
    • Noda, T.1    Fujita, N.2    Yoshimori, T.3
  • 65
    • 65249090334 scopus 로고    scopus 로고
    • Autophagy is involved in influenza A virus replication
    • Zhou Z, Jiang X, Liu D, Fan Z, Hu X, et al. (2009) Autophagy is involved in influenza A virus replication. Autophagy 5: 321-328.
    • (2009) Autophagy , vol.5 , pp. 321-328
    • Zhou, Z.1    Jiang, X.2    Liu, D.3    Fan, Z.4    Hu, X.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.