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Volumn 50, Issue 1, 2010, Pages 375-399

Identification of substrates for cyclin dependent kinases

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN DEPENDENT KINASE; CYCLINE; ISOPROTEIN;

EID: 77951760865     PISSN: 00652571     EISSN: None     Source Type: Book Series    
DOI: 10.1016/j.advenzreg.2009.12.001     Document Type: Article
Times cited : (106)

References (153)
  • 1
    • 0035095973 scopus 로고    scopus 로고
    • Regulation of the retinoblastoma tumor suppressor protein by cyclin/cdks
    • Adams P.D. Regulation of the retinoblastoma tumor suppressor protein by cyclin/cdks. Biochim Biophys Acta 2001, 1471:M123-M133.
    • (2001) Biochim Biophys Acta , vol.1471
    • Adams, P.D.1
  • 2
    • 0035844158 scopus 로고    scopus 로고
    • Phosphorylation by cdc2-CyclinB1 kinase releases cytoplasmic dynein from membranes
    • Addinall S.G., Mayr P.S., Doyle S., Sheehan J.K., Woodman P.G., Allan V.J. Phosphorylation by cdc2-CyclinB1 kinase releases cytoplasmic dynein from membranes. J Biol Chem 2001, 276:15939-15944.
    • (2001) J Biol Chem , vol.276 , pp. 15939-15944
    • Addinall, S.G.1    Mayr, P.S.2    Doyle, S.3    Sheehan, J.K.4    Woodman, P.G.5    Allan, V.J.6
  • 3
    • 0032511884 scopus 로고    scopus 로고
    • Histone acetyltransferase activity of CBP is controlled by cycle-dependent kinases and oncoprotein E1A
    • Ait-Si-Ali S., Ramirez S., Barre F.X., Dkhissi F., Magnaghi-Jaulin L., Girault J.A., et al. Histone acetyltransferase activity of CBP is controlled by cycle-dependent kinases and oncoprotein E1A. Nature 1998, 396:184-186.
    • (1998) Nature , vol.396 , pp. 184-186
    • Ait-Si-Ali, S.1    Ramirez, S.2    Barre, F.X.3    Dkhissi, F.4    Magnaghi-Jaulin, L.5    Girault, J.A.6
  • 4
    • 0026048097 scopus 로고
    • Microtubule destabilization by cdc2/H1 histone kinase: phosphorylation of a "pro-rich region" in the microtubule-binding domain of MAP-4
    • Aizawa H., Kamijo M., Ohba Y., Mori A., Okuhara K., Kawasaki H., et al. Microtubule destabilization by cdc2/H1 histone kinase: phosphorylation of a "pro-rich region" in the microtubule-binding domain of MAP-4. Biochem Biophys Res Commun 1991, 179:1620-1626.
    • (1991) Biochem Biophys Res Commun , vol.179 , pp. 1620-1626
    • Aizawa, H.1    Kamijo, M.2    Ohba, Y.3    Mori, A.4    Okuhara, K.5    Kawasaki, H.6
  • 5
    • 0024294002 scopus 로고
    • Cdc2 is a component of the M phase-specific histone H1 kinase: evidence for identity with MPF
    • Arion D., Meijer L., Brizuela L., Beach D. cdc2 is a component of the M phase-specific histone H1 kinase: evidence for identity with MPF. Cell 1988, 55:371-378.
    • (1988) Cell , vol.55 , pp. 371-378
    • Arion, D.1    Meijer, L.2    Brizuela, L.3    Beach, D.4
  • 6
    • 29244464759 scopus 로고    scopus 로고
    • The oncogenic serine/threonine kinase Pim-1 directly phosphorylates and activates the G2/M specific phosphatase Cdc25C
    • Bachmann M., Kosan C., Xing P.X., Montenarh M., Hoffmann I., Moroy T. The oncogenic serine/threonine kinase Pim-1 directly phosphorylates and activates the G2/M specific phosphatase Cdc25C. Int J Biochem Cell Biol 2006, 38:430-443.
    • (2006) Int J Biochem Cell Biol , vol.38 , pp. 430-443
    • Bachmann, M.1    Kosan, C.2    Xing, P.X.3    Montenarh, M.4    Hoffmann, I.5    Moroy, T.6
  • 7
    • 0025364329 scopus 로고
    • Protein phosphorylation during meiotic maturation of Xenopus oocytes: cdc2 protein kinase targets
    • Belle R., Cormier P., Poulhe R., Morales J., Huchon D., Mulner-Lorillon O. Protein phosphorylation during meiotic maturation of Xenopus oocytes: cdc2 protein kinase targets. Int J Dev Biol 1990, 34:111-115.
    • (1990) Int J Dev Biol , vol.34 , pp. 111-115
    • Belle, R.1    Cormier, P.2    Poulhe, R.3    Morales, J.4    Huchon, D.5    Mulner-Lorillon, O.6
  • 8
    • 48249132443 scopus 로고    scopus 로고
    • Eco1-dependent cohesin acetylation during establishment of sister chromatid cohesion
    • Ben-Shahar T.R., Heeger S., Lehane C., East P., Flynn H., Skehel M., et al. Eco1-dependent cohesin acetylation during establishment of sister chromatid cohesion. Science 2008, 321:563-566.
    • (2008) Science , vol.321 , pp. 563-566
    • Ben-Shahar, T.R.1    Heeger, S.2    Lehane, C.3    East, P.4    Flynn, H.5    Skehel, M.6
  • 9
    • 0027292675 scopus 로고
    • Multiple phosphorylation of stathmin. Identification of four sites phosphorylated in intact cells and in vitro by cyclic AMP-dependent protein kinase and p34cdc2
    • Beretta L., Dobransky T., Sobel A. Multiple phosphorylation of stathmin. Identification of four sites phosphorylated in intact cells and in vitro by cyclic AMP-dependent protein kinase and p34cdc2. J Biol Chem 1993, 268:20076-20084.
    • (1993) J Biol Chem , vol.268 , pp. 20076-20084
    • Beretta, L.1    Dobransky, T.2    Sobel, A.3
  • 10
    • 33749643800 scopus 로고    scopus 로고
    • AML1/RUNX1 phosphorylation by cyclin-dependent kinases regulates the degradation of AML1/RUNX1 by the anaphase-promoting complex
    • Biggs J.R., Peterson L.F., Zhang Y., Kraft A.S., Zhang D.E. AML1/RUNX1 phosphorylation by cyclin-dependent kinases regulates the degradation of AML1/RUNX1 by the anaphase-promoting complex. Mol Cell Biol 2006, 26:7420-7429.
    • (2006) Mol Cell Biol , vol.26 , pp. 7420-7429
    • Biggs, J.R.1    Peterson, L.F.2    Zhang, Y.3    Kraft, A.S.4    Zhang, D.E.5
  • 11
    • 0029417238 scopus 로고
    • Phosphorylation by p34cdc2 regulates spindle association of human Eg5, a kinesin-related motor essential for bipolar spindle formation in vivo
    • Blangy A., Lane H.A., d'Herin P., Harper M., Kress M., Nigg E.A. Phosphorylation by p34cdc2 regulates spindle association of human Eg5, a kinesin-related motor essential for bipolar spindle formation in vivo. Cell 1995, 83:1159-1169.
    • (1995) Cell , vol.83 , pp. 1159-1169
    • Blangy, A.1    Lane, H.A.2    d'Herin, P.3    Harper, M.4    Kress, M.5    Nigg, E.A.6
  • 12
    • 20344396122 scopus 로고    scopus 로고
    • Preventing re-replication of chromosomal DNA
    • Blow J.J., Dutta A. Preventing re-replication of chromosomal DNA. Nat Rev Mol Cell Biol 2005, 6:476-486.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 476-486
    • Blow, J.J.1    Dutta, A.2
  • 13
    • 0028790644 scopus 로고
    • Phosphorylation of casein kinase II by p34cdc2. Identification of phosphorylation sites using phosphorylation site mutants in vitro
    • Bosc D.G., Slominski E., Sichler C., Litchfield D.W. Phosphorylation of casein kinase II by p34cdc2. Identification of phosphorylation sites using phosphorylation site mutants in vitro. J Biol Chem 1995, 270:25872-25878.
    • (1995) J Biol Chem , vol.270 , pp. 25872-25878
    • Bosc, D.G.1    Slominski, E.2    Sichler, C.3    Litchfield, D.W.4
  • 14
    • 0033224309 scopus 로고    scopus 로고
    • The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases
    • Brown N.R., Noble M.E., Endicott J.A., Johnson L.N. The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases. Nat Cell Biol 1999, 1:438-443.
    • (1999) Nat Cell Biol , vol.1 , pp. 438-443
    • Brown, N.R.1    Noble, M.E.2    Endicott, J.A.3    Johnson, L.N.4
  • 16
    • 34547411003 scopus 로고    scopus 로고
    • ETV1 is a novel androgen receptor-regulated gene that mediates prostate cancer cell invasion
    • Cai C., Hsieh C.L., Omwancha J., Zheng Z., Chen S.Y., Baert J.L., et al. ETV1 is a novel androgen receptor-regulated gene that mediates prostate cancer cell invasion. Mol Endocrinol 2007.
