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Volumn 5, Issue SEP, 2014, Pages 1-25

The dynamics of signal amplification by macromolecular assemblies for the control of chromosome segregation

Author keywords

Cancer; Cell cycle regulation; Chromosome segregation; genome instability; Kinetochore microtubules network; Protein protein interactions; Signal amplification; Spindle assembly checkpoint (SAC)

Indexed keywords

BUB3 PROTEIN; CELL CYCLE PROTEIN 20; PROTEIN MAD1; PROTEIN MAD2; UBIQUITIN PROTEIN LIGASE E3;

EID: 84907932112     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2014.00368     Document Type: Article
Times cited : (5)

References (134)
  • 3
    • 84866463338 scopus 로고    scopus 로고
    • Structural biology. Versatility from protein disorder
    • Babu, M. M., Kriwacki, R. W., and Pappu, R. V. (2012). Structural biology. Versatility from protein disorder. Science 337, 1460-1461
    • (2012) Science , vol.337 , pp. 1460-1461
    • Babu, M.M.1    Kriwacki, R.W.2    Pappu, R.V.3
  • 4
    • 79961113679 scopus 로고    scopus 로고
    • HJURP is a CENP-A chromatin assembly factor sufficient to form a functional de novo kinetochore
    • Barnhart, M. C., Kuich, P. H., Stellfox, M. E., Ward, J. A., Bassett, E. A., Black, B. E., and Foltz, D. R. (2011). HJURP is a CENP-A chromatin assembly factor sufficient to form a functional de novo kinetochore. J. Cell Biol. 194, 229-243
    • (2011) J. Cell Biol , vol.194 , pp. 229-243
    • Barnhart, M.C.1    Kuich, P.H.2    Stellfox, M.E.3    Ward, J.A.4    Bassett, E.A.5    Black, B.E.6    Foltz, D.R.7
  • 5
    • 27744475701 scopus 로고    scopus 로고
    • Anomalous Diffusion of Proteins Due to Molecular Crowding
    • Banks, D. S., and Fradin, C. (2005). Anomalous Diffusion of Proteins Due to Molecular Crowding. Biophys. J. 89, 2960-2971
    • (2005) Biophys. J , vol.89 , pp. 2960-2971
    • Banks, D.S.1    Fradin, C.2
  • 7
    • 84861925556 scopus 로고    scopus 로고
    • Spatial and temporal organisation of multiprotein assemblies: achieving sensitive control in information-rich cell regulatory systems
    • Bolanos-Garcia, V. M., Wu, Q., Ochi, T., Chirgadze, D. Y., Sibanda, B. L., and Blundell, T. L. (2012). Spatial and temporal organisation of multiprotein assemblies: achieving sensitive control in information-rich cell regulatory systems. Philos. Transact. A Math. Phys. Eng. Sci. 370, 3023-3039
    • (2012) Philos. Transact. A Math. Phys. Eng. Sci , vol.370 , pp. 3023-3039
    • Bolanos-Garcia, V.M.1    Wu, Q.2    Ochi, T.3    Chirgadze, D.Y.4    Sibanda, B.L.5    Blundell, T.L.6
  • 8
    • 79952445057 scopus 로고    scopus 로고
    • BUB1 and BUBR1: multifaceted kinases of the cell cycle
    • Bolanos-Garcia, V. M., and Blundell, T. L. (2011). BUB1 and BUBR1: multifaceted kinases of the cell cycle. Trends Biochem. Sci. 36, 141-150
    • (2011) Trends Biochem. Sci , vol.36 , pp. 141-150
    • Bolanos-Garcia, V.M.1    Blundell, T.L.2
  • 10
    • 33947731702 scopus 로고    scopus 로고
    • Bub1 is essential for assembly of the functional inner centromere
    • Boyarchuk, Y., Salic, A., Dasso, M., and Arnaoutov, A. (2007). Bub1 is essential for assembly of the functional inner centromere. J. Cell Biol. 176, 919-928
    • (2007) J. Cell Biol , vol.176 , pp. 919-928
    • Boyarchuk, Y.1    Salic, A.2    Dasso, M.3    Arnaoutov, A.4
  • 12
    • 33748286796 scopus 로고    scopus 로고
    • A signature of chromosomal instability inferred from gene expression profiles predicts clinical outcome in multiple human cancers
    • Carter, S. L., Eklund, A. C., Kohane, I. S., Harris, L. N., and Szallasi, Z. (2006). A signature of chromosomal instability inferred from gene expression profiles predicts clinical outcome in multiple human cancers. Nat. Genet. 38, 1043-1048
    • (2006) Nat. Genet , vol.38 , pp. 1043-1048
    • Carter, S.L.1    Eklund, A.C.2    Kohane, I.S.3    Harris, L.N.4    Szallasi, Z.5
  • 14
    • 33751232957 scopus 로고    scopus 로고
    • The conserved KMN network constitutes the core microtubule-binding site of the kinetochore
    • Cheeseman, I. M., Chappie, J. S., Wilson-Kubalek, E. M., and Desai, A. (2006). The conserved KMN network constitutes the core microtubule-binding site of the kinetochore. Cell 127, 983-997
    • (2006) Cell , vol.127 , pp. 983-997
    • Cheeseman, I.M.1    Chappie, J.S.2    Wilson-Kubalek, E.M.3    Desai, A.4
  • 15
    • 39449096363 scopus 로고    scopus 로고
    • KNL1 and the CENP-H/I/K complex coordinately direct kinetochore assembly in vertebrates
    • Cheeseman, I. M., Hori, T., Fukagawa, T., and Desai, A. (2008). KNL1 and the CENP-H/I/K complex coordinately direct kinetochore assembly in vertebrates. Mol. Biol. Cell 19, 587-594
    • (2008) Mol. Biol. Cell , vol.19 , pp. 587-594
    • Cheeseman, I.M.1    Hori, T.2    Fukagawa, T.3    Desai, A.4
  • 16
    • 0035999976 scopus 로고    scopus 로고
    • Spindle checkpoint requires Mad1-bound and Mad1-free Mad2
    • Chung, E., and Chen, R. H. (2002). Spindle checkpoint requires Mad1-bound and Mad1-free Mad2. Mol. Biol. Cell 13, 1501-1511
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1501-1511
    • Chung, E.1    Chen, R.H.2
  • 19
    • 84870015758 scopus 로고    scopus 로고
    • Effects of Molecular Crowding on the Dynamics of Intrinsically Disordered Proteins
