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Volumn 37, Issue 3, 2015, Pages 248-256

MAPping the Ndc80 loop in cancer: A possible link between Ndc80/Hec1 overproduction and cancer formation

Author keywords

Cancer; Ch TOG; Kinesin 8; Loop; Ndc80 Hec1; Overexpression; TACC

Indexed keywords

CELL PROTEIN; HEC1 PROTEIN; MICROTUBULE ASSOCIATED PROTEIN; NDC80 COMPLEX; TACC PROTEIN; TOG PROTEIN; UNCLASSIFIED DRUG; NDC80 PROTEIN, HUMAN; NUCLEAR PROTEIN;

EID: 84925656186     PISSN: 02659247     EISSN: 15211878     Source Type: Journal    
DOI: 10.1002/bies.201400175     Document Type: Article
Times cited : (33)

References (102)
  • 2
    • 0031004175 scopus 로고    scopus 로고
    • Genetic instability in colorectal cancers
    • Lengauer C, Kinzler KW, Vogelstein B. 1997. Genetic instability in colorectal cancers. Nature 386: 623-7.
    • (1997) Nature , vol.386 , pp. 623-627
    • Lengauer, C.1    Kinzler, K.W.2    Vogelstein, B.3
  • 3
    • 0028823831 scopus 로고
    • Characterization of the cDNA and pattern of expression of a new gene over-expressed in human hepatomas and colonic tumors
    • Charrasse S, Mazel M, Taviaux S, Berta P, et al. 1995. Characterization of the cDNA and pattern of expression of a new gene over-expressed in human hepatomas and colonic tumors. Eur J Biochem 234: 406-13.
    • (1995) Eur J Biochem , vol.234 , pp. 406-413
    • Charrasse, S.1    Mazel, M.2    Taviaux, S.3    Berta, P.4
  • 4
    • 0033152107 scopus 로고    scopus 로고
    • The third member of the transforming acidic coiled coil-containing gene family, TACC3, maps in 4p16, close to translocation breakpoints in multiple myeloma, and is upregulated in various cancer cell lines
    • Still IH, Vince P, Cowell JK. 1999. The third member of the transforming acidic coiled coil-containing gene family, TACC3, maps in 4p16, close to translocation breakpoints in multiple myeloma, and is upregulated in various cancer cell lines. Genomics 58: 165-70.
    • (1999) Genomics , vol.58 , pp. 165-170
    • Still, I.H.1    Vince, P.2    Cowell, J.K.3
  • 6
    • 79959416796 scopus 로고    scopus 로고
    • Bub1 overexpression induces aneuploidy and tumor formation through Aurora B kinase hyperactivation
    • Ricke RM, Jeganathan KB, van Deursen JM. 2011. Bub1 overexpression induces aneuploidy and tumor formation through Aurora B kinase hyperactivation. J Cell Biol 193: 1049-64.
    • (2011) J Cell Biol , vol.193 , pp. 1049-1064
    • Ricke, R.M.1    Jeganathan, K.B.2    van Deursen, J.M.3
  • 7
    • 84900833119 scopus 로고    scopus 로고
    • Spindle and kinetochore-associated protein 1 is overexpressed in gastric cancer and modulates cell growth
    • Sun W, Yao L, Jiang B, Guo L, et al. 2014. Spindle and kinetochore-associated protein 1 is overexpressed in gastric cancer and modulates cell growth. Mol Cell Biochem 391: 167-74.
    • (2014) Mol Cell Biochem , vol.391 , pp. 167-174
    • Sun, W.1    Yao, L.2    Jiang, B.3    Guo, L.4
  • 8
    • 77956276018 scopus 로고    scopus 로고
    • Kif18A is involved in human breast carcinogenesis
    • Zhang C, Zhu C, Chen H, Li L, et al. 2010. Kif18A is involved in human breast carcinogenesis. Carcinogenesis 31: 1676-84.
    • (2010) Carcinogenesis , vol.31 , pp. 1676-1684
    • Zhang, C.1    Zhu, C.2    Chen, H.3    Li, L.4
  • 9
    • 80053308276 scopus 로고    scopus 로고
    • Kinesin 18A expression: clinical relevance to colorectal cancer progression
    • Nagahara M, Nishida N, Iwatsuki M, Ishimaru S, et al. 2011. Kinesin 18A expression: clinical relevance to colorectal cancer progression. Int J Cancer 129: 2543-52.
    • (2011) Int J Cancer , vol.129 , pp. 2543-2552
    • Nagahara, M.1    Nishida, N.2    Iwatsuki, M.3    Ishimaru, S.4
  • 10
    • 0030864009 scopus 로고    scopus 로고
    • HEC, a novel nuclear protein rich in leucine heptad repeats specifically involved in mitosis
    • Chen Y, Riley DJ, Chen PL, Lee WH. 1997. HEC, a novel nuclear protein rich in leucine heptad repeats specifically involved in mitosis. Mol Cell Biol 17: 6049-56.
    • (1997) Mol Cell Biol , vol.17 , pp. 6049-6056
    • Chen, Y.1    Riley, D.J.2    Chen, P.L.3    Lee, W.H.4
  • 11
    • 33751278753 scopus 로고    scopus 로고
    • Activation of CDCA1-KNTC2, members of centromere protein complex, involved in pulmonary carcinogenesis
    • Hayama S, Daigo Y, Kato T, Ishikawa N, et al. 2006. Activation of CDCA1-KNTC2, members of centromere protein complex, involved in pulmonary carcinogenesis. Cancer Res 66: 10339-48.
    • (2006) Cancer Res , vol.66 , pp. 10339-10348
    • Hayama, S.1    Daigo, Y.2    Kato, T.3    Ishikawa, N.4
  • 12
    • 55949096605 scopus 로고    scopus 로고
    • Hec1 overexpression hyperactivates the mitotic checkpoint and induces tumor formation in vivo
    • Diaz-Rodriguez E, Sotillo R, Schvartzman JM, Benezra R. 2008. Hec1 overexpression hyperactivates the mitotic checkpoint and induces tumor formation in vivo. Proc Natl Acad Sci USA 105: 16719-24.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 16719-16724
    • Diaz-Rodriguez, E.1    Sotillo, R.2    Schvartzman, J.M.3    Benezra, R.4
  • 13
    • 35948960798 scopus 로고    scopus 로고
    • Transforming acidic coiled-coil 3 and Aurora-A interact in human thyrocytes and their expression is deregulated in thyroid cancer tissues
    • Ulisse S, Baldini E, Toller M, Delcros JG, et al. 2007. Transforming acidic coiled-coil 3 and Aurora-A interact in human thyrocytes and their expression is deregulated in thyroid cancer tissues. Endocr Relat Cancer 14: 827-37.
