메뉴 건너뛰기




Volumn 20, Issue 8, 2010, Pages 470-481

Armadillo-repeat protein functions: Questions for little creatures

Author keywords

[No Author keywords available]

Indexed keywords

ARMADILLO REPEAT CONTAINING PROTEIN 8; ARMADILLO REPEAT PROTEIN; BETA CATENIN; CELL PROTEIN; CHAPERONE; INTERLEUKIN RECEPTOR; KINESIN; KINESIN ASSOCIATED PROTEIN 3; METHENAMINE; PHOSPHOTRANSFERASE; PROTEIN CATENIN BETA LIKE 1; PROTEIN REGULATOR OF CELL DIFFERENTIATION 1; TOLL INTERLEUKIN RECEPTOR; UNCLASSIFIED DRUG;

EID: 77955335145     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2010.05.003     Document Type: Review
Times cited : (210)

References (141)
  • 1
    • 0028266975 scopus 로고
    • A repeating amino acid motif shared by proteins with diverse cellular roles
    • Peifer M., et al. A repeating amino acid motif shared by proteins with diverse cellular roles. Cell 1994, 76:789-791.
    • (1994) Cell , vol.76 , pp. 789-791
    • Peifer, M.1
  • 2
    • 12344281930 scopus 로고    scopus 로고
    • Structure of the armadillo repeat domain of plakophilin 1
    • Choi H.J., Weis W.I. Structure of the armadillo repeat domain of plakophilin 1. J. Mol. Biol. 2005, 346:367-376.
    • (2005) J. Mol. Biol. , vol.346 , pp. 367-376
    • Choi, H.J.1    Weis, W.I.2
  • 3
    • 0032563246 scopus 로고    scopus 로고
    • Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha
    • Conti E., et al. Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha. Cell 1998, 94:193-204.
    • (1998) Cell , vol.94 , pp. 193-204
    • Conti, E.1
  • 4
    • 0030800831 scopus 로고    scopus 로고
    • Three-dimensional structure of the armadillo repeat region of beta-catenin
    • Huber A.H., et al. Three-dimensional structure of the armadillo repeat region of beta-catenin. Cell 1997, 90:871-882.
    • (1997) Cell , vol.90 , pp. 871-882
    • Huber, A.H.1
  • 5
    • 43049135909 scopus 로고    scopus 로고
    • The C. elegans SYS-1 protein is a bona fide beta-catenin
    • Liu J., et al. The C. elegans SYS-1 protein is a bona fide beta-catenin. Dev. Cell 2008, 14:751-761.
    • (2008) Dev. Cell , vol.14 , pp. 751-761
    • Liu, J.1
  • 6
    • 20844439387 scopus 로고    scopus 로고
    • Structural basis of Rho GTPase-mediated activation of the formin mDia1
    • Otomo T., et al. Structural basis of Rho GTPase-mediated activation of the formin mDia1. Mol. Cell 2005, 18:273-281.
    • (2005) Mol. Cell , vol.18 , pp. 273-281
    • Otomo, T.1
  • 7
    • 19544386803 scopus 로고    scopus 로고
    • Structural and mechanistic insights into the interaction between Rho and mammalian Dia
    • Rose R., et al. Structural and mechanistic insights into the interaction between Rho and mammalian Dia. Nature 2005, 435:513-518.
    • (2005) Nature , vol.435 , pp. 513-518
    • Rose, R.1
  • 8
    • 13244278043 scopus 로고    scopus 로고
    • Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange
    • Shomura Y., et al. Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange. Mol. Cell 2005, 17:367-379.
    • (2005) Mol. Cell , vol.17 , pp. 367-379
    • Shomura, Y.1
  • 9
    • 77749304932 scopus 로고    scopus 로고
    • Armadillo motifs involved in vesicular transport
    • Striegl H., et al. Armadillo motifs involved in vesicular transport. PLoS One 2010, 5:e8991.
    • (2010) PLoS One , vol.5
    • Striegl, H.1
  • 10
    • 35649014889 scopus 로고    scopus 로고
    • Inaugural article: structure and function of the yeast U-box-containing ubiquitin ligase Ufd2p
    • Tu D., et al. Inaugural article: structure and function of the yeast U-box-containing ubiquitin ligase Ufd2p. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:15599-15606.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 15599-15606
    • Tu, D.1
  • 11
    • 70349502243 scopus 로고    scopus 로고
    • An Armadillo motif in Ufd3 interacts with Cdc48 and is involved in ubiquitin homeostasis and protein degradation
    • Zhao G., et al. An Armadillo motif in Ufd3 interacts with Cdc48 and is involved in ubiquitin homeostasis and protein degradation. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:16197-16202.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 16197-16202
    • Zhao, G.1
  • 12
    • 20444383880 scopus 로고    scopus 로고
    • A beta-catenin identified by functional rather than sequence criteria and its role in Wnt/MAPK signaling
    • Kidd A.R., et al. A beta-catenin identified by functional rather than sequence criteria and its role in Wnt/MAPK signaling. Cell 2005, 121:761-772.
    • (2005) Cell , vol.121 , pp. 761-772
    • Kidd, A.R.1
  • 13
    • 0142106808 scopus 로고    scopus 로고
    • Armadillo repeat proteins: beyond the animal kingdom
    • Coates J.C. Armadillo repeat proteins: beyond the animal kingdom. Trends Cell Biol. 2003, 13:463-471.
    • (2003) Trends Cell Biol. , vol.13 , pp. 463-471
    • Coates, J.C.1
  • 14
    • 70349512813 scopus 로고    scopus 로고
    • Highly sensitive detection of individual HEAT and ARM repeats with HHpred and COACH
    • Kippert F., Gerloff D.L. Highly sensitive detection of individual HEAT and ARM repeats with HHpred and COACH. PLoS One 2009, 4:e7148.
    • (2009) PLoS One , vol.4
    • Kippert, F.1    Gerloff, D.L.2
  • 15
    • 77149174855 scopus 로고    scopus 로고
    • Wnt signaling from development to disease: insights from model systems
    • Cadigan K.M., Peifer M. Wnt signaling from development to disease: insights from model systems. Cold Spring Harb. Perspect. Biol. 2009, 1:a002881.
    • (2009) Cold Spring Harb. Perspect. Biol. , vol.1
    • Cadigan, K.M.1    Peifer, M.2
  • 16
    • 67650230896 scopus 로고    scopus 로고
    • Wnt/beta-catenin signaling: components, mechanisms, and diseases
    • MacDonald B.T., et al. Wnt/beta-catenin signaling: components, mechanisms, and diseases. Dev. Cell 2009, 17:9-26.
    • (2009) Dev. Cell , vol.17 , pp. 9-26
    • MacDonald, B.T.1
  • 17
    • 35648965654 scopus 로고    scopus 로고
    • Mechanistic insights from structural studies of beta-catenin and its binding partners
    • Xu W., Kimelman D. Mechanistic insights from structural studies of beta-catenin and its binding partners. J. Cell Sci. 2007, 120:3337-3344.