    • Cino, E. A., Karttunen, M., and Choy, W-Y. (2012). Effects of Molecular Crowding on the Dynamics of Intrinsically Disordered Proteins. PLoS ONE 7, e49876
    • (2012) PLoS ONE , vol.7 , pp. e49876
    • Cino, E.A.1    Karttunen, M.2    Choy, W.-Y.3
  • 20
    • 0003845223 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System
    • (San Carlos, CA: DeLano Scientific)
    • DeLano, W.L. (2002). The PyMOL Molecular Graphics System (San Carlos, CA: DeLano Scientific)
    • (2002)
    • DeLano, W.L.1
  • 21
    • 33750999318 scopus 로고    scopus 로고
    • Disorder and sequence repeats in hub proteins and their implications for network evolution
    • Dosztanyi, Z., Chen, J., Dunker, A. K., Simon, I., and Tompa, P. (2006). Disorder and sequence repeats in hub proteins and their implications for network evolution. J. Proteome Res. 5, 2985-2995
    • (2006) J. Proteome Res , vol.5 , pp. 2985-2995
    • Dosztanyi, Z.1    Chen, J.2    Dunker, A.K.3    Simon, I.4    Tompa, P.5
  • 24
    • 27144464910 scopus 로고    scopus 로고
    • Flexible nets: the roles of intrinsic disorder in protein interaction networks
    • Dunker, A. K., Cortese, M. S., Romero, P., Iakoucheva, L. M., and Uversky, V. N. (2005). Flexible nets: the roles of intrinsic disorder in protein interaction networks. FEBS J. 272, 5129-5148
    • (2005) FEBS J , vol.272 , pp. 5129-5148
    • Dunker, A.K.1    Cortese, M.S.2    Romero, P.3    Iakoucheva, L.M.4    Uversky, V.N.5
  • 26
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson, H. J., and Wright, P. E. (2002). Coupling of folding and binding for unstructured proteins. Curr. Opin. Struct. Biol. 12, 54-60
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 27
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H. J., and Wright, P. E. (2005). Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 6, 197-208
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 28
    • 77951298407 scopus 로고    scopus 로고
    • Models of macromolecular crowding effects and the need for quantitative comparisons with experiment
    • Elcock, A. H. (2010). Models of macromolecular crowding effects and the need for quantitative comparisons with experiment. Curr. Opin. Struct. Biol. 20, 196-206
    • (2010) Curr. Opin. Struct. Biol , vol.20 , pp. 196-206
    • Elcock, A.H.1
  • 29
    • 79960316552 scopus 로고    scopus 로고
    • Bub1 and BubR1: at the Interface between Chromosome Attachment and the Spindle Checkpoint
    • Elowe, S. (2011). Bub1 and BubR1: at the Interface between Chromosome Attachment and the Spindle Checkpoint. Mol. Cell. Biol. 31, 3085-3093
    • (2011) Mol. Cell. Biol , vol.31 , pp. 3085-3093
    • Elowe, S.1
  • 31
    • 84871530214 scopus 로고    scopus 로고
    • Microtubule attachment and spindle assembly checkpoint signalling at the kinetochore
    • Foley, E A., and Kapoor, T. M. (2013). Microtubule attachment and spindle assembly checkpoint signalling at the kinetochore. Nat. Rev. Mol. Cell Biol. 14, 25-37
    • (2013) Nat. Rev. Mol. Cell Biol , vol.14 , pp. 25-37
    • Foley, E.A.1    Kapoor, T.M.2
  • 32
    • 84878587815 scopus 로고    scopus 로고
    • Making an effective switch at the kinetochore by phosphorylation and dephosphorylation
    • Funabiki, H., and Wynne, D. J. (2013). Making an effective switch at the kinetochore by phosphorylation and dephosphorylation. Chromosoma 122,135-158
    • (2013) Chromosoma , vol.122 , pp. 135-158
    • Funabiki, H.1    Wynne, D.J.2
  • 34
    • 69949105161 scopus 로고    scopus 로고
    • The rules of disorder or why disorder rules
    • Gsponer, J., and Babu, M. M. (2009). The rules of disorder or why disorder rules. Prog. Biophys. Mol. Biol. 99, 94-103
    • (2009) Prog. Biophys. Mol. Biol , vol.99 , pp. 94-103
    • Gsponer, J.1    Babu, M.M.2
  • 35
    • 0037011119 scopus 로고    scopus 로고
    • Identification of a MAD2-binding protein, CMT2, and its role in mitosis
    • Habu, T., Kim, S. H., Weinstein, J., and Matsumoto, T. (2002). Identification of a MAD2-binding protein, CMT2, and its role in mitosis. EMBO J. 21, 6419-6428
    • (2002) EMBO J , vol.21 , pp. 6419-6428
    • Habu, T.1    Kim, S.H.2    Weinstein, J.3    Matsumoto, T.4
  • 36
    • 84859997953 scopus 로고    scopus 로고
    • Structure of Metaphase Chromosomes: A Role for Effects of Macromolecular Crowding
    • Hancock, R. (2012). Structure of Metaphase Chromosomes: A Role for Effects of Macromolecular Crowding. PLoS ONE 7, e36045
    • (2012) PLoS ONE , vol.7 , pp. e36045
    • Hancock, R.1
  • 37
    • 0034611013 scopus 로고    scopus 로고
    • MAD3 encodes a novel component of the spindle checkpoint which interacts with Bub3p, CDC20p, and MAD2p
    • Hardwick, K. G., Johnston, R. C., Smith, D. L., and Murray, A. W. (2000). MAD3 encodes a novel component of the spindle checkpoint which interacts with Bub3p, CDC20p, and MAD2p. J. Cell Biol. 148, 871-882
    • (2000) J. Cell Biol , vol.148 , pp. 871-882
    • Hardwick, K.G.1    Johnston, R.C.2    Smith, D.L.3    Murray, A.W.4
  • 38
    • 0028842802 scopus 로고
    • Mad1p, a phosphoprotein component of the spindle assembly checkpoint in budding yeast
    • Hardwick, K.G., and Murray, A.W. (1995). Mad1p, a phosphoprotein component of the spindle assembly checkpoint in budding yeast. J. Cell Biol. 131, 709-720
    • (1995) J. Cell Biol , vol.131 , pp. 709-720
    • Hardwick, K.G.1    Murray, A.W.2
  • 39
    • 84887925042 scopus 로고    scopus 로고
