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Volumn 12, Issue 1, 2012, Pages

Evolution of the eukaryotic dynactin complex, the activator of cytoplasmic dynein

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEXATION; CYTOPLASM; EUKARYOTE; GENOME; PHYLOGENETICS; PROTEIN; TREE;

EID: 84862531800     PISSN: None     EISSN: 14712148     Source Type: Journal    
DOI: 10.1186/1471-2148-12-95     Document Type: Article
Times cited : (32)

References (121)
  • 1
    • 0026345013 scopus 로고
    • Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein
    • 10.1083/jcb.115.6.1639 1836789
    • Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein. Gill SR, Schroer TA, Szilak I, Steuer ER, Sheetz MP, Cleveland DW, J Cell Biol 1991 115 1639 1650 10.1083/jcb.115.6.1639 1836789
    • (1991) J Cell Biol , vol.115 , pp. 1639-1650
    • Gill, S.R.1    Schroer, T.A.2    Szilak, I.3    Steuer, E.R.4    Sheetz, M.P.5    Cleveland, D.W.6
  • 2
    • 0025789647 scopus 로고
    • Two activators of microtubule-based vesicle transport
    • 10.1083/jcb.115.5.1309 1835460
    • Two activators of microtubule-based vesicle transport. Schroer TA, Sheetz MP, J Cell Biol 1991 115 1309 1318 10.1083/jcb.115.5.1309 1835460
    • (1991) J Cell Biol , vol.115 , pp. 1309-1318
    • Schroer, T.A.1    Sheetz, M.P.2
  • 3
    • 0030803260 scopus 로고    scopus 로고
    • The involvement of the intermediate chain of cytoplasmic dynein in binding the motor complex to membranous organelles of Xenopus oocytes
    • 9348543
    • The involvement of the intermediate chain of cytoplasmic dynein in binding the motor complex to membranous organelles of Xenopus oocytes. Steffen W, Karki S, Vaughan KT, Vallee RB, Holzbaur EL, Weiss DG, Kuznetsov SA, Mol Biol Cell 1997 8 2077 2088 9348543
    • (1997) Mol Biol Cell , vol.8 , pp. 2077-2088
    • Steffen, W.1    Karki, S.2    Vaughan, K.T.3    Vallee, R.B.4    Holzbaur, E.L.5    Weiss, D.G.6    Kuznetsov, S.A.7
  • 5
    • 0033789351 scopus 로고    scopus 로고
    • Dynactin increases the processivity of the cytoplasmic dynein motor
    • 10.1038/71338 10620802
    • Dynactin increases the processivity of the cytoplasmic dynein motor. King SJ, Schroer TA, Nat Cell Biol 2000 2 20 24 10.1038/71338 10620802
    • (2000) Nat Cell Biol , vol.2 , pp. 20-24
    • King, S.J.1    Schroer, T.A.2
  • 6
    • 33744826279 scopus 로고    scopus 로고
    • Processive bidirectional motion of dynein-dynactin complexes in vitro
    • 10.1038/ncb1421 16715075
    • Processive bidirectional motion of dynein-dynactin complexes in vitro. Ross JL, Wallace K, Shuman H, Goldman YE, Holzbaur EL, Nat Cell Biol 2006 8 562 570 10.1038/ncb1421 16715075
    • (2006) Nat Cell Biol , vol.8 , pp. 562-570
    • Ross, J.L.1    Wallace, K.2    Shuman, H.3    Goldman, Y.E.4    Holzbaur, E.L.5
  • 7
    • 33644747344 scopus 로고    scopus 로고
    • A microtubule-binding domain in dynactin increases dynein processivity by skating along microtubules
    • 10.1038/ncb1370 16474384
    • A microtubule-binding domain in dynactin increases dynein processivity by skating along microtubules. Culver-Hanlon TL, Lex SA, Stephens AD, Quintyne NJ, King SJ, Nat Cell Biol 2006 8 264 270 10.1038/ncb1370 16474384
    • (2006) Nat Cell Biol , vol.8 , pp. 264-270
    • Culver-Hanlon, T.L.1    Lex, S.A.2    Stephens, A.D.3    Quintyne, N.J.4    King, S.J.5
  • 8
    • 65249170094 scopus 로고    scopus 로고
    • Regulation of the processivity and intracellular localization of Saccharomyces cerevisiae dynein by dynactin
    • 10.1073/pnas.0900976106 19293377
    • Regulation of the processivity and intracellular localization of Saccharomyces cerevisiae dynein by dynactin. Kardon JR, Reck-Peterson SL, Vale RD, Proc Natl Acad Sci USA 2009 106 5669 5674 10.1073/pnas.0900976106 19293377
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 5669-5674
    • Kardon, J.R.1    Reck-Peterson, S.L.2    Vale, R.D.3
  • 9
    • 0037191081 scopus 로고    scopus 로고
    • Distinct cell cycle-dependent roles for dynactin and dynein at centrosomes
    • 10.1083/jcb.200203089 12391026
    • Distinct cell cycle-dependent roles for dynactin and dynein at centrosomes. Quintyne NJ, Schroer TA, J Cell Biol 2002 159 245 254 10.1083/jcb.200203089 12391026
    • (2002) J Cell Biol , vol.159 , pp. 245-254
    • Quintyne, N.J.1    Schroer, T.A.2
  • 11
    • 0037198709 scopus 로고    scopus 로고
    • Dynactin is necessary for synapse stabilization
    • 10.1016/S0896-6273(02)00721-3 12062020
    • Dynactin is necessary for synapse stabilization. Eaton BA, Fetter RD, Davis GW, Neuron 2002 34 729 741 10.1016/S0896-6273(02)00721-3 12062020
    • (2002) Neuron , vol.34 , pp. 729-741
    • Eaton, B.A.1    Fetter, R.D.2    Davis, G.W.3
  • 12
    • 0035945356 scopus 로고    scopus 로고
    • Cytoplasmic dynein/dynactin drives kinetochore protein transport to the spindle poles and has a role in mitotic spindle checkpoint inactivation
    • 10.1083/jcb.200105093 11756470
    • Cytoplasmic dynein/dynactin drives kinetochore protein transport to the spindle poles and has a role in mitotic spindle checkpoint inactivation. Howell BJ, McEwen BF, Canman JC, Hoffman DB, Farrar EM, Rieder CL, Salmon ED, J Cell Biol 2001 155 1159 1172 10.1083/jcb.200105093 11756470
    • (2001) J Cell Biol , vol.155 , pp. 1159-1172
    • Howell, B.J.1    McEwen, B.F.2    Canman, J.C.3    Hoffman, D.B.4    Farrar, E.M.5    Rieder, C.L.6    Salmon, E.D.7
  • 13
    • 0037415644 scopus 로고    scopus 로고
    • The role of the lissencephaly protein Pac1 during nuclear migration in budding yeast
    • 10.1083/jcb.200209022 12566428
    • The role of the lissencephaly protein Pac1 during nuclear migration in budding yeast. Lee WL, Oberle JR, Cooper JA, J Cell Biol 2003 160 355 364 10.1083/jcb.200209022 12566428
    • (2003) J Cell Biol , vol.160 , pp. 355-364
    • Lee, W.L.1    Oberle, J.R.2    Cooper, J.A.3
  • 14
    • 0030298137 scopus 로고    scopus 로고
    • A complex of numa and cytoplasmic dynein is essential for mitotic spindle assembly
    • 10.1016/S0092-8674(00)81365-3 8898198
    • A Complex of NuMA and Cytoplasmic Dynein Is Essential for Mitotic Spindle Assembly. Merdes A, Ramyar K, Vechio JD, Cleveland DW, Cell 1996 87 447 458 10.1016/S0092-8674(00)81365-3 8898198
    • (1996) Cell , vol.87 , pp. 447-458
    • Merdes, A.1    Ramyar, K.2    Vechio, J.D.3    Cleveland, D.W.4
  • 15
    • 33847343375 scopus 로고    scopus 로고
    • Microtubule binding by dynactin is required for microtubule organization but not cargo transport