    • (2007) J. Cell Sci. , vol.120 , pp. 3337-3344
    • Xu, W.1    Kimelman, D.2
  • 18
    • 28344446744 scopus 로고    scopus 로고
    • Can 1000 reviews be wrong? Actin, alpha-catenin, and adherens junctions
    • Gates J., Peifer M. Can 1000 reviews be wrong? Actin, alpha-catenin, and adherens junctions. Cell 2005, 123:769-772.
    • (2005) Cell , vol.123 , pp. 769-772
    • Gates, J.1    Peifer, M.2
  • 19
    • 38149118802 scopus 로고    scopus 로고
    • Beta-catenin is a Nek2 substrate involved in centrosome separation
    • Bahmanyar S., et al. beta-catenin is a Nek2 substrate involved in centrosome separation. Genes Dev. 2008, 22:91-105.
    • (2008) Genes Dev. , vol.22 , pp. 91-105
    • Bahmanyar, S.1
  • 20
    • 77950368590 scopus 로고    scopus 로고
    • Conductin/axin2 and Wnt signalling regulates centrosome cohesion
    • Hadjihannas M.V., et al. Conductin/axin2 and Wnt signalling regulates centrosome cohesion. EMBO Rep. 2010, 11:317-324.
    • (2010) EMBO Rep. , vol.11 , pp. 317-324
    • Hadjihannas, M.V.1
  • 21
    • 34347364625 scopus 로고    scopus 로고
    • A novel role of phospho-beta-catenin in microtubule regrowth at centrosome
    • Huang P., et al. A novel role of phospho-beta-catenin in microtubule regrowth at centrosome. Oncogene 2007, 26:4357-4371.
    • (2007) Oncogene , vol.26 , pp. 4357-4371
    • Huang, P.1
  • 22
    • 35648988947 scopus 로고    scopus 로고
    • Adenomatous polyposis coli (APC): a multi-functional tumor suppressor gene
    • Aoki K., Taketo M.M. Adenomatous polyposis coli (APC): a multi-functional tumor suppressor gene. J Cell Sci 2007, 120:3327-3335.
    • (2007) J Cell Sci , vol.120 , pp. 3327-3335
    • Aoki, K.1    Taketo, M.M.2
  • 23
    • 34249061491 scopus 로고    scopus 로고
    • Wilms tumor suppressor WTX negatively regulates WNT/beta-catenin signaling
    • Major M.B., et al. Wilms tumor suppressor WTX negatively regulates WNT/beta-catenin signaling. Science 2007, 316:1043-1046.
    • (2007) Science , vol.316 , pp. 1043-1046
    • Major, M.B.1
  • 24
    • 53349162212 scopus 로고    scopus 로고
    • Jade-1 inhibits Wnt signalling by ubiquitylating beta-catenin and mediates Wnt pathway inhibition by pVHL
    • Chitalia V.C., et al. Jade-1 inhibits Wnt signalling by ubiquitylating beta-catenin and mediates Wnt pathway inhibition by pVHL. Nat. Cell Biol. 2008, 10:1208-1216.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1208-1216
    • Chitalia, V.C.1
  • 25
    • 77951565432 scopus 로고    scopus 로고
    • Direct ubiquitination of β-catenin by siah-1 and regulation by the exchange factor TBL1
    • Dimitrova Y.N., et al. Direct ubiquitination of β-catenin by siah-1 and regulation by the exchange factor TBL1. J. Biol. Chem. 2010, 285:13507-13516.
    • (2010) J. Biol. Chem. , vol.285 , pp. 13507-13516
    • Dimitrova, Y.N.1
  • 26
    • 21644472189 scopus 로고    scopus 로고
    • Formation of the head organizer in hydra involves the canonical Wnt pathway
    • Broun M., et al. Formation of the head organizer in hydra involves the canonical Wnt pathway. Development 2005, 132:2907-2916.
    • (2005) Development , vol.132 , pp. 2907-2916
    • Broun, M.1
  • 27
    • 67149094717 scopus 로고    scopus 로고
    • WNT/beta-catenin signalling and epithelial patterning in the homoscleromorph sponge Oscarella
    • Lapebie P., et al. WNT/beta-catenin signalling and epithelial patterning in the homoscleromorph sponge Oscarella. PLoS One 2009, 4:e5823.
    • (2009) PLoS One , vol.4
    • Lapebie, P.1
  • 28
    • 33747606753 scopus 로고    scopus 로고
    • Early evolution of animal cell signaling and adhesion genes
    • Nichols S.A., et al. Early evolution of animal cell signaling and adhesion genes. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:12451-12456.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 12451-12456
    • Nichols, S.A.1
  • 29
    • 0037762832 scopus 로고    scopus 로고
    • Protein evolution: structure-function relationships of the oncogene beta-catenin in the evolution of multicellular animals
    • Schneider S.Q., et al. Protein evolution: structure-function relationships of the oncogene beta-catenin in the evolution of multicellular animals. J. Exp. Zool. B Mol. Dev. Evol. 2003, 295:25-44.
    • (2003) J. Exp. Zool. B Mol. Dev. Evol. , vol.295 , pp. 25-44
    • Schneider, S.Q.1
  • 30
    • 33646155329 scopus 로고    scopus 로고
    • Essential and opposing roles of zebrafish beta-catenins in the formation of dorsal axial structures and neurectoderm
    • Bellipanni G., et al. Essential and opposing roles of zebrafish beta-catenins in the formation of dorsal axial structures and neurectoderm. Development 2006, 133:1299-1309.
    • (2006) Development , vol.133 , pp. 1299-1309
    • Bellipanni, G.1
  • 31
    • 67650267476 scopus 로고    scopus 로고
    • A new look at TCF and beta-catenin through the lens of a divergent C. elegans Wnt pathway
    • Phillips B.T., Kimble J. A new look at TCF and beta-catenin through the lens of a divergent C. elegans Wnt pathway. Dev. Cell 2009, 17:27-34.
    • (2009) Dev. Cell , vol.17 , pp. 27-34
    • Phillips, B.T.1    Kimble, J.2
  • 32
    • 34250365241 scopus 로고    scopus 로고
    • Desmosomes: a role in cancer?
    • Chidgey M., Dawson C. Desmosomes: a role in cancer?. Br. J. Cancer 2007, 96:1783-1787.
    • (2007) Br. J. Cancer , vol.96 , pp. 1783-1787
    • Chidgey, M.1    Dawson, C.2
  • 33
    • 59649083176 scopus 로고    scopus 로고
    • Plakoglobin has both structural and signalling roles in zebrafish development
    • Martin E.D., et al. Plakoglobin has both structural and signalling roles in zebrafish development. Dev. Biol. 2009, 327:83-96.
    • (2009) Dev. Biol. , vol.327 , pp. 83-96
    • Martin, E.D.1
  • 34
    • 53349133034 scopus 로고    scopus 로고
    • Desmosomes: just cell adhesion or is there more?
    • Schmidt A., Koch P.J. Desmosomes: just cell adhesion or is there more?. Cell Adh. Migr. 2007, 1:28-32.
    • (2007) Cell Adh. Migr. , vol.1 , pp. 28-32
    • Schmidt, A.1    Koch, P.J.2
  • 35
    • 14844340468 scopus 로고    scopus 로고
    • The p120 family of cell adhesion molecules
    • Hatzfeld M. The p120 family of cell adhesion molecules. Eur. J. Cell Biol. 2005, 84:205-214.