    • (2007) Endocr Relat Cancer , vol.14 , pp. 827-837
    • Ulisse, S.1    Baldini, E.2    Toller, M.3    Delcros, J.G.4
  • 14
    • 9144253124 scopus 로고    scopus 로고
    • Slippage of mitotic arrest and enhanced tumor development in mice with BubR1 haploinsufficiency
    • Dai W, Wang Q, Liu T, Swamy M, et al. 2004. Slippage of mitotic arrest and enhanced tumor development in mice with BubR1 haploinsufficiency. Cancer Res 64: 440-5.
    • (2004) Cancer Res , vol.64 , pp. 440-445
    • Dai, W.1    Wang, Q.2    Liu, T.3    Swamy, M.4
  • 15
    • 1842533070 scopus 로고    scopus 로고
    • Complete loss of the tumor suppressor MAD2 causes premature cyclin B degradation and mitotic failure in human somatic cells
    • Michel L, Diaz-Rodriguez E, Narayan G, Hernando E, et al. 2004. Complete loss of the tumor suppressor MAD2 causes premature cyclin B degradation and mitotic failure in human somatic cells. Proc Natl Acad Sci USA 101: 4459-64.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4459-4464
    • Michel, L.1    Diaz-Rodriguez, E.2    Narayan, G.3    Hernando, E.4
  • 16
    • 23844460843 scopus 로고    scopus 로고
    • Architecture of the human ndc80-hec1 complex, a critical constituent of the outer kinetochore
    • Ciferri C, De Luca J, Monzani S, Ferrari KJ, et al. 2005. Architecture of the human ndc80-hec1 complex, a critical constituent of the outer kinetochore. J Biol Chem 280: 29088-95.
    • (2005) J Biol Chem , vol.280 , pp. 29088-29095
    • Ciferri, C.1    De Luca, J.2    Monzani, S.3    Ferrari, K.J.4
  • 17
    • 17244363408 scopus 로고    scopus 로고
    • Molecular organization of the Ndc80 complex, an essential kinetochore component
    • Wei RR, Sorger PK, Harrison SC. 2005. Molecular organization of the Ndc80 complex, an essential kinetochore component. Proc Natl Acad Sci USA 102: 5363-7.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 5363-5367
    • Wei, R.R.1    Sorger, P.K.2    Harrison, S.C.3
  • 18
    • 43049146221 scopus 로고    scopus 로고
    • Implications for kinetochore-microtubule attachment from the structure of an engineered Ndc80 complex
    • Ciferri C, Pasqualato S, Screpanti E, Varetti G, et al. 2008. Implications for kinetochore-microtubule attachment from the structure of an engineered Ndc80 complex. Cell 133: 427-39.
    • (2008) Cell , vol.133 , pp. 427-439
    • Ciferri, C.1    Pasqualato, S.2    Screpanti, E.3    Varetti, G.4
  • 19
    • 33846100785 scopus 로고    scopus 로고
    • The Ndc80/HEC1 complex is a contact point for kinetochore-microtubule attachment
    • Wei RR, Al-Bassam J, Harrison SC. 2007. The Ndc80/HEC1 complex is a contact point for kinetochore-microtubule attachment. Nat Struct Mol Biol 14: 54-9.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 54-59
    • Wei, R.R.1    Al-Bassam, J.2    Harrison, S.C.3
  • 20
    • 56349089656 scopus 로고    scopus 로고
    • Kinetochore-microtubule attachment relies on the disordered N-terminal tail domain of Hec1
    • Guimaraes GJ, Dong Y, McEwen BF, Deluca JG. 2008. Kinetochore-microtubule attachment relies on the disordered N-terminal tail domain of Hec1. Curr Biol 18: 1778-84.
    • (2008) Curr Biol , vol.18 , pp. 1778-1784
    • Guimaraes, G.J.1    Dong, Y.2    McEwen, B.F.3    Deluca, J.G.4
  • 21
    • 56349098273 scopus 로고    scopus 로고
    • Kinetochore attachments require an interaction between unstructured tails on microtubules and Ndc80(Hec1)
    • Miller SA, Johnson ML, Stukenberg PT. 2008. Kinetochore attachments require an interaction between unstructured tails on microtubules and Ndc80(Hec1). Curr Biol 18: 1785-91.
    • (2008) Curr Biol , vol.18 , pp. 1785-1791
    • Miller, S.A.1    Johnson, M.L.2    Stukenberg, P.T.3
  • 22
    • 79954598474 scopus 로고    scopus 로고
    • The Ndc80 complex employs a tripartite attachment point to couple microtubule depolymerization to chromosome movement
    • Tooley JG, Miller SA, Stukenberg PT. 2011. The Ndc80 complex employs a tripartite attachment point to couple microtubule depolymerization to chromosome movement. Mol Biol Cell 22: 1217-26.
    • (2011) Mol Biol Cell , vol.22 , pp. 1217-1226
    • Tooley, J.G.1    Miller, S.A.2    Stukenberg, P.T.3
  • 23
    • 33751232957 scopus 로고    scopus 로고
    • The conserved KMN network constitutes the core microtubule-binding site of the kinetochore
    • Cheeseman IM, Chappie JS, Wilson-Kubalek EM, Desai A. 2006. The conserved KMN network constitutes the core microtubule-binding site of the kinetochore. Cell 127: 983-97.
    • (2006) Cell , vol.127 , pp. 983-997
    • Cheeseman, I.M.1    Chappie, J.S.2    Wilson-Kubalek, E.M.3    Desai, A.4
  • 24
    • 0037131572 scopus 로고    scopus 로고
    • Phospho-regulation of kinetochore-microtubule attachments by the Aurora kinase Ipl1p
    • Cheeseman IM, Anderson S, Jwa M, Green EM, et al. 2002. Phospho-regulation of kinetochore-microtubule attachments by the Aurora kinase Ipl1p. Cell 111: 163-72.
    • (2002) Cell , vol.111 , pp. 163-172
    • Cheeseman, I.M.1    Anderson, S.2    Jwa, M.3    Green, E.M.4
  • 25
    • 33751227843 scopus 로고    scopus 로고
    • Kinetochore microtubule dynamics and attachment stability are regulated by Hec1
    • DeLuca JG, Gall WE, Ciferri C, Cimini D, et al. 2006. Kinetochore microtubule dynamics and attachment stability are regulated by Hec1. Cell 127: 969-82.
    • (2006) Cell , vol.127 , pp. 969-982
    • DeLuca, J.G.1    Gall, W.E.2    Ciferri, C.3    Cimini, D.4
  • 26
    • 84904618315 scopus 로고    scopus 로고
    • Accurate phosphoregulation of kinetochore-microtubule affinity requires unconstrained molecular interactions
    • Zaytsev AV, Sundin LJ, DeLuca KF, Grishchuk EL, et al. 2014. Accurate phosphoregulation of kinetochore-microtubule affinity requires unconstrained molecular interactions. J Cell Biol 206: 45-59.