    • 10.1083/jcb.200608128 17325206
    • Microtubule binding by dynactin is required for microtubule organization but not cargo transport. Kim H, Ling S-C, Rogers GC, Kural C, Selvin PR, Rogers SL, Gelfand VI, J Cell Biol 2007 176 641 651 10.1083/jcb.200608128 17325206
    • (2007) J Cell Biol , vol.176 , pp. 641-651
    • Kim, H.1    Ling, S.-C.2    Rogers, G.C.3    Kural, C.4    Selvin, P.R.5    Rogers, S.L.6    Gelfand, V.I.7
  • 17
    • 33846199544 scopus 로고    scopus 로고
    • Dynactin enhances the processivity of kinesin-2
    • 10.1111/j.1600-0854.2006.00517.x 17181772
    • Dynactin enhances the processivity of kinesin-2. Berezuk MA, Schroer TA, Traffic 2007 8 124 129 10.1111/j.1600-0854.2006.00517.x 17181772
    • (2007) Traffic , vol.8 , pp. 124-129
    • Berezuk, M.A.1    Schroer, T.A.2
  • 18
    • 0030612145 scopus 로고    scopus 로고
    • Phosphorylation by p34cdc2 protein kinase regulates binding of the kinesin-related motor HsEg5 to the dynactin subunit p150
    • 10.1074/jbc.272.31.19418 9235942
    • Phosphorylation by p34cdc2 protein kinase regulates binding of the kinesin-related motor HsEg5 to the dynactin subunit p150. Blangy A, Arnaud L, Nigg EA, J Biol Chem 1997 272 19418 19424 10.1074/jbc.272.31.19418 9235942
    • (1997) J Biol Chem , vol.272 , pp. 19418-19424
    • Blangy, A.1    Arnaud, L.2    Nigg, E.A.3
  • 19
    • 4444249640 scopus 로고    scopus 로고
    • Dynactin
    • 10.1146/annurev.cellbio.20.012103.094623 15473859
    • Dynactin. Schroer TA, Annu Rev Cell Dev Biol 2004 20 759 779 10.1146/annurev.cellbio.20.012103.094623 15473859
    • (2004) Annu Rev Cell Dev Biol , vol.20 , pp. 759-779
    • Schroer, T.A.1
  • 21
    • 0032728976 scopus 로고    scopus 로고
    • Analysis of dynactin subcomplexes reveals a novel actin-related protein associated with the arp1 minifilament pointed end
    • 10.1083/jcb.147.2.307 10525537
    • Analysis of dynactin subcomplexes reveals a novel actin-related protein associated with the arp1 minifilament pointed end. Eckley DM, Gill SR, Melkonian KA, Bingham JB, Goodson HV, Heuser JE, Schroer TA, J Cell Biol 1999 147 307 320 10.1083/jcb.147.2.307 10525537
    • (1999) J Cell Biol , vol.147 , pp. 307-320
    • Eckley, D.M.1    Gill, S.R.2    Melkonian, K.A.3    Bingham, J.B.4    Goodson, H.V.5    Heuser, J.E.6    Schroer, T.A.7
  • 22
    • 0028304474 scopus 로고
    • Ultrastructural analysis of the dynactin complex: An actin-related protein is a component of a filament that resembles F-actin
    • 10.1083/jcb.126.2.403 7518465
    • Ultrastructural analysis of the dynactin complex: an actin-related protein is a component of a filament that resembles F-actin. Schafer DA, Gill SR, Cooper JA, Heuser JE, Schroer TA, J Cell Biol 1994 126 403 412 10.1083/jcb.126.2.403 7518465
    • (1994) J Cell Biol , vol.126 , pp. 403-412
    • Schafer, D.A.1    Gill, S.R.2    Cooper, J.A.3    Heuser, J.E.4    Schroer, T.A.5
  • 23
    • 0028986631 scopus 로고
    • The p150Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1)
    • 10.1073/pnas.92.5.1634 7878030
    • The p150Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1). Waterman-Storer CM, Karki S, Holzbaur EL, Proc Natl Acad Sci U S A 1995 92 1634 1638 10.1073/pnas.92.5.1634 7878030
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 1634-1638
    • Waterman-Storer, C.M.1    Karki, S.2    Holzbaur, E.L.3
  • 24
    • 12344320203 scopus 로고    scopus 로고
    • Microtubule plus-end-tracking proteins: Mechanisms and functions
    • 10.1016/j.ceb.2004.11.001 15661518
    • Microtubule plus-end-tracking proteins: mechanisms and functions. Akhmanova A, Hoogenraad CC, Curr Opin Cell Biol 2005 17 47 54 10.1016/j.ceb.2004.11.001 15661518
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 47-54
    • Akhmanova, A.1    Hoogenraad, C.C.2
  • 26
    • 0029563632 scopus 로고
    • Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p150Glued
    • 10.1083/jcb.131.6.1507 8522607
    • Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p150Glued. Vaughan KT, Vallee RB, J Cell Biol 1995 131 1507 1516 10.1083/jcb.131.6.1507 8522607
    • (1995) J Cell Biol , vol.131 , pp. 1507-1516
    • Vaughan, K.T.1    Vallee, R.B.2
  • 27
    • 0028806377 scopus 로고
    • Affinity chromatography demonstrates a direct binding between cytoplasmic dynein and the dynactin complex
    • 10.1074/jbc.270.48.28806 7499404
    • Affinity chromatography demonstrates a direct binding between cytoplasmic dynein and the dynactin complex. Karki S, Holzbaur EL, J Biol Chem 1995 270 28806 28811 10.1074/jbc.270.48.28806 7499404
    • (1995) J Biol Chem , vol.270 , pp. 28806-28811
    • Karki, S.1    Holzbaur, E.L.2
  • 28
    • 0029913484 scopus 로고    scopus 로고
    • Molecular characterization of the 50-kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization during mitosis
    • 10.1083/jcb.132.4.617 8647893
    • Molecular characterization of the 50-kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization during mitosis. Echeverri CJ, Paschal BM, Vaughan KT, Vallee RB, J Cell Biol 1996 132 617 633 10.1083/jcb.132.4.617 8647893
    • (1996) J Cell Biol , vol.132 , pp. 617-633
    • Echeverri, C.J.1    Paschal, B.M.2    Vaughan, K.T.3    Vallee, R.B.4
  • 29
    • 77954939494 scopus 로고    scopus 로고
    • Molecular and functional basis for the scaffolding role of the p50/dynamitin subunit of the microtubule-associated dynactin complex
    • 10.1074/jbc.M110.100602 20463029
    • Molecular and functional basis for the scaffolding role of the p50/dynamitin subunit of the microtubule-associated dynactin complex. Jacquot G, Maidou-Peindara P, Benichou S, J Biol Chem 2010 285 23019 23031 10.1074/jbc.M110.100602 20463029
    • (2010) J Biol Chem , vol.285 , pp. 23019-23031
    • Jacquot, G.1    Maidou-Peindara, P.2    Benichou, S.3
  • 30
    • 34547118366 scopus 로고    scopus 로고
    • Mechanism of dynamitin-mediated disruption of dynactin
    • 10.1074/jbc.M700003200 17449914
    • Mechanism of Dynamitin-mediated Disruption of Dynactin. Melkonian KA, Maier KC, Godfrey JE, Rodgers M, Schroer TA, J Biol Chem 2007 282 19355 19364 10.1074/jbc.M700003200 17449914
    • (2007) J Biol Chem , vol.282 , pp. 19355-19364
    • Melkonian, K.A.1    Maier, K.C.2    Godfrey, J.E.3    Rodgers, M.4    Schroer, T.A.5
  • 31
    • 77958578801 scopus 로고    scopus 로고
    • Caenorhabditis elegans ortholog of the p24/p22 subunit, DNC-3, is essential for the formation of the dynactin complex by bridging DNC-1/p150Glued and DNC-2/dynamitin