    • (2007) Mol Endocrinol
    • Cai, C.1    Hsieh, C.L.2    Omwancha, J.3    Zheng, Z.4    Chen, S.Y.5    Baert, J.L.6
  • 17
    • 2942614689 scopus 로고    scopus 로고
    • Cdk2-dependent phosphorylation of the NF-Y transcription factor is essential for the expression of the cell cycle-regulatory genes and cell cycle G1/S and G2/M transitions
    • Chae H.D., Yun J., Bang Y.J., Shin D.Y. Cdk2-dependent phosphorylation of the NF-Y transcription factor is essential for the expression of the cell cycle-regulatory genes and cell cycle G1/S and G2/M transitions. Oncogene 2004, 23:4084-4088.
    • (2004) Oncogene , vol.23 , pp. 4084-4088
    • Chae, H.D.1    Yun, J.2    Bang, Y.J.3    Shin, D.Y.4
  • 18
    • 0032941755 scopus 로고    scopus 로고
    • Ribonucleotide reductase R2 protein is phosphorylated at serine-20 by P34cdc2 kinase
    • Chan A.K., Persad S., Litchfield D.W., Wright J.A. Ribonucleotide reductase R2 protein is phosphorylated at serine-20 by P34cdc2 kinase. Biochim Biophys Acta 1999, 1448:363-371.
    • (1999) Biochim Biophys Acta , vol.1448 , pp. 363-371
    • Chan, A.K.1    Persad, S.2    Litchfield, D.W.3    Wright, J.A.4
  • 19
    • 84879798456 scopus 로고    scopus 로고
    • Prediction of cyclin-dependent kinase phosphorylation substrates
    • Chang E.J., Begum R., Chait B.T., Gaasterland T. Prediction of cyclin-dependent kinase phosphorylation substrates. PLoS One 2007, 2:e656.
    • (2007) PLoS One , vol.2
    • Chang, E.J.1    Begum, R.2    Chait, B.T.3    Gaasterland, T.4
  • 20
    • 0029784513 scopus 로고    scopus 로고
    • Cyclin-binding motifs are essential for the function of p21CIP1
    • Chen J., Saha P., Kornbluth S., Dynlacht B.D., Dutta A. Cyclin-binding motifs are essential for the function of p21CIP1. Mol Cell Biol 1996, 16:4673-4682.
    • (1996) Mol Cell Biol , vol.16 , pp. 4673-4682
    • Chen, J.1    Saha, P.2    Kornbluth, S.3    Dynlacht, B.D.4    Dutta, A.5
  • 21
    • 33750452673 scopus 로고    scopus 로고
    • Androgen receptor phosphorylation and stabilization in prostate cancer by cyclin-dependent kinase 1
    • Chen S., Xu Y., Yuan X., Bubley G.J., Balk S.P. Androgen receptor phosphorylation and stabilization in prostate cancer by cyclin-dependent kinase 1. Proc Natl Acad Sci U S A 2006, 103:15969-15974.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 15969-15974
    • Chen, S.1    Xu, Y.2    Yuan, X.3    Bubley, G.J.4    Balk, S.P.5
  • 23
    • 20744454423 scopus 로고    scopus 로고
    • Srs2 and Sgs1 DNA helicases associate with Mre11 in different subcomplexes following checkpoint activation and CDK1-mediated Srs2 phosphorylation
    • Chiolo I., Carotenuto W., Maffioletti G., Petrini J.H., Foiani M., Liberi G. Srs2 and Sgs1 DNA helicases associate with Mre11 in different subcomplexes following checkpoint activation and CDK1-mediated Srs2 phosphorylation. Mol Cell Biol 2005, 25:5738-5751.
    • (2005) Mol Cell Biol , vol.25 , pp. 5738-5751
    • Chiolo, I.1    Carotenuto, W.2    Maffioletti, G.3    Petrini, J.H.4    Foiani, M.5    Liberi, G.6
  • 24
    • 0025130177 scopus 로고
    • Intermediate filament reorganization during mitosis is mediated by p34cdc2 phosphorylation of vimentin
    • Chou Y.H., Bischoff J.R., Beach D., Goldman R.D. Intermediate filament reorganization during mitosis is mediated by p34cdc2 phosphorylation of vimentin. Cell 1990, 62:1063-1071.
    • (1990) Cell , vol.62 , pp. 1063-1071
    • Chou, Y.H.1    Bischoff, J.R.2    Beach, D.3    Goldman, R.D.4
  • 25
    • 0038709375 scopus 로고    scopus 로고
    • Nestin promotes the phosphorylation-dependent disassembly of vimentin intermediate filaments during mitosis
    • Chou Y.H., Khuon S., Herrmann H., Goldman R.D. Nestin promotes the phosphorylation-dependent disassembly of vimentin intermediate filaments during mitosis. Mol Biol Cell 2003, 14:1468-1478.
    • (2003) Mol Biol Cell , vol.14 , pp. 1468-1478
    • Chou, Y.H.1    Khuon, S.2    Herrmann, H.3    Goldman, R.D.4
  • 26
    • 0026783801 scopus 로고
    • The lamin B receptor of the inner nuclear membrane undergoes mitosis-specific phosphorylation and is a substrate for p34cdc2-type protein kinase
    • Courvalin J.C., Segil N., Blobel G., Worman H.J. The lamin B receptor of the inner nuclear membrane undergoes mitosis-specific phosphorylation and is a substrate for p34cdc2-type protein kinase. J Biol Chem 1992, 267:19035-19038.
    • (1992) J Biol Chem , vol.267 , pp. 19035-19038
    • Courvalin, J.C.1    Segil, N.2    Blobel, G.3    Worman, H.J.4
  • 28
    • 0037090578 scopus 로고    scopus 로고
    • Actopaxin is phosphorylated during mitosis and is a substrate for cyclin B1/cdc2 kinase
    • Curtis M., Nikolopoulos S.N., Turner C.E. Actopaxin is phosphorylated during mitosis and is a substrate for cyclin B1/cdc2 kinase. Biochem J 2002, 363:233-242.
    • (2002) Biochem J , vol.363 , pp. 233-242
    • Curtis, M.1    Nikolopoulos, S.N.2    Turner, C.E.3
  • 29
    • 0035833254 scopus 로고    scopus 로고
    • Nuclear pore complexes form immobile networks and have a very low turnover in live mammalian cells
    • Daigle N., Beaudouin J., Hartnell L., Imreh G., Hallberg E., Lippincott-Schwartz J., et al. Nuclear pore complexes form immobile networks and have a very low turnover in live mammalian cells. J Cell Biol 2001, 154:71-84.
    • (2001) J Cell Biol , vol.154 , pp. 71-84
    • Daigle, N.1    Beaudouin, J.2    Hartnell, L.3    Imreh, G.4    Hallberg, E.5    Lippincott-Schwartz, J.6
  • 30
    • 0032541346 scopus 로고    scopus 로고
    • Detergent-salt resistance of LAP2alpha in interphase nuclei and phosphorylation-dependent association with chromosomes early in nuclear assembly implies functions in nuclear structure dynamics
    • Dechat T., Gotzmann J., Stockinger A., Harris C.A., Talle M.A., Siekierka J.J., et al. Detergent-salt resistance of LAP2alpha in interphase nuclei and phosphorylation-dependent association with chromosomes early in nuclear assembly implies functions in nuclear structure dynamics. EMBO J 1998, 17:4887-4902.
    • (1998) EMBO J , vol.17 , pp. 4887-4902
    • Dechat, T.1    Gotzmann, J.2    Stockinger, A.3    Harris, C.A.4    Talle, M.A.5    Siekierka, J.J.6
  • 31
    • 10044284508 scopus 로고    scopus 로고
    • Cyclin/CDK regulates the nucleocytoplasmic localization of the human papillomavirus E1 DNA helicase
    • Deng W., Lin B.Y., Jin G., Wheeler C.G., Ma T., Harper J.W., et al. Cyclin/CDK regulates the nucleocytoplasmic localization of the human papillomavirus E1 DNA helicase. J Virol 2004, 78:13954-13965.
    • (2004) J Virol , vol.78 , pp. 13954-13965
    • Deng, W.1    Lin, B.Y.2    Jin, G.3    Wheeler, C.G.4    Ma, T.5    Harper, J.W.6
  • 32
    • 4043162062 scopus 로고    scopus 로고
    • Identification of interaction partners and substrates of the cyclin A1-CDK2 complex
    • Diederichs S., Baumer N., Ji P., Metzelder S.K., Idos G.E., Cauvet T., et al. Identification of interaction partners and substrates of the cyclin A1-CDK2 complex. J Biol Chem 2004, 279:33727-33741.
    • (2004) J Biol Chem , vol.279 , pp. 33727-33741
    • Diederichs, S.1    Baumer, N.2    Ji, P.3    Metzelder, S.K.4    Idos, G.E.5    Cauvet, T.6
  • 33
    • 0034731445 scopus 로고    scopus 로고
    • Extracellular matrix components cooperate to activate phosphatidyl inositol-4-phosphate 5-kinase
    • Dunlop M.E., Muggli E.E. Extracellular matrix components cooperate to activate phosphatidyl inositol-4-phosphate 5-kinase. Biochem Biophys Res Commun 2000, 279:931-937.
    • (2000) Biochem Biophys Res Commun , vol.279 , pp. 931-937
    • Dunlop, M.E.1    Muggli, E.E.2
  • 34
    • 47749101085 scopus 로고    scopus 로고
    • The role of GRASP55 in Golgi fragmentation and entry of cells into mitosis
    • Duran J.M., Kinseth M., Bossard C., Rose D.W., Polishchuk R., Wu C.C., et al. The role of GRASP55 in Golgi fragmentation and entry of cells into mitosis. Mol Biol Cell 2008, 19:2579-2587.