    • The spindle assembly checkpoint: progress and persistent puzzles
    • Hauf, S. (2013). The spindle assembly checkpoint: progress and persistent puzzles. Biochem. Soc. Trans. 41, 1755-1760
    • (2013) Biochem. Soc. Trans , vol.41 , pp. 1755-1760
    • Hauf, S.1
  • 42
    • 84872063204 scopus 로고    scopus 로고
    • The CCAN recruits CENP-A to the centromere and forms the structural core for kinetochore assembly
    • Hori, T., Shang, W. H., Takeuchi, K., and Fukagawa, T. (2013). The CCAN recruits CENP-A to the centromere and forms the structural core for kinetochore assembly. J. Cell Biol. 200, 45-60
    • (2013) J. Cell Biol , vol.200 , pp. 45-60
    • Hori, T.1    Shang, W.H.2    Takeuchi, K.3    Fukagawa, T.4
  • 43
    • 0035833246 scopus 로고    scopus 로고
    • Activity of the APC(Cdh1) form of the anaphase-promoting complex persists until S phase and prevents the premature expression of Cdc20p
    • Huang, J. N., Park, I., Ellingson, E., Littlepage, L. E., and Pellman, D. (2001). Activity of the APC(Cdh1) form of the anaphase-promoting complex persists until S phase and prevents the premature expression of Cdc20p. J. Cell Biol. 154, 85-94
    • (2001) J. Cell Biol , vol.154 , pp. 85-94
    • Huang, J.N.1    Park, I.2    Ellingson, E.3    Littlepage, L.E.4    Pellman, D.5
  • 44
    • 84869046948 scopus 로고    scopus 로고
    • Mad2 and the APC/C compete for the same site on Cdc20 to ensure proper chromosome segregation
    • Izawa, D., and Pines, J. (2012). Mad2 and the APC/C compete for the same site on Cdc20 to ensure proper chromosome segregation. J. Cell Biol. 199, 27-37
    • (2012) J. Cell Biol , vol.199 , pp. 27-37
    • Izawa, D.1    Pines, J.2
  • 45
    • 73149101630 scopus 로고    scopus 로고
    • Elevating the frequency of chromosome missegregation as a strategy to kill tumor cells
    • Janssen, A., Kops, G. J., and Medema, R. H. (2009). Elevating the frequency of chromosome missegregation as a strategy to kill tumor cells. Proc. Natl. Acad. Sci. U. S. A. 106, 19108-19113
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 19108-19113
    • Janssen, A.1    Kops, G.J.2    Medema, R.H.3
  • 46
    • 84878156617 scopus 로고    scopus 로고
    • Tracking spindle checkpoint signals from kinetochores to APC/C
    • Jia, L., Kim, S., and Yu, H. (2013). Tracking spindle checkpoint signals from kinetochores to APC/C. Trends Biochem. Sci. 38, 302-311
    • (2013) Trends Biochem. Sci , vol.38 , pp. 302-311
    • Jia, L.1    Kim, S.2    Yu, H.3
  • 47
    • 65649085265 scopus 로고    scopus 로고
    • Chromosome segregation: Ndc80 can carry the load
    • Joglekar, A. P., and DeLuca, J. G. (2009). Chromosome segregation: Ndc80 can carry the load. Curr. Biol. 19, R404-R407
    • (2009) Curr. Biol , vol.19 , pp. R404-R407
    • Joglekar, A.P.1    DeLuca, J.G.2
  • 50
    • 78650569571 scopus 로고    scopus 로고
    • Phosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition
    • Kim, S., Sun, H., Ball, H. L., Wassmann, K., Luo, X., and Yu, H. (2010). Phosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition. Proc. Natl. Acad. Sci. U. S. A. 107, 19772-19777
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 19772-19777
    • Kim, S.1    Sun, H.2    Ball, H.L.3    Wassmann, K.4    Luo, X.5    Yu, H.6
  • 51
    • 33845875196 scopus 로고    scopus 로고
    • Relating three-dimensional structures to protein networks provides evolutionary insights
    • Kim, P. M., Lu, L. J., Xia, Y., and Gerstein, M. B. (2006a) Relating three-dimensional structures to protein networks provides evolutionary insights. Science 314, 1938-1941
    • (2006) Science , vol.314 , pp. 1938-1941
    • Kim, P.M.1    Lu, L.J.2    Xia, Y.3    Gerstein, M.B.4
  • 53
    • 79952269227 scopus 로고    scopus 로고
    • Protein interaction domain mapping of human kinetochore protein Blinkin reveals a consensus motif for binding of spindle assembly checkpoint proteins Bub1 and BubR1
    • Kiyomitsu, T., Murakami, H., and Yanagida, M. (2011). Protein interaction domain mapping of human kinetochore protein Blinkin reveals a consensus motif for binding of spindle assembly checkpoint proteins Bub1 and BubR1. Mol. Cell. Biol. 31, 998-1011
    • (2011) Mol. Cell. Biol , vol.31 , pp. 998-1011
    • Kiyomitsu, T.1    Murakami, H.2    Yanagida, M.3
  • 54
    • 35649019314 scopus 로고    scopus 로고
    • Human Blinkin/AF15q14 is required for chromosome alignment and the mitotic checkpoint through direct interaction with Bub1 and BubR1
    • Kiyomitsu, T., Obuse, C., and Yanagida, M. (2007). Human Blinkin/AF15q14 is required for chromosome alignment and the mitotic checkpoint through direct interaction with Bub1 and BubR1. Dev. Cell 13, 663-676
    • (2007) Dev. Cell , vol.13 , pp. 663-676
    • Kiyomitsu, T.1    Obuse, C.2    Yanagida, M.3
  • 55
    • 84859983402 scopus 로고    scopus 로고
    • Structural analysis reveals features of the spindle checkpoint kinase Bub1-kinetochore subunit Knl1 interaction
    • Krenn, V., Wehenkel, A., Li, X., Santaguida, S., and Musacchio, A. (2012). Structural analysis reveals features of the spindle checkpoint kinase Bub1-kinetochore subunit Knl1 interaction. J. Cell Biol. 196, 451-467
    • (2012) J. Cell Biol , vol.196 , pp. 451-467
    • Krenn, V.1    Wehenkel, A.2    Li, X.3    Santaguida, S.4    Musacchio, A.5
  • 56
    • 8544242697 scopus 로고    scopus 로고
    • Crystal structure of the spindle assembly checkpoint protein Bub3
