메뉴 건너뛰기




Volumn 26, Issue 12, 2015, Pages 2205-2216

The Ubp15 deubiquitinase promotes timely entry into S phase in Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

ANAPHASE PROMOTING COMPLEX; CYCLINE; DEUBIQUITINASE; HYDROXYUREA; PROTEASOME; PROTEIN CLB5; PROTEIN UBP15; UNCLASSIFIED DRUG; CDH1 PROTEIN, S CEREVISIAE; CLB5 PROTEIN, S CEREVISIAE; CYCLIN B; FIZZY RELATED PROTEIN; PROTEINASE; SACCHAROMYCES CEREVISIAE PROTEIN; UBP15 PROTEIN, S CEREVISIAE;

EID: 84930913107     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E14-09-1400     Document Type: Article
Times cited : (15)

References (68)
  • 1
    • 9644268864 scopus 로고    scopus 로고
    • Mechanism and function of deubiquitinating enzymes
    • Amerik AY, Hochstrasser M. (2004). Mechanism and function of deubiquitinating enzymes. Biochim Biophys Acta 1695, 189-207.
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 189-207
    • Amerik, A.Y.1    Hochstrasser, M.2
  • 2
    • 0033783007 scopus 로고    scopus 로고
    • Analysis of the deubiquitinating enzymes of the yeast saccharomyces cerevisiae
    • Amerik AY, Li SJ, Hochstrasser M. (2000). Analysis of the deubiquitinating enzymes of the yeast Saccharomyces cerevisiae. Biol Chem 381, 981-992.
    • (2000) Biol Chem , vol.381 , pp. 981-992
    • Amerik, A.Y.1    Li, S.J.2    Hochstrasser, M.3
  • 3
    • 79960535289 scopus 로고    scopus 로고
    • Biochemical characterization of a multidomain deubiquitinating enzyme ubp15 and the regulatory role of its terminal domains
    • Bozza W.P., Zhuang Z. (2011). Biochemical characterization of a multidomain deubiquitinating enzyme Ubp15 and the regulatory role of its terminal domains. Biochemistry 50, 6423-6432.
    • (2011) Biochemistry , vol.50 , pp. 6423-6432
    • Bozza, W.P.1    Zhuang, Z.2
  • 4
    • 84869020017 scopus 로고    scopus 로고
    • betaTrCP)-mediated destruction of the ubiquitin-specific protease USP37 during G2-phase promotes mitotic entry
    • betaTrCP)-mediated destruction of the ubiquitin-specific protease USP37 during G2-phase promotes mitotic entry. J Biol Chem 287, 39021-39029.
    • (2012) J Biol Chem , vol.287 , pp. 39021-39029
    • Burrows, A.C.1    Prokop, J.2    Summers, M.K.3
  • 5
    • 19444374383 scopus 로고    scopus 로고
    • Assembly of an APC-cdh1substrate complex is stimulated by engagement of a destruction box
    • Burton JL, Tsakraklides V, Solomon M.J. (2005). Assembly of an APC-Cdh1substrate complex is stimulated by engagement of a destruction box. Mol Cell 18, 533-542.
    • (2005) Mol Cell , vol.18 , pp. 533-542
    • Burton, J.L.1    Tsakraklides, V.2    Solomon, M.J.3
  • 6
    • 4444318673 scopus 로고    scopus 로고
    • The SCF ubiquitin ligase: Insights into a molecular machine
    • Cardozo T, Pagano M. (2004). The SCF ubiquitin ligase: insights into a molecular machine. Nat Rev Mol Cell Biol 5, 739-751.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 739-751
    • Cardozo, T.1    Pagano, M.2
  • 7
    • 3242774545 scopus 로고    scopus 로고
    • HAUSP is required for p53 destabilization
    • Cummins JM, Vogelstein B. (2004). HAUSP is required for p53 destabilization. Cell Cycle 3, 689-692.