    • (2008) Mol Biol Cell , vol.19 , pp. 2579-2587
    • Duran, J.M.1    Kinseth, M.2    Bossard, C.3    Rose, D.W.4    Polishchuk, R.5    Wu, C.C.6
  • 35
    • 17844385110 scopus 로고    scopus 로고
    • Phosphorylation of MdmX by CDK2/Cdc2(p34) is required for nuclear export of Mdm2
    • Elias B., Laine A., Ronai Z. Phosphorylation of MdmX by CDK2/Cdc2(p34) is required for nuclear export of Mdm2. Oncogene 2005, 24:2574-2579.
    • (2005) Oncogene , vol.24 , pp. 2574-2579
    • Elias, B.1    Laine, A.2    Ronai, Z.3
  • 36
    • 35448949105 scopus 로고    scopus 로고
    • Tipin is required for stalled replication forks to resume DNA replication after removal of aphidicolin in Xenopus egg extracts
    • Errico A., Costanzo V., Hunt T. Tipin is required for stalled replication forks to resume DNA replication after removal of aphidicolin in Xenopus egg extracts. Proc Natl Acad Sci U S A 2007, 104:14929-14934.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 14929-14934
    • Errico, A.1    Costanzo, V.2    Hunt, T.3
  • 37
    • 15844373362 scopus 로고    scopus 로고
    • CDK-dependent phosphorylation of BRCA2 as a regulatory mechanism for recombinational repair
    • Esashi F., Christ N., Gannon J., Liu Y., Hunt T., Jasin M., et al. CDK-dependent phosphorylation of BRCA2 as a regulatory mechanism for recombinational repair. Nature 2005, 434:598-604.
    • (2005) Nature , vol.434 , pp. 598-604
    • Esashi, F.1    Christ, N.2    Gannon, J.3    Liu, Y.4    Hunt, T.5    Jasin, M.6
  • 39
    • 0035896503 scopus 로고    scopus 로고
    • Amphiphysin 1 binds the cyclin-dependent kinase (cdk) 5 regulatory subunit p35 and is phosphorylated by cdk5 and cdc2
    • Floyd S.R., Porro E.B., Slepnev V.I., Ochoa G.C., Tsai L.H., De Camilli P. Amphiphysin 1 binds the cyclin-dependent kinase (cdk) 5 regulatory subunit p35 and is phosphorylated by cdk5 and cdc2. J Biol Chem 2001, 276:8104-8110.
    • (2001) J Biol Chem , vol.276 , pp. 8104-8110
    • Floyd, S.R.1    Porro, E.B.2    Slepnev, V.I.3    Ochoa, G.C.4    Tsai, L.H.5    De Camilli, P.6
  • 41
    • 24944591014 scopus 로고    scopus 로고
    • Phosphorylation of human DNA polymerase lambda by the cyclin-dependent kinase Cdk2/cyclin A complex is modulated by its association with proliferating cell nuclear antigen
    • Frouin I., Toueille M., Ferrari E., Shevelev I., Hubscher U. Phosphorylation of human DNA polymerase lambda by the cyclin-dependent kinase Cdk2/cyclin A complex is modulated by its association with proliferating cell nuclear antigen. Nucleic Acids Res 2005, 33:5354-5361.
    • (2005) Nucleic Acids Res , vol.33 , pp. 5354-5361
    • Frouin, I.1    Toueille, M.2    Ferrari, E.3    Shevelev, I.4    Hubscher, U.5
  • 43
    • 0034747803 scopus 로고    scopus 로고
    • Reciprocal activation by cyclin-dependent kinases 2 and 7 is directed by substrate specificity determinants outside the T loop
    • Garrett S., Barton W.A., Knights R., Jin P., Morgan D.O., Fisher R.P. Reciprocal activation by cyclin-dependent kinases 2 and 7 is directed by substrate specificity determinants outside the T loop. Mol Cell Biol 2001, 21:88-99.
    • (2001) Mol Cell Biol , vol.21 , pp. 88-99
    • Garrett, S.1    Barton, W.A.2    Knights, R.3    Jin, P.4    Morgan, D.O.5    Fisher, R.P.6
  • 46
    • 21244467405 scopus 로고    scopus 로고
    • Mutual inhibition of separase and Cdk1 by two-step complex formation
    • Gorr I.H., Boos D., Stemmann O. Mutual inhibition of separase and Cdk1 by two-step complex formation. Mol Cell 2005, 19:135-141.
    • (2005) Mol Cell , vol.19 , pp. 135-141
    • Gorr, I.H.1    Boos, D.2    Stemmann, O.3
  • 47
    • 33244490241 scopus 로고    scopus 로고
    • Complex formation of Plk1 and INCENP required for metaphase-anaphase transition
    • Goto H., Kiyono T., Tomono Y., Kawajiri A., Urano T., Furukawa K., et al. Complex formation of Plk1 and INCENP required for metaphase-anaphase transition. Nat Cell Biol 2006, 8:180-187.
    • (2006) Nat Cell Biol , vol.8 , pp. 180-187
    • Goto, H.1    Kiyono, T.2    Tomono, Y.3    Kawajiri, A.4    Urano, T.5    Furukawa, K.6
  • 48
    • 33645316790 scopus 로고    scopus 로고
    • Phosphorylation of RIalpha by cyclin-dependent kinase CDK 2/cyclin E modulates the dissociation of the RIalpha-RFC40 complex
    • Gupte R.S., Traganos F., Darzynkiewicz Z., Lee M.Y. Phosphorylation of RIalpha by cyclin-dependent kinase CDK 2/cyclin E modulates the dissociation of the RIalpha-RFC40 complex. Cell Cycle 2006, 5:653-660.
    • (2006) Cell Cycle , vol.5 , pp. 653-660
    • Gupte, R.S.1    Traganos, F.2    Darzynkiewicz, Z.3    Lee, M.Y.4
  • 49
    • 0035131425 scopus 로고    scopus 로고
    • HIRA, the human homologue of yeast Hir1 p and Hir2 p, is a novel cyclin-cdk2 substrate whose expression blocks S-phase progression
    • Hall C., Nelson D.M., Ye X., Baker K., DeCaprio J.A., Seeholzer S., et al. HIRA, the human homologue of yeast Hir1 p and Hir2 p, is a novel cyclin-cdk2 substrate whose expression blocks S-phase progression. Mol Cell Biol 2001, 21:1854-1865.
    • (2001) Mol Cell Biol , vol.21 , pp. 1854-1865
    • Hall, C.1    Nelson, D.M.2    Ye, X.3    Baker, K.4    DeCaprio, J.A.5    Seeholzer, S.6
  • 50
    • 31544476883 scopus 로고    scopus 로고
    • Cytokinesis regulator ECT2 changes its conformation through phosphorylation at Thr-341 in G2/M phase
    • Hara T., Abe M., Inoue H., Yu L.R., Veenstra T.D., Kang Y.H., et al. Cytokinesis regulator ECT2 changes its conformation through phosphorylation at Thr-341 in G2/M phase. Oncogene 2006, 25:566-578.
    • (2006) Oncogene , vol.25 , pp. 566-578
    • Hara, T.1    Abe, M.2    Inoue, H.3    Yu, L.R.4    Veenstra, T.D.5    Kang, Y.H.6
  • 51
    • 0033578816 scopus 로고    scopus 로고
    • Cdk phosphorylation triggers sequential intramolecular interactions that progressively block Rb functions as cells move through G1
    • Harbour J.W., Luo R.X., Dei Santi A., Postigo A.A., Dean D.C. Cdk phosphorylation triggers sequential intramolecular interactions that progressively block Rb functions as cells move through G1. Cell 1999, 98:859-869.
    • (1999) Cell , vol.98 , pp. 859-869
    • Harbour, J.W.1    Luo, R.X.2    Dei Santi, A.3    Postigo, A.A.4    Dean, D.C.5
  • 53
    • 0042168729 scopus 로고    scopus 로고
    • Cell cycle-dependent phosphorylation of Disabled-2 by cdc2
    • He J., Xu J., Xu X.X., Hall R.A. Cell cycle-dependent phosphorylation of Disabled-2 by cdc2. Oncogene 2003, 22:4524-4530.
    • (2003) Oncogene , vol.22 , pp. 4524-4530
    • He, J.1    Xu, J.2    Xu, X.X.3    Hall, R.A.4
  • 54
    • 0025352896 scopus 로고
    • Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis
    • Heald R., McKeon F. Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis. Cell 1990, 61:579-589.
    • (1990) Cell , vol.61 , pp. 579-589
    • Heald, R.1    McKeon, F.2
  • 55
    • 0033525007 scopus 로고    scopus 로고
    • Requirement of Cdk2-cyclin E activity for repeated centrosome reproduction in Xenopus egg extracts
    • Hinchcliffe E.H., Li C., Thompson E.A., Maller J.L., Sluder G. Requirement of Cdk2-cyclin E activity for repeated centrosome reproduction in Xenopus egg extracts. Science 1999, 283:851-854.
    • (1999) Science , vol.283 , pp. 851-854
    • Hinchcliffe, E.H.1    Li, C.2    Thompson, E.A.3    Maller, J.L.4    Sluder, G.5
  • 56
    • 14844307019 scopus 로고    scopus 로고
    • The structure of cyclin E1/CDK2: implications for CDK2 activation and CDK2-independent roles
    • Honda R., Lowe E.D., Dubinina E., Skamnaki V., Cook A., Brown N.R., et al. The structure of cyclin E1/CDK2: implications for CDK2 activation and CDK2-independent roles. EMBO J 2005, 24:452-463.