    • Larsen, N. A., and Harrison, S. C. (2004). Crystal structure of the spindle assembly checkpoint protein Bub3. J. Mol. Biol. 344, 885-892
    • (2004) J. Mol. Biol , vol.344 , pp. 885-892
    • Larsen, N.A.1    Harrison, S.C.2
  • 57
    • 33846629576 scopus 로고    scopus 로고
    • Structural analysis of Bub3 interactions in the mitotic spindle checkpoint
    • Larsen, N. A., and Harrison, S. C. (2007). Structural analysis of Bub3 interactions in the mitotic spindle checkpoint. Proc. Natl. Acad. Sci. USA 104, 1201-1206
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 1201-1206
    • Larsen, N.A.1    Harrison, S.C.2
  • 58
    • 84857030052 scopus 로고    scopus 로고
    • Mad2 and Mad3 cooperate to arrest budding yeast in mitosis
    • Lau, D.T., and Murray, A. W. (2012). Mad2 and Mad3 cooperate to arrest budding yeast in mitosis. Curr. Biol. 22, 180-190
    • (2012) Curr. Biol , vol.22 , pp. 180-190
    • Lau, D.T.1    Murray, A.W.2
  • 60
    • 84897468285 scopus 로고    scopus 로고
    • Molecular dynamics simulation on the conformational transition of the mad2 protein from the open to the closed state
    • Li, C., Zhu, Y., Wang, Y., and Chen, G. (2014). Molecular dynamics simulation on the conformational transition of the mad2 protein from the open to the closed state. Int. J. Mol. Sci. 15, 5553-5569
    • (2014) Int. J. Mol. Sci , vol.15 , pp. 5553-5569
    • Li, C.1    Zhu, Y.2    Wang, Y.3    Chen, G.4
  • 61
    • 77949762923 scopus 로고    scopus 로고
    • Regulated targeting of protein phosphatase 1 to the outer kinetochore by KNL1 opposes Aurora B kinase
    • Liu, D., Vleugel, M., Backer, C. B., Hori, T., Fukagawa, T., Cheeseman, I. M., and Lampson, L. A. (2010). Regulated targeting of protein phosphatase 1 to the outer kinetochore by KNL1 opposes Aurora B kinase. J. Cell Biol. 188, 809-920
    • (2010) J. Cell Biol , vol.188 , pp. 809-920
    • Liu, D.1    Vleugel, M.2    Backer, C.B.3    Hori, T.4    Fukagawa, T.5    Cheeseman, I.M.6    Lampson, L.A.7
  • 62
    • 84861532305 scopus 로고    scopus 로고
    • Phosphoregulation of Spc105 by Mps1 and PP1 regulates Bub1 localization to kinetochores
    • London, N., Ceto, S., Ranish, J. A., and Biggins, S. (2012). Phosphoregulation of Spc105 by Mps1 and PP1 regulates Bub1 localization to kinetochores. Curr. Biol. 22, 900-906
    • (2012) Curr. Biol , vol.22 , pp. 900-906
    • London, N.1    Ceto, S.2    Ranish, J.A.3    Biggins, S.4
  • 63
    • 55249120526 scopus 로고    scopus 로고
    • Protein metamorphosis: the two-state behavior of Mad2
    • Luo, X., and Yu, H. (2008). Protein metamorphosis: the two-state behavior of Mad2. Structure 16, 1616-1625
    • (2008) Structure , vol.16 , pp. 1616-1625
    • Luo, X.1    Yu, H.2
  • 64
    • 0036161468 scopus 로고    scopus 로고
    • The MAD2 spindle checkpoint protein undergoes similar major conformational changes upon binding to either MAD1 or CDC20
    • Luo, X., Tang, Z., Rizo, J., and Yu, H. (2002). The MAD2 spindle checkpoint protein undergoes similar major conformational changes upon binding to either MAD1 or CDC20. Mol. Cell 9, 59-71
    • (2002) Mol. Cell , vol.9 , pp. 59-71
    • Luo, X.1    Tang, Z.2    Rizo, J.3    Yu, H.4
  • 65
    • 0343986407 scopus 로고    scopus 로고
    • Structure of the MAD2 spindle assembly checkpoint protein and its interaction with CDC20
    • Luo, X., Fang, G., Coldiron, M., Lin, Y., Yu, H., Kirschner, M. W., and Wagner, G. (2000). Structure of the MAD2 spindle assembly checkpoint protein and its interaction with CDC20. Nat. Struct. Biol. 7, 224-229
    • (2000) Nat. Struct. Biol , vol.7 , pp. 224-229
    • Luo, X.1    Fang, G.2    Coldiron, M.3    Lin, Y.4    Yu, H.5    Kirschner, M.W.6    Wagner, G.7
  • 66
    • 77954706607 scopus 로고    scopus 로고
    • Mps1 directs the assembly of Cdc20 inhibitory complexes during interphase and mitosis to control M phase timing and spindle checkpoint signaling
    • Maciejowski, J., George, K. A., Terret, M. E., Zhang, C., Shokat, K. M., and Jallepalli, P. V. (2010). Mps1 directs the assembly of Cdc20 inhibitory complexes during interphase and mitosis to control M phase timing and spindle checkpoint signaling. J. Cell Biol. 190, 89-100
    • (2010) J. Cell Biol , vol.190 , pp. 89-100
    • Maciejowski, J.1    George, K.A.2    Terret, M.E.3    Zhang, C.4    Shokat, K.M.5    Jallepalli, P.V.6
  • 67
    • 0038446875 scopus 로고    scopus 로고
    • Activating and silencing the mitotic checkpoint through CENP-E-dependent activation/inactivation of BubR1
    • Mao, Y., Abrieu, A., and Cleveland, D. W. (2003). Activating and silencing the mitotic checkpoint through CENP-E-dependent activation/inactivation of BubR1. Cell 114, 87-98
    • (2003) Cell , vol.114 , pp. 87-98
    • Mao, Y.1    Abrieu, A.2    Cleveland, D.W.3
  • 68
    • 79960622503 scopus 로고    scopus 로고
    • Biogenesis and function of nuclear bodies
    • Mao, Y. S., Zhang, B., and Spector, D. L. (2011). Biogenesis and function of nuclear bodies. Trends Genet. 27, 295-306
    • (2011) Trends Genet , vol.27 , pp. 295-306
    • Mao, Y.S.1    Zhang, B.2    Spector, D.L.3
  • 69
    • 79953299278 scopus 로고    scopus 로고
    • Constitutive Mad1 targeting to kinetochores uncouples checkpoint signalling from chromosome biorientation
    • Erratum in: Nat Cell Biol. 13, 633