    • (2005) Eur. J. Cell Biol. , vol.84 , pp. 205-214
    • Hatzfeld, M.1
  • 36
    • 1342304120 scopus 로고    scopus 로고
    • P120 catenin associates with microtubules: inverse relationship between microtubule binding and Rho GTPase regulation
    • Franz C.M., Ridley A.J. p120 catenin associates with microtubules: inverse relationship between microtubule binding and Rho GTPase regulation. J. Biol. Chem. 2004, 279:6588-6594.
    • (2004) J. Biol. Chem. , vol.279 , pp. 6588-6594
    • Franz, C.M.1    Ridley, A.J.2
  • 37
    • 33845576801 scopus 로고    scopus 로고
    • Dancing in and out of the nucleus: p120(ctn) and the transcription factor Kaiso
    • Daniel J.M. Dancing in and out of the nucleus: p120(ctn) and the transcription factor Kaiso. Biochim. Biophys. Acta 2007, 1773:59-68.
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 59-68
    • Daniel, J.M.1
  • 38
    • 10344261485 scopus 로고    scopus 로고
    • Non-canonical Wnt signals are modulated by the Kaiso transcriptional repressor and p120-catenin
    • Kim S.W., et al. Non-canonical Wnt signals are modulated by the Kaiso transcriptional repressor and p120-catenin. Nat. Cell Biol. 2004, 6:1212-1220.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1212-1220
    • Kim, S.W.1
  • 39
    • 19944425163 scopus 로고    scopus 로고
    • Kaiso/p120-catenin and TCF/beta-catenin complexes coordinately regulate canonical Wnt gene targets
    • Park J.I., et al. Kaiso/p120-catenin and TCF/beta-catenin complexes coordinately regulate canonical Wnt gene targets. Dev. Cell 2005, 8:843-854.
    • (2005) Dev. Cell , vol.8 , pp. 843-854
    • Park, J.I.1
  • 40
    • 70350389741 scopus 로고    scopus 로고
    • GSK-3 phosphorylates delta-catenin and negatively regulates its stability via ubiquitination/proteosome-mediated proteolysis
    • Oh M., et al. GSK-3 phosphorylates delta-catenin and negatively regulates its stability via ubiquitination/proteosome-mediated proteolysis. J. Biol. Chem. 2009, 284:28579-28589.
    • (2009) J. Biol. Chem. , vol.284 , pp. 28579-28589
    • Oh, M.1
  • 41
    • 60049097838 scopus 로고    scopus 로고
    • Kaiso is a bimodal modulator for Wnt/beta-catenin signaling
    • Iioka H., et al. Kaiso is a bimodal modulator for Wnt/beta-catenin signaling. FEBS Lett. 2009, 583:627-632.
    • (2009) FEBS Lett. , vol.583 , pp. 627-632
    • Iioka, H.1
  • 42
    • 33750469721 scopus 로고    scopus 로고
    • Frodo links Dishevelled to the p120-catenin/Kaiso pathway: distinct catenin subfamilies promote Wnt signals
    • Park J.I., et al. Frodo links Dishevelled to the p120-catenin/Kaiso pathway: distinct catenin subfamilies promote Wnt signals. Dev. Cell 2006, 11:683-695.
    • (2006) Dev. Cell , vol.11 , pp. 683-695
    • Park, J.I.1
  • 43
    • 45149113604 scopus 로고    scopus 로고
    • A role for the cleaved cytoplasmic domain of E-cadherin in the nucleus
    • Ferber E.C., et al. A role for the cleaved cytoplasmic domain of E-cadherin in the nucleus. J. Biol. Chem. 2008, 283:12691-12700.
    • (2008) J. Biol. Chem. , vol.283 , pp. 12691-12700
    • Ferber, E.C.1
  • 44
    • 70349333829 scopus 로고    scopus 로고
    • Plakophilins: multifunctional scaffolds for adhesion and signaling
    • Bass-Zubek A.E., et al. Plakophilins: multifunctional scaffolds for adhesion and signaling. Curr. Opin. Cell Biol. 2009, 21:708-716.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 708-716
    • Bass-Zubek, A.E.1
  • 45
    • 77149126807 scopus 로고    scopus 로고
    • Plakophilin 1 stimulates translation by promoting eIF4A1 activity
    • Wolf A., et al. Plakophilin 1 stimulates translation by promoting eIF4A1 activity. J. Cell Biol. 2010, 188:463-471.
    • (2010) J. Cell Biol. , vol.188 , pp. 463-471
    • Wolf, A.1
  • 47
    • 0032498794 scopus 로고    scopus 로고
    • Vac8p, a vacuolar protein with armadillo repeats, functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole
    • Wang Y.X., et al. Vac8p, a vacuolar protein with armadillo repeats, functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole. J. Cell Biol. 1998, 140:1063-1074.
    • (1998) J. Cell Biol. , vol.140 , pp. 1063-1074
    • Wang, Y.X.1
  • 48
    • 33748527156 scopus 로고    scopus 로고
    • Vac8p, an armadillo repeat protein, coordinates vacuole inheritance with multiple vacuolar processes
    • Tang F., et al. Vac8p, an armadillo repeat protein, coordinates vacuole inheritance with multiple vacuolar processes. Traffic 2006, 7:1368-1377.
    • (2006) Traffic , vol.7 , pp. 1368-1377
    • Tang, F.1
  • 49
    • 32944479483 scopus 로고    scopus 로고
    • Candida albicans VAC8 is required for vacuolar inheritance and normal hyphal branching
    • Barelle C.J., et al. Candida albicans VAC8 is required for vacuolar inheritance and normal hyphal branching. Eukaryot. Cell 2006, 5:359-367.
    • (2006) Eukaryot. Cell , vol.5 , pp. 359-367
    • Barelle, C.J.1
  • 50
    • 58149302496 scopus 로고    scopus 로고
    • Vacuole inheritance regulates cell size and branching frequency of Candida albicans hyphae
    • Veses V., et al. Vacuole inheritance regulates cell size and branching frequency of Candida albicans hyphae. Mol. Microbiol. 2009, 71:505-519.
    • (2009) Mol. Microbiol. , vol.71 , pp. 505-519
    • Veses, V.1
  • 51
    • 55949117660 scopus 로고    scopus 로고
    • Molecular phylogeny of choanoflagellates, the sister group to Metazoa
    • Carr M., et al. Molecular phylogeny of choanoflagellates, the sister group to Metazoa. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:16641-16646.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 16641-16646
    • Carr, M.1
  • 52
    • 39349100667 scopus 로고    scopus 로고
    • The premetazoan ancestry of cadherins
    • Abedin M., King N. The premetazoan ancestry of cadherins. Science 2008, 319:946-948.
    • (2008) Science , vol.319 , pp. 946-948
    • Abedin, M.1    King, N.2
  • 53
    • 31944434046 scopus 로고    scopus 로고
    • Armadillo-related proteins promote lateral root development in Arabidopsis
    • Coates J.C., et al. Armadillo-related proteins promote lateral root development in Arabidopsis. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:1621-1626.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 1621-1626
    • Coates, J.C.1
  • 54
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • Petroski M.D., Deshaies R.J. Function and regulation of cullin-RING ubiquitin ligases. Nat. Rev. Mol. Cell Biol. 2005, 6:9-20.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 55
    • 57749088579 scopus 로고    scopus 로고
    • F-actin organization and pollen tube tip growth in Arabidopsis are dependent on the gametophyte-specific Armadillo repeat protein ARO1
    • Gebert M., et al. F-actin organization and pollen tube tip growth in Arabidopsis are dependent on the gametophyte-specific Armadillo repeat protein ARO1. Plant Cell 2008, 20:2798-2814.