    • (2004) Cell Cycle , vol.3 , pp. 689-692
    • Cummins, J.M.1    Vogelstein, B.2
  • 8
    • 84890190983 scopus 로고    scopus 로고
    • Regulation of proteolysis by human deubiquitinating enzymes
    • Eletr ZM, Wilkinson K.D. (2014). Regulation of proteolysis by human deubiquitinating enzymes. Biochim Biophys Acta 1843, 114-128.
    • (2014) Biochim Biophys Acta , vol.1843 , pp. 114-128
    • Eletr, Z.M.1    Wilkinson, K.D.2
  • 9
    • 43449139689 scopus 로고    scopus 로고
    • Modulation of the mitotic regulatory network by APC-dependent destruction of the cdh1 inhibitor acm1
    • Enquist-Newman M., Sullivan M, Morgan D.O. (2008). Modulation of the mitotic regulatory network by APC-dependent destruction of the Cdh1 inhibitor Acm1. Mol Cell 30, 437-446.
    • (2008) Mol Cell , vol.30 , pp. 437-446
    • Enquist-Newman, M.1    Sullivan, M.2    Morgan, D.O.3
  • 10
    • 0026699308 scopus 로고
    • CLB5: A novel B cyclin from budding yeast with a role in S phase
    • Epstein CB, Cross F.R. (1992). CLB5: a novel B cyclin from budding yeast with a role in S phase. Genes Dev 6, 1695-1706.
    • (1992) Genes Dev , vol.6 , pp. 1695-1706
    • Epstein, C.B.1    Cross, F.R.2
  • 11
    • 80053594090 scopus 로고    scopus 로고
    • Mechanism of USP7/HAUSP activation by its C-terminal ubiquitin-like domain and allosteric regulation by GMP-synthetase
    • Faesen AC, Dirac AM, Shanmugham A, Ovaa H., Perrakis A, Sixma T.K. (2011). Mechanism of USP7/HAUSP activation by its C-terminal ubiquitin-like domain and allosteric regulation by GMP-synthetase. Mol Cell 44, 147-159.
    • (2011) Mol Cell , vol.44 , pp. 147-159
    • Faesen, A.C.1    Dirac, A.M.2    Shanmugham, A.3    Ovaa, H.4    Perrakis, A.5    Sixma, T.K.6
  • 12
    • 0032133145 scopus 로고    scopus 로고
    • Direct binding of CDC20 protein family members activates the anaphase-promoting complex in mitosis and G1
    • Fang G, Yu H, Kirschner M.W. (1998). Direct binding of CDC20 protein family members activates the anaphase-promoting complex in mitosis and G1. Mol Cell 2, 163-171.
    • (1998) Mol Cell , vol.2 , pp. 163-171
    • Fang, G.1    Yu, H.2    Kirschner, M.W.3
  • 13
    • 0030695025 scopus 로고    scopus 로고
    • A complex of cdc4p, skp1p, and cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor sic1p
    • Feldman RM, Correll CC, Kaplan K.B., Deshaies R.J. (1997). A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p. Cell 91, 221-230.
    • (1997) Cell , vol.91 , pp. 221-230
    • Feldman, R.M.1    Correll, C.C.2    Kaplan, K.B.3    Deshaies, R.J.4
  • 15
    • 84866850568 scopus 로고    scopus 로고
    • The APC/C subunit mnd2/Apc15 promotes cdc20 autoubiquitination and spindle assembly checkpoint inactivation
    • Foster SA, Morgan D.O. (2012). The APC/C subunit Mnd2/Apc15 promotes Cdc20 autoubiquitination and spindle assembly checkpoint inactivation. Mol Cell 47, 921-932.
    • (2012) Mol Cell , vol.47 , pp. 921-932
    • Foster, S.A.1    Morgan, D.O.2
  • 16
    • 0035795408 scopus 로고    scopus 로고
    • Anaphase-promoting complex/cyclosome-dependent proteolysis of human cyclin A starts at the beginning of mitosis and is not subject to the spindle assembly checkpoint
    • Geley S, Kramer E, Gieffers C., Gannon J, Peters JM, Hunt T. (2001). Anaphase-promoting complex/cyclosome-dependent proteolysis of human cyclin A starts at the beginning of mitosis and is not subject to the spindle assembly checkpoint. J Cell Biol 153, 137-147.