    • Maldonado, M., and Kapoor, T. M. (2011). Constitutive Mad1 targeting to kinetochores uncouples checkpoint signalling from chromosome biorientation. Nat Cell Biol.13, 475-482. Erratum in: Nat Cell Biol. (2011) 13, 633
    • (2011) Nat Cell Biol , vol.13 , pp. 475-482
    • Maldonado, M.1    Kapoor, T.M.2
  • 70
    • 36049044125 scopus 로고    scopus 로고
    • The Mad2 conformational dimer: structure and implications for the spindle assembly checkpoint
    • Mapelli, M., Massimiliano, L., Santaguida, S., and Musacchio, A. (2007). The Mad2 conformational dimer: structure and implications for the spindle assembly checkpoint. Cell 131, 730-743
    • (2007) Cell , vol.131 , pp. 730-743
    • Mapelli, M.1    Massimiliano, L.2    Santaguida, S.3    Musacchio, A.4
  • 71
    • 0035172929 scopus 로고    scopus 로고
    • CENP-E is essential for reliable bioriented spindle attachment, but chromosome alignment can be achieved via redundant mechanisms in mammalian cells
    • McEwen, B. F., Chan, G. K., Zubrowski, B., Savoian, M. S., Sauer, M. T., and Yen, T. J. (2001). CENP-E is essential for reliable bioriented spindle attachment, but chromosome alignment can be achieved via redundant mechanisms in mammalian cells. Mol. Biol. Cell 12, 2776-2789
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2776-2789
    • McEwen, B.F.1    Chan, G.K.2    Zubrowski, B.3    Savoian, M.S.4    Sauer, M.T.5    Yen, T.J.6
  • 72
    • 77950792003 scopus 로고    scopus 로고
    • Diffusion, crowding & protein stability in a dynamic molecular model of the bacterial cytoplasm
    • McGuffee, S. R., and Elcock, A. H. (2010). Diffusion, crowding & protein stability in a dynamic molecular model of the bacterial cytoplasm. PLoS Comput. Biol. 6, e1000694
    • (2010) PLoS Comput. Biol. , vol.6 , pp. e1000694
    • McGuffee, S.R.1    Elcock, A.H.2
  • 73
    • 80555125093 scopus 로고    scopus 로고
    • Drosophila CENH3 is sufficient for centromere formation
    • Mendiburo, M. J., Padeken, J., Fulop, S., Schepers, A., and Heun, P. (2011). Drosophila CENH3 is sufficient for centromere formation. Science 334, 686-690
    • (2011) Science , vol.334 , pp. 686-690
    • Mendiburo, M.J.1    Padeken, J.2    Fulop, S.3    Schepers, A.4    Heun, P.5
  • 74
    • 84874394494 scopus 로고    scopus 로고
    • Mps1 and Ipl1/Aurora B Act Sequentially to Correctly Orient Chromosomes on the Meiotic Spindle of Budding Yeast
    • Meyer, R. E., Kim, S., Obeso, D., Straight, P. D., Winey, M., and Dawson, D. S. (2013). Mps1 and Ipl1/Aurora B Act Sequentially to Correctly Orient Chromosomes on the Meiotic Spindle of Budding Yeast. Science 339, 1071-1074
    • (2013) Science , vol.339 , pp. 1071-1074
    • Meyer, R.E.1    Kim, S.2    Obeso, D.3    Straight, P.D.4    Winey, M.5    Dawson, D.S.6
  • 75
    • 24944592549 scopus 로고    scopus 로고
    • BUB1 and aurora B cooperate to maintain BubR1-mediated inhibition of APC/CCDC20
    • Morrow, C. J., Tighe, A., Johnson, V. L., Scott, M. I., Ditchfield, C., and Taylor, S. S. (2005). BUB1 and aurora B cooperate to maintain BubR1-mediated inhibition of APC/CCDC20. J. Cell Sci. 118, 3639-3652
    • (2005) J. Cell Sci , vol.118 , pp. 3639-3652
    • Morrow, C.J.1    Tighe, A.2    Johnson, V.L.3    Scott, M.I.4    Ditchfield, C.5    Taylor, S.S.6
  • 76
    • 34247333444 scopus 로고    scopus 로고
    • The spindle-assembly checkpoint in space and time
    • Musacchio, A., and Salmon, E. D. (2007). The spindle-assembly checkpoint in space and time. Nat. Rev. Mol. Cell Biol. 8, 379-393
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 379-393
    • Musacchio, A.1    Salmon, E.D.2
  • 78
    • 57049097535 scopus 로고    scopus 로고
    • The APC/C maintains the spindle assembly checkpoint by targeting Cdc20 for destruction
    • Nilsson, J., Yekezare, M., Minshull, J., and Pines, J. (2008). The APC/C maintains the spindle assembly checkpoint by targeting Cdc20 for destruction. Nat. Cell Biol. 10, 1411-1420
    • (2008) Nat. Cell Biol , vol.10 , pp. 1411-1420
    • Nilsson, J.1    Yekezare, M.2    Minshull, J.3    Pines, J.4
  • 79
    • 0025763392 scopus 로고
    • Purification of the centromerespecific protein CENP-A and demonstration that it is a distinctive histone
    • Palmer, D. K., O'Day, K., Trong, H. L., Charbonneau, H., and Margolis, R. L. (1991). Purification of the centromerespecific protein CENP-A and demonstration that it is a distinctive histone. Proc. Natl Acad. Sci. U. S. A. 88, 3734-3738
    • (1991) Proc. Natl Acad. Sci. U. S. A. , vol.88 , pp. 3734-3738
    • Palmer, D.K.1    O'Day, K.2    Trong, H.L.3    Charbonneau, H.4    Margolis, R.L.5
  • 80
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • Pawson, T., and Nash, P. (2003). Assembly of cell regulatory systems through protein interaction domains. Science 300, 445-452
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 81
  • 83
    • 0034654399 scopus 로고    scopus 로고
    • The KEN box: an APC recognition signal distinct from the D box targeted by Cdh1
    • Pfleger, C. M., and Kirschner, M. W. (2000). The KEN box: an APC recognition signal distinct from the D box targeted by Cdh1. Genes Dev. 14, 655-665
    • (2000) Genes Dev , vol.14 , pp. 655-665
    • Pfleger, C.M.1    Kirschner, M.W.2
  • 85
    • 73349105276 scopus 로고    scopus 로고
    • The kinetochore and the centromere: a working long distance relationship