    • (2014) J Cell Biol , vol.206 , pp. 45-59
    • Zaytsev, A.V.1    Sundin, L.J.2    DeLuca, K.F.3    Grishchuk, E.L.4
  • 27
    • 62149111407 scopus 로고    scopus 로고
    • Sensing chromosome bi-orientation by spatial separation of aurora B kinase from kinetochore substrates
    • Liu D, Vader G, Vromans MJ, Lampson MA, et al. 2009. Sensing chromosome bi-orientation by spatial separation of aurora B kinase from kinetochore substrates. Science 323: 1350-3.
    • (2009) Science , vol.323 , pp. 1350-1353
    • Liu, D.1    Vader, G.2    Vromans, M.J.3    Lampson, M.A.4
  • 28
    • 0036178929 scopus 로고    scopus 로고
    • Evidence that the Ipl1-Sli15 (Aurora kinase-INCENP) complex promotes chromosome bi-orientation by altering kinetochore-spindle pole connections
    • Tanaka TU, Rachidi N, Janke C, Pereira G, et al. 2002. Evidence that the Ipl1-Sli15 (Aurora kinase-INCENP) complex promotes chromosome bi-orientation by altering kinetochore-spindle pole connections. Cell 108: 317-29.
    • (2002) Cell , vol.108 , pp. 317-329
    • Tanaka, T.U.1    Rachidi, N.2    Janke, C.3    Pereira, G.4
  • 29
    • 79952107079 scopus 로고    scopus 로고
    • Sensing centromere tension: Aurora B and the regulation of kinetochore function
    • Lampson MA, Cheeseman IM. 2011. Sensing centromere tension: Aurora B and the regulation of kinetochore function. Trends Cell Biol 21: 133-40.
    • (2011) Trends Cell Biol , vol.21 , pp. 133-140
    • Lampson, M.A.1    Cheeseman, I.M.2
  • 30
    • 84877575218 scopus 로고    scopus 로고
    • Tension sensing by Aurora B kinase is independent of survivin-based centromere localization
    • Campbell CS, Desai A. 2013. Tension sensing by Aurora B kinase is independent of survivin-based centromere localization. Nature 497: 118-21.
    • (2013) Nature , vol.497 , pp. 118-121
    • Campbell, C.S.1    Desai, A.2
  • 31
    • 67349247484 scopus 로고    scopus 로고
    • Mimicking Ndc80 phosphorylation triggers spindle assembly checkpoint signalling
    • Kemmler S, Stach M, Knapp M, Ortiz J, et al. 2009. Mimicking Ndc80 phosphorylation triggers spindle assembly checkpoint signalling. EMBO J 28: 1099-110.
    • (2009) EMBO J , vol.28 , pp. 1099-1110
    • Kemmler, S.1    Stach, M.2    Knapp, M.3    Ortiz, J.4
  • 32
    • 0347579850 scopus 로고    scopus 로고
    • Phosphorylation of the mitotic regulator protein Hec1 by Nek2 kinase is essential for faithful chromosome segregation
    • Chen Y, Riley DJ, Zheng L, Chen PL, et al. 2002. Phosphorylation of the mitotic regulator protein Hec1 by Nek2 kinase is essential for faithful chromosome segregation. J Biol Chem 277: 49408-16.
    • (2002) J Biol Chem , vol.277 , pp. 49408-49416
    • Chen, Y.1    Riley, D.J.2    Zheng, L.3    Chen, P.L.4
  • 33
    • 53149128681 scopus 로고    scopus 로고
    • Architecture and flexibility of the yeast Ndc80 kinetochore complex
    • Wang HW, Long S, Ciferri C, Westermann S, et al. 2008. Architecture and flexibility of the yeast Ndc80 kinetochore complex. J Mol Biol 383: 894-903.
    • (2008) J Mol Biol , vol.383 , pp. 894-903
    • Wang, H.W.1    Long, S.2    Ciferri, C.3    Westermann, S.4
  • 34
    • 65049088564 scopus 로고    scopus 로고
    • In vivo protein architecture of the eukaryotic kinetochore with nanometer scale accuracy
    • Joglekar AP, Bloom K, Salmon ED. 2009. In vivo protein architecture of the eukaryotic kinetochore with nanometer scale accuracy. Curr Biol 19: 694-9.
    • (2009) Curr Biol , vol.19 , pp. 694-699
    • Joglekar, A.P.1    Bloom, K.2    Salmon, E.D.3
  • 35
    • 65549149069 scopus 로고    scopus 로고
    • Protein architecture of the human kinetochore microtubule attachment site
    • Wan X, O'Quinn RP, Pierce HL, Joglekar AP, et al. 2009. Protein architecture of the human kinetochore microtubule attachment site. Cell 137: 672-84.
    • (2009) Cell , vol.137 , pp. 672-684
    • Wan, X.1    O'Quinn, R.P.2    Pierce, H.L.3    Joglekar, A.P.4
  • 36
    • 84868545650 scopus 로고    scopus 로고
    • The Ndc80 internal loop is required for recruitment of the Ska complex to establish end-on microtubule attachment to kinetochores
    • Zhang G, Kelstrup CD, Hu XW, Kaas Hansen MJ, et al. 2012. The Ndc80 internal loop is required for recruitment of the Ska complex to establish end-on microtubule attachment to kinetochores. J Cell Sci 125: 3243-53.
    • (2012) J Cell Sci , vol.125 , pp. 3243-3253
    • Zhang, G.1    Kelstrup, C.D.2    Hu, X.W.3    Kaas Hansen, M.J.4
  • 37
    • 84894260637 scopus 로고    scopus 로고
    • Modular assembly of RWD domains on the Mis12 complex underlies outer kinetochore organization
    • Petrovic A, Mosalaganti S, Keller J, Mattiuzzo M, et al. 2014. Modular assembly of RWD domains on the Mis12 complex underlies outer kinetochore organization. Mol Cell 53: 591-605.
    • (2014) Mol Cell , vol.53 , pp. 591-605
    • Petrovic, A.1    Mosalaganti, S.2    Keller, J.3    Mattiuzzo, M.4
  • 38
    • 84883758590 scopus 로고    scopus 로고
    • Coupling unbiased mutagenesis to high-throughput DNA sequencing uncovers functional domains in the Ndc80 kinetochore protein of Saccharomyces cerevisiae
    • Tien JF, Fong KK, Umbreit NT, Payen C, et al. 2013. Coupling unbiased mutagenesis to high-throughput DNA sequencing uncovers functional domains in the Ndc80 kinetochore protein of Saccharomyces cerevisiae. Genetics 195: 159-70.
    • (2013) Genetics , vol.195 , pp. 159-170
    • Tien, J.F.1    Fong, K.K.2    Umbreit, N.T.3    Payen, C.4
  • 39
    • 84915747999 scopus 로고    scopus 로고
    • Kinetochore biorientation in Saccharomyces cerevisiae requires a tightly folded conformation of the Ndc80 complex
    • Tien JF, Umbreit NT, Zelter A, Riffle M, et al. 2014. Kinetochore biorientation in Saccharomyces cerevisiae requires a tightly folded conformation of the Ndc80 complex. Genetics, 198: 1483-93.