    • (2001) J Cell Biol , vol.153 , pp. 137-147
    • Geley, S.1    Kramer, E.2    Gieffers, C.3    Gannon, J.4    Peters, J.M.5    Hunt, T.6
  • 18
    • 0026089183 scopus 로고
    • Cyclin is degraded by the ubiquitin pathway
    • Glotzer M, Murray AW, Kirschner M.W. (1991). Cyclin is degraded by the ubiquitin pathway. Nature 349, 132-138.
    • (1991) Nature , vol.349 , pp. 132-138
    • Glotzer, M.1    Murray, A.W.2    Kirschner, M.W.3
  • 21
    • 33244490784 scopus 로고    scopus 로고
    • Structural basis of competitive recognition of p53 and MDM2 by HAUSP/USP7: Implications for the regulation of the p53-MDM2 pathway
    • Hu M, Gu L, Li M., Jeffrey PD, Gu W, Shi Y. (2006). Structural basis of competitive recognition of p53 and MDM2 by HAUSP/USP7: implications for the regulation of the p53-MDM2 pathway. PLoS Biol 4, e27.
    • (2006) PLoS Biol , vol.4 , pp. e27
    • Hu, M.1    Gu, L.2    Li, M.3    Jeffrey, P.D.4    Gu, W.5    Shi, Y.6
  • 23
    • 0030839209 scopus 로고    scopus 로고
    • The anaphase-promoting complex is required in G1 arrested yeast cells to inhibit B-type cyclin accumulation and to prevent uncontrolled entry into S-phase
    • Irniger S, Nasmyth K. (1997). The anaphase-promoting complex is required in G1 arrested yeast cells to inhibit B-type cyclin accumulation and to prevent uncontrolled entry into S-phase. J Cell Sci 110, 1523-1531.
    • (1997) J Cell Sci , vol.110 , pp. 1523-1531
    • Irniger, S.1    Nasmyth, K.2
  • 24
    • 33644776864 scopus 로고    scopus 로고
    • Distinct mechanisms control the stability of the related S-phase cyclins clb5 and clb6
    • Jackson L.P., Reed SI, Haase S.B. (2006). Distinct mechanisms control the stability of the related S-phase cyclins Clb5 and Clb6. Mol Cell Biol 26, 2456-2466.
    • (2006) Mol Cell Biol , vol.26 , pp. 2456-2466
    • Jackson, L.P.1    Reed, S.I.2    Haase, S.B.3
  • 25
  • 27
    • 0033545694 scopus 로고    scopus 로고
    • Inhibitory phosphorylation of the APC regulator hct1 is controlled by the kinase cdc28 and the phosphatase cdc14
    • Jaspersen SL, Charles JF, Morgan D.O. (1999). Inhibitory phosphorylation of the APC regulator Hct1 is controlled by the kinase Cdc28 and the phosphatase Cdc14. Curr Biol 9, 227-236.
    • (1999) Curr Biol , vol.9 , pp. 227-236
    • Jaspersen, S.L.1    Charles, J.F.2    Morgan, D.O.3
  • 28
    • 4344654668 scopus 로고    scopus 로고
    • Cdc28/Cdk1 regulates spindle pole body duplication through phosphorylation of spc42 and mps1
    • Jaspersen SL, Huneycutt BJ, Giddings TH Jr, Resing KA, Ahn NG, Winey M. (2004). Cdc28/Cdk1 regulates spindle pole body duplication through phosphorylation of Spc42 and Mps1. Dev Cell 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
  • 29
    • 22744456248 scopus 로고    scopus 로고
    • The rsp5 ubiquitin ligase is coupled to and antagonized by the ubp2 deubiquitinating enzyme
    • Kee Y, Lyon N, Huibregtse J.M. (2005). The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme. EMBO J 24, 2414-2424.