    • 10.1111/j.1365-2443.2010.01451.x 20964796
    • Caenorhabditis elegans ortholog of the p24/p22 subunit, DNC-3, is essential for the formation of the dynactin complex by bridging DNC-1/p150Glued and DNC-2/dynamitin. Terasawa M, Toya M, Motegi F, Mana M, Nakamura K, Sugimoto A, Genes Cells 2010 15 1145 1157 10.1111/j.1365-2443.2010.01451.x 20964796
    • (2010) Genes Cells , vol.15 , pp. 1145-1157
    • Terasawa, M.1    Toya, M.2    Motegi, F.3    Mana, M.4    Nakamura, K.5    Sugimoto, A.6
  • 32
    • 0030479303 scopus 로고    scopus 로고
    • Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles
    • 10.1083/jcb.135.6.1815 8991093
    • Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles. Holleran EA, Tokito MK, Karki S, Holzbaur EL, J Cell Biol 1996 135 1815 1829 10.1083/jcb.135.6.1815 8991093
    • (1996) J Cell Biol , vol.135 , pp. 1815-1829
    • Holleran, E.A.1    Tokito, M.K.2    Karki, S.3    Holzbaur, E.L.4
  • 33
    • 33749015997 scopus 로고    scopus 로고
    • Microtubule motors at the intersection of trafficking and transport
    • 10.1016/j.tcb.2006.08.002 16938456
    • Microtubule motors at the intersection of trafficking and transport. Caviston JP, Holzbaur ELF, Trends Cell Biol 2006 16 530 537 10.1016/j.tcb.2006. 08.002 16938456
    • (2006) Trends Cell Biol , vol.16 , pp. 530-537
    • Caviston, J.P.1    Holzbaur, E.L.F.2
  • 34
    • 0035166330 scopus 로고    scopus 로고
    • Null mutants of the neurospora actin-related protein 1 pointed-end complex show distinct phenotypes
    • 11452013
    • Null Mutants of the Neurospora Actin-related Protein 1 Pointed-End Complex Show Distinct Phenotypes. Lee IH, Kumar S, Plamann M, Mol Biol Cell 2001 12 2195 2206 11452013
    • (2001) Mol Biol Cell , vol.12 , pp. 2195-2206
    • Lee, I.H.1    Kumar, S.2    Plamann, M.3
  • 35
    • 0028067033 scopus 로고
    • Cytoplasmic dynein and actin-related protein Arp1 are required for normal nuclear distribution in filamentous fungi
    • 10.1083/jcb.127.1.139 7929559
    • Cytoplasmic dynein and actin-related protein Arp1 are required for normal nuclear distribution in filamentous fungi. Plamann M, Minke PF, Tinsley JH, Bruno KS, J Cell Biol 1994 127 139 149 10.1083/jcb.127.1.139 7929559
    • (1994) J Cell Biol , vol.127 , pp. 139-149
    • Plamann, M.1    Minke, P.F.2    Tinsley, J.H.3    Bruno, K.S.4
  • 36
    • 0029034391 scopus 로고
    • A fungal actin-related protein involved in nuclear migration
    • 10.1007/BF00290350 7603438
    • A fungal actin-related protein involved in nuclear migration. Robb MJ, Wilson MA, Vierula PJ, Mol Gen Genet 1995 247 583 590 10.1007/BF00290350 7603438
    • (1995) Mol Gen Genet , vol.247 , pp. 583-590
    • Robb, M.J.1    Wilson, M.A.2    Vierula, P.J.3
  • 37
    • 0030943888 scopus 로고    scopus 로고
    • A gene required for nuclear migration in Neurospora crassa codes for a protein with cysteine-rich, LIM/RING-like domains
    • 10.1046/j.1365-2958.1997.3461704.x 9159520
    • A gene required for nuclear migration in Neurospora crassa codes for a protein with cysteine-rich, LIM/RING-like domains. Vierula PJ, Mais JM, Mol Microbiol 1997 24 331 340 10.1046/j.1365-2958.1997.3461704.x 9159520
    • (1997) Mol Microbiol , vol.24 , pp. 331-340
    • Vierula, P.J.1    Mais, J.M.2
  • 38
    • 0029658940 scopus 로고    scopus 로고
    • P150Glued, the largest subunit of the dynactin complex, is nonessential in Neurospora but required for nuclear distribution
    • 8744947
    • p150Glued, the largest subunit of the dynactin complex, is nonessential in Neurospora but required for nuclear distribution. Tinsley JH, Minke PF, Bruno KS, Plamann M, Mol Biol Cell 1996 7 731 742 8744947
    • (1996) Mol Biol Cell , vol.7 , pp. 731-742
    • Tinsley, J.H.1    Minke, P.F.2    Bruno, K.S.3    Plamann, M.4
  • 39
    • 0029978499 scopus 로고    scopus 로고
    • Genetic interactions among cytoplasmic dynein, dynactin, and nuclear distribution mutants of Neurospora crassa
    • 10.1073/pnas.93.10.4775 8643479
    • Genetic interactions among cytoplasmic dynein, dynactin, and nuclear distribution mutants of Neurospora crassa. Bruno KS, Tinsley JH, Minke PF, Plamann M, Proc Natl Acad Sci U S A 1996 93 4775 4780 10.1073/pnas.93.10.4775 8643479
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 4775-4780
    • Bruno, K.S.1    Tinsley, J.H.2    Minke, P.F.3    Plamann, M.4
  • 40
    • 40849141236 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Homolog of p24 Is Essential for Maintaining the Association of p150Glued with the Dynactin Complex
    • 10.1534/genetics.107.079103 18245366
    • The Saccharomyces cerevisiae Homolog of p24 Is Essential for Maintaining the Association of p150Glued With the Dynactin Complex. Amaro IA, Costanzo M, Boone C, Huffaker TC, Genetics 2008 178 703 709 10.1534/genetics.107.079103 18245366
    • (2008) Genetics , vol.178 , pp. 703-709
    • Amaro, I.A.1    Costanzo, M.2    Boone, C.3    Huffaker, T.C.4
  • 41
    • 31944450213 scopus 로고    scopus 로고
    • Arp10p is a pointed-end-associated component of yeast dynactin
    • 16291862
    • Arp10p is a pointed-end-associated component of yeast dynactin. Clark SW, Rose MD, Mol Biol Cell 2006 17 738 748 16291862
    • (2006) Mol Biol Cell , vol.17 , pp. 738-748
    • Clark, S.W.1    Rose, M.D.2
  • 42
    • 0031845220 scopus 로고    scopus 로고
    • The yeast dynactin complex is involved in partitioning the mitotic spindle between mother and daughter cells during anaphase B
    • 9658168
    • The yeast dynactin complex is involved in partitioning the mitotic spindle between mother and daughter cells during anaphase B. Kahana JA, Schlenstedt G, Evanchuk DM, Geiser JR, Hoyt MA, Silver PA, Mol Biol Cell 1998 9 1741 1756 9658168
    • (1998) Mol Biol Cell , vol.9 , pp. 1741-1756
    • Kahana, J.A.1    Schlenstedt, G.2    Evanchuk, D.M.3    Geiser, J.R.4    Hoyt, M.A.5    Silver, P.A.6
  • 43
    • 0028025571 scopus 로고
    • A yeast actin-related protein homologous to that in vertebrate dynactin complex is important for spindle orientation and nuclear migration
    • 10.1016/0092-8674(94)90531-2 8069915
    • A yeast actin-related protein homologous to that in vertebrate dynactin complex is important for spindle orientation and nuclear migration. Muhua L, Karpova TS, Cooper JA, Cell 1994 78 669 679 10.1016/0092-8674(94)90531-2 8069915
    • (1994) Cell , vol.78 , pp. 669-679
    • Muhua, L.1    Karpova, T.S.2    Cooper, J.A.3
  • 44