    • (2005) EMBO J , vol.24 , pp. 452-463
    • Honda, R.1    Lowe, E.D.2    Dubinina, E.3    Skamnaki, V.4    Cook, A.5    Brown, N.R.6
  • 57
    • 33750032892 scopus 로고    scopus 로고
    • CDK2-dependent phosphorylation of FOXO1 as an apoptotic response to DNA damage
    • Huang H., Regan K.M., Lou Z., Chen J., Tindall D.J. CDK2-dependent phosphorylation of FOXO1 as an apoptotic response to DNA damage. Science 2006, 314:294-297.
    • (2006) Science , vol.314 , pp. 294-297
    • Huang, H.1    Regan, K.M.2    Lou, Z.3    Chen, J.4    Tindall, D.J.5
  • 58
    • 2942744850 scopus 로고    scopus 로고
    • Phosphorylation regulates the dynamic interaction of RCC1 with chromosomes during mitosis
    • Hutchins J.R., Moore W.J., Hood F.E., Wilson J.S., Andrews P.D., Swedlow J.R., et al. Phosphorylation regulates the dynamic interaction of RCC1 with chromosomes during mitosis. Curr Biol 2004, 14:1099-1104.
    • (2004) Curr Biol , vol.14 , pp. 1099-1104
    • Hutchins, J.R.1    Moore, W.J.2    Hood, F.E.3    Wilson, J.S.4    Andrews, P.D.5    Swedlow, J.R.6
  • 59
    • 4344654668 scopus 로고    scopus 로고
    • Cdc28/Cdk1 regulates spindle pole body duplication through phosphorylation of Spc42 and Mps1
    • Jaspersen S.L., Huneycutt B.J., Giddings T.H., Resing K.A., Ahn N.G., Winey M. Cdc28/Cdk1 regulates spindle pole body duplication through phosphorylation of Spc42 and Mps1. Dev Cell 2004, 7:263-274.
    • (2004) Dev Cell , vol.7 , pp. 263-274
    • Jaspersen, S.L.1    Huneycutt, B.J.2    Giddings, T.H.3    Resing, K.A.4    Ahn, N.G.5    Winey, M.6
  • 60
    • 67650638697 scopus 로고    scopus 로고
    • Cyclin A is redundant in fibroblasts but essential in hematopoietic and embryonic stem cells
    • Kalaszczynska I., Geng Y., Iino T., Mizuno S., Choi Y., Kondratiuk I., et al. Cyclin A is redundant in fibroblasts but essential in hematopoietic and embryonic stem cells. Cell 2009, 138:352-365.
    • (2009) Cell , vol.138 , pp. 352-365
    • Kalaszczynska, I.1    Geng, Y.2    Iino, T.3    Mizuno, S.4    Choi, Y.5    Kondratiuk, I.6
  • 61
    • 0031974956 scopus 로고    scopus 로고
    • Cdc2-mediated phosphorylation of the gap junction protein, connexin43, during mitosis
    • Kanemitsu M.Y., Jiang W., Eckhart W. Cdc2-mediated phosphorylation of the gap junction protein, connexin43, during mitosis. Cell Growth Differ 1998, 9:13-21.
    • (1998) Cell Growth Differ , vol.9 , pp. 13-21
    • Kanemitsu, M.Y.1    Jiang, W.2    Eckhart, W.3
  • 62
    • 0032538511 scopus 로고    scopus 로고
    • Phosphorylation and activation of 13S condensin by Cdc2 in vitro
    • Kimura K., Hirano M., Kobayashi R., Hirano T. Phosphorylation and activation of 13S condensin by Cdc2 in vitro. Science 1998, 282:487-490.
    • (1998) Science , vol.282 , pp. 487-490
    • Kimura, K.1    Hirano, M.2    Kobayashi, R.3    Hirano, T.4
  • 63
    • 0032935671 scopus 로고    scopus 로고
    • Cdk1- and cdk2-mediated phosphorylation of MyoD Ser200 in growing C2 myoblasts: role in modulating MyoD half-life and myogenic activity
    • Kitzmann M., Vandromme M., Schaeffer V., Carnac G., Labbe J.C., Lamb N., et al. cdk1- and cdk2-mediated phosphorylation of MyoD Ser200 in growing C2 myoblasts: role in modulating MyoD half-life and myogenic activity. Mol Cell Biol 1999, 19:3167-3176.
    • (1999) Mol Cell Biol , vol.19 , pp. 3167-3176
    • Kitzmann, M.1    Vandromme, M.2    Schaeffer, V.3    Carnac, G.4    Labbe, J.C.5    Lamb, N.6
  • 64
    • 0025734356 scopus 로고
    • Human cyclin E, a new cyclin that interacts with two members of the CDC2 gene family
    • Koff A., Cross F., Fisher A., Schumacher J., Leguellec K., Philippe M., et al. Human cyclin E, a new cyclin that interacts with two members of the CDC2 gene family. Cell 1991, 66:1217-1228.
    • (1991) Cell , vol.66 , pp. 1217-1228
    • Koff, A.1    Cross, F.2    Fisher, A.3    Schumacher, J.4    Leguellec, K.5    Philippe, M.6
  • 65
    • 0036282745 scopus 로고    scopus 로고
    • Cdc2 phosphorylation of BAD links the cell cycle to the cell death machinery
    • Konishi Y., Lehtinen M., Donovan N., Bonni A. Cdc2 phosphorylation of BAD links the cell cycle to the cell death machinery. Mol Cell 2002, 9:1005-1016.
    • (2002) Mol Cell , vol.9 , pp. 1005-1016
    • Konishi, Y.1    Lehtinen, M.2    Donovan, N.3    Bonni, A.4
  • 66
    • 47049128024 scopus 로고    scopus 로고
    • Phosphorylation of threonine 61 by cyclin a/Cdk1 triggers degradation of stem-loop binding protein at the end of S phase
    • Koseoglu M.M., Graves L.M., Marzluff W.F. Phosphorylation of threonine 61 by cyclin a/Cdk1 triggers degradation of stem-loop binding protein at the end of S phase. Mol Cell Biol 2008, 28:4469-4479.
    • (2008) Mol Cell Biol , vol.28 , pp. 4469-4479
    • Koseoglu, M.M.1    Graves, L.M.2    Marzluff, W.F.3
  • 67
    • 0026847260 scopus 로고
    • Cell cycle regulation of vertebrate p34cdc2 activity: identification of Thr161 as an essential in vivo phosphorylation site
    • Krek W., Nigg E.A. Cell cycle regulation of vertebrate p34cdc2 activity: identification of Thr161 as an essential in vivo phosphorylation site. New Biol 1992, 4:323-329.
    • (1992) New Biol , vol.4 , pp. 323-329
    • Krek, W.1    Nigg, E.A.2
  • 68
    • 0027244958 scopus 로고
    • Cdc2 kinase phosphorylation of desmin at three serine/threonine residues in the amino-terminal head domain
    • Kusubata M., Matsuoka Y., Tsujimura K., Ito H., Ando S., Kamijo M., et al. cdc2 kinase phosphorylation of desmin at three serine/threonine residues in the amino-terminal head domain. Biochem Biophys Res Commun 1993, 190:927-934.
    • (1993) Biochem Biophys Res Commun , vol.190 , pp. 927-934
    • Kusubata, M.1    Matsuoka, Y.2    Tsujimura, K.3    Ito, H.4    Ando, S.5    Kamijo, M.6
  • 69
    • 0025869168 scopus 로고
    • Cloning by differential screening of a Xenopus cDNA that encodes a kinesin-related protein
    • Le Guellec R., Paris J., Couturier A., Roghi C., Philippe M. Cloning by differential screening of a Xenopus cDNA that encodes a kinesin-related protein. Mol Cell Biol 1991, 11:3395-3398.
    • (1991) Mol Cell Biol , vol.11 , pp. 3395-3398
    • Le Guellec, R.1    Paris, J.2    Couturier, A.3    Roghi, C.4    Philippe, M.5
  • 70
    • 0026039676 scopus 로고
    • The retinoblastoma protein is phosphorylated on multiple sites by human cdc2
    • Lees J.A., Buchkovich K.J., Marshak D.R., Anderson C.W., Harlow E. The retinoblastoma protein is phosphorylated on multiple sites by human cdc2. EMBO J 1991, 10:4279-4290.
    • (1991) EMBO J , vol.10 , pp. 4279-4290
    • Lees, J.A.1    Buchkovich, K.J.2    Marshak, D.R.3    Anderson, C.W.4    Harlow, E.5
  • 71
    • 0025850767 scopus 로고
    • Isolation of three novel human cyclins by rescue of G1 cyclin (Cln) function in yeast
    • Lew D.J., Dulic V., Reed S.I. Isolation of three novel human cyclins by rescue of G1 cyclin (Cln) function in yeast. Cell 1991, 66:1197-1206.
    • (1991) Cell , vol.66 , pp. 1197-1206
    • Lew, D.J.1    Dulic, V.2    Reed, S.I.3
  • 72
    • 33646468623 scopus 로고    scopus 로고
    • Phosphorylation of the Pro-X-Thr-Pro site in phosphatase inhibitor-2 by cyclin-dependent protein kinase during M-phase of the cell cycle
    • Li M., Stefansson B., Wang W., Schaefer E.M., Brautigan D.L. Phosphorylation of the Pro-X-Thr-Pro site in phosphatase inhibitor-2 by cyclin-dependent protein kinase during M-phase of the cell cycle. Cell Signal 2006, 18:1318-1326.