    • Przewloka, M. R., and Glover, D. M. (2009). The kinetochore and the centromere: a working long distance relationship. Annu. Rev. Genet. 43, 439-465
    • (2009) Annu. Rev. Genet , vol.43 , pp. 439-465
    • Przewloka, M.R.1    Glover, D.M.2
  • 88
    • 33749243774 scopus 로고    scopus 로고
    • The CRY box: a second APCcdh1-dependent degron in mammalian cdc20
    • Reis, A., Levasseur, M,. Chang, H. Y., Elliott, D. J., and Jones, K. T. (2006). The CRY box: a second APCcdh1-dependent degron in mammalian cdc20. EMBO Rep. 7, 1040-1045
    • (2006) EMBO Rep , vol.7 , pp. 1040-1045
    • Reis, A.1    Levasseur, M.2    Chang, H.Y.3    Elliott, D.J.4    Jones, K.T.5
  • 89
    • 79958021557 scopus 로고    scopus 로고
    • KNL1/Spc105 recruits PP1 to silence the spindle assembly checkpoint
    • Rosenberg, J. S., Cross, F. R., and Funabiki, H. (2011). KNL1/Spc105 recruits PP1 to silence the spindle assembly checkpoint. Curr. Biol. 21, 942-947
    • (2011) Curr. Biol , vol.21 , pp. 942-947
    • Rosenberg, J.S.1    Cross, F.R.2    Funabiki, H.3
  • 90
    • 69849107380 scopus 로고    scopus 로고
    • The life and miracles of kinetochores
    • Santaguida, S., and Musacchio, A. (2009). The life and miracles of kinetochores. EMBO J. 28, 2511-2531
    • (2009) EMBO J , vol.28 , pp. 2511-2531
    • Santaguida, S.1    Musacchio, A.2
  • 91
    • 0037470574 scopus 로고    scopus 로고
    • Effect of dextran on protein stability and conformation attributed to macromolecular crowding
    • Sasahara, K., McPhie, P., and Minton, A. P. (2003). Effect of dextran on protein stability and conformation attributed to macromolecular crowding. J. Mol. Biol. 326, 1227-1237
    • (2003) J. Mol. Biol , vol.326 , pp. 1227-1237
    • Sasahara, K.1    McPhie, P.2    Minton, A.P.3
  • 92
    • 0031468113 scopus 로고    scopus 로고
    • CENPE function at kinetochores is essential for chromosome alignment
    • Schaar, B. T., Chan, G. K., Maddox, P., Salmon, E. D., and Yen, T. J. (1997). CENPE function at kinetochores is essential for chromosome alignment. J. Cell Biol. 139, 1373-1382
    • (1997) J. Cell Biol , vol.139 , pp. 1373-1382
    • Schaar, B.T.1    Chan, G.K.2    Maddox, P.3    Salmon, E.D.4    Yen, T.J.5
  • 93
    • 34547599318 scopus 로고    scopus 로고
    • Natively unstructured loops differ from other loops
    • Schlessinger, A., Liu, J., and Rost, B. (2007). Natively unstructured loops differ from other loops. PLoS Comput. Biol. 3, e140
    • (2007) PLoS Comput. Biol , vol.3 , pp. e140
    • Schlessinger, A.1    Liu, J.2    Rost, B.3
  • 94
    • 84872201584 scopus 로고    scopus 로고
    • The Mad1-Mad2 balancing act - a damaged spindle checkpoint in chromosome instability and cancer
    • Schuyler, S. C., Wu, Y. F., Kuan, V. J. (2012). The Mad1-Mad2 balancing act - a damaged spindle checkpoint in chromosome instability and cancer. J Cell Sci. 125, 4197-4206
    • (2012) J Cell Sci , vol.125 , pp. 4197-4206
    • Schuyler, S.C.1    Wu, Y.F.2    Kuan, V.J.3
  • 95
    • 79958733630 scopus 로고    scopus 로고
    • Mad2 is a critical mediator of the chromosome instability observed upon Rb and p53 pathway inhibition
    • Schvartzman, J. M., Duijf, P. H., Sotillo, R., Coker, C., and Benezra, R. (2011). Mad2 is a critical mediator of the chromosome instability observed upon Rb and p53 pathway inhibition. Cancer Cell 19, 701-714
    • (2011) Cancer Cell , vol.19 , pp. 701-714
    • Schvartzman, J.M.1    Duijf, P.H.2    Sotillo, R.3    Coker, C.4    Benezra, R.5
  • 96
    • 84872849589 scopus 로고    scopus 로고
    • Mechanisms controlling the temporal degradation of Nek2A and Kif18A by the APC/C-Cdc20 complex
    • Sedgwick, G. G., Hayward, D. G., Di Fiore, B., Pardo, M., Yu, L., Pines, J., and Nilsson, J. (2013). Mechanisms controlling the temporal degradation of Nek2A and Kif18A by the APC/C-Cdc20 complex. EMBO J. 32, 303-314
    • (2013) EMBO J , vol.32 , pp. 303-314
    • Sedgwick, G.G.1    Hayward, D.G.2    Di Fiore, B.3    Pardo, M.4    Yu, L.5    Pines, J.6    Nilsson, J.7
  • 97
  • 100
    • 33746591154 scopus 로고    scopus 로고
    • Fast local backbone dynamics of encapsulated ubiquitin
    • Simorellis, A. K., and Flynn, P. F. (2006). Fast local backbone dynamics of encapsulated ubiquitin. J. Am. Chem. Soc. 128, 9580-9581
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 9580-9581
    • Simorellis, A.K.1    Flynn, P.F.2
  • 101
    • 0037093326 scopus 로고    scopus 로고
    • Crystal structure of the tetrameric Mad1-Mad2 core complex: implications of a 'safety belt' binding mechanism for the spindle checkpoint
    • Sironi, L., Mapelli, M., Knapp, S., De Antoni, A., Jeang, K. T., and Musacchio, A. (2002). Crystal structure of the tetrameric Mad1-Mad2 core complex: implications of a 'safety belt' binding mechanism for the spindle checkpoint. EMBO J. 21, 2496-2506
    • (2002) EMBO J , vol.21 , pp. 2496-2506
    • Sironi, L.1    Mapelli, M.2    Knapp, S.3    De Antoni, A.4    Jeang, K.T.5    Musacchio, A.6
  • 102
    • 0035890057 scopus 로고    scopus 로고
    • Mad2 binding to Mad1 and Cdc20, rather than oligomerization, is required for the spindle checkpoint
    • Sironi, L., Melixetian, M., Faretta, M., Prosperini, E., Helin, K., and Musacchio, A. (2001). Mad2 binding to Mad1 and Cdc20, rather than oligomerization, is required for the spindle checkpoint. EMBO J. 20, 6371-6382
    • (2001) EMBO J , vol.20 , pp. 6371-6382