    • 0025891138 scopus 로고
    • Homology of a 150K cytoplasmic dynein-associated polypeptide with the Drosophila gene Glued
    • 10.1038/351579a0 1828535
    • Homology of a 150K cytoplasmic dynein-associated polypeptide with the Drosophila gene Glued. Holzbaur ELF, Hammarback JA, Paschal BM, Kravit NG, Pfister KK, Vallee RB, Nature 1991 351 579 583 10.1038/351579a0 1828535
    • (1991) Nature , vol.351 , pp. 579-583
    • Holzbaur, E.L.F.1    Hammarback, J.A.2    Paschal, B.M.3    Kravit, N.G.4    Pfister, K.K.5    Vallee, R.B.6
  • 45
    • 0038107541 scopus 로고    scopus 로고
    • Interactions between the evolutionarily conserved, actin-related protein, arp11, actin, and arp1
    • 10.1091/mbc.E03-01-0049 12857853
    • Interactions between the Evolutionarily Conserved, Actin-related Protein, Arp11, Actin, and Arp1. Eckley DM, Schroer TA, Mol Biol Cell 2003 14 2645 2654 10.1091/mbc.E03-01-0049 12857853
    • (2003) Mol Biol Cell , vol.14 , pp. 2645-2654
    • Eckley, D.M.1    Schroer, T.A.2
  • 46
    • 0032497694 scopus 로고    scopus 로고
    • The dynactin complex is required for cleavage plane specification in early Caenorhabditis elegans embryos
    • 10.1016/S0960-9822(98)70465-8 9778526
    • The dynactin complex is required for cleavage plane specification in early Caenorhabditis elegans embryos. Skop AR, White JG, Curr Biol 1998 8 1110 1116 10.1016/S0960-9822(98)70465-8 9778526
    • (1998) Curr Biol , vol.8 , pp. 1110-1116
    • Skop, A.R.1    White, J.G.2
  • 47
    • 0342265157 scopus 로고    scopus 로고
    • Cytoplasmic dynein is required for distinct aspects of MTOC positioning, including centrosome separation, in the one cell stage Caenorhabditis elegans embryo
    • 10.1083/jcb.147.1.135 10508861
    • Cytoplasmic dynein is required for distinct aspects of MTOC positioning, including centrosome separation, in the one cell stage Caenorhabditis elegans embryo. Gönczy P, Pichler S, Kirkham M, Hyman AA, J Cell Biol 1999 147 135 150 10.1083/jcb.147.1.135 10508861
    • (1999) J Cell Biol , vol.147 , pp. 135-150
    • Gönczy, P.1    Pichler, S.2    Kirkham, M.3    Hyman, A.A.4
  • 48
    • 65449172831 scopus 로고    scopus 로고
    • Reconstructing the phylogeny of 21 completely sequenced arthropod species based on their motor proteins
    • 10.1186/1471-2164-10-173 19383156
    • Reconstructing the phylogeny of 21 completely sequenced arthropod species based on their motor proteins. Odronitz F, Becker S, Kollmar M, BMC Genomics 2009 10 173 10.1186/1471-2164-10-173 19383156
    • (2009) BMC Genomics , vol.10 , pp. 173
    • Odronitz, F.1    Becker, S.2    Kollmar, M.3
  • 49
    • 84859898660 scopus 로고    scopus 로고
    • A beginner's guide to eukaryotic genome annotation
    • 10.1038/nrg3174 22510764
    • A beginner's guide to eukaryotic genome annotation. Yandell M, Ence D, Nat Rev Genet 2012 13 329 342 10.1038/nrg3174 22510764
    • (2012) Nat Rev Genet , vol.13 , pp. 329-342
    • Yandell, M.1    Ence, D.2
  • 50
    • 37549069575 scopus 로고    scopus 로고
    • Drawing the tree of eukaryotic life based on the analysis of 2,269 manually annotated myosins from 328 species
    • 10.1186/gb-2007-8-9-r196 17877792
    • Drawing the tree of eukaryotic life based on the analysis of 2,269 manually annotated myosins from 328 species. Odronitz F, Kollmar M, Genome Biol 2007 8 196 10.1186/gb-2007-8-9-r196 17877792
    • (2007) Genome Biol , vol.8 , pp. 18196
    • Odronitz, F.1    Kollmar, M.2
  • 51
    • 80053173098 scopus 로고    scopus 로고
    • A holistic phylogeny of the coronin gene family reveals an ancient origin of the tandem-coronin, defines a new subfamily, and predicts protein function
    • 10.1186/1471-2148-11-268 21943019
    • A holistic phylogeny of the coronin gene family reveals an ancient origin of the tandem-coronin, defines a new subfamily, and predicts protein function. Eckert C, Hammesfahr B, Kollmar M, BMC Evol Biol 2011 11 268 10.1186/1471-2148-11-268 21943019
    • (2011) BMC Evol Biol , vol.11 , pp. 268
    • Eckert, C.1    Hammesfahr, B.2    Kollmar, M.3
  • 52
    • 84858136256 scopus 로고    scopus 로고
    • Evolution of the eukaryotic ARP2/3 activators of the WASP family: WASP, WAVE, WASH, and WHAMM, and the proposed new family members WAWH and WAML
    • 10.1186/1756-0500-5-88 22316129
    • Evolution of the eukaryotic ARP2/3 activators of the WASP family: WASP, WAVE, WASH, and WHAMM, and the proposed new family members WAWH and WAML. Kollmar M, Lbik D, Enge S, BMC Res Notes 2012 5 88 10.1186/1756-0500-5-88 22316129
    • (2012) BMC Res Notes , vol.5 , pp. 88
    • Kollmar, M.1    Lbik, D.2    Enge, S.3
  • 53
    • 60849120779 scopus 로고    scopus 로고
    • WebScipio: An online tool for the determination of gene structures using protein sequences
    • 10.1186/1471-2164-9-422 18801164
    • WebScipio: an online tool for the determination of gene structures using protein sequences. Odronitz F, Pillmann H, Keller O, Waack S, Kollmar M, BMC Genomics 2008 9 422 10.1186/1471-2164-9-422 18801164
    • (2008) BMC Genomics , vol.9 , pp. 422
    • Odronitz, F.1    Pillmann, H.2    Keller, O.3    Waack, S.4    Kollmar, M.5
  • 55
    • 0030820735 scopus 로고    scopus 로고
    • Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors
    • 10.1083/jcb.138.4.821 9265649
    • Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors. Tian G, Lewis SA, Feierbach B, Stearns T, Rommelaere H, Ampe C, Cowan NJ, J Cell Biol 1997 138 821 832 10.1083/jcb.138.4.821 9265649
    • (1997) J Cell Biol , vol.138 , pp. 821-832
    • Tian, G.1    Lewis, S.A.2    Feierbach, B.3    Stearns, T.4    Rommelaere, H.5    Ampe, C.6    Cowan, N.J.7
  • 57
    • 0032497796 scopus 로고    scopus 로고
    • The genomic structure of DCTN1, a candidate gene for limb-girdle muscular dystrophy (LGMD2B)
    • 10.1016/S0167-4781(98)00195-X 9805007
    • The genomic structure of DCTN1, a candidate gene for limb-girdle muscular dystrophy (LGMD2B). Tokito MK, Holzbaur EL, Biochim Biophys Acta 1998 1442 432 436 10.1016/S0167-4781(98)00195-X 9805007
    • (1998) Biochim Biophys Acta , vol.1442 , pp. 432-436
    • Tokito, M.K.1    Holzbaur, E.L.2
  • 58
    • 57749110732 scopus 로고    scopus 로고
    • Regulation of Dynactin through the Differential Expression of p150Glued Isoforms
    • 10.1074/jbc.M804840200 18812314
    • Regulation of Dynactin through the Differential Expression of p150Glued Isoforms. Dixit R, Levy JR, Tokito M, Ligon LA, Holzbaur ELF, J Biol Chem 2008 283 33611 33619 10.1074/jbc.M804840200 18812314