    • (2006) Cell Signal , vol.18 , pp. 1318-1326
    • Li, M.1    Stefansson, B.2    Wang, W.3    Schaefer, E.M.4    Brautigan, D.L.5
  • 73
    • 0037459058 scopus 로고    scopus 로고
    • Asymmetric loading of Kar9 onto spindle poles and microtubules ensures proper spindle alignment
    • Liakopoulos D., Kusch J., Grava S., Vogel J., Barral Y. Asymmetric loading of Kar9 onto spindle poles and microtubules ensures proper spindle alignment. Cell 2003, 112:561-574.
    • (2003) Cell , vol.112 , pp. 561-574
    • Liakopoulos, D.1    Kusch, J.2    Grava, S.3    Vogel, J.4    Barral, Y.5
  • 74
    • 0033740931 scopus 로고    scopus 로고
    • Peripheral Golgi protein GRASP65 is a target of mitotic polo-like kinase (Plk) and Cdc2
    • Lin C.Y., Madsen M.L., Yarm F.R., Jang Y.J., Liu X., Erikson R.L. Peripheral Golgi protein GRASP65 is a target of mitotic polo-like kinase (Plk) and Cdc2. Proc Natl Acad Sci U S A 2000, 97:12589-12594.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 12589-12594
    • Lin, C.Y.1    Madsen, M.L.2    Yarm, F.R.3    Jang, Y.J.4    Liu, X.5    Erikson, R.L.6
  • 75
    • 2342449334 scopus 로고    scopus 로고
    • Mitotic phosphorylation of the peripheral Golgi protein Nir2 by Cdk1 provides a docking mechanism for Plk1 and affects cytokinesis completion
    • Litvak V., Argov R., Dahan N., Ramachandran S., Amarilio R., Shainskaya A., et al. Mitotic phosphorylation of the peripheral Golgi protein Nir2 by Cdk1 provides a docking mechanism for Plk1 and affects cytokinesis completion. Mol Cell 2004, 14:319-330.
    • (2004) Mol Cell , vol.14 , pp. 319-330
    • Litvak, V.1    Argov, R.2    Dahan, N.3    Ramachandran, S.4    Amarilio, R.5    Shainskaya, A.6
  • 76
    • 0026762801 scopus 로고
    • Dephosphorylation of cdc2 on threonine 161 is required for cdc2 kinase inactivation and normal anaphase
    • Lorca T., Labbe J.C., Devault A., Fesquet D., Capony J.P., Cavadore J.C., et al. Dephosphorylation of cdc2 on threonine 161 is required for cdc2 kinase inactivation and normal anaphase. EMBO J 1992, 11:2381-2390.
    • (1992) EMBO J , vol.11 , pp. 2381-2390
    • Lorca, T.1    Labbe, J.C.2    Devault, A.3    Fesquet, D.4    Capony, J.P.5    Cavadore, J.C.6
  • 77
    • 0032544440 scopus 로고    scopus 로고
    • Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis
    • Lowe M., Rabouille C., Nakamura N., Watson R., Jackman M., Jamsa E., et al. Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis. Cell 1998, 94:783-793.
    • (1998) Cell , vol.94 , pp. 783-793
    • Lowe, M.1    Rabouille, C.2    Nakamura, N.3    Watson, R.4    Jackman, M.5    Jamsa, E.6
  • 78
    • 0031951182 scopus 로고    scopus 로고
    • Functional inactivation of the retinoblastoma protein requires sequential modification by at least two distinct cyclin-cdk complexes
    • Lundberg A.S., Weinberg R.A. Functional inactivation of the retinoblastoma protein requires sequential modification by at least two distinct cyclin-cdk complexes. Mol Cell Biol 1998, 18:753-761.
    • (1998) Mol Cell Biol , vol.18 , pp. 753-761
    • Lundberg, A.S.1    Weinberg, R.A.2
  • 79
    • 33644882481 scopus 로고    scopus 로고
    • Regulation of the transcription factor FOXM1c by Cyclin E/CDK2
    • Luscher-Firzlaff J.M., Lilischkis R., Luscher B. Regulation of the transcription factor FOXM1c by Cyclin E/CDK2. FEBS Lett 2006, 580:1716-1722.
    • (2006) FEBS Lett , vol.580 , pp. 1716-1722
    • Luscher-Firzlaff, J.M.1    Lilischkis, R.2    Luscher, B.3
  • 80
    • 0034665635 scopus 로고    scopus 로고
    • Cell cycle-regulated phosphorylation of p220(NPAT) by cyclin E/Cdk2 in Cajal bodies promotes histone gene transcription
    • Ma T., Van Tine B.A., Wei Y., Garrett M.D., Nelson D., Adams P.D., et al. Cell cycle-regulated phosphorylation of p220(NPAT) by cyclin E/Cdk2 in Cajal bodies promotes histone gene transcription. Genes Dev 2000, 14:2298-2313.
    • (2000) Genes Dev , vol.14 , pp. 2298-2313
    • Ma, T.1    Van Tine, B.A.2    Wei, Y.3    Garrett, M.D.4    Nelson, D.5    Adams, P.D.6
  • 81
    • 0025919760 scopus 로고
    • Phosphorylation of caldesmon by p34cdc2 kinase. Identification of phosphorylation sites
    • Mak A.S., Carpenter M., Smillie L.B., Wang J.H. Phosphorylation of caldesmon by p34cdc2 kinase. Identification of phosphorylation sites. J Biol Chem 1991, 266:19971-19975.
    • (1991) J Biol Chem , vol.266 , pp. 19971-19975
    • Mak, A.S.1    Carpenter, M.2    Smillie, L.B.3    Wang, J.H.4
  • 82
    • 0033564223 scopus 로고    scopus 로고
    • Phosphorylation of the myristoylated protein kinase C substrate MARCKS by the cyclin E-cyclin-dependent kinase 2 complex in vitro
    • Manenti S., Yamauchi E., Sorokine O., Knibiehler M., Van Dorsselaer A., Taniguchi H., et al. Phosphorylation of the myristoylated protein kinase C substrate MARCKS by the cyclin E-cyclin-dependent kinase 2 complex in vitro. Biochem J 1999, 340(Pt 3):775-782.
    • (1999) Biochem J , vol.340 , Issue.PART 3 , pp. 775-782
    • Manenti, S.1    Yamauchi, E.2    Sorokine, O.3    Knibiehler, M.4    Van Dorsselaer, A.5    Taniguchi, H.6
  • 83
    • 21744462069 scopus 로고    scopus 로고
    • The Ski oncoprotein is upregulated and localized at the centrosomes and mitotic spindle during mitosis
    • Marcelain K., Hayman M.J. The Ski oncoprotein is upregulated and localized at the centrosomes and mitotic spindle during mitosis. Oncogene 2005, 24:4321-4329.
    • (2005) Oncogene , vol.24 , pp. 4321-4329
    • Marcelain, K.1    Hayman, M.J.2
  • 84
    • 0242389822 scopus 로고    scopus 로고
    • PP1 control of M phase entry exerted through 14-3-3-regulated Cdc25 dephosphorylation
    • Margolis S.S., Walsh S., Weiser D.C., Yoshida M., Shenolikar S., Kornbluth S. PP1 control of M phase entry exerted through 14-3-3-regulated Cdc25 dephosphorylation. EMBO J 2003, 22:5734-5745.
    • (2003) EMBO J , vol.22 , pp. 5734-5745
    • Margolis, S.S.1    Walsh, S.2    Weiser, D.C.3    Yoshida, M.4    Shenolikar, S.5    Kornbluth, S.6
  • 85
    • 0028146122 scopus 로고
    • Serine 16 of oncoprotein 18 is a major cytosolic target for the Ca2+/calmodulin-dependent kinase-Gr
    • Marklund U., Larsson N., Brattsand G., Osterman O., Chatila T.A., Gullberg M. Serine 16 of oncoprotein 18 is a major cytosolic target for the Ca2+/calmodulin-dependent kinase-Gr. Eur J Biochem 1994, 225:53-60.
    • (1994) Eur J Biochem , vol.225 , pp. 53-60
    • Marklund, U.1    Larsson, N.2    Brattsand, G.3    Osterman, O.4    Chatila, T.A.5    Gullberg, M.6
  • 86
    • 0034666016 scopus 로고    scopus 로고
    • Human Cdc7-related kinase complex. In vitro phosphorylation of MCM by concerted actions of Cdks and Cdc7 and that of a criticial threonine residue of Cdc7 bY Cdks
    • Masai H., Matsui E., You Z., Ishimi Y., Tamai K., Arai K. Human Cdc7-related kinase complex. In vitro phosphorylation of MCM by concerted actions of Cdks and Cdc7 and that of a criticial threonine residue of Cdc7 bY Cdks. J Biol Chem 2000, 275:29042-29052.
    • (2000) J Biol Chem , vol.275 , pp. 29042-29052
    • Masai, H.1    Matsui, E.2    You, Z.3    Ishimi, Y.4    Tamai, K.5    Arai, K.6
  • 88
    • 0024470772 scopus 로고
    • Cyclin is a component of the sea urchin egg M-phase specific histone H1 kinase
    • Meijer L., Arion D., Golsteyn R., Pines J., Brizuela L., Hunt T., et al. Cyclin is a component of the sea urchin egg M-phase specific histone H1 kinase. EMBO J 1989, 8:2275-2282.