    • (2008) Plant Cell , vol.20 , pp. 2798-2814
    • Gebert, M.1
  • 56
    • 0034237677 scopus 로고    scopus 로고
    • Drivers and passengers wanted! The role of kinesin-associated proteins
    • Manning B.D., Snyder M. Drivers and passengers wanted! The role of kinesin-associated proteins. Trends Cell Biol. 2000, 10:281-289.
    • (2000) Trends Cell Biol. , vol.10 , pp. 281-289
    • Manning, B.D.1    Snyder, M.2
  • 57
    • 33645220954 scopus 로고    scopus 로고
    • Role of the kinesin-2 family protein, KIF3, during mitosis
    • Haraguchi K., et al. Role of the kinesin-2 family protein, KIF3, during mitosis. J. Biol. Chem. 2006, 281:4094-4099.
    • (2006) J. Biol. Chem. , vol.281 , pp. 4094-4099
    • Haraguchi, K.1
  • 58
    • 57349120548 scopus 로고    scopus 로고
    • Kinesin superfamily-associated protein 3 is preferentially expressed in glutamatergic neurons and contributes to the excitatory control of female puberty
    • Choi J., et al. Kinesin superfamily-associated protein 3 is preferentially expressed in glutamatergic neurons and contributes to the excitatory control of female puberty. Endocrinology 2008, 149:6146-6156.
    • (2008) Endocrinology , vol.149 , pp. 6146-6156
    • Choi, J.1
  • 59
    • 60549104791 scopus 로고    scopus 로고
    • Mutant SOD1 impairs axonal transport of choline acetyltransferase and acetylcholine release by sequestering KAP3
    • Tateno M., et al. Mutant SOD1 impairs axonal transport of choline acetyltransferase and acetylcholine release by sequestering KAP3. Hum. Mol. Genet. 2009, 18:942-955.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 942-955
    • Tateno, M.1
  • 60
    • 67049155508 scopus 로고    scopus 로고
    • Reduced expression of the Kinesin-Associated Protein 3 (KIFAP3) gene increases survival in sporadic amyotrophic lateral sclerosis
    • Landers J.E., et al. Reduced expression of the Kinesin-Associated Protein 3 (KIFAP3) gene increases survival in sporadic amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:9004-9009.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 9004-9009
    • Landers, J.E.1
  • 61
    • 39149110563 scopus 로고    scopus 로고
    • The genome of the choanoflagellate Monosiga brevicollis and the origin of metazoans
    • King N., et al. The genome of the choanoflagellate Monosiga brevicollis and the origin of metazoans. Nature 2008, 451:783-788.
    • (2008) Nature , vol.451 , pp. 783-788
    • King, N.1
  • 62
    • 35348896591 scopus 로고    scopus 로고
    • The Chlamydomonas genome reveals the evolution of key animal and plant functions
    • Merchant S.S., et al. The Chlamydomonas genome reveals the evolution of key animal and plant functions. Science 2007, 318:245-250.
    • (2007) Science , vol.318 , pp. 245-250
    • Merchant, S.S.1
  • 63
    • 64849088316 scopus 로고    scopus 로고
    • Green evolution and dynamic adaptations revealed by genomes of the marine picoeukaryotes Micromonas
    • Worden A.Z., et al. Green evolution and dynamic adaptations revealed by genomes of the marine picoeukaryotes Micromonas. Science 2009, 324:268-272.
    • (2009) Science , vol.324 , pp. 268-272
    • Worden, A.Z.1
  • 64
    • 6044252163 scopus 로고    scopus 로고
    • The genome of the diatom Thalassiosira pseudonana: ecology, evolution, and metabolism
    • Armbrust E.V., et al. The genome of the diatom Thalassiosira pseudonana: ecology, evolution, and metabolism. Science 2004, 306:79-86.
    • (2004) Science , vol.306 , pp. 79-86
    • Armbrust, E.V.1
  • 65
    • 58149200936 scopus 로고    scopus 로고
    • GiardiaDB and TrichDB: integrated genomic resources for the eukaryotic protist pathogens Giardia lamblia and Trichomonas vaginalis
    • Aurrecoechea C., et al. GiardiaDB and TrichDB: integrated genomic resources for the eukaryotic protist pathogens Giardia lamblia and Trichomonas vaginalis. Nucleic Acids Res. 2009, 37:D526-D530.
    • (2009) Nucleic Acids Res. , vol.37
    • Aurrecoechea, C.1
  • 66
    • 33750858684 scopus 로고    scopus 로고
    • Global trends of whole-genome duplications revealed by the ciliate Paramecium tetraurelia
    • Aury J.M., et al. Global trends of whole-genome duplications revealed by the ciliate Paramecium tetraurelia. Nature 2006, 444:171-178.
    • (2006) Nature , vol.444 , pp. 171-178
    • Aury, J.M.1
  • 67
    • 58149307926 scopus 로고    scopus 로고
    • Refined annotation and assembly of the Tetrahymena thermophila genome sequence through EST analysis, comparative genomic hybridization, and targeted gap closure
    • Coyne R.S., et al. Refined annotation and assembly of the Tetrahymena thermophila genome sequence through EST analysis, comparative genomic hybridization, and targeted gap closure. BMC Genomics 2008, 9:562.
    • (2008) BMC Genomics , vol.9 , pp. 562
    • Coyne, R.S.1
  • 68
    • 70349281388 scopus 로고    scopus 로고
    • Genome sequence and analysis of the Irish potato famine pathogen Phytophthora infestans
    • Haas B.J., et al. Genome sequence and analysis of the Irish potato famine pathogen Phytophthora infestans. Nature 2009, 461:393-398.
    • (2009) Nature , vol.461 , pp. 393-398
    • Haas, B.J.1
  • 69
    • 33748329373 scopus 로고    scopus 로고
    • Phytophthora genome sequences uncover evolutionary origins and mechanisms of pathogenesis
    • Tyler B.M., et al. Phytophthora genome sequences uncover evolutionary origins and mechanisms of pathogenesis. Science 2006, 313:1261-1266.
    • (2006) Science , vol.313 , pp. 1261-1266
    • Tyler, B.M.1
  • 70
    • 18344395923 scopus 로고    scopus 로고
    • The genome of the social amoeba Dictyostelium discoideum
    • Eichinger L., et al. The genome of the social amoeba Dictyostelium discoideum. Nature 2005, 435:43-57.
    • (2005) Nature , vol.435 , pp. 43-57
    • Eichinger, L.1
  • 71
    • 72949110575 scopus 로고    scopus 로고
    • Unleashing formins to remodel the actin and microtubule cytoskeletons
    • Chesarone M.A., et al. Unleashing formins to remodel the actin and microtubule cytoskeletons. Nat. Rev. Mol. Cell Biol. 2010, 11:62-74.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 62-74
    • Chesarone, M.A.1
  • 72
    • 70350217766 scopus 로고    scopus 로고
    • Actin bundling in plants
    • Thomas C., et al. Actin bundling in plants. Cell Motil. Cytoskeleton 2009, 66:940-957.