    • (2008) J Biol Chem , vol.283 , pp. 33611-33619
    • Dixit, R.1    Levy, J.R.2    Tokito, M.3    Ligon, L.A.4    Holzbaur, E.L.F.5
  • 60
    • 23744433896 scopus 로고    scopus 로고
    • Structural Basis for the Activation of Microtubule Assembly by the EB1 and p150Glued Complex
    • 10.1016/j.molcel.2005.06.034 16109370
    • Structural Basis for the Activation of Microtubule Assembly by the EB1 and p150Glued Complex. Hayashi I, Wilde A, Mal TK, Ikura M, Mol Cell 2005 19 449 460 10.1016/j.molcel.2005.06.034 16109370
    • (2005) Mol Cell , vol.19 , pp. 449-460
    • Hayashi, I.1    Wilde, A.2    Mal, T.K.3    Ikura, M.4
  • 61
    • 34948902333 scopus 로고    scopus 로고
    • CLIP170 autoinhibition mimics intermolecular interactions with p150Glued or EB1
    • 10.1038/nsmb1299 17828275
    • CLIP170 autoinhibition mimics intermolecular interactions with p150Glued or EB1. Hayashi I, Plevin MJ, Ikura M, Nat Struct Mol Biol 2007 14 980 981 10.1038/nsmb1299 17828275
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 980-981
    • Hayashi, I.1    Plevin, M.J.2    Ikura, M.3
  • 62
    • 0028787443 scopus 로고
    • Regulation of cytoplasmic dynein function in vivo by the Drosophila Glued complex
    • 10.1083/jcb.131.2.411 7593168
    • Regulation of cytoplasmic dynein function in vivo by the Drosophila Glued complex. McGrail M, Gepner J, Silvanovich A, Ludmann S, Serr M, Hays TS, J Cell Biol 1995 131 411 425 10.1083/jcb.131.2.411 7593168
    • (1995) J Cell Biol , vol.131 , pp. 411-425
    • McGrail, M.1    Gepner, J.2    Silvanovich, A.3    Ludmann, S.4    Serr, M.5    Hays, T.S.6
  • 65
    • 77953898430 scopus 로고    scopus 로고
    • Disease-Associated Mutations in the p150Glued Subunit Destabilize the CAP-gly Domain
    • 10.1021/bi100235z 20518521
    • Disease-Associated Mutations in the p150Glued Subunit Destabilize the CAP-gly Domain. Ahmed S, Sun S, Siglin AE, Polenova T, Williams JC, Biochemistry 2010 49 5083 5085 10.1021/bi100235z 20518521
    • (2010) Biochemistry , vol.49 , pp. 5083-5085
    • Ahmed, S.1    Sun, S.2    Siglin, A.E.3    Polenova, T.4    Williams, J.C.5
  • 66
    • 0034604703 scopus 로고    scopus 로고
    • Protein Kinase C-regulated Dynamitin-Macrophage-enriched Myristoylated Alanine-Rice C Kinase Substrate Interaction Is Involved in Macrophage Cell Spreading
    • 10.1074/jbc.M001845200 10827182
    • Protein Kinase C-regulated Dynamitin-Macrophage-enriched Myristoylated Alanine-Rice C Kinase Substrate Interaction Is Involved in Macrophage Cell Spreading. Yue L, Lu S, Garces J, Jin T, Li J, J Biol Chem 2000 275 23948 23956 10.1074/jbc.M001845200 10827182
    • (2000) J Biol Chem , vol.275 , pp. 23948-23956
    • Yue, L.1    Lu, S.2    Garces, J.3    Jin, T.4    Li, J.5
  • 67
    • 40449083576 scopus 로고    scopus 로고
    • Dynamitin Mutagenesis Reveals Protein-Protein Interactions Important for Dynactin Structure
    • 10.1111/j.1600-0854.2008.00702.x 18182012
    • Dynamitin Mutagenesis Reveals Protein-Protein Interactions Important for Dynactin Structure. Maier KC, Godfrey JE, Echeverri CJ, Cheong FKY, Schroer TA, Traffic 2008 9 481 491 10.1111/j.1600-0854.2008.00702.x 18182012
    • (2008) Traffic , vol.9 , pp. 481-491
    • Maier, K.C.1    Godfrey, J.E.2    Echeverri, C.J.3    Cheong, F.K.Y.4    Schroer, T.A.5
  • 68
    • 0033576598 scopus 로고    scopus 로고
    • Interaction of the p62 subunit of dynactin with Arp1 and the cortical actin cytoskeleton
    • 10.1016/S0960-9822(00)80122-0 10607597
    • Interaction of the p62 subunit of dynactin with Arp1 and the cortical actin cytoskeleton. Garces JA, Clark IB, Meyer DI, Vallee RB, Curr Biol 1999 9 1497 1500 10.1016/S0960-9822(00)80122-0 10607597
    • (1999) Curr Biol , vol.9 , pp. 1497-1500
    • Garces, J.A.1    Clark, I.B.2    Meyer, D.I.3    Vallee, R.B.4
  • 69
    • 0034681316 scopus 로고    scopus 로고
    • A Dynactin Subunit with a Highly Conserved Cysteine-rich Motif Interacts Directly with Arp1
    • 10.1074/jbc.275.7.4834 10671518
    • A Dynactin Subunit with a Highly Conserved Cysteine-rich Motif Interacts Directly with Arp1. Karki S, Tokito MK, Holzbaur ELF, J Biol Chem 2000 275 4834 4839 10.1074/jbc.275.7.4834 10671518
    • (2000) J Biol Chem , vol.275 , pp. 4834-4839
    • Karki, S.1    Tokito, M.K.2    Holzbaur, E.L.F.3
  • 70
    • 34250162899 scopus 로고    scopus 로고
    • The ring between ring fingers (RBR) protein family
    • 10.1186/gb-2007-8-3-209 17367545
    • The ring between ring fingers (RBR) protein family. Eisenhaber B, Chumak N, Eisenhaber F, Hauser M-T, Genome Biol 2007 8 209 10.1186/gb-2007-8-3-209 17367545
    • (2007) Genome Biol , vol.8 , pp. 209
    • Eisenhaber, B.1    Chumak, N.2    Eisenhaber, F.3    Hauser, M.-T.4
  • 71
    • 8444240109 scopus 로고    scopus 로고
    • The LIM domain: From the cytoskeleton to the nucleus
    • 10.1038/nrm1499 15520811
    • The LIM domain: from the cytoskeleton to the nucleus. Kadrmas JL, Beckerle MC, Nat Rev Mol Cell Biol 2004 5 920 931 10.1038/nrm1499 15520811
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 920-931
    • Kadrmas, J.L.1    Beckerle, M.C.2
  • 72
    • 0037439997 scopus 로고    scopus 로고
    • Structural classification of zinc fingers
    • 10.1093/nar/gkg161 12527760
    • Structural classification of zinc fingers. Krishna SS, Majumdar I, Grishin NV, Nucleic Acids Res 2003 31 532 550 10.1093/nar/gkg161 12527760
    • (2003) Nucleic Acids Res , vol.31 , pp. 532-550
    • Krishna, S.S.1    Majumdar, I.2    Grishin, N.V.3
  • 73
    • 0031017595 scopus 로고    scopus 로고
    • Molecular dissection of a LIM domain
    • 9190203
    • Molecular dissection of a LIM domain. Schmeichel KL, Beckerle MC, Mol Biol Cell 1997 8 219 230 9190203
    • (1997) Mol Biol Cell , vol.8 , pp. 219-230
    • Schmeichel, K.L.1    Beckerle, M.C.2
  • 74
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • 10.1093/nar/gkn238 18463136
    • The Jpred 3 secondary structure prediction server. Cole C, Barber JD, Barton GJ, Nucleic Acids Res 2008 36 197 W201 10.1093/nar/gkn238 18463136
    • (2008) Nucleic Acids Res , vol.36
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 75
    • 34347209089 scopus 로고    scopus 로고
    • Independent sorting-out of thousands of duplicated gene pairs in two yeast species descended from a whole-genome duplication
    • 10.1073/pnas.0608218104 17494770