    • (2014) Genetics , vol.198 , pp. 1483-1493
    • Tien, J.F.1    Umbreit, N.T.2    Zelter, A.3    Riffle, M.4
  • 40
    • 84904060990 scopus 로고    scopus 로고
    • Assembling the protein architecture of the budding yeast kinetochore-microtubule attachment using FRET
    • Aravamudhan P, Felzer-Kim I, Gurunathan K, Joglekar AP. 2014. Assembling the protein architecture of the budding yeast kinetochore-microtubule attachment using FRET. Curr Biol 24: 1437-46.
    • (2014) Curr Biol , vol.24 , pp. 1437-1446
    • Aravamudhan, P.1    Felzer-Kim, I.2    Gurunathan, K.3    Joglekar, A.P.4
  • 41
    • 79551716041 scopus 로고    scopus 로고
    • The Ndc80 loop region facilitates formation of kinetochore attachment to the dynamic microtubule plus end
    • Maure JF, Komoto S, Oku Y, Mino A, et al. 2011. The Ndc80 loop region facilitates formation of kinetochore attachment to the dynamic microtubule plus end. Curr Biol 21: 207-13.
    • (2011) Curr Biol , vol.21 , pp. 207-213
    • Maure, J.F.1    Komoto, S.2    Oku, Y.3    Mino, A.4
  • 42
    • 79551705112 scopus 로고    scopus 로고
    • Ndc80 internal loop interacts with Dis1/TOG to ensure proper kinetochore-spindle attachment in fission yeast
    • Hsu KS, Toda T. 2011. Ndc80 internal loop interacts with Dis1/TOG to ensure proper kinetochore-spindle attachment in fission yeast. Curr Biol 21: 214-20.
    • (2011) Curr Biol , vol.21 , pp. 214-220
    • Hsu, K.S.1    Toda, T.2
  • 43
    • 84876585771 scopus 로고    scopus 로고
    • The internal loop of fission yeast Ndc80 binds Alp7/TACC-Alp14/TOG and ensures proper chromosome attachment
    • Tang NH, Takada H, Hsu KS, Toda T. 2013. The internal loop of fission yeast Ndc80 binds Alp7/TACC-Alp14/TOG and ensures proper chromosome attachment. Mol Biol Cell 24: 1122-33.
    • (2013) Mol Biol Cell , vol.24 , pp. 1122-1133
    • Tang, N.H.1    Takada, H.2    Hsu, K.S.3    Toda, T.4
  • 44
    • 84861602372 scopus 로고    scopus 로고
    • Recruitment of the human Cdt1 replication licensing protein by the loop domain of Hec1 is required for stable kinetochore-microtubule attachment
    • Varma D, Chandrasekaran S, Sundin LJR, Reidy KT, et al. 2012. Recruitment of the human Cdt1 replication licensing protein by the loop domain of Hec1 is required for stable kinetochore-microtubule attachment. Nat Cell Biol 14: 593-603.
    • (2012) Nat Cell Biol , vol.14 , pp. 593-603
    • Varma, D.1    Chandrasekaran, S.2    Sundin, L.J.R.3    Reidy, K.T.4
  • 45
    • 84869126336 scopus 로고    scopus 로고
    • Looping in on Ndc80 - How does a protein loop at the kinetochore control chromosome segregation
    • Nilsson J. 2012. Looping in on Ndc80 - How does a protein loop at the kinetochore control chromosome segregation? BioEssays 34: 1070-7.
    • (2012) BioEssays , vol.34 , pp. 1070-1077
    • Nilsson, J.1
  • 46
    • 85040645978 scopus 로고    scopus 로고
    • Ndc80 Loop as a protein-protein interaction motif
    • Tang NH, Toda T. 2013. Ndc80 Loop as a protein-protein interaction motif. Cell Div 8: 2.
    • (2013) Cell Div , vol.8 , pp. 2
    • Tang, N.H.1    Toda, T.2
  • 47
    • 84921396318 scopus 로고    scopus 로고
    • Alp7/TACC recruits kinesin-8-PP1 to the Ndc80 kinetochore protein for timely mitotic progression and chromosome movement
    • Tang NH, Toda T. 2015. Alp7/TACC recruits kinesin-8-PP1 to the Ndc80 kinetochore protein for timely mitotic progression and chromosome movement. J Cell Sci DOI: 10.1242/jcs.160036.
    • (2015) J Cell Sci
    • Tang, N.H.1    Toda, T.2
  • 48
    • 84896869775 scopus 로고    scopus 로고
    • The Spindle and kinetochore-associated (Ska) complex enhances binding of the Anaphase-Promoting Complex/Cyclosome (APC/C) to chromosomes and promotes mitotic exit
    • Sivakumar S, Daum JR, Tipton AR, Rankin S, et al. 2014. The Spindle and kinetochore-associated (Ska) complex enhances binding of the Anaphase-Promoting Complex/Cyclosome (APC/C) to chromosomes and promotes mitotic exit. Mol Biol Cell 25: 594-605.
    • (2014) Mol Biol Cell , vol.25 , pp. 594-605
    • Sivakumar, S.1    Daum, J.R.2    Tipton, A.R.3    Rankin, S.4
  • 49
    • 0033536197 scopus 로고    scopus 로고
    • Cloning of TACC1, an embryonically expressed, potentially transforming coiled coil containing gene, from the 8p11 breast cancer amplicon
    • Still IH, Hamilton M, Vince P, Wolfman A, et al. 1999. Cloning of TACC1, an embryonically expressed, potentially transforming coiled coil containing gene, from the 8p11 breast cancer amplicon. Oncogene 18: 4032-8.
    • (1999) Oncogene , vol.18 , pp. 4032-4038
    • Still, I.H.1    Hamilton, M.2    Vince, P.3    Wolfman, A.4
  • 50
    • 0034677206 scopus 로고    scopus 로고
    • D-TACC: a novel centrosomal protein required for normal spindle function in the early Drosophila embryo
    • Gergely F, Kidd D, Jeffers K, Wakefield JG, et al. 2000. D-TACC: a novel centrosomal protein required for normal spindle function in the early Drosophila embryo. EMBO J 19: 241-52.
    • (2000) EMBO J , vol.19 , pp. 241-252
    • Gergely, F.1    Kidd, D.2    Jeffers, K.3    Wakefield, J.G.4
  • 51
    • 0042921206 scopus 로고    scopus 로고
    • Caenorhabditis elegans TAC-1 and ZYG-9 form a complex that is essential for long astral and spindle microtubules
    • Srayko M, Quintin S, Schwager A, Hyman AA. 2003. Caenorhabditis elegans TAC-1 and ZYG-9 form a complex that is essential for long astral and spindle microtubules. Curr Biol 13: 1506-11.