    • (2009) Cell Motil. Cytoskeleton , vol.66 , pp. 940-957
    • Thomas, C.1
  • 73
    • 58049213341 scopus 로고    scopus 로고
    • Specificity of interactions between mDia isoforms and Rho proteins
    • Lammers M., et al. Specificity of interactions between mDia isoforms and Rho proteins. J. Biol. Chem. 2008, 283:35236-35246.
    • (2008) J. Biol. Chem. , vol.283 , pp. 35236-35246
    • Lammers, M.1
  • 74
    • 4444360489 scopus 로고    scopus 로고
    • EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and promote cell migration
    • Wen Y., et al. EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and promote cell migration. Nat. Cell Biol. 2004, 6:820-830.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 820-830
    • Wen, Y.1
  • 75
    • 33748759561 scopus 로고    scopus 로고
    • Conserved and specific functions of axoneme components in trypanosome motility
    • Branche C., et al. Conserved and specific functions of axoneme components in trypanosome motility. J. Cell Sci. 2006, 119:3443-3455.
    • (2006) J. Cell Sci. , vol.119 , pp. 3443-3455
    • Branche, C.1
  • 76
    • 33646272170 scopus 로고    scopus 로고
    • Flagellar motility contributes to cytokinesis in Trypanosoma brucei and is modulated by an evolutionarily conserved dynein regulatory system
    • Ralston K.S., et al. Flagellar motility contributes to cytokinesis in Trypanosoma brucei and is modulated by an evolutionarily conserved dynein regulatory system. Eukaryot. Cell 2006, 5:696-711.
    • (2006) Eukaryot. Cell , vol.5 , pp. 696-711
    • Ralston, K.S.1
  • 77
    • 37849032457 scopus 로고    scopus 로고
    • The Physcomitrella genome reveals evolutionary insights into the conquest of land by plants
    • Rensing S.A., et al. The Physcomitrella genome reveals evolutionary insights into the conquest of land by plants. Science 2008, 319:64-69.
    • (2008) Science , vol.319 , pp. 64-69
    • Rensing, S.A.1
  • 78
    • 65549170297 scopus 로고    scopus 로고
    • Fused has evolved divergent roles in vertebrate Hedgehog signalling and motile ciliogenesis
    • Wilson C.W., et al. Fused has evolved divergent roles in vertebrate Hedgehog signalling and motile ciliogenesis. Nature 2009, 459:98-102.
    • (2009) Nature , vol.459 , pp. 98-102
    • Wilson, C.W.1
  • 79
    • 22244458310 scopus 로고    scopus 로고
    • Proteomic analysis of a eukaryotic cilium
    • Pazour G.J., et al. Proteomic analysis of a eukaryotic cilium. J. Cell Biol. 2005, 170:103-113.
    • (2005) J. Cell Biol. , vol.170 , pp. 103-113
    • Pazour, G.J.1
  • 80
    • 33645744387 scopus 로고    scopus 로고
    • Radial spoke proteins of Chlamydomonas flagella
    • Yang P., et al. Radial spoke proteins of Chlamydomonas flagella. J. Cell Sci. 2006, 119:1165-1174.
    • (2006) J. Cell Sci. , vol.119 , pp. 1165-1174
    • Yang, P.1
  • 81
    • 40049098664 scopus 로고    scopus 로고
    • Molecular characterization of axonemal proteins and signaling molecules responsible for chemoattractant-induced sperm activation in Ciona intestinalis
    • Hozumi A., et al. Molecular characterization of axonemal proteins and signaling molecules responsible for chemoattractant-induced sperm activation in Ciona intestinalis. Cell Motil. Cytoskeleton 2008, 65:249-267.
    • (2008) Cell Motil. Cytoskeleton , vol.65 , pp. 249-267
    • Hozumi, A.1
  • 82
    • 33947219266 scopus 로고    scopus 로고
    • Large-scale mapping of human protein-protein interactions by mass spectrometry
    • Ewing R.M., et al. Large-scale mapping of human protein-protein interactions by mass spectrometry. Mol. Syst. Biol. 2007, 3:89.
    • (2007) Mol. Syst. Biol. , vol.3 , pp. 89
    • Ewing, R.M.1
  • 83
    • 0035868595 scopus 로고    scopus 로고
    • Isolation, characterization, and mapping of the mouse and human WDR8 genes, members of a novel WD-repeat gene family
    • Koshizuka Y., et al. Isolation, characterization, and mapping of the mouse and human WDR8 genes, members of a novel WD-repeat gene family. Genomics 2001, 72:252-259.
    • (2001) Genomics , vol.72 , pp. 252-259
    • Koshizuka, Y.1
  • 84
    • 28444448427 scopus 로고    scopus 로고
    • A divergent cellular role for the FUSED kinase family in the plant-specific cytokinetic phragmoplast
    • Oh S.A., et al. A divergent cellular role for the FUSED kinase family in the plant-specific cytokinetic phragmoplast. Curr. Biol. 2005, 15:2107-2111.
    • (2005) Curr. Biol. , vol.15 , pp. 2107-2111
    • Oh, S.A.1
  • 85
    • 50049103371 scopus 로고    scopus 로고
    • Tsunami, the Dictyostelium homolog of the Fused kinase, is required for polarization and chemotaxis
    • Tang L., et al. tsunami, the Dictyostelium homolog of the Fused kinase, is required for polarization and chemotaxis. Genes Dev. 2008, 22:2278-2290.
    • (2008) Genes Dev. , vol.22 , pp. 2278-2290
    • Tang, L.1
  • 86
    • 57749205263 scopus 로고    scopus 로고
    • A possible role of mouse Fused (STK36) in Hedgehog signaling and Gli transcription factor regulation
    • Maloveryan A., et al. A possible role of mouse Fused (STK36) in Hedgehog signaling and Gli transcription factor regulation. J. Cell Commun. Signal. 2007, 1:165-173.
    • (2007) J. Cell Commun. Signal. , vol.1 , pp. 165-173
    • Maloveryan, A.1
  • 87
    • 23344442477 scopus 로고    scopus 로고
    • Loss of the serine/threonine kinase fused results in postnatal growth defects and lethality due to progressive hydrocephalus
    • Merchant M., et al. Loss of the serine/threonine kinase fused results in postnatal growth defects and lethality due to progressive hydrocephalus. Mol. Cell. Biol. 2005, 25:7054-7068.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 7054-7068
    • Merchant, M.1
  • 88
    • 33645977763 scopus 로고    scopus 로고
    • Fused regulates germline cyst mitosis and differentiation during Drosophila oogenesis
    • Narbonne-Reveau K., et al. fused regulates germline cyst mitosis and differentiation during Drosophila oogenesis. Mech. Dev. 2006, 123:197-209.
    • (2006) Mech. Dev. , vol.123 , pp. 197-209
    • Narbonne-Reveau, K.1
  • 89
    • 33749238361 scopus 로고    scopus 로고
    • The protein kinase genes MAP3K epsilon 1 and MAP3K epsilon 2 are required for pollen viability in Arabidopsis thaliana
    • Chaiwongsar S., et al. The protein kinase genes MAP3K epsilon 1 and MAP3K epsilon 2 are required for pollen viability in Arabidopsis thaliana. Plant J. 2006, 48:193-205.