    • Independent sorting-out of thousands of duplicated gene pairs in two yeast species descended from a whole-genome duplication. Scannell DR, Frank AC, Conant GC, Byrne KP, Woolfit M, Wolfe KH, Proc Natl Acad Sci U S A 2007 104 8397 8402 10.1073/pnas.0608218104 17494770
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 8397-8402
    • Scannell, D.R.1    Frank, A.C.2    Conant, G.C.3    Byrne, K.P.4    Woolfit, M.5    Wolfe, K.H.6
  • 76
    • 79960239534 scopus 로고    scopus 로고
    • The p25 subunit of the dynactin complex is required for dynein-early endosome interaction
    • 10.1083/jcb.201011022 21708978
    • The p25 subunit of the dynactin complex is required for dynein-early endosome interaction. Zhang J, Yao X, Fischer L, Abenza JF, Peñalva MA, Xiang X, J Cell Biol 2011 193 1245 1255 10.1083/jcb.201011022 21708978
    • (2011) J Cell Biol , vol.193 , pp. 1245-1255
    • Zhang, J.1    Yao, X.2    Fischer, L.3    Abenza, J.F.4    Peñalva, M.A.5    Xiang, X.6
  • 77
    • 0026783380 scopus 로고
    • A vertebrate actin-related protein is a component of a multisubunit complex involved in microtubule-based vesicle motility
    • 10.1038/359244a0 1528266
    • A vertebrate actin-related protein is a component of a multisubunit complex involved in microtubule-based vesicle motility. Lees-Miller JP, Helfman DM, Schroer TA, Nature 1992 359 244 246 10.1038/359244a0 1528266
    • (1992) Nature , vol.359 , pp. 244-246
    • Lees-Miller, J.P.1    Helfman, D.M.2    Schroer, T.A.3
  • 78
    • 0026686929 scopus 로고
    • Centractin is an actin homologue associated with the centrosome
    • 10.1038/359246a0 1356230
    • Centractin is an actin homologue associated with the centrosome. Clark SW, Meyer DI, Nature 1992 359 246 250 10.1038/359246a0 1356230
    • (1992) Nature , vol.359 , pp. 246-250
    • Clark, S.W.1    Meyer, D.I.2
  • 79
    • 0028670191 scopus 로고
    • Beta-centractin: Characterization and distribution of a new member of the centractin family of actin-related proteins
    • 7696711
    • Beta-centractin: characterization and distribution of a new member of the centractin family of actin-related proteins. Clark SW, Staub O, Clark IB, Holzbaur EL, Paschal BM, Vallee RB, Meyer DI, Mol Biol Cell 1994 5 1301 1310 7696711
    • (1994) Mol Biol Cell , vol.5 , pp. 1301-1310
    • Clark, S.W.1    Staub, O.2    Clark, I.B.3    Holzbaur, E.L.4    Paschal, B.M.5    Vallee, R.B.6    Meyer, D.I.7
  • 80
    • 75549089647 scopus 로고    scopus 로고
    • 2R or not 2R is not the question anymore
    • 20084088
    • 2R or not 2R is not the question anymore. Van de Peer Y, Maere S, Meyer A, Nat Rev Genet 2010 11 166 20084088
    • (2010) Nat Rev Genet , vol.11 , pp. 166
    • Van De Peer, Y.1    Maere, S.2    Meyer, A.3
  • 82
    • 0030754347 scopus 로고    scopus 로고
    • Who's Who among the Saccharomyces cerevisiae Actin-Related Proteins? A Classification and Nomenclature Proposal for a Large Family
    • Who's Who among the Saccharomyces cerevisiae Actin-Related Proteins? A Classification and Nomenclature Proposal for a Large Family. Poch O, Winsor B, Yeast 1998 13 1053 1058
    • (1998) Yeast , vol.13 , pp. 1053-1058
    • Poch, O.1    Winsor, B.2
  • 83
    • 28644433381 scopus 로고    scopus 로고
    • Sequence and Comparative Genomic Analysis of Actin-related Proteins
    • 10.1091/mbc.E05-06-0508 16195354
    • Sequence and Comparative Genomic Analysis of Actin-related Proteins. Muller J, Oma Y, Vallar L, Friederich E, Poch O, Winsor B, Mol Biol Cell 2005 16 5736 5748 10.1091/mbc.E05-06-0508 16195354
    • (2005) Mol Biol Cell , vol.16 , pp. 5736-5748
    • Muller, J.1    Oma, Y.2    Vallar, L.3    Friederich, E.4    Poch, O.5    Winsor, B.6
  • 84
    • 33244466796 scopus 로고    scopus 로고
    • Comprehensive multigene phylogenies of excavate protists reveal the evolutionary positions of "primitive" eukaryotes
    • 16308337
    • Comprehensive multigene phylogenies of excavate protists reveal the evolutionary positions of "primitive" eukaryotes. Simpson AGB, Inagaki Y, Roger AJ, Mol Biol Evol 2006 23 615 625 16308337
    • (2006) Mol Biol Evol , vol.23 , pp. 615-625
    • Simpson, A.G.B.1    Inagaki, Y.2    Roger, A.J.3
  • 87
    • 73149111994 scopus 로고    scopus 로고
    • Phylogenetic positions of Glaucophyta, green plants (Archaeplastida) and Haptophyta (Chromalveolata) as deduced from slowly evolving nuclear genes
    • 10.1016/j.ympev.2009.08.015 19698794
    • Phylogenetic positions of Glaucophyta, green plants (Archaeplastida) and Haptophyta (Chromalveolata) as deduced from slowly evolving nuclear genes. Nozaki H, Maruyama S, Matsuzaki M, Nakada T, Kato S, Misawa K, Mol Phylogenet Evol 2009 53 872 880 10.1016/j.ympev.2009.08.015 19698794
    • (2009) Mol Phylogenet Evol , vol.53 , pp. 872-880
    • Nozaki, H.1    Maruyama, S.2    Matsuzaki, M.3    Nakada, T.4    Kato, S.5    Misawa, K.6
  • 88
    • 61849183735 scopus 로고    scopus 로고
    • Chromalveolates and the evolution of plastids by secondary endosymbiosis
    • 10.1111/j.1550-7408.2008.00371.x 19335769
    • Chromalveolates and the evolution of plastids by secondary endosymbiosis. Keeling PJ, J Eukaryot Microbiol 2009 56 1 8 10.1111/j.1550-7408.2008.00371.x 19335769
    • (2009) J Eukaryot Microbiol , vol.56 , pp. 1-8
    • Keeling, P.J.1
  • 89
    • 34547754024 scopus 로고    scopus 로고
    • Phylogenomic analysis supports the monophyly of cryptophytes and haptophytes and the association of rhizaria with chromalveolates
    • 10.1093/molbev/msm089 17488740
    • Phylogenomic analysis supports the monophyly of cryptophytes and haptophytes and the association of rhizaria with chromalveolates. Hackett JD, Yoon HS, Li S, Reyes-Prieto A, Rümmele SE, Bhattacharya D, Mol Biol Evol 2007 24 1702 1713 10.1093/molbev/msm089 17488740
    • (2007) Mol Biol Evol , vol.24 , pp. 1702-1713
    • Hackett, J.D.1    Yoon, H.S.2    Li, S.3    Reyes-Prieto, A.4    Rümmele, S.E.5    Bhattacharya, D.6
  • 90
    • 46949092431 scopus 로고    scopus 로고
    • Phylogenomics reveals a new "megagroup" including most photosynthetic eukaryotes
    • 10.1098/rsbl.2008.0224 18522922
    • Phylogenomics reveals a new "megagroup" including most photosynthetic eukaryotes. Burki F, Shalchian-Tabrizi K, Pawlowski J, Biol Lett 2008 4 366 369 10.1098/rsbl.2008.0224 18522922
    • (2008) Biol Lett , vol.4 , pp. 366-369
    • Burki, F.1    Shalchian-Tabrizi, K.2    Pawlowski, J.3
  • 92
    • 62649113993 scopus 로고    scopus 로고
    • Phylogenomic analyses support the monophyly of Excavata and resolve relationships among eukaryotic "supergroups"
    • 10.1073/pnas.0807880106 19237557