    • (1989) EMBO J , vol.8 , pp. 2275-2282
    • Meijer, L.1    Arion, D.2    Golsteyn, R.3    Pines, J.4    Brizuela, L.5    Hunt, T.6
  • 90
    • 0027427603 scopus 로고
    • Phosphorylation of dystrophin. The carboxyl-terminal region of dystrophin is a substrate for in vitro phosphorylation by p34cdc2 protein kinase
    • Milner R.E., Busaan J.L., Holmes C.F., Wang J.H., Michalak M. Phosphorylation of dystrophin. The carboxyl-terminal region of dystrophin is a substrate for in vitro phosphorylation by p34cdc2 protein kinase. J Biol Chem 1993, 268:21901-21905.
    • (1993) J Biol Chem , vol.268 , pp. 21901-21905
    • Milner, R.E.1    Busaan, J.L.2    Holmes, C.F.3    Wang, J.H.4    Michalak, M.5
  • 93
    • 0035798672 scopus 로고    scopus 로고
    • Cyclin A-dependent phosphorylation of the ETS-related protein, MEF, restricts its activity to the G1 phase of the cell cycle
    • Miyazaki Y., Boccuni P., Mao S., Zhang J., Erdjument-Bromage H., Tempst P., et al. Cyclin A-dependent phosphorylation of the ETS-related protein, MEF, restricts its activity to the G1 phase of the cell cycle. J Biol Chem 2001, 276:40528-40536.
    • (2001) J Biol Chem , vol.276 , pp. 40528-40536
    • Miyazaki, Y.1    Boccuni, P.2    Mao, S.3    Zhang, J.4    Erdjument-Bromage, H.5    Tempst, P.6
  • 94
    • 33847782587 scopus 로고    scopus 로고
    • Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry
    • Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A 2007, 104:2199-2204.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 2199-2204
    • Molina, H.1    Horn, D.M.2    Tang, N.3    Mathivanan, S.4    Pandey, A.5
  • 95
    • 0025764782 scopus 로고
    • The role of phosphorylation and the CDC28 protein kinase in cell cycle-regulated nuclear import of the S. cerevisiae transcription factor SWI5
    • Moll T., Tebb G., Surana U., Robitsch H., Nasmyth K. The role of phosphorylation and the CDC28 protein kinase in cell cycle-regulated nuclear import of the S. cerevisiae transcription factor SWI5. Cell 1991, 66:743-758.
    • (1991) Cell , vol.66 , pp. 743-758
    • Moll, T.1    Tebb, G.2    Surana, U.3    Robitsch, H.4    Nasmyth, K.5
  • 97
    • 0037655970 scopus 로고    scopus 로고
    • Unmasking the S-phase-promoting potential of cyclin B1
    • Moore J.D., Kirk J.A., Hunt T. Unmasking the S-phase-promoting potential of cyclin B1. Science 2003, 300:987-990.
    • (2003) Science , vol.300 , pp. 987-990
    • Moore, J.D.1    Kirk, J.A.2    Hunt, T.3
  • 98
    • 0031466305 scopus 로고    scopus 로고
    • Cyclin-dependent kinases: engines, clocks, and microprocessors
    • Morgan D.O. Cyclin-dependent kinases: engines, clocks, and microprocessors. Annu Rev Cell Dev Biol 1997, 13:261-291.
    • (1997) Annu Rev Cell Dev Biol , vol.13 , pp. 261-291
    • Morgan, D.O.1
  • 99
    • 33845796538 scopus 로고    scopus 로고
    • NDEL1 phosphorylation by Aurora-A kinase is essential for centrosomal maturation, separation, and TACC3 recruitment
    • Mori D., Yano Y., Toyo-oka K., Yoshida N., Yamada M., Muramatsu M., et al. NDEL1 phosphorylation by Aurora-A kinase is essential for centrosomal maturation, separation, and TACC3 recruitment. Mol Cell Biol 2007, 27:352-367.
    • (2007) Mol Cell Biol , vol.27 , pp. 352-367
    • Mori, D.1    Yano, Y.2    Toyo-oka, K.3    Yoshida, N.4    Yamada, M.5    Muramatsu, M.6
  • 100
    • 18644380521 scopus 로고    scopus 로고
    • WARTS tumor suppressor is phosphorylated by Cdc2/cyclin B at spindle poles during mitosis
    • Morisaki T., Hirota T., Iida S., Marumoto T., Hara T., Nishiyama Y., et al. WARTS tumor suppressor is phosphorylated by Cdc2/cyclin B at spindle poles during mitosis. FEBS Lett 2002, 529:319-324.
    • (2002) FEBS Lett , vol.529 , pp. 319-324
    • Morisaki, T.1    Hirota, T.2    Iida, S.3    Marumoto, T.4    Hara, T.5    Nishiyama, Y.6
  • 102
    • 34447527882 scopus 로고    scopus 로고
    • Clustering of phosphorylation site recognition motifs can be exploited to predict the targets of cyclin-dependent kinase
    • Moses A.M., Heriche J.K., Durbin R. Clustering of phosphorylation site recognition motifs can be exploited to predict the targets of cyclin-dependent kinase. Genome Biol 2007, 8:R23.
    • (2007) Genome Biol , vol.8
    • Moses, A.M.1    Heriche, J.K.2    Durbin, R.3
  • 103
    • 0030614383 scopus 로고    scopus 로고
    • Ca2+-calmodulin binding to mouse alpha1 syntrophin: syntrophin is also a Ca2+-binding protein
    • Newbell B.J., Anderson J.T., Jarrett H.W. Ca2+-calmodulin binding to mouse alpha1 syntrophin: syntrophin is also a Ca2+-binding protein. Biochemistry 1997, 36:1295-1305.
    • (1997) Biochemistry , vol.36 , pp. 1295-1305
    • Newbell, B.J.1    Anderson, J.T.2    Jarrett, H.W.3
  • 104
    • 0037073704 scopus 로고    scopus 로고
    • AGAP1, an endosome-associated, phosphoinositide-dependent ADP-ribosylation factor GTPase-activating protein that affects actin cytoskeleton
    • Nie Z., Stanley K.T., Stauffer S., Jacques K.M., Hirsch D.S., Takei J., et al. AGAP1, an endosome-associated, phosphoinositide-dependent ADP-ribosylation factor GTPase-activating protein that affects actin cytoskeleton. J Biol Chem 2002, 277:48965-48975.
    • (2002) J Biol Chem , vol.277 , pp. 48965-48975
    • Nie, Z.1    Stanley, K.T.2    Stauffer, S.3    Jacques, K.M.4    Hirsch, D.S.5    Takei, J.6
  • 105
    • 0025724096 scopus 로고
    • Phosphorylation by cdc2 kinase modulates DNA binding activity of high mobility group I nonhistone chromatin protein
    • Nissen M.S., Langan T.A., Reeves R. Phosphorylation by cdc2 kinase modulates DNA binding activity of high mobility group I nonhistone chromatin protein. J Biol Chem 1991, 266:19945-19952.
    • (1991) J Biol Chem , vol.266 , pp. 19945-19952
    • Nissen, M.S.1    Langan, T.A.2    Reeves, R.3
  • 106
    • 0037006806 scopus 로고    scopus 로고
    • CDK phosphorylation of Drc1 regulates DNA replication in fission yeast
    • Noguchi E., Shanahan P., Noguchi C., Russell P. CDK phosphorylation of Drc1 regulates DNA replication in fission yeast. Curr Biol 2002, 12:599-605.
    • (2002) Curr Biol , vol.12 , pp. 599-605
    • Noguchi, E.1    Shanahan, P.2    Noguchi, C.3    Russell, P.4
  • 109
    • 0038185196 scopus 로고    scopus 로고
    • Cdc2-mediated phosphorylation of Kid controls its distribution to spindle and chromosomes
    • Ohsugi M., Tokai-Nishizumi N., Shiroguchi K., Toyoshima Y.Y., Inoue J., Yamamoto T. Cdc2-mediated phosphorylation of Kid controls its distribution to spindle and chromosomes. EMBO J 2003, 22:2091-2103.
    • (2003) EMBO J , vol.22 , pp. 2091-2103
    • Ohsugi, M.1    Tokai-Nishizumi, N.2    Shiroguchi, K.3    Toyoshima, Y.Y.4    Inoue, J.5    Yamamoto, T.6
  • 110
  • 111
    • 0034730321 scopus 로고    scopus 로고
    • Nucleophosmin/B23 is a target of CDK2/cyclin E in centrosome duplication
    • Okuda M., Horn H.F., Tarapore P., Tokuyama Y., Smulian A.G., Chan P.K., et al. Nucleophosmin/B23 is a target of CDK2/cyclin E in centrosome duplication. Cell 2000, 103:127-140.
    • (2000) Cell , vol.103 , pp. 127-140
    • Okuda, M.1    Horn, H.F.2    Tarapore, P.3    Tokuyama, Y.4    Smulian, A.G.5    Chan, P.K.6
  • 112
    • 0035006828 scopus 로고    scopus 로고
    • Molecular cloning of a mammalian nuclear phosphoprotein NUCKS, which serves as a substrate for Cdk1 in vivo
    • Ostvold A.C., Norum J.H., Mathiesen S., Wanvik B., Sefland I., Grundt K. Molecular cloning of a mammalian nuclear phosphoprotein NUCKS, which serves as a substrate for Cdk1 in vivo. Eur J Biochem 2001, 268:2430-2440.