    • (2006) Plant J. , vol.48 , pp. 193-205
    • Chaiwongsar, S.1
  • 90
    • 0028240790 scopus 로고
    • The cdc7 protein kinase is a dosage dependent regulator of septum formation in fission yeast
    • Fankhauser C., Simanis V. The cdc7 protein kinase is a dosage dependent regulator of septum formation in fission yeast. EMBO J. 1994, 13:3011-3019.
    • (1994) EMBO J. , vol.13 , pp. 3011-3019
    • Fankhauser, C.1    Simanis, V.2
  • 91
    • 70350214795 scopus 로고    scopus 로고
    • The STE group kinase SepA controls cleavage furrow formation in Dictyostelium
    • Muller-Taubenberger A., et al. The STE group kinase SepA controls cleavage furrow formation in Dictyostelium. Cell Motil. Cytoskeleton 2009, 66:929-939.
    • (2009) Cell Motil. Cytoskeleton , vol.66 , pp. 929-939
    • Muller-Taubenberger, A.1
  • 92
    • 0038739131 scopus 로고    scopus 로고
    • Never say never. The NIMA-related protein kinases in mitotic control
    • O'Connell M.J., et al. Never say never. The NIMA-related protein kinases in mitotic control. Trends Cell Biol. 2003, 13:221-228.
    • (2003) Trends Cell Biol. , vol.13 , pp. 221-228
    • O'Connell, M.J.1
  • 93
    • 37249032403 scopus 로고    scopus 로고
    • Armadillo repeat-containing kinesins and a NIMA-related kinase are required for epidermal-cell morphogenesis in Arabidopsis
    • Sakai T., et al. Armadillo repeat-containing kinesins and a NIMA-related kinase are required for epidermal-cell morphogenesis in Arabidopsis. Plant J. 2008, 53:157-171.
    • (2008) Plant J. , vol.53 , pp. 157-171
    • Sakai, T.1
  • 94
    • 33846250885 scopus 로고    scopus 로고
    • Multifunctional arm repeat domains in plants
    • Samuel M.A., et al. Multifunctional arm repeat domains in plants. Int. Rev. Cytol. 2006, 253:1-26.
    • (2006) Int. Rev. Cytol. , vol.253 , pp. 1-26
    • Samuel, M.A.1
  • 95
    • 64949084332 scopus 로고    scopus 로고
    • The diversity of plant U-box E3 ubiquitin ligases: from upstream activators to downstream target substrates
    • Yee D., Goring D.R. The diversity of plant U-box E3 ubiquitin ligases: from upstream activators to downstream target substrates. J. Exp. Bot. 2009, 60:1109-1121.
    • (2009) J. Exp. Bot. , vol.60 , pp. 1109-1121
    • Yee, D.1    Goring, D.R.2
  • 96
    • 43949116605 scopus 로고    scopus 로고
    • Armadillo repeat proteins: versatile regulators of plant development and signalling
    • Springer, L. Bogre, G. Beemster (Eds.)
    • Coates J.C. Armadillo repeat proteins: versatile regulators of plant development and signalling. Plant Growth Signalling 2008, 299-314. Springer. L. Bogre, G. Beemster (Eds.).
    • (2008) Plant Growth Signalling , pp. 299-314
    • Coates, J.C.1
  • 97
    • 31444434131 scopus 로고    scopus 로고
    • A synthetic defect in protein degradation caused by loss of Ufd4 and Rad23
    • Ju D., Xie Y. A synthetic defect in protein degradation caused by loss of Ufd4 and Rad23. Biochem. Biophys. Res. Commun. 2006, 341:648-652.
    • (2006) Biochem. Biophys. Res. Commun. , vol.341 , pp. 648-652
    • Ju, D.1    Xie, Y.2
  • 98
    • 34250674456 scopus 로고    scopus 로고
    • RanBPM, Muskelin, p48EMLP, p44CTLH, and the armadillo-repeat proteins ARMC8alpha and ARMC8beta are components of the CTLH complex
    • Kobayashi N., et al. RanBPM, Muskelin, p48EMLP, p44CTLH, and the armadillo-repeat proteins ARMC8alpha and ARMC8beta are components of the CTLH complex. Gene 2007, 396:236-247.
    • (2007) Gene , vol.396 , pp. 236-247
    • Kobayashi, N.1
  • 99
    • 42449094535 scopus 로고    scopus 로고
    • Proteasome-dependent degradation of alpha-catenin is regulated by interaction with ARMc8alpha
    • Suzuki T., et al. Proteasome-dependent degradation of alpha-catenin is regulated by interaction with ARMc8alpha. Biochem. J. 2008, 411:581-591.
    • (2008) Biochem. J. , vol.411 , pp. 581-591
    • Suzuki, T.1
  • 100
    • 85056025345 scopus 로고    scopus 로고
    • Armadillo repeat containing 8alpha binds to HRS and promotes HRS interaction with ubiquitinated proteins
    • Tomaru K., et al. Armadillo repeat containing 8alpha binds to HRS and promotes HRS interaction with ubiquitinated proteins. Open Biochem. J. 2010, 4:1-8.
    • (2010) Open Biochem. J. , vol.4 , pp. 1-8
    • Tomaru, K.1
  • 101
    • 0037346955 scopus 로고    scopus 로고
    • Sequence, gene structure, and expression pattern of CTNNBL1, a minor-class intron-containing gene - evidence for a role in apoptosis
    • Jabbour L., et al. Sequence, gene structure, and expression pattern of CTNNBL1, a minor-class intron-containing gene - evidence for a role in apoptosis. Genomics 2003, 81:292-303.
    • (2003) Genomics , vol.81 , pp. 292-303
    • Jabbour, L.1
  • 102
    • 49349112190 scopus 로고    scopus 로고
    • Interaction between antibody-diversification enzyme AID and spliceosome-associated factor CTNNBL1
    • Conticello S.G., et al. Interaction between antibody-diversification enzyme AID and spliceosome-associated factor CTNNBL1. Mol. Cell 2008, 31:474-484.
    • (2008) Mol. Cell , vol.31 , pp. 474-484
    • Conticello, S.G.1
  • 103
    • 42649115803 scopus 로고    scopus 로고
    • Role of osteopontin in cellular signaling and metastatic phenotype
    • El-Tanani M.K. Role of osteopontin in cellular signaling and metastatic phenotype. Front. Biosci. 2008, 13:4276-4284.
    • (2008) Front. Biosci. , vol.13 , pp. 4276-4284
    • El-Tanani, M.K.1
  • 104
    • 33846539150 scopus 로고    scopus 로고
    • Atomic model of human Rcd-1 reveals an armadillo-like-repeat protein with in vitro nucleic acid binding properties
    • Garces R.G., et al. Atomic model of human Rcd-1 reveals an armadillo-like-repeat protein with in vitro nucleic acid binding properties. Protein Sci. 2007, 16:176-188.