    • Sironi, L.1    Melixetian, M.2    Faretta, M.3    Prosperini, E.4    Helin, K.5    Musacchio, A.6
  • 104
    • 77949773695 scopus 로고    scopus 로고
    • Mad2-induced chromosome instability leads to lung tumour relapse after oncogene withdrawal
    • Sotillo, R., Schvartzman, J. M., Socci, N. D., and Benezra, R. (2010). Mad2-induced chromosome instability leads to lung tumour relapse after oncogene withdrawal. Nature 464, 436-440
    • (2010) Nature , vol.464 , pp. 436-440
    • Sotillo, R.1    Schvartzman, J.M.2    Socci, N.D.3    Benezra, R.4
  • 106
    • 0028946805 scopus 로고
    • A mutation in CSE4, an essential gene encoding a novel chromatin-associated protein in yeast, causes chromosome nondisjunction and cell cycle arrest at mitosis
    • Stoler, S., Keith, K. C., Curnick, K. E., and Fitzgerald-Hayes, M. (1995). A mutation in CSE4, an essential gene encoding a novel chromatin-associated protein in yeast, causes chromosome nondisjunction and cell cycle arrest at mitosis. Genes Dev. 9, 573-586
    • (1995) Genes Dev , vol.9 , pp. 573-586
    • Stoler, S.1    Keith, K.C.2    Curnick, K.E.3    Fitzgerald-Hayes, M.4
  • 107
    • 0034303480 scopus 로고    scopus 로고
    • Activation of the Drosophila NF-kappaB factor Relish by rapid endoproteolytic cleavage
    • Stöven, S., Ando, I., Kadalayil, L., Engström, Y., and Hultmark, D. (2000). Activation of the Drosophila NF-kappaB factor Relish by rapid endoproteolytic cleavage. EMBO Rep. 1, 347-352
    • (2000) EMBO Rep , vol.1 , pp. 347-352
    • Stöven, S.1    Ando, I.2    Kadalayil, L.3    Engström, Y.4    Hultmark, D.5
  • 109
    • 84873723524 scopus 로고    scopus 로고
    • Regulatory mechanisms of kinetochore-microtubule interaction in mitosis
    • Tanaka, K. (2013). Regulatory mechanisms of kinetochore-microtubule interaction in mitosis. Cell Mol. Life Sci. 70, 559-579
    • (2013) Cell Mol. Life Sci , vol.70 , pp. 559-579
    • Tanaka, K.1
  • 111
    • 7744230752 scopus 로고    scopus 로고
    • Phosphorylation of CDC20 by Bub1 provides a catalytic mechanism for APC/C inhibition by the spindle checkpoint
    • Tang, Z., Shu, H., Oncel, D., Chen, S., and Yu, H. (2004). Phosphorylation of CDC20 by Bub1 provides a catalytic mechanism for APC/C inhibition by the spindle checkpoint. Mol. Cell 16, 387-397
    • (2004) Mol. Cell , vol.16 , pp. 387-397
    • Tang, Z.1    Shu, H.2    Oncel, D.3    Chen, S.4    Yu, H.5
  • 112
    • 3343013148 scopus 로고    scopus 로고
    • Gene silencing of CENP-E by small interfering RNA in HeLa cells leads to missegregation of chromosomes after a mitotic delay
    • Tanudji, M., Shoemaker, J., L'Italien, L., Russell, L., Chin, G., and Schebye, X. M. (2004). Gene silencing of CENP-E by small interfering RNA in HeLa cells leads to missegregation of chromosomes after a mitotic delay. Mol. Biol. Cell 15, 3771-3781
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3771-3781
    • Tanudji, M.1    Shoemaker, J.2    L'Italien, L.3    Russell, L.4    Chin, G.5    Schebye, X.M.6
  • 113
    • 84894333045 scopus 로고    scopus 로고
    • Monopolar spindle 1 (MPS1) kinase promotes production of closed MAD2 (C-MAD2) conformer and assembly of the mitotic checkpoint complex
    • Tipton, A. R., Ji, W., Sturt-Gillespie, B., Bekier, M. E. 2nd., Wang, K., Taylor, W. R., and Liu, S. T. (2013). Monopolar spindle 1 (MPS1) kinase promotes production of closed MAD2 (C-MAD2) conformer and assembly of the mitotic checkpoint complex. J Biol Chem. 288, 35149-35158
    • (2013) J Biol Chem , vol.288 , pp. 35149-35158
    • Tipton, A.R.1    Ji, W.2    Sturt-Gillespie, B.3    Bekier II, M.E.4    Wang, K.5    Taylor, W.R.6    Liu, S.T.7
  • 114
    • 18044396994 scopus 로고    scopus 로고
    • Bub1 and the multilayered inhibition of CDC20-APC/C in mitosis
    • Vanoosthuyse, V., and Hardwick, K. G. (2005). Bub1 and the multilayered inhibition of CDC20-APC/C in mitosis. Trends Cell Biol. 15, 231-233
    • (2005) Trends Cell Biol , vol.15 , pp. 231-233
    • Vanoosthuyse, V.1    Hardwick, K.G.2
  • 115
    • 67649635978 scopus 로고    scopus 로고
    • Intrinsic protein disorder and interaction promiscuity are widely associated with dosage sensitivity
    • Vavouri, T., Semple, J. I., Garcia-Verdugo, R., and Lehner, B. (2009). Intrinsic protein disorder and interaction promiscuity are widely associated with dosage sensitivity. Cell 138, 198-208
    • (2009) Cell , vol.138 , pp. 198-208
    • Vavouri, T.1    Semple, J.I.2    Garcia-Verdugo, R.3    Lehner, B.4
  • 119
    • 84866543814 scopus 로고    scopus 로고
    • SUMOylation in control of accurate chromosome segregation during mitosis
    • Wan, J., Subramonian, D., and Zhang, X. D. (2012). SUMOylation in control of accurate chromosome segregation during mitosis. Curr. Protein Pept. Sci. 13, 467-481
    • (2012) Curr. Protein Pept. Sci , vol.13 , pp. 467-481
    • Wan, J.1    Subramonian, D.2    Zhang, X.D.3
  • 120
    • 77955686807 scopus 로고    scopus 로고
    • Effects of proteins on protein diffusion
    • Wang, Y., Li, C., and Pielak, G. J. (2010). Effects of proteins on protein diffusion. J. Am. Chem. Soc. 132, 9392-9397
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 9392-9397
    • Wang, Y.1    Li, C.2    Pielak, G.J.3
  • 122
    • 17244363408 scopus 로고    scopus 로고
    • Molecular organization of the Ndc80 complex, an essential kinetochore component