    • (2001) Eur J Biochem , vol.268 , pp. 2430-2440
    • Ostvold, A.C.1    Norum, J.H.2    Mathiesen, S.3    Wanvik, B.4    Sefland, I.5    Grundt, K.6
  • 113
    • 0026583746 scopus 로고
    • Cyclin A is required at two points in the human cell cycle
    • Pagano M., Pepperkok R., Verde F., Ansorge W., Draetta G. Cyclin A is required at two points in the human cell cycle. EMBO J 1992, 11:961-971.
    • (1992) EMBO J , vol.11 , pp. 961-971
    • Pagano, M.1    Pepperkok, R.2    Verde, F.3    Ansorge, W.4    Draetta, G.5
  • 114
    • 0027207334 scopus 로고
    • A- and B-type cyclins differentially modulate substrate specificity of cyclin-cdk complexes
    • Peeper D.S., Parker L.L., Ewen M.E., Toebes M., Hall F.L., Xu M., et al. A- and B-type cyclins differentially modulate substrate specificity of cyclin-cdk complexes. EMBO J 1993, 12:1947-1954.
    • (1993) EMBO J , vol.12 , pp. 1947-1954
    • Peeper, D.S.1    Parker, L.L.2    Ewen, M.E.3    Toebes, M.4    Hall, F.L.5    Xu, M.6
  • 115
    • 0025736038 scopus 로고
    • Disassembly of in vitro formed lamin head-to-tail polymers by CDC2 kinase
    • Peter M., Heitlinger E., Haner M., Aebi U., Nigg E.A. Disassembly of in vitro formed lamin head-to-tail polymers by CDC2 kinase. EMBO J 1991, 10:1535-1544.
    • (1991) EMBO J , vol.10 , pp. 1535-1544
    • Peter, M.1    Heitlinger, E.2    Haner, M.3    Aebi, U.4    Nigg, E.A.5
  • 116
    • 0025370462 scopus 로고
    • In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase
    • Peter M., Nakagawa J., Doree M., Labbe J.C., Nigg E.A. In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase. Cell 1990, 61:591-602.
    • (1990) Cell , vol.61 , pp. 591-602
    • Peter, M.1    Nakagawa, J.2    Doree, M.3    Labbe, J.C.4    Nigg, E.A.5
  • 117
    • 0033556238 scopus 로고    scopus 로고
    • Phosphorylation of mammalian CDC6 by cyclin A/CDK2 regulates its subcellular localization
    • Petersen B.O., Lukas J., Sorensen C.S., Bartek J., Helin K. Phosphorylation of mammalian CDC6 by cyclin A/CDK2 regulates its subcellular localization. EMBO J 1999, 18:396-410.
    • (1999) EMBO J , vol.18 , pp. 396-410
    • Petersen, B.O.1    Lukas, J.2    Sorensen, C.S.3    Bartek, J.4    Helin, K.5
  • 118
    • 0027933911 scopus 로고
    • The differential localization of human cyclins A and B is due to a cytoplasmic retention signal in cyclin B
    • Pines J., Hunter T. The differential localization of human cyclins A and B is due to a cytoplasmic retention signal in cyclin B. EMBO J 1994, 13:3772-3781.
    • (1994) EMBO J , vol.13 , pp. 3772-3781
    • Pines, J.1    Hunter, T.2
  • 119
    • 33646507278 scopus 로고    scopus 로고
    • Downregulation of PP2A(Cdc55) phosphatase by separase initiates mitotic exit in budding yeast
    • Queralt E., Lehane C., Novak B., Uhlmann F. Downregulation of PP2A(Cdc55) phosphatase by separase initiates mitotic exit in budding yeast. Cell 2006, 125:719-732.
    • (2006) Cell , vol.125 , pp. 719-732
    • Queralt, E.1    Lehane, C.2    Novak, B.3    Uhlmann, F.4
  • 120
    • 70549085855 scopus 로고    scopus 로고
    • Eukaryotic DNA replication control: lock and load, then fire
    • Remus D., Diffley J.F. Eukaryotic DNA replication control: lock and load, then fire. Curr Opin Cell Biol 2009.
    • (2009) Curr Opin Cell Biol
    • Remus, D.1    Diffley, J.F.2
  • 121
    • 0030754045 scopus 로고    scopus 로고
    • Purification and reconstitution of cyclin-dependent kinase 2 in four states of activity
    • Russo A.A. Purification and reconstitution of cyclin-dependent kinase 2 in four states of activity. Meth Enzymol 1997, 283:3-12.
    • (1997) Meth Enzymol , vol.283 , pp. 3-12
    • Russo, A.A.1
  • 122
    • 0037090823 scopus 로고    scopus 로고
    • Regulation of the ubiquitin-conjugating enzyme hHR6A by CDK-mediated phosphorylation
    • Sarcevic B., Mawson A., Baker R.T., Sutherland R.L. Regulation of the ubiquitin-conjugating enzyme hHR6A by CDK-mediated phosphorylation. EMBO J 2002, 21:2009-2018.
    • (2002) EMBO J , vol.21 , pp. 2009-2018
    • Sarcevic, B.1    Mawson, A.2    Baker, R.T.3    Sutherland, R.L.4
  • 123
    • 0026648333 scopus 로고
    • Phosphorylation of myosin-II regulatory light chain by cyclin-p34cdc2: a mechanism for the timing of cytokinesis
    • Satterwhite L.L., Lohka M.J., Wilson K.L., Scherson T.Y., Cisek L.J., Corden J.L., et al. Phosphorylation of myosin-II regulatory light chain by cyclin-p34cdc2: a mechanism for the timing of cytokinesis. J Cell Biol 1992, 118:595-605.
    • (1992) J Cell Biol , vol.118 , pp. 595-605
    • Satterwhite, L.L.1    Lohka, M.J.2    Wilson, K.L.3    Scherson, T.Y.4    Cisek, L.J.5    Corden, J.L.6
  • 124
    • 0032569780 scopus 로고    scopus 로고
    • The cell-cycle regulated transcription factor B-Myb is phosphorylated by cyclin A/Cdk2 at sites that enhance its transactivation properties
    • Saville M.K., Watson R.J. The cell-cycle regulated transcription factor B-Myb is phosphorylated by cyclin A/Cdk2 at sites that enhance its transactivation properties. Oncogene 1998, 17:2679-2689.
    • (1998) Oncogene , vol.17 , pp. 2679-2689
    • Saville, M.K.1    Watson, R.J.2
  • 126
    • 0033564697 scopus 로고    scopus 로고
    • CDK inhibitors: positive and negative regulators of G1-phase progression
    • Sherr C.J., Roberts J.M. CDK inhibitors: positive and negative regulators of G1-phase progression. Genes Dev 1999, 13:1501-1512.
    • (1999) Genes Dev , vol.13 , pp. 1501-1512
    • Sherr, C.J.1    Roberts, J.M.2
  • 127
    • 0036441193 scopus 로고    scopus 로고
    • Golgi architecture and inheritance
    • Shorter J., Warren G. Golgi architecture and inheritance. Annu Rev Cell Dev Biol 2002, 18:379-420.
    • (2002) Annu Rev Cell Dev Biol , vol.18 , pp. 379-420
    • Shorter, J.1    Warren, G.2
  • 128
    • 4344714027 scopus 로고    scopus 로고
    • Cell cycle-dependent phosphorylation of C/EBPbeta mediates oncogenic cooperativity between C/EBPbeta and H-RasV12
    • Shuman J.D., Sebastian T., Kaldis P., Copeland T.D., Zhu S., Smart R.C., et al. Cell cycle-dependent phosphorylation of C/EBPbeta mediates oncogenic cooperativity between C/EBPbeta and H-RasV12. Mol Cell Biol 2004, 24:7380-7391.
    • (2004) Mol Cell Biol , vol.24 , pp. 7380-7391
    • Shuman, J.D.1    Sebastian, T.2    Kaldis, P.3    Copeland, T.D.4    Zhu, S.5    Smart, R.C.6
  • 129
    • 37249063516 scopus 로고    scopus 로고
    • Redundant ubiquitin ligase activities regulate wee1 degradation and mitotic entry
    • Smith A., Simanski S., Fallahi M., Ayad N.G. Redundant ubiquitin ligase activities regulate wee1 degradation and mitotic entry. Cell Cycle 2007, 6:2795-2799.
    • (2007) Cell Cycle , vol.6 , pp. 2795-2799
    • Smith, A.1    Simanski, S.2    Fallahi, M.3    Ayad, N.G.4
  • 130
    • 0027007963 scopus 로고
    • Role of phosphorylation in p34cdc2 activation: identification of an activating kinase
    • Solomon M.J., Lee T., Kirschner M.W. Role of phosphorylation in p34cdc2 activation: identification of an activating kinase. Mol Biol Cell 1992, 3:13-27.
    • (1992) Mol Biol Cell , vol.3 , pp. 13-27
    • Solomon, M.J.1    Lee, T.2    Kirschner, M.W.3
  • 132
    • 0037698170 scopus 로고    scopus 로고
    • A role for the phosphorylation of hRad9 in checkpoint signaling
    • St Onge R.P., Besley B.D., Pelley J.L., Davey S. A role for the phosphorylation of hRad9 in checkpoint signaling. J Biol Chem 2003, 278:26620-26628.
    • (2003) J Biol Chem , vol.278 , pp. 26620-26628
    • St Onge, R.P.1    Besley, B.D.2    Pelley, J.L.3    Davey, S.4
  • 134
    • 0035910422 scopus 로고    scopus 로고
    • A bipartite substrate recognition motif for cyclin-dependent kinases
    • Takeda D.Y., Wohlschlegel J.A., Dutta A. A bipartite substrate recognition motif for cyclin-dependent kinases. J Biol Chem 2001, 276:1993-1997.