    • (2005) EMBO J , vol.24 , pp. 2414-2424
    • Kee, Y.1    Lyon, N.2    Huibregtse, J.M.3
  • 31
    • 77957893483 scopus 로고    scopus 로고
    • A global census of fission yeast deubiquitinating enzyme localization and interaction networks reveals distinct compartmentalization profiles and overlapping functions in endocytosis and polarity
    • Kouranti I, McLean JR, Feoktistova A, Liang P., Johnson AE, Roberts-Galbraith RH, Gould K.L. (2010). A global census of fission yeast deubiquitinating enzyme localization and interaction networks reveals distinct compartmentalization profiles and overlapping functions in endocytosis and polarity. PLoS Biol 8, 100471.
    • (2010) PLoS Biol , vol.8
    • Kouranti, I.1    McLean, J.R.2    Feoktistova, A.3    Liang, P.4    Johnson, A.E.5    Roberts-Galbraith, R.H.6    Gould, K.L.7
  • 32
    • 0037061508 scopus 로고    scopus 로고
    • Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization
    • Li M, Chen D, Shiloh A., Luo J, Nikolaev AY, Qin J, Gu W. (2002). Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization. Nature 416, 648-653.
    • (2002) Nature , vol.416 , pp. 648-653
    • Li, M.1    Chen, D.2    Shiloh, A.3    Luo, J.4    Nikolaev, A.Y.5    Qin, J.6    Gu, W.7
  • 33
  • 35
    • 33845448198 scopus 로고    scopus 로고
    • Acm1 is a negative regulator of the CDH1-dependent anaphase-promoting complex/cyclosome in budding yeast
    • Martinez JS, Jeong DE, Choi E, Billings B.M., Hall M.C. (2006). Acm1 is a negative regulator of the CDH1-dependent anaphase-promoting complex/cyclosome in budding yeast. Mol Cell Biol 26, 9162-9176.
    • (2006) Mol Cell Biol , vol.26 , pp. 9162-9176
    • Martinez, J.S.1    Jeong, D.E.2    Choi, E.3    Billings, B.M.4    Hall, M.C.5
  • 36
    • 70449397570 scopus 로고    scopus 로고
    • Mechanisms of ubiquitin transfer by the anaphase-promoting complex
    • Matyskiela ME, Rodrigo-Brenni MC, Morgan D.O. (2009). Mechanisms of ubiquitin transfer by the anaphase-promoting complex. J Biol 8, 92.
    • (2009) J Biol , vol.8 , pp. 92
    • Matyskiela, M.E.1    Rodrigo-Brenni, M.C.2    Morgan, D.O.3
  • 37
    • 30044444178 scopus 로고    scopus 로고
    • The CLIP-170 homologue bik1p promotes the phosphorylation and asymmetric localization of kar9p
    • Moore JK, D'Silva S, Miller R.K. (2006). The CLIP-170 homologue Bik1p promotes the phosphorylation and asymmetric localization of Kar9p. Mol Biol Cell 17, 178-191.
    • (2006) Mol Biol Cell , vol.17 , pp. 178-191
    • Moore, J.K.1    D'Silva, S.2    Miller, R.K.3
  • 38
    • 0035963372 scopus 로고    scopus 로고
    • Cyclin-dependent kinases prevent DNA re-replication through multiple mechanisms
    • Nguyen VQ, Co C, Li J.J. (2001). Cyclin-dependent kinases prevent DNA re-replication through multiple mechanisms. Nature 411, 1068-1073.
    • (2001) Nature , vol.411 , pp. 1068-1073
    • Nguyen, V.Q.1    Co, C.2    Li, J.J.3
  • 39
    • 0034673282 scopus 로고    scopus 로고
    • Human p55/Cdc20 associates with cyclin A and is phosphorylated by the cyclin A-cdk2 complex
    • Ohtoshi A, Maeda T, Higashi H., Ashizawa S, Hatakeyama M. (2000). Human p55/Cdc20 associates with cyclin A and is phosphorylated by the cyclin A-Cdk2 complex. Biochem Biophys Res Commun 268, 530-534.