    • (2003) Curr Biol , vol.13 , pp. 1506-1511
    • Srayko, M.1    Quintin, S.2    Schwager, A.3    Hyman, A.A.4
  • 52
    • 1642464705 scopus 로고    scopus 로고
    • Interdependency of fission yeast Alp14/TOG and coiled coil protein Alp7 in microtubule localization and bipolar spindle formation
    • Sato M, Vardy L, Angel Garcia M, Koonrugsa N, et al. 2004. Interdependency of fission yeast Alp14/TOG and coiled coil protein Alp7 in microtubule localization and bipolar spindle formation. Mol Biol Cell 15: 1609-22.
    • (2004) Mol Biol Cell , vol.15 , pp. 1609-1622
    • Sato, M.1    Vardy, L.2    Angel Garcia, M.3    Koonrugsa, N.4
  • 53
    • 13444279931 scopus 로고    scopus 로고
    • Structure-function evolution of the transforming acidic coiled coil genes revealed by analysis of phylogenetically diverse organisms
    • Still IH, Vettaikkorumakankauv AK, DiMatteo A, Liang P. 2004. Structure-function evolution of the transforming acidic coiled coil genes revealed by analysis of phylogenetically diverse organisms. BMC Evol Biol 4: 16.
    • (2004) BMC Evol Biol , vol.4 , pp. 16
    • Still, I.H.1    Vettaikkorumakankauv, A.K.2    DiMatteo, A.3    Liang, P.4
  • 54
    • 79952281843 scopus 로고    scopus 로고
    • A TACC3/ch-TOG/clathrin complex stabilises kinetochore fibres by inter-microtubule bridging
    • Booth DG, Hood FE, Prior IA, Royle SJ. 2011. A TACC3/ch-TOG/clathrin complex stabilises kinetochore fibres by inter-microtubule bridging. EMBO J 30: 906-19.
    • (2011) EMBO J , vol.30 , pp. 906-919
    • Booth, D.G.1    Hood, F.E.2    Prior, I.A.3    Royle, S.J.4
  • 55
    • 84858143588 scopus 로고    scopus 로고
    • The role of clathrin in mitotic spindle organisation
    • Royle SJ. 2012. The role of clathrin in mitotic spindle organisation. J Cell Sci 125: 19-28.
    • (2012) J Cell Sci , vol.125 , pp. 19-28
    • Royle, S.J.1
  • 56
    • 84883174686 scopus 로고    scopus 로고
    • Coordination of adjacent domains mediates TACC3-ch-TOG-clathrin assembly and mitotic spindle binding
    • Hood FE, Williams SJ, Burgess SG, Richards MW, et al. 2013. Coordination of adjacent domains mediates TACC3-ch-TOG-clathrin assembly and mitotic spindle binding. J Cell Biol 202: 463-78.
    • (2013) J Cell Biol , vol.202 , pp. 463-478
    • Hood, F.E.1    Williams, S.J.2    Burgess, S.G.3    Richards, M.W.4
  • 57
    • 84888119772 scopus 로고    scopus 로고
    • Role of centrosomal adaptor proteins of the TACC family in the regulation of microtubule dynamics during mitotic cell division
    • Thakur HC, Singh M, Nagel-Steger L, Prumbaum D, et al. 2013. Role of centrosomal adaptor proteins of the TACC family in the regulation of microtubule dynamics during mitotic cell division. Biol Chem 394: 1411-23.
    • (2013) Biol Chem , vol.394 , pp. 1411-1423
    • Thakur, H.C.1    Singh, M.2    Nagel-Steger, L.3    Prumbaum, D.4
  • 58
    • 84891676441 scopus 로고    scopus 로고
    • The centrosomal adaptor TACC3 and the microtubule polymerase chTOG interact via defined C-terminal subdomains in an Aurora-A kinase-independent manner
    • Thakur HC, Singh M, Nagel-Steger L, Kremer J, et al. 2014. The centrosomal adaptor TACC3 and the microtubule polymerase chTOG interact via defined C-terminal subdomains in an Aurora-A kinase-independent manner. J Biol Chem 289: 74-88.
    • (2014) J Biol Chem , vol.289 , pp. 74-88
    • Thakur, H.C.1    Singh, M.2    Nagel-Steger, L.3    Kremer, J.4
  • 59
    • 78149297473 scopus 로고    scopus 로고
    • Clathrin recruits phosphorylated TACC3 to spindle poles for bipolar spindle assembly and chromosome alignment
    • Fu W, Tao W, Zheng P, Fu J, et al. 2010. Clathrin recruits phosphorylated TACC3 to spindle poles for bipolar spindle assembly and chromosome alignment. J Cell Sci 123: 3645-51.
    • (2010) J Cell Sci , vol.123 , pp. 3645-3651
    • Fu, W.1    Tao, W.2    Zheng, P.3    Fu, J.4
  • 60
    • 77952344256 scopus 로고    scopus 로고
    • Quantitative proteomics combined with BAC TransgeneOmics reveals in vivo protein interactions
    • Hubner NC, Bird AW, Cox J, Splettstoesser B, et al. 2010. Quantitative proteomics combined with BAC TransgeneOmics reveals in vivo protein interactions. J Cell Biol 189: 739-54.
    • (2010) J Cell Biol , vol.189 , pp. 739-754
    • Hubner, N.C.1    Bird, A.W.2    Cox, J.3    Splettstoesser, B.4
  • 61
    • 77954393655 scopus 로고    scopus 로고
    • Clathrin heavy chain mediates TACC3 targeting to mitotic spindles to ensure spindle stability
    • Lin CH, Hu CK, Shih HM. 2010. Clathrin heavy chain mediates TACC3 targeting to mitotic spindles to ensure spindle stability. J Cell Biol 189: 1097-105.
    • (2010) J Cell Biol , vol.189 , pp. 1097-1105
    • Lin, C.H.1    Hu, C.K.2    Shih, H.M.3
  • 62
    • 34249103992 scopus 로고    scopus 로고
    • Alp7/TACC is a crucial target in Ran-GTPase-dependent spindle formation in fission yeast
    • Sato M, Toda T. 2007. Alp7/TACC is a crucial target in Ran-GTPase-dependent spindle formation in fission yeast. Nature 447: 334-7.
    • (2007) Nature , vol.447 , pp. 334-337
    • Sato, M.1    Toda, T.2
  • 63
    • 84906241999 scopus 로고    scopus 로고
    • Targeting Alp7/TACC to the spindle pole body is essential for mitotic spindle assembly in fission yeast
    • Tang NH, Okada N, Fong CS, Arai K, et al. 2014. Targeting Alp7/TACC to the spindle pole body is essential for mitotic spindle assembly in fission yeast. FEBS Lett 588: 2814-21.