    • (2001) J Biol Chem , vol.276 , pp. 1993-1997
    • Takeda, D.Y.1    Wohlschlegel, J.A.2    Dutta, A.3
  • 136
    • 0035877719 scopus 로고    scopus 로고
    • Specific phosphorylation of nucleophosmin on Thr(199) by cyclin-dependent kinase 2-cyclin E and its role in centrosome duplication
    • Tokuyama Y., Horn H.F., Kawamura K., Tarapore P., Fukasawa K. Specific phosphorylation of nucleophosmin on Thr(199) by cyclin-dependent kinase 2-cyclin E and its role in centrosome duplication. J Biol Chem 2001, 276:21529-21537.
    • (2001) J Biol Chem , vol.276 , pp. 21529-21537
    • Tokuyama, Y.1    Horn, H.F.2    Kawamura, K.3    Tarapore, P.4    Fukasawa, K.5
  • 137
    • 0030868950 scopus 로고    scopus 로고
    • Phosphorylation of the tumor suppressor adenomatous polyposis coli (APC) by the cyclin-dependent kinase p34
    • Trzepacz C., Lowy A.M., Kordich J.J., Groden J. Phosphorylation of the tumor suppressor adenomatous polyposis coli (APC) by the cyclin-dependent kinase p34. J Biol Chem 1997, 272:21681-21684.
    • (1997) J Biol Chem , vol.272 , pp. 21681-21684
    • Trzepacz, C.1    Lowy, A.M.2    Kordich, J.J.3    Groden, J.4
  • 138
    • 0025885070 scopus 로고
    • Isolation of the human cdk2 gene that encodes the cyclin A- and adenovirus E1A-associated p33 kinase
    • Tsai L.H., Harlow E., Meyerson M. Isolation of the human cdk2 gene that encodes the cyclin A- and adenovirus E1A-associated p33 kinase. Nature 1991, 353:174-177.
    • (1991) Nature , vol.353 , pp. 174-177
    • Tsai, L.H.1    Harlow, E.2    Meyerson, M.3
  • 141
    • 0026446550 scopus 로고
    • Reversible phosphorylation-dephosphorylation determines the localization of rab4 during the cell cycle
    • van der Sluijs P., Hull M., Huber L.A., Male P., Goud B., Mellman I. Reversible phosphorylation-dephosphorylation determines the localization of rab4 during the cell cycle. EMBO J 1992, 11:4379-4389.
    • (1992) EMBO J , vol.11 , pp. 4379-4389
    • van der Sluijs, P.1    Hull, M.2    Huber, L.A.3    Male, P.4    Goud, B.5    Mellman, I.6
  • 142
    • 0033118941 scopus 로고    scopus 로고
    • Phosphorylation by G1-specific cdk-cyclin complexes activates the nucleolar transcription factor UBF
    • Voit R., Hoffmann M., Grummt I. Phosphorylation by G1-specific cdk-cyclin complexes activates the nucleolar transcription factor UBF. EMBO J 1999, 18:1891-1899.
    • (1999) EMBO J , vol.18 , pp. 1891-1899
    • Voit, R.1    Hoffmann, M.2    Grummt, I.3
  • 143
    • 23844525856 scopus 로고    scopus 로고
    • Cyclin-dependent kinase (CDK) phosphorylation destabilizes somatic Wee1 via multiple pathways
    • Watanabe N., Arai H., Iwasaki J., Shiina M., Ogata K., Hunter T., et al. Cyclin-dependent kinase (CDK) phosphorylation destabilizes somatic Wee1 via multiple pathways. Proc Natl Acad Sci U S A 2005, 102:11663-11668.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 11663-11668
    • Watanabe, N.1    Arai, H.2    Iwasaki, J.3    Shiina, M.4    Ogata, K.5    Hunter, T.6
  • 144
    • 33747851970 scopus 로고    scopus 로고
    • Phospho-regulation of the Cdc14/Clp1 phosphatase delays late mitotic events in S. pombe
    • Wolfe B.A., McDonald W.H., Yates J.R., Gould K.L. Phospho-regulation of the Cdc14/Clp1 phosphatase delays late mitotic events in S. pombe. Dev Cell 2006, 11:423-430.
    • (2006) Dev Cell , vol.11 , pp. 423-430
    • Wolfe, B.A.1    McDonald, W.H.2    Yates, J.R.3    Gould, K.L.4
  • 145
    • 36349025888 scopus 로고    scopus 로고
    • Cdk1 phosphorylation of BubR1 controls spindle checkpoint arrest and Plk1-mediated formation of the 3F3/2 epitope
    • Wong O.K., Fang G. Cdk1 phosphorylation of BubR1 controls spindle checkpoint arrest and Plk1-mediated formation of the 3F3/2 epitope. J Cell Biol 2007, 179:611-617.
    • (2007) J Cell Biol , vol.179 , pp. 611-617
    • Wong, O.K.1    Fang, G.2
  • 146
    • 33845932302 scopus 로고    scopus 로고
    • Role of Hcn1 and its phosphorylation in fission yeast anaphase-promoting complex/cyclosome function
    • Yoon H.J., Feoktistova A., Chen J.S., Jennings J.L., Link A.J., Gould K.L. Role of Hcn1 and its phosphorylation in fission yeast anaphase-promoting complex/cyclosome function. J Biol Chem 2006, 281:32284-32293.
    • (2006) J Biol Chem , vol.281 , pp. 32284-32293
    • Yoon, H.J.1    Feoktistova, A.2    Chen, J.S.3    Jennings, J.L.4    Link, A.J.5    Gould, K.L.6
  • 147
    • 70249141638 scopus 로고    scopus 로고
    • Regulation of aurora B expression by the bromodomain protein Brd4
    • You J., Li Q., Wu C., Kim J., Ottinger M., Howley P.M. Regulation of aurora B expression by the bromodomain protein Brd4. Mol Cell Biol 2009, 29:5094-5103.
    • (2009) Mol Cell Biol , vol.29 , pp. 5094-5103
    • You, J.1    Li, Q.2    Wu, C.3    Kim, J.4    Ottinger, M.5    Howley, P.M.6
  • 148
    • 23944499922 scopus 로고    scopus 로고
    • An ECT2-centralspindlin complex regulates the localization and function of RhoA
    • Yuce O., Piekny A., Glotzer M. An ECT2-centralspindlin complex regulates the localization and function of RhoA. J Cell Biol 2005, 170:571-582.
    • (2005) J Cell Biol , vol.170 , pp. 571-582
    • Yuce, O.1    Piekny, A.2    Glotzer, M.3
  • 149
    • 0034630750 scopus 로고    scopus 로고
    • Phosphorylation of Cdc20/fizzy negatively regulates the mammalian cyclosome/APC in the mitotic checkpoint
    • Yudkovsky Y., Shteinberg M., Listovsky T., Brandeis M., Hershko A. Phosphorylation of Cdc20/fizzy negatively regulates the mammalian cyclosome/APC in the mitotic checkpoint. Biochem Biophys Res Commun 2000, 271:299-304.
    • (2000) Biochem Biophys Res Commun , vol.271 , pp. 299-304
    • Yudkovsky, Y.1    Shteinberg, M.2    Listovsky, T.3    Brandeis, M.4    Hershko, A.5
  • 150
    • 0141591674 scopus 로고    scopus 로고
    • Cdk2-dependent phosphorylation of the NF-Y transcription factor and its involvement in the p53-p21 signaling pathway
    • Yun J., Chae H.D., Choi T.S., Kim E.H., Bang Y.J., Chung J., et al. Cdk2-dependent phosphorylation of the NF-Y transcription factor and its involvement in the p53-p21 signaling pathway. J Biol Chem 2003, 278:36966-36972.
    • (2003) J Biol Chem , vol.278 , pp. 36966-36972
    • Yun, J.1    Chae, H.D.2    Choi, T.S.3    Kim, E.H.4    Bang, Y.J.5    Chung, J.6
  • 151
    • 0033567387 scopus 로고    scopus 로고
    • Whose end is destruction: cell division and the anaphase-promoting complex
    • Zachariae W., Nasmyth K. Whose end is destruction: cell division and the anaphase-promoting complex. Genes Dev 1999, 13:2039-2058.
    • (1999) Genes Dev , vol.13 , pp. 2039-2058
    • Zachariae, W.1    Nasmyth, K.2
  • 152
    • 0032520093 scopus 로고    scopus 로고
    • Expression of NPAT, a novel substrate of cyclin E-CDK2, promotes S-phase entry
    • Zhao J., Dynlacht B., Imai T., Hori T., Harlow E. Expression of NPAT, a novel substrate of cyclin E-CDK2, promotes S-phase entry. Genes Dev 1998, 12:456-461.
    • (1998) Genes Dev , vol.12 , pp. 456-461
    • Zhao, J.1    Dynlacht, B.2    Imai, T.3    Hori, T.4    Harlow, E.5
  • 153
    • 0033007105 scopus 로고    scopus 로고
    • Nucleolin, defective for MPF phosphorylation, localizes normally during mitosis and nucleologenesis
    • Zhu Y., Lu D., DiMario P. Nucleolin, defective for MPF phosphorylation, localizes normally during mitosis and nucleologenesis. Histochem Cell Biol 1999, 111:477-487.
    • (1999) Histochem Cell Biol , vol.111 , pp. 477-487
    • Zhu, Y.1    Lu, D.2    DiMario, P.3


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