    • Phylogenomic analyses support the monophyly of Excavata and resolve relationships among eukaryotic "supergroups" Hampl V, Hug L, Leigh JW, Dacks JB, Lang BF, Simpson AGB, Roger AJ, Proc Natl Acad Sci U S A 2009 106 3859 3864 10.1073/pnas.0807880106 19237557
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 3859-3864
    • Hampl, V.1    Hug, L.2    Leigh, J.W.3    Dacks, J.B.4    Lang, B.F.5    Simpson, A.G.B.6    Roger, A.J.7
  • 93
    • 84858411861 scopus 로고    scopus 로고
    • Rooting the eukaryotic tree with mitochondrial and bacterial proteins
    • 10.1093/molbev/msr295 22135192
    • Rooting the eukaryotic tree with mitochondrial and bacterial proteins. Derelle R, Lang BF, Mol Biol Evol 2012 29 1277 1289 10.1093/molbev/msr295 22135192
    • (2012) Mol Biol Evol , vol.29 , pp. 1277-1289
    • Derelle, R.1    Lang, B.F.2
  • 95
    • 0041955201 scopus 로고    scopus 로고
    • Phylogenetic analysis of eukaryotes using heat-shock protein Hsp90
    • 10.1007/s00239-003-2490-x 14708574
    • Phylogenetic analysis of eukaryotes using heat-shock protein Hsp90. Stechmann A, Cavalier-Smith T, J Mol Evol 2003 57 408 419 10.1007/s00239-003- 2490-x 14708574
    • (2003) J Mol Evol , vol.57 , pp. 408-419
    • Stechmann, A.1    Cavalier-Smith, T.2
  • 96
    • 77953231719 scopus 로고    scopus 로고
    • Analysis of rare genomic changes does not support the unikont-bikont phylogeny and suggests cyanobacterial symbiosis as the point of primary radiation of eukaryotes
    • 20333181
    • Analysis of rare genomic changes does not support the unikont-bikont phylogeny and suggests cyanobacterial symbiosis as the point of primary radiation of eukaryotes. Rogozin IB, Basu MK, Csürös M, Koonin EV, Genome Biol Evol 2009 1 99 113 20333181
    • (2009) Genome Biol Evol , vol.1 , pp. 99-113
    • Rogozin, I.B.1    Basu, M.K.2    Csürös, M.3    Koonin, E.V.4
  • 97
    • 77955039174 scopus 로고    scopus 로고
    • The origin and early evolution of eukaryotes in the light of phylogenomics
    • 10.1186/gb-2010-11-5-209 20441612
    • The origin and early evolution of eukaryotes in the light of phylogenomics. Koonin EV, Genome Biol 2010 11 209 10.1186/gb-2010-11-5-209 20441612
    • (2010) Genome Biol , vol.11 , pp. 209
    • Koonin, E.V.1
  • 98
    • 80053175251 scopus 로고    scopus 로고
    • The phylogenomic analysis of the anaphase promoting complex and its targets points to complex and modern-like control of the cell cycle in the last common ancestor of eukaryotes
    • 10.1186/1471-2148-11-265 21943402
    • The phylogenomic analysis of the anaphase promoting complex and its targets points to complex and modern-like control of the cell cycle in the last common ancestor of eukaryotes. Eme L, Trilles A, Moreira D, Brochier-Armanet C, BMC Evol Biol 2011 11 265 10.1186/1471-2148-11-265 21943402
    • (2011) BMC Evol Biol , vol.11 , pp. 265
    • Eme, L.1    Trilles, A.2    Moreira, D.3    Brochier-Armanet, C.4
  • 99
    • 79961032041 scopus 로고    scopus 로고
    • The evolution of respiratory chain complex i from a smaller last common ancestor consisting of 11 protein subunits
    • 10.1007/s00239-011-9447-2 21597881
    • The evolution of respiratory chain complex I from a smaller last common ancestor consisting of 11 protein subunits. Moparthi VK, Hägerhäll C, J Mol Evol 2011 72 484 497 10.1007/s00239-011-9447-2 21597881
    • (2011) J Mol Evol , vol.72 , pp. 484-497
    • Moparthi, V.K.1    Hägerhäll, C.2
  • 100
    • 0029742626 scopus 로고    scopus 로고
    • Functionally distinct isoforms of dynactin are expressed in human neurons
    • 8856662
    • Functionally distinct isoforms of dynactin are expressed in human neurons. Tokito MK, Howland DS, Lee VM, Holzbaur EL, Mol Biol Cell 1996 7 1167 1180 8856662
    • (1996) Mol Biol Cell , vol.7 , pp. 1167-1180
    • Tokito, M.K.1    Howland, D.S.2    Lee, V.M.3    Holzbaur, E.L.4
  • 102
    • 0037157845 scopus 로고    scopus 로고
    • A role for regulated binding of p150(Glued) to microtubule plus ends in organelle transport
    • 10.1083/jcb.200201029 12119357
    • A role for regulated binding of p150(Glued) to microtubule plus ends in organelle transport. Vaughan PS, Miura P, Henderson M, Byrne B, Vaughan KT, J Cell Biol 2002 158 305 319 10.1083/jcb.200201029 12119357
    • (2002) J Cell Biol , vol.158 , pp. 305-319
    • Vaughan, P.S.1    Miura, P.2    Henderson, M.3    Byrne, B.4    Vaughan, K.T.5
  • 103
    • 1642358246 scopus 로고    scopus 로고
    • Dynactins p25 and p27 are predicted to adopt the LbetaH fold
    • 10.1016/S0014-5793(04)00165-6 15043994
    • Dynactins p25 and p27 are predicted to adopt the LbetaH fold. Parisi G, Fornasari MS, Echave J, FEBS Lett 2004 562 1 4 10.1016/S0014-5793(04)00165-6 15043994
    • (2004) FEBS Lett , vol.562 , pp. 1-4
    • Parisi, G.1    Fornasari, M.S.2    Echave, J.3
  • 104
    • 0029155542 scopus 로고
    • Spindle dynamics and cell cycle regulation of dynein in the budding yeast, Saccharomyces cerevisiae
    • 10.1083/jcb.130.3.687 7622568
    • Spindle dynamics and cell cycle regulation of dynein in the budding yeast, Saccharomyces cerevisiae. Yeh E, Skibbens RV, Cheng JW, Salmon ED, Bloom K, J Cell Biol 1995 130 687 700 10.1083/jcb.130.3.687 7622568
    • (1995) J Cell Biol , vol.130 , pp. 687-700
    • Yeh, E.1    Skibbens, R.V.2    Cheng, J.W.3    Salmon, E.D.4    Bloom, K.5
  • 105
    • 40449130757 scopus 로고    scopus 로고
    • Dynactin function in mitotic spindle positioning
    • 10.1111/j.1600-0854.2008.00710.x 18221362
    • Dynactin function in mitotic spindle positioning. Moore JK, Li J, Cooper JA, Traffic 2008 9 510 527 10.1111/j.1600-0854.2008.00710.x 18221362
    • (2008) Traffic , vol.9 , pp. 510-527
    • Moore, J.K.1    Li, J.2    Cooper, J.A.3
  • 106
    • 79451469119 scopus 로고    scopus 로고
    • Phylogeny of the ascomycetous yeasts and the renaming of Pichia anomala to Wickerhamomyces anomalus
    • 10.1007/s10482-010-9505-6 20838888
    • Phylogeny of the ascomycetous yeasts and the renaming of Pichia anomala to Wickerhamomyces anomalus. Kurtzman CP, Antonie Van Leeuwenhoek 2011 99 13 23 10.1007/s10482-010-9505-6 20838888
    • (2011) Antonie Van Leeuwenhoek , vol.99 , pp. 13-23
    • Kurtzman, C.P.1
  • 107
    • 84859021892 scopus 로고    scopus 로고
    • De-Novo Assembly and Analysis of the Heterozygous Triploid Genome of the Wine Spoilage Yeast Dekkera bruxellensis AWRI1499
    • 10.1371/journal.pone.0033840 22470482