    • (2007) Protein Sci. , vol.16 , pp. 176-188
    • Garces, R.G.1
  • 105
    • 43749087387 scopus 로고    scopus 로고
    • Components of the CCR4-NOT complex function as nuclear hormone receptor coactivators via association with the NRC-interacting Factor NIF-1
    • Garapaty S., et al. Components of the CCR4-NOT complex function as nuclear hormone receptor coactivators via association with the NRC-interacting Factor NIF-1. J. Biol. Chem. 2008, 283:6806-6816.
    • (2008) J. Biol. Chem. , vol.283 , pp. 6806-6816
    • Garapaty, S.1
  • 106
    • 3042606545 scopus 로고    scopus 로고
    • C-Myb protein interacts with Rcd-1, a component of the CCR4 transcription mediator complex
    • Haas M., et al. c-Myb protein interacts with Rcd-1, a component of the CCR4 transcription mediator complex. Biochemistry 2004, 43:8152-8159.
    • (2004) Biochemistry , vol.43 , pp. 8152-8159
    • Haas, M.1
  • 107
    • 0036790655 scopus 로고    scopus 로고
    • Mammalian Rcd1 is a novel transcriptional cofactor that mediates retinoic acid-induced cell differentiation
    • Hiroi N., et al. Mammalian Rcd1 is a novel transcriptional cofactor that mediates retinoic acid-induced cell differentiation. EMBO J. 2002, 21:5235-5244.
    • (2002) EMBO J. , vol.21 , pp. 5235-5244
    • Hiroi, N.1
  • 108
    • 3042609939 scopus 로고    scopus 로고
    • The expanding family of MyD88-like adaptors in Toll-like receptor signal transduction
    • McGettrick A.F., O'Neill L.A. The expanding family of MyD88-like adaptors in Toll-like receptor signal transduction. Mol. Immunol. 2004, 41:577-582.
    • (2004) Mol. Immunol. , vol.41 , pp. 577-582
    • McGettrick, A.F.1    O'Neill, L.A.2
  • 109
    • 0038112138 scopus 로고    scopus 로고
    • The role of adaptor protein Ste50-dependent regulation of the MAPKKK Ste11 in multiple signalling pathways of yeast
    • Ramezani-Rad M. The role of adaptor protein Ste50-dependent regulation of the MAPKKK Ste11 in multiple signalling pathways of yeast. Curr. Genet. 2003, 43:161-170.
    • (2003) Curr. Genet. , vol.43 , pp. 161-170
    • Ramezani-Rad, M.1
  • 110
    • 51349158231 scopus 로고    scopus 로고
    • Signalling adaptors used by Toll-like receptors: an update
    • Kenny E.F., O'Neill L.A. Signalling adaptors used by Toll-like receptors: an update. Cytokine 2008, 43:342-349.
    • (2008) Cytokine , vol.43 , pp. 342-349
    • Kenny, E.F.1    O'Neill, L.A.2
  • 111
    • 69449098052 scopus 로고    scopus 로고
    • The immune adaptor molecule SARM modulates tumor necrosis factor alpha production and microglia activation in the brainstem and restricts West Nile Virus pathogenesis
    • Szretter K.J., et al. The immune adaptor molecule SARM modulates tumor necrosis factor alpha production and microglia activation in the brainstem and restricts West Nile Virus pathogenesis. J. Virol. 2009, 83:9329-9338.
    • (2009) J. Virol. , vol.83 , pp. 9329-9338
    • Szretter, K.J.1
  • 112
    • 33748880024 scopus 로고    scopus 로고
    • DisSARMing Toll-like receptor signaling
    • O'Neill L.A. DisSARMing Toll-like receptor signaling. Nat. Immunol. 2006, 7:1023-1025.
    • (2006) Nat. Immunol. , vol.7 , pp. 1023-1025
    • O'Neill, L.A.1
  • 113
  • 114
    • 44649176937 scopus 로고    scopus 로고
    • Protein quality control gets muscle into shape
    • Kim J., et al. Protein quality control gets muscle into shape. Trends Cell Biol. 2008, 18:264-272.
    • (2008) Trends Cell Biol. , vol.18 , pp. 264-272
    • Kim, J.1
  • 115
    • 35548988452 scopus 로고    scopus 로고
    • Hypermethylation of TTC12 gene in acute lymphoblastic leukemia
    • Wattanawaraporn R., et al. Hypermethylation of TTC12 gene in acute lymphoblastic leukemia. Leukemia 2007, 21:2370-2373.
    • (2007) Leukemia , vol.21 , pp. 2370-2373
    • Wattanawaraporn, R.1
  • 116
    • 57249083992 scopus 로고    scopus 로고
    • Haplotypic variants in DRD2, ANKK1, TTC12, and NCAM1 are associated with comorbid alcohol and drug dependence
    • Yang B.Z., et al. Haplotypic variants in DRD2, ANKK1, TTC12, and NCAM1 are associated with comorbid alcohol and drug dependence. Alcohol Clin. Exp. Res. 2008, 32:2117-2127.
    • (2008) Alcohol Clin. Exp. Res. , vol.32 , pp. 2117-2127
    • Yang, B.Z.1
  • 117
    • 64949154995 scopus 로고    scopus 로고
    • Evolution of the metazoan-specific importin alpha gene family
    • Mason D.A., et al. Evolution of the metazoan-specific importin alpha gene family. J. Mol. Evol. 2009, 68:351-365.
    • (2009) J. Mol. Evol. , vol.68 , pp. 351-365
    • Mason, D.A.1
  • 118
    • 4444291705 scopus 로고    scopus 로고
    • Importin alpha: a multipurpose nuclear-transport receptor
    • Goldfarb D.S., et al. Importin alpha: a multipurpose nuclear-transport receptor. Trends Cell Biol. 2004, 14:505-514.
    • (2004) Trends Cell Biol. , vol.14 , pp. 505-514
    • Goldfarb, D.S.1
  • 119
    • 38949210293 scopus 로고    scopus 로고
    • Regulation of nuclear import during differentiation; the imp alpha gene family and spermatogenesis
    • Holt J.E., et al. Regulation of nuclear import during differentiation; the imp alpha gene family and spermatogenesis. Curr. Genomics 2007, 8:323-334.
    • (2007) Curr. Genomics , vol.8 , pp. 323-334
    • Holt, J.E.1
  • 120
    • 68049136117 scopus 로고    scopus 로고
    • Role of importin alpha8, a new member of the importin alpha family of nuclear transport proteins, in early embryonic development in cattle
    • Tejomurtula J., et al. Role of importin alpha8, a new member of the importin alpha family of nuclear transport proteins, in early embryonic development in cattle. Biol. Reprod. 2009, 81:333-342.
    • (2009) Biol. Reprod. , vol.81 , pp. 333-342
    • Tejomurtula, J.1
  • 121
    • 40849134397 scopus 로고    scopus 로고
    • Drosophila importin alpha1 performs paralog-specific functions essential for gametogenesis
    • Ratan R., et al. Drosophila importin alpha1 performs paralog-specific functions essential for gametogenesis. Genetics 2008, 178:839-850.
    • (2008) Genetics , vol.178 , pp. 839-850
    • Ratan, R.1
  • 122
    • 54849442381 scopus 로고    scopus 로고
    • IMPa-4, an Arabidopsis importin alpha isoform, is preferentially involved in agrobacterium-mediated plant transformation
    • Bhattacharjee S., et al. IMPa-4, an Arabidopsis importin alpha isoform, is preferentially involved in agrobacterium-mediated plant transformation. Plant Cell 2008, 20:2661-2680.