    • (2014) FEBS Lett , vol.588 , pp. 2814-2821
    • Tang, N.H.1    Okada, N.2    Fong, C.S.3    Arai, K.4
  • 64
    • 84907192425 scopus 로고    scopus 로고
    • Csi1p recruits alp7p/TACC to the spindle pole bodies for bipolar spindle formation
    • Zheng F, Li T, Jin DY, Syrovatkina V, et al. 2014. Csi1p recruits alp7p/TACC to the spindle pole bodies for bipolar spindle formation. Mol Biol Cell 25: 2750-60.
    • (2014) Mol Biol Cell , vol.25 , pp. 2750-2760
    • Zheng, F.1    Li, T.2    Jin, D.Y.3    Syrovatkina, V.4
  • 65
    • 0037314330 scopus 로고    scopus 로고
    • The ch-TOG/XMAP215 protein is essential for spindle pole organization in human somatic cells
    • Gergely F, Draviam VM, Raff JW. 2003. The ch-TOG/XMAP215 protein is essential for spindle pole organization in human somatic cells. Genes Dev 17: 336-41.
    • (2003) Genes Dev , vol.17 , pp. 336-341
    • Gergely, F.1    Draviam, V.M.2    Raff, J.W.3
  • 66
    • 84866409575 scopus 로고    scopus 로고
    • Clathrin promotes centrosome integrity in early mitosis through stabilization of centrosomal ch-TOG
    • Foraker AB, Camus SM, Evans TM, Majeed SR, et al. 2012. Clathrin promotes centrosome integrity in early mitosis through stabilization of centrosomal ch-TOG. J Cell Biol 198: 591-605.
    • (2012) J Cell Biol , vol.198 , pp. 591-605
    • Foraker, A.B.1    Camus, S.M.2    Evans, T.M.3    Majeed, S.R.4
  • 67
    • 0036607995 scopus 로고    scopus 로고
    • XMA P215: a key component of the dynamic microtubule cytoskeleton
    • Kinoshita K, Habermann B, Hyman AA. 2002. XMA P215: a key component of the dynamic microtubule cytoskeleton. Trends Cell Biol 12: 267-73.
    • (2002) Trends Cell Biol , vol.12 , pp. 267-273
    • Kinoshita, K.1    Habermann, B.2    Hyman, A.A.3
  • 68
    • 80053112323 scopus 로고    scopus 로고
    • Regulation of microtubule dynamics by TOG-domain proteins XMAP215/Dis1 and CLASP
    • Al-Bassam J, Chang F. 2011. Regulation of microtubule dynamics by TOG-domain proteins XMAP215/Dis1 and CLASP. Trends Cell Biol 21: 604-14.
    • (2011) Trends Cell Biol , vol.21 , pp. 604-614
    • Al-Bassam, J.1    Chang, F.2
  • 70
    • 79952598938 scopus 로고    scopus 로고
    • XMAP215 polymerase activity is built by combining multiple tubulin-binding TOG domains and a basic lattice-binding region
    • Widlund PO, Stear JH, Pozniakovsky A, Zanic M, et al. 2011. XMAP215 polymerase activity is built by combining multiple tubulin-binding TOG domains and a basic lattice-binding region. Proc Natl Acad Sci USA 108: 2741-6.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 2741-2746
    • Widlund, P.O.1    Stear, J.H.2    Pozniakovsky, A.3    Zanic, M.4
  • 71
    • 84864759021 scopus 로고    scopus 로고
    • Fission yeast Alp14 is a dose dependent plus end tracking microtubule polymerase
    • Al-Bassam J, Kim H, Flor-Parra I, Lal N, et al. 2012. Fission yeast Alp14 is a dose dependent plus end tracking microtubule polymerase. Mol Biol Cell 23: 2878-90.
    • (2012) Mol Biol Cell , vol.23 , pp. 2878-2890
    • Al-Bassam, J.1    Kim, H.2    Flor-Parra, I.3    Lal, N.4
  • 72
    • 84907906510 scopus 로고    scopus 로고
    • Stu2, the budding yeast XMAP215/Dis1 homolog, promotes assembly of yeast microtubules by increasing growth rate and decreasing catastrophe frequency
    • Podolski M, Mahamdeh M, Howard J. 2014. Stu2, the budding yeast XMAP215/Dis1 homolog, promotes assembly of yeast microtubules by increasing growth rate and decreasing catastrophe frequency. J Biol Chem 289: 28087-93.
    • (2014) J Biol Chem , vol.289 , pp. 28087-28093
    • Podolski, M.1    Mahamdeh, M.2    Howard, J.3
  • 73
    • 84865074275 scopus 로고    scopus 로고
    • A TOG:alphabeta-tubulin complex structure reveals conformation-based mechanisms for a microtubule polymerase
    • Ayaz P, Ye X, Huddleston P, Brautigam CA, et al. 2012. A TOG:alphabeta-tubulin complex structure reveals conformation-based mechanisms for a microtubule polymerase. Science 337: 857-60.
    • (2012) Science , vol.337 , pp. 857-860
    • Ayaz, P.1    Ye, X.2    Huddleston, P.3    Brautigam, C.A.4
  • 74
    • 84908330392 scopus 로고    scopus 로고
    • A tethered delivery mechanism explains the catalytic action of a microtubule polymerase
    • Ayaz P, Munyoki S, Geyer EA, Piedra FA, et al. 2014. A tethered delivery mechanism explains the catalytic action of a microtubule polymerase. eLife 3: e03069.
    • (2014) eLife , vol.3 , pp. e03069
    • Ayaz, P.1    Munyoki, S.2    Geyer, E.A.3    Piedra, F.A.4
  • 75
    • 33847639293 scopus 로고    scopus 로고
    • Crystal structure of a TOG domain: conserved features of XMAP215/Dis1-family TOG domains and implications for tubulin binding
    • Al-Bassam J, Larsen NA, Hyman AA, Harrison SC. 2007. Crystal structure of a TOG domain: conserved features of XMAP215/Dis1-family TOG domains and implications for tubulin binding. Structure 15: 355-62.
    • (2007) Structure , vol.15 , pp. 355-362
    • Al-Bassam, J.1    Larsen, N.A.2    Hyman, A.A.3    Harrison, S.C.4
  • 76
    • 34748862943 scopus 로고    scopus 로고
    • Structural basis of microtubule plus end tracking by XMAP215, CLIP-170, and EB1
    • Slep KC, Vale RD. 2007. Structural basis of microtubule plus end tracking by XMAP215, CLIP-170, and EB1. Mol Cell 27: 976-91.
    • (2007) Mol Cell , vol.27 , pp. 976-991
    • Slep, K.C.1    Vale, R.D.2
  • 77
    • 84905976506 scopus 로고    scopus 로고
    • The XMAP215 family drives microtubule polymerization using a structurally diverse TOG array
    • Fox JC, Howard AE, Currie JD, Rogers SL, et al. 2014. The XMAP215 family drives microtubule polymerization using a structurally diverse TOG array. Mol Biol Cell 25: 2375-92.