    • De-Novo Assembly and Analysis of the Heterozygous Triploid Genome of the Wine Spoilage Yeast Dekkera bruxellensis AWRI1499. Curtin CD, Borneman AR, Chambers PJ, Pretorius IS, PLoS One 2012 7 33840 10.1371/journal.pone.0033840 22470482
    • (2012) PLoS One , vol.7 , pp. 533840
    • Curtin, C.D.1    Borneman, A.R.2    Chambers, P.J.3    Pretorius, I.S.4
  • 108
    • 33845605457 scopus 로고    scopus 로고
    • Pfarao: A web application for protein family analysis customized for cytoskeletal and motor proteins (CyMoBase)
    • 10.1186/1471-2164-7-300 17134497
    • Pfarao: a web application for protein family analysis customized for cytoskeletal and motor proteins (CyMoBase). Odronitz F, Kollmar M, BMC Genomics 2006 7 300 10.1186/1471-2164-7-300 17134497
    • (2006) BMC Genomics , vol.7 , pp. 300
    • Odronitz, F.1    Kollmar, M.2
  • 109
    • 79960655604 scopus 로고    scopus 로고
    • Cross-species protein sequence and gene structure prediction with fine-tuned Webscipio 2.0 and Scipio
    • 10.1186/1756-0500-4-265 21798037
    • Cross-species protein sequence and gene structure prediction with fine-tuned Webscipio 2.0 and Scipio. Hatje K, Keller O, Hammesfahr B, Pillmann H, Waack S, Kollmar M, BMC Res Notes 2011 4 265 10.1186/1756-0500-4-265 21798037
    • (2011) BMC Res Notes , vol.4 , pp. 265
    • Hatje, K.1    Keller, O.2    Hammesfahr, B.3    Pillmann, H.4    Waack, S.5    Kollmar, M.6
  • 111
    • 34547489084 scopus 로고    scopus 로고
    • Improvement of phylogenies after removing divergent and ambiguously aligned blocks from protein sequence alignments
    • 10.1080/10635150701472164 17654362
    • Improvement of phylogenies after removing divergent and ambiguously aligned blocks from protein sequence alignments. Talavera G, Castresana J, Syst Biol 2007 56 564 577 10.1080/10635150701472164 17654362
    • (2007) Syst Biol , vol.56 , pp. 564-577
    • Talavera, G.1    Castresana, J.2
  • 112
    • 0347823003 scopus 로고    scopus 로고
    • MatGAT: An application that generates similarity/identity matrices using protein or DNA sequences
    • 10.1186/1471-2105-4-29
    • MatGAT: an application that generates similarity/identity matrices using protein or DNA sequences. Campanella JJ, Bitincka L, Smalley J, BMC Bioinforma 2003 4 29 10.1186/1471-2105-4-29
    • (2003) BMC Bioinforma , vol.4 , pp. 29
    • Campanella, J.J.1    Bitincka, L.2    Smalley, J.3
  • 113
    • 79954529507 scopus 로고    scopus 로고
    • ProtTest 3: Fast selection of best-fit models of protein evolution
    • 10.1093/bioinformatics/btr088 21335321
    • ProtTest 3: fast selection of best-fit models of protein evolution. Darriba D, Taboada GL, Doallo R, Posada D, Bioinformatics 2011 27 1164 1165 10.1093/bioinformatics/btr088 21335321
    • (2011) Bioinformatics , vol.27 , pp. 1164-1165
    • Darriba, D.1    Taboada, G.L.2    Doallo, R.3    Posada, D.4
  • 114
    • 45849154166 scopus 로고    scopus 로고
    • An improved general amino acid replacement matrix
    • 10.1093/molbev/msn067 18367465
    • An improved general amino acid replacement matrix. Le SQ, Gascuel O, Mol Biol Evol 2008 25 1307 1320 10.1093/molbev/msn067 18367465
    • (2008) Mol Biol Evol , vol.25 , pp. 1307-1320
    • Le, S.Q.1    Gascuel, O.2
  • 115
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • 1633570
    • The rapid generation of mutation data matrices from protein sequences. Jones DT, Taylor WR, Thornton JM, Comput Appl Biosci 1992 8 275 282 1633570
    • (1992) Comput Appl Biosci , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 116
    • 50249100595 scopus 로고    scopus 로고
    • A rapid bootstrap algorithm for the RAxML Web servers
    • 10.1080/10635150802429642 18853362
    • A rapid bootstrap algorithm for the RAxML Web servers. Stamatakis A, Hoover P, Rougemont J, Syst Biol 2008 57 758 771 10.1080/10635150802429642 18853362
    • (2008) Syst Biol , vol.57 , pp. 758-771
    • Stamatakis, A.1    Hoover, P.2    Rougemont, J.3
  • 117
    • 0041386108 scopus 로고    scopus 로고
    • MrBayes 3: Bayesian phylogenetic inference under mixed models
    • 10.1093/bioinformatics/btg180 12912839
    • MrBayes 3: Bayesian phylogenetic inference under mixed models. Ronquist F, Huelsenbeck JP, Bioinformatics 2003 19 1572 1574 10.1093/bioinformatics/ btg180 12912839
    • (2003) Bioinformatics , vol.19 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 118
    • 1342309210 scopus 로고    scopus 로고
    • Parallel Metropolis coupled Markov chain Monte Carlo for Bayesian phylogenetic inference
    • 10.1093/bioinformatics/btg427 14960467
    • Parallel Metropolis coupled Markov chain Monte Carlo for Bayesian phylogenetic inference. Altekar G, Dwarkadas S, Huelsenbeck JP, Ronquist F, Bioinformatics 2004 20 407 415 10.1093/bioinformatics/btg427 14960467
    • (2004) Bioinformatics , vol.20 , pp. 407-415
    • Altekar, G.1    Dwarkadas, S.2    Huelsenbeck, J.P.3    Ronquist, F.4
  • 119
    • 0035031966 scopus 로고    scopus 로고
    • A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach
    • 10.1093/oxfordjournals.molbev.a003851 11319253
    • A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach. Whelan S, Goldman N, Mol Biol Evol 2001 18 691 699 10.1093/oxfordjournals.molbev.a003851 11319253
    • (2001) Mol Biol Evol , vol.18 , pp. 691-699
    • Whelan, S.1    Goldman, N.2
  • 120
    • 79959670380 scopus 로고    scopus 로고
    • Predicting mutually exclusive spliced exons based on exon length, splice site and reading frame conservation, and exon sequence homology
    • 10.1186/1471-2105-12-270
    • Predicting mutually exclusive spliced exons based on exon length, splice site and reading frame conservation, and exon sequence homology. Pillmann H, Hatje K, Odronitz F, Hammesfahr B, Kollmar M, BMC Bioinforma 2011 12 270 10.1186/1471-2105-12-270
    • (2011) BMC Bioinforma , vol.12 , pp. 270
    • Pillmann, H.1    Hatje, K.2    Odronitz, F.3    Hammesfahr, B.4    Kollmar, M.5
  • 121
    • 0027959864 scopus 로고
    • Differential localization and sequence analysis of capping protein beta-subunit isoforms of vertebrates
    • 10.1083/jcb.127.2.453 7929588
    • Differential localization and sequence analysis of capping protein beta-subunit isoforms of vertebrates. Schafer DA, Korshunova YO, Schroer TA, Cooper JA, J Cell Biol 1994 127 453 465 10.1083/jcb.127.2.453 7929588
    • (1994) J Cell Biol , vol.127 , pp. 453-465
    • Schafer, D.A.1    Korshunova, Y.O.2    Schroer, T.A.3    Cooper, J.A.4


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