    • Wei, R. R., Sorger, P. K., and Harrison, S. C. (2005). Molecular organization of the Ndc80 complex, an essential kinetochore component. Proc. Natl Acad. Sci. U. S. A. 102, 5363-5367
    • (2005) Proc. Natl Acad. Sci. U. S. A. , vol.102 , pp. 5363-5367
    • Wei, R.R.1    Sorger, P.K.2    Harrison, S.C.3
  • 123
    • 33846100785 scopus 로고    scopus 로고
    • The Ndc80/HEC1 complex is a contact point for kinetochore-microtubule attachment
    • Wei, R. R., Al-Bassam, J., and Harrison, S. C. (2007). The Ndc80/HEC1 complex is a contact point for kinetochore-microtubule attachment. Nat. Struct. Mol. Biol. 14, 54-55
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 54-55
    • Wei, R.R.1    Al-Bassam, J.2    Harrison, S.C.3
  • 124
    • 0030066347 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae spindle pole body duplication gene MPS1 is part of a mitotic checkpoint
    • Weiss, E., and Winey, M. (1996). The Saccharomyces cerevisiae spindle pole body duplication gene MPS1 is part of a mitotic checkpoint. J. Cell Biol. 132, 111-123
    • (1996) J. Cell Biol , vol.132 , pp. 111-123
    • Weiss, E.1    Winey, M.2
  • 125
    • 38549086019 scopus 로고    scopus 로고
    • FBW7 ubiquitin ligase: a tumour suppressor at the crossroads of cell division, growth and differentiation
    • Welcker, M., and Clurman, B.E. (2008). FBW7 ubiquitin ligase: a tumour suppressor at the crossroads of cell division, growth and differentiation. Nat. Rev. Cancer 8, 83-93
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 83-93
    • Welcker, M.1    Clurman, B.E.2
  • 126
    • 84879239743 scopus 로고    scopus 로고
    • Functions of the centromere and kinetochore in chromosome segregation
    • Westhorpe, F. G., and Straight, A. F. (2013). Functions of the centromere and kinetochore in chromosome segregation. Curr. Opin. Cell Biol. 25, 334-340
    • (2013) Curr. Opin. Cell Biol , vol.25 , pp. 334-340
    • Westhorpe, F.G.1    Straight, A.F.2
  • 127
    • 20444495306 scopus 로고    scopus 로고
    • The 1.1-angstrom structure of the spindle checkpoint protein Bub3p reveals functional regions
    • Wilson, D. K., Cerna, D., and Chew, E. (2005). The 1.1-angstrom structure of the spindle checkpoint protein Bub3p reveals functional regions. J. Biol. Chem. 280, 13944-13951
    • (2005) J. Biol. Chem , vol.280 , pp. 13944-13951
    • Wilson, D.K.1    Cerna, D.2    Chew, E.3
  • 128
    • 0037048281 scopus 로고    scopus 로고
    • Centrosomes and checkpoints: the MPS1 family of kinases
    • Winey, M., and Huneycutt, B. J. (2002). Centrosomes and checkpoints: the MPS1 family of kinases. Oncogene 21, 6161-6169
    • (2002) Oncogene , vol.21 , pp. 6161-6169
    • Winey, M.1    Huneycutt, B.J.2
  • 129
    • 4143076016 scopus 로고    scopus 로고
    • Conformation-specific binding of p31(comet) antagonizes the function of Mad2 in the spindle checkpoint
    • Xia, G., Luo, X., Habu, T., Rizo, J., Matsumoto, T., and Yu, H. (2004). Conformation-specific binding of p31(comet) antagonizes the function of Mad2 in the spindle checkpoint. EMBO J. 23, 3133-3143
    • (2004) EMBO J , vol.23 , pp. 3133-3143
    • Xia, G.1    Luo, X.2    Habu, T.3    Rizo, J.4    Matsumoto, T.5    Yu, H.6
  • 130
    • 36049028674 scopus 로고    scopus 로고
    • p31comet blocks Mad2 activation through structural mimicry
    • Yang, M., Li, B., Tomchick, D. R., Machius, M., Rizo, J., Yu, H., and Luo, X. (2007). p31comet blocks Mad2 activation through structural mimicry. Cell 131, 744-755
    • (2007) Cell , vol.131 , pp. 744-755
    • Yang, M.1    Li, B.2    Tomchick, D.R.3    Machius, M.4    Rizo, J.5    Yu, H.6    Luo, X.7
  • 131
    • 84860280333 scopus 로고    scopus 로고
    • Mitotic checkpoint control and chromatin remodeling
    • Yao, Y., and Dai, W. (2012). Mitotic checkpoint control and chromatin remodeling. Front. Biosci. 17, 976-983
    • (2012) Front. Biosci , vol.17 , pp. 976-983
    • Yao, Y.1    Dai, W.2
  • 132
    • 0001665802 scopus 로고    scopus 로고
    • CENPE forms a link between attachment of spindle microtubules to kinetochores and the mitotic checkpoint
    • Yao, X., Abrieu, A., Zheng, Y., Sullivan, K. F., and Cleveland, D. W. (2000). CENPE forms a link between attachment of spindle microtubules to kinetochores and the mitotic checkpoint. Nat. Cell Biol. 2, 484-491
    • (2000) Nat. Cell Biol , vol.2 , pp. 484-491
    • Yao, X.1    Abrieu, A.2    Zheng, Y.3    Sullivan, K.F.4    Cleveland, D.W.5
  • 133
    • 84895984956 scopus 로고    scopus 로고
    • Functional characterization of Anaphase Promoting Complex/Cyclosome (APC/C) E3 ubiquitin ligases in tumorigenesis
    • Zhang, J., Wan, L., Dai, X., Sun, Y., and Wei, W. (2014). Functional characterization of Anaphase Promoting Complex/Cyclosome (APC/C) E3 ubiquitin ligases in tumorigenesis. Biochim. Biophys. Acta. 1845, 277-293
    • (2014) Biochim. Biophys. Acta , vol.1845 , pp. 277-293
    • Zhang, J.1    Wan, L.2    Dai, X.3    Sun, Y.4    Wei, W.5
  • 134
    • 84877107994 scopus 로고    scopus 로고
    • Genetically engineered mouse models for functional studies of SKP1-CUL1-F-box-protein (SCF) E3 ubiquitin ligases
    • Zhou, W., Wei, W., and Sun, Y. (2013). Genetically engineered mouse models for functional studies of SKP1-CUL1-F-box-protein (SCF) E3 ubiquitin ligases. Cell Res. 23, 599-619
    • (2013) Cell Res , vol.23 , pp. 599-619
    • Zhou, W.1    Wei, W.2    Sun, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.