    • (2008) Plant Cell , vol.20 , pp. 2661-2680
    • Bhattacharjee, S.1
  • 123
    • 20544446717 scopus 로고    scopus 로고
    • An importin alpha homolog, MOS6, plays an important role in plant innate immunity
    • Palma K., et al. An importin alpha homolog, MOS6, plays an important role in plant innate immunity. Curr. Biol. 2005, 15:1129-1135.
    • (2005) Curr. Biol. , vol.15 , pp. 1129-1135
    • Palma, K.1
  • 124
    • 17144404877 scopus 로고    scopus 로고
    • Comparative genomics, evolution and origins of the nuclear envelope and nuclear pore complex
    • Mans B.J., et al. Comparative genomics, evolution and origins of the nuclear envelope and nuclear pore complex. Cell Cycle 2004, 3:1612-1637.
    • (2004) Cell Cycle , vol.3 , pp. 1612-1637
    • Mans, B.J.1
  • 125
    • 33744812407 scopus 로고    scopus 로고
    • Comparative genomics and structural biology of the molecular innovations of eukaryotes
    • Aravind L., et al. Comparative genomics and structural biology of the molecular innovations of eukaryotes. Curr. Opin. Struct. Biol. 2006, 16:409-419.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 409-419
    • Aravind, L.1
  • 126
    • 0032510103 scopus 로고    scopus 로고
    • Nuclear localization signal-independent and importin/karyopherin-independent nuclear import of beta-catenin
    • Fagotto F., et al. Nuclear localization signal-independent and importin/karyopherin-independent nuclear import of beta-catenin. Curr. Biol. 1998, 8:181-190.
    • (1998) Curr. Biol. , vol.8 , pp. 181-190
    • Fagotto, F.1
  • 127
    • 0038558166 scopus 로고    scopus 로고
    • Importin alpha-regulated nucleation of microtubules by TPX2
    • Schatz C.A., et al. Importin alpha-regulated nucleation of microtubules by TPX2. EMBO J. 2003, 22:2060-2070.
    • (2003) EMBO J. , vol.22 , pp. 2060-2070
    • Schatz, C.A.1
  • 128
    • 0027145102 scopus 로고
    • Kingdom protozoa and its 18 phyla
    • Cavalier-Smith T. Kingdom protozoa and its 18 phyla. Microbiol. Rev. 1993, 57:953-994.
    • (1993) Microbiol. Rev. , vol.57 , pp. 953-994
    • Cavalier-Smith, T.1
  • 129
    • 58749104911 scopus 로고    scopus 로고
    • An overview of the Babesia, Plasmodium and Theileria genomes: a comparative perspective
    • Lau A.O. An overview of the Babesia, Plasmodium and Theileria genomes: a comparative perspective. Mol. Biochem. Parasitol. 2009, 164:1-8.
    • (2009) Mol. Biochem. Parasitol. , vol.164 , pp. 1-8
    • Lau, A.O.1
  • 130
    • 4644353894 scopus 로고    scopus 로고
    • Comparative analysis of apicomplexa and genomic diversity in eukaryotes
    • Templeton T.J., et al. Comparative analysis of apicomplexa and genomic diversity in eukaryotes. Genome Res. 2004, 14:1686-1695.
    • (2004) Genome Res. , vol.14 , pp. 1686-1695
    • Templeton, T.J.1
  • 131
    • 67650076197 scopus 로고    scopus 로고
    • The origins of apicomplexan sequence innovation
    • Wasmuth J., et al. The origins of apicomplexan sequence innovation. Genome Res. 2009, 19:1202-1213.
    • (2009) Genome Res. , vol.19 , pp. 1202-1213
    • Wasmuth, J.1
  • 132
    • 33846120023 scopus 로고    scopus 로고
    • ApiDB: integrated resources for the apicomplexan bioinformatics resource center
    • Aurrecoechea C., et al. ApiDB: integrated resources for the apicomplexan bioinformatics resource center. Nucleic Acids Res. 2007, 35:D427-D430.
    • (2007) Nucleic Acids Res. , vol.35
    • Aurrecoechea, C.1
  • 133
    • 0033764838 scopus 로고    scopus 로고
    • The development of genetic tools for dissecting the biology of malaria parasites
    • de Koning-Ward T.F., et al. The development of genetic tools for dissecting the biology of malaria parasites. Annu. Rev. Microbiol. 2000, 54:157-185.
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 157-185
    • de Koning-Ward, T.F.1
  • 134
    • 67649415132 scopus 로고    scopus 로고
    • Role of the parasite and host cytoskeleton in apicomplexa parasitism
    • Frenal K., Soldati-Favre D. Role of the parasite and host cytoskeleton in apicomplexa parasitism. Cell Host Microbe 2009, 5:602-611.
    • (2009) Cell Host Microbe , vol.5 , pp. 602-611
    • Frenal, K.1    Soldati-Favre, D.2
  • 135
    • 4143126756 scopus 로고    scopus 로고
    • More than one way to build a flagellum: comparative genomics of parasitic protozoa
    • Briggs L.J., et al. More than one way to build a flagellum: comparative genomics of parasitic protozoa. Curr. Biol. 2004, 14:R611-R612.
    • (2004) Curr. Biol. , vol.14
    • Briggs, L.J.1
  • 136
    • 0020759092 scopus 로고
    • Sexuality in piroplasms as revealed by electron microscopy in Babesia microti
    • Rudzinska M.A., et al. Sexuality in piroplasms as revealed by electron microscopy in Babesia microti. Proc. Natl. Acad. Sci. U. S. A. 1983, 80:2966-2970.
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 2966-2970
    • Rudzinska, M.A.1
  • 137
    • 0034708216 scopus 로고    scopus 로고
    • The U box is a modified RING finger - a common domain in ubiquitination
    • Aravind L., Koonin E.V. The U box is a modified RING finger - a common domain in ubiquitination. Curr. Biol. 2000, 10:R132-R134.
    • (2000) Curr. Biol. , vol.10
    • Aravind, L.1    Koonin, E.V.2
  • 138
    • 56249098614 scopus 로고    scopus 로고
    • The Phaeodactylum genome reveals the evolutionary history of diatom genomes
    • Bowler C., et al. The Phaeodactylum genome reveals the evolutionary history of diatom genomes. Nature 2008, 456:239-244.
    • (2008) Nature , vol.456 , pp. 239-244
    • Bowler, C.1
  • 139
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: application to microtubules and the ribosome
    • Baker N.A., et al. Electrostatics of nanosystems: application to microtubules and the ribosome. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:10037-10041.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 10037-10041
    • Baker, N.A.1
  • 140
    • 0012293235 scopus 로고    scopus 로고
    • DeLano Scientific LLC
    • DeLano W.L. PyMol 2008, DeLano Scientific LLC.
    • (2008) PyMol
    • DeLano, W.L.1
  • 141
    • 0037841805 scopus 로고    scopus 로고
    • The deep roots of eukaryotes
    • Baldauf S.L. The deep roots of eukaryotes. Science 2003, 300:1703-1706.
    • (2003) Science , vol.300 , pp. 1703-1706
    • Baldauf, S.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.