    • (2014) Mol Biol Cell , vol.25 , pp. 2375-2392
    • Fox, J.C.1    Howard, A.E.2    Currie, J.D.3    Rogers, S.L.4
  • 78
    • 0028983320 scopus 로고
    • p93dis1, which is required for sister chromatid separation, is a novel microtubule and spindle pole body-associating protein phosphorylated at the Cdc2 target sites
    • Nabeshima K, Kurooka H, Takeuchi M, Kinoshita K, et al. 1995. p93dis1, which is required for sister chromatid separation, is a novel microtubule and spindle pole body-associating protein phosphorylated at the Cdc2 target sites. Genes Dev 9: 1572-85.
    • (1995) Genes Dev , vol.9 , pp. 1572-1585
    • Nabeshima, K.1    Kurooka, H.2    Takeuchi, M.3    Kinoshita, K.4
  • 79
    • 0035796586 scopus 로고    scopus 로고
    • Fission yeast ch-TOG/XMAP215 homologue Alp14 connects mitotic spindles with the kinetochore and is a component of the Mad2-dependent spindle checkpoint
    • Garcia MA, Vardy L, Koonrugsa N, Toda T. 2001. Fission yeast ch-TOG/XMAP215 homologue Alp14 connects mitotic spindles with the kinetochore and is a component of the Mad2-dependent spindle checkpoint. EMBO J 20: 3389-401.
    • (2001) EMBO J , vol.20 , pp. 3389-3401
    • Garcia, M.A.1    Vardy, L.2    Koonrugsa, N.3    Toda, T.4
  • 80
    • 0035901596 scopus 로고    scopus 로고
    • M phase-specific kinetochore proteins in fission yeast: microtubule-associating Dis1 and Mtc1 display rapid separation and segregation during anaphase
    • Nakaseko Y, Goshima G, Morishita J, Yanagida M. 2001. M phase-specific kinetochore proteins in fission yeast: microtubule-associating Dis1 and Mtc1 display rapid separation and segregation during anaphase. Curr Biol 11: 537-49.
    • (2001) Curr Biol , vol.11 , pp. 537-549
    • Nakaseko, Y.1    Goshima, G.2    Morishita, J.3    Yanagida, M.4
  • 81
    • 18744393712 scopus 로고    scopus 로고
    • Spindle-kinetochore attachment requires the combined action of Kin I-like Klp5/6 and Alp14/Dis1-MAPs in fission yeast
    • Garcia MA, Koonrugsa N, Toda T. 2002. Spindle-kinetochore attachment requires the combined action of Kin I-like Klp5/6 and Alp14/Dis1-MAPs in fission yeast. EMBO J 21: 6015-24.
    • (2002) EMBO J , vol.21 , pp. 6015-6024
    • Garcia, M.A.1    Koonrugsa, N.2    Toda, T.3
  • 82
    • 0023239517 scopus 로고
    • Functional inactivation of genes by dominant negative mutations
    • Herskowitz I. 1987. Functional inactivation of genes by dominant negative mutations. Nature 329: 219-22.
    • (1987) Nature , vol.329 , pp. 219-222
    • Herskowitz, I.1
  • 83
    • 81355149553 scopus 로고    scopus 로고
    • CENP-A exceeds microtubule attachment sites in centromere clusters of both budding and fission yeast
    • Coffman VC, Wu P, Parthun MR, Wu JQ. 2011. CENP-A exceeds microtubule attachment sites in centromere clusters of both budding and fission yeast. J Cell Biol 195: 563-72.
    • (2011) J Cell Biol , vol.195 , pp. 563-572
    • Coffman, V.C.1    Wu, P.2    Parthun, M.R.3    Wu, J.Q.4
  • 84
    • 81355161263 scopus 로고    scopus 로고
    • Point centromeres contain more than a single centromere-specific Cse4 (CENP-A) nucleosome
    • Lawrimore J, Bloom KS, Salmon ED. 2011. Point centromeres contain more than a single centromere-specific Cse4 (CENP-A) nucleosome. J Cell Biol 195: 573-82.
    • (2011) J Cell Biol , vol.195 , pp. 573-582
    • Lawrimore, J.1    Bloom, K.S.2    Salmon, E.D.3
  • 85
    • 0027391206 scopus 로고
    • Three-dimensional reconstruction and analysis of mitotic spindles from the yeast, Schizosaccharomyces pombe
    • Ding R, McDonald KL, McIntosh JR. 1993. Three-dimensional reconstruction and analysis of mitotic spindles from the yeast, Schizosaccharomyces pombe. J Cell Biol 120: 141-51.
    • (1993) J Cell Biol , vol.120 , pp. 141-151
    • Ding, R.1    McDonald, K.L.2    McIntosh, J.R.3
  • 86
    • 84874366606 scopus 로고    scopus 로고
    • Conserved and divergent features of kinetochores and spindle microtubule ends from five species
    • McIntosh JR, O'Toole E, Zhudenkov K, Morphew M, et al. 2013. Conserved and divergent features of kinetochores and spindle microtubule ends from five species. J Cell Biol 200: 459-74.
    • (2013) J Cell Biol , vol.200 , pp. 459-474
    • McIntosh, J.R.1    O'Toole, E.2    Zhudenkov, K.3    Morphew, M.4
  • 87
    • 84868028972 scopus 로고    scopus 로고
    • Quantitative analysis of fission yeast transcriptomes and proteomes in proliferating and quiescent cells
    • Marguerat S, Schmidt A, Codlin S, Chen W, et al. 2012. Quantitative analysis of fission yeast transcriptomes and proteomes in proliferating and quiescent cells. Cell 151: 671-83.
    • (2012) Cell , vol.151 , pp. 671-683
    • Marguerat, S.1    Schmidt, A.2    Codlin, S.3    Chen, W.4
  • 88
    • 84905252531 scopus 로고    scopus 로고
    • Absolute proteome and phosphoproteome dynamics during the cell cycle of Schizosaccharomyces pombe (fission yeast)
    • Carpy A, Krug K, Graf S, Koch A, et al. 2014. Absolute proteome and phosphoproteome dynamics during the cell cycle of Schizosaccharomyces pombe (fission yeast). Mol Cell Proteomics 13: 1925-36.
    • (2014) Mol Cell Proteomics , vol.13 , pp. 1925-1936
    • Carpy, A.1    Krug, K.2    Graf, S.3    Koch, A.4
  • 89
    • 0027390036 scopus 로고
    • Thiamine-repressible expression vectors pREP and pRIP for fission yeast
    • Maundrell K. 1993. Thiamine-repressible expression vectors pREP and pRIP for fission yeast. Gene 123: 127-30.
    • (1993) Gene , vol.123 , pp. 127-130
    • Maundrell, K.1
  • 90
    • 0034687657 scopus 로고    scopus 로고
    • The TACC domain identifies a family of centrosomal proteins that can interact with microtubules
    • Gergely F, Karlsson C, Still I, Cowell J, et al. 2000. The TACC domain identifies a family of centrosomal proteins that can interact with microtubules. Proc Natl Acad Sci USA 97: 14352-7.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 14352-14357
    • Gergely, F.1    Karlsson, C.2    Still, I.3    Cowell, J.4
  • 91
    • 84880329053 scopus 로고    scopus 로고
    • Microtubules and Alp7-Alp14 (TACC-TOG) reposition chromosomes before meiotic segregation
    • Kakui Y, Sato M, Okada N, Toda T, et al. 2013. Microtubules and Alp7-Alp14 (TACC-TOG) reposition chromosomes before meiotic segregation. Nat Cell Biol 15: 786-96.
    • (2013) Nat Cell Biol , vol.15 , pp. 786-796
    • Kakui, Y.1    Sato, M.2    Okada, N.3    Toda, T.4
  • 92
    • 84902679614 scopus 로고    scopus 로고
    • Activity of a novel Hec1-targeted anticancer compound against breast cancer cell lines in vitro and in vivo
    • Huang LY, Chang CC, Lee YS, Chang JM, et al. 2014. Activity of a novel Hec1-targeted anticancer compound against breast cancer cell lines in vitro and in vivo. Mol Cancer Ther 13: 1419-30.
    • (2014) Mol Cancer Ther , vol.13 , pp. 1419-1430
    • Huang, L.Y.1    Chang, C.C.2    Lee, Y.S.3    Chang, J.M.4
  • 93
    • 84903533964 scopus 로고    scopus 로고
    • Kinetochore genes are coordinately up-regulated in human tumors as part of a FoxM1-related cell division program
    • Thiru P, Kern DM, McKinley KL, Monda JK, et al. 2014. Kinetochore genes are coordinately up-regulated in human tumors as part of a FoxM1-related cell division program. Mol Biol Cell 25: 1983-94.
    • (2014) Mol Biol Cell , vol.25 , pp. 1983-1994
    • Thiru, P.1    Kern, D.M.2    McKinley, K.L.3    Monda, J.K.4
  • 94
    • 84896406827 scopus 로고    scopus 로고
    • Novel small molecules disrupting Hec1/Nek2 interaction ablate tumor progression by triggering Nek2 degradation through a death-trap mechanism
    • in press
    • Hu CM, Zhu J, Guo XE, Chen W, et al. 2014. Novel small molecules disrupting Hec1/Nek2 interaction ablate tumor progression by triggering Nek2 degradation through a death-trap mechanism. Oncogene, in press doi: 10.1038/onc.2014.67.
    • (2014) Oncogene
    • Hu, C.M.1    Zhu, J.2    Guo, X.E.3    Chen, W.4
  • 95
    • 29244473831 scopus 로고    scopus 로고
    • RNA interference against Hec1 inhibits tumor growth in vivo
    • Gurzov EN, Izquierdo M. 2006. RNA interference against Hec1 inhibits tumor growth in vivo. Gene Ther 13: 1-7.
    • (2006) Gene Ther , vol.13 , pp. 1-7
    • Gurzov, E.N.1    Izquierdo, M.2
  • 96
    • 54249132168 scopus 로고    scopus 로고
    • Small molecule targeting the Hec1/Nek2 mitotic pathway suppresses tumor cell growth in culture and in animal
    • Wu G, Qiu XL, Zhou L, Zhu J, et al. 2008. Small molecule targeting the Hec1/Nek2 mitotic pathway suppresses tumor cell growth in culture and in animal. Cancer Res 68: 8393-9.
    • (2008) Cancer Res , vol.68 , pp. 8393-8399
    • Wu, G.1    Qiu, X.L.2    Zhou, L.3    Zhu, J.4
  • 97
    • 84892154921 scopus 로고    scopus 로고
    • Characterization of the biological activity of a potent small molecule Hec1 inhibitor TAI-1
    • Huang LY, Lee YS, Huang JJ, Chang CC, et al. 2014. Characterization of the biological activity of a potent small molecule Hec1 inhibitor TAI-1. J Exp Clin Cancer Res 33: 6.
    • (2014) J Exp Clin Cancer Res , vol.33 , pp. 6
    • Huang, L.Y.1    Lee, Y.S.2    Huang, J.J.3    Chang, C.C.4
  • 98
    • 84855776388 scopus 로고    scopus 로고
    • Disruption of Tacc3 function leads to in vivo tumor regression
    • Yao R, Natsume Y, Saiki Y, Shioya H, et al. 2012. Disruption of Tacc3 function leads to in vivo tumor regression. Oncogene 31: 135-48.
    • (2012) Oncogene , vol.31 , pp. 135-148
    • Yao, R.1    Natsume, Y.2    Saiki, Y.3    Shioya, H.4
  • 99
    • 84906222181 scopus 로고    scopus 로고
    • A small compound targeting TACC3 revealed its different spatiotemporal contributions for spindle assembly in cancer cells
    • Yao R, Kondoh Y, Natsume Y, Yamanaka H, et al. 2013. A small compound targeting TACC3 revealed its different spatiotemporal contributions for spindle assembly in cancer cells. Oncogene 33: 4242-52.
    • (2013) Oncogene , vol.33 , pp. 4242-4252
    • Yao, R.1    Kondoh, Y.2    Natsume, Y.3    Yamanaka, H.4
  • 100
    • 84874582530 scopus 로고    scopus 로고
    • Slk19 clusters kinetochores and facilitates chromosome bipolar attachment
    • Richmond D, Rizkallah R, Liang F, Hurt MM, et al. 2013. Slk19 clusters kinetochores and facilitates chromosome bipolar attachment. Mol Biol Cell 24: 566-77.
    • (2013) Mol Biol Cell , vol.24 , pp. 566-577
    • Richmond, D.1    Rizkallah, R.2    Liang, F.3    Hurt, M.M.4
  • 101
    • 0033606818 scopus 로고    scopus 로고
    • Slk19p is a centromere protein that functions to stabilize mitotic spindles
    • Zeng X, Kahana JA, Silver PA, Morphew MK, et al. 1999. Slk19p is a centromere protein that functions to stabilize mitotic spindles. J Cell Biol 146: 415-25.
    • (1999) J Cell Biol , vol.146 , pp. 415-425
    • Zeng, X.1    Kahana, J.A.2    Silver, P.A.3    Morphew, M.K.4
  • 102
    • 84925655418 scopus 로고    scopus 로고
    • Cancer cell death induced by novel small molecules degrading the TACC3 protein via the ubiquitin-proteasome pathway
    • Ohoka N, Nagai K, Hattori T, Okuhira K, et al. 2014. Cancer cell death induced by novel small molecules degrading the TACC3 protein via the ubiquitin-proteasome pathway. Cell Death Disease 5: e1513.
    • (2014) Cell Death Disease , vol.5 , pp. e1513
    • Ohoka, N.1    Nagai, K.2    Hattori, T.3    Okuhira, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.