    • (2000) Biochem Biophys Res Commun , vol.268 , pp. 530-534
    • Ohtoshi, A.1    Maeda, T.2    Higashi, H.3    Ashizawa, S.4    Hatakeyama, M.5
  • 40
    • 47949105016 scopus 로고    scopus 로고
    • Pseudosubstrate inhibition of the anaphase-promoting complex by acm1: Regulation by proteolysis and cdc28 phosphorylation
    • Ostapenko D, Burton JL, Wang R, Solomon M.J. (2008). Pseudosubstrate inhibition of the anaphase-promoting complex by Acm1: regulation by proteolysis and Cdc28 phosphorylation. Mol Cell Biol 28, 4653-4664.
    • (2008) Mol Cell Biol , vol.28 , pp. 4653-4664
    • Ostapenko, D.1    Burton, J.L.2    Wang, R.3    Solomon, M.J.4
  • 41
    • 79959872461 scopus 로고    scopus 로고
    • Anaphase promoting complex-dependent degradation of transcriptional repressors nrm1 and yhp1 in saccharomyces cerevisiae
    • Ostapenko D, Solomon M.J. (2011). Anaphase promoting complex-dependent degradation of transcriptional repressors Nrm1 and Yhp1 in Saccharomyces cerevisiae. Mol Biol Cell 22, 2175-2184.
    • (2011) Mol Biol Cell , vol.22 , pp. 2175-2184
    • Ostapenko, D.1    Solomon, M.J.2
  • 43
    • 0036284778 scopus 로고    scopus 로고
    • The anaphase-promoting complex: Proteolysis in mitosis and beyond
    • Peters JM (2002). The anaphase-promoting complex: proteolysis in mitosis and beyond. Mol Cell 9, 931-943.
    • (2002) Mol Cell , vol.9 , pp. 931-943
    • Peters, J.M.1
  • 44
    • 33747589184 scopus 로고    scopus 로고
    • The anaphase promoting complex/cyclosome: A machine designed to destroy
    • Peters JM (2006). The anaphase promoting complex/cyclosome: a machine designed to destroy. Nat Rev Mol Cell Biol 7, 644-656.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 644-656
    • Peters, J.M.1
  • 45
    • 0035883946 scopus 로고    scopus 로고
    • Substrate recognition by the cdc20 and cdh1 components of the anaphase-promoting complex
    • Pfleger CM, Lee E, Kirschner M.W. (2001). Substrate recognition by the Cdc20 and Cdh1 components of the anaphase-promoting complex. Genes Dev 15, 2396-2407.
    • (2001) Genes Dev , vol.15 , pp. 2396-2407
    • Pfleger, C.M.1    Lee, E.2    Kirschner, M.W.3
  • 46
    • 0032543552 scopus 로고    scopus 로고
    • The regulation of cdc20 proteolysis reveals a role for APC components cdc23 and cdc27 during S phase and early mitosis
    • Prinz S, Hwang ES, Visintin R, Amon A. (1998). The regulation of Cdc20 proteolysis reveals a role for APC components Cdc23 and Cdc27 during S phase and early mitosis. Curr Biol 8, 750-760.
    • (1998) Curr Biol , vol.8 , pp. 750-760
    • Prinz, S.1    Hwang, E.S.2    Visintin, R.3    Amon, A.4
  • 47
    • 67650620318 scopus 로고    scopus 로고
    • Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes
    • Reyes-Turcu F.E., Ventii KH, Wilkinson K.D. (2009). Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes. Annu Rev Biochem 78, 363-397.
    • (2009) Annu Rev Biochem , vol.78 , pp. 363-397
    • Reyes-Turcu, F.E.1    Ventii, K.H.2    Wilkinson, K.D.3
  • 48
    • 0025979877 scopus 로고
    • Targeting, disruption, replacement, and allele rescue: Integrative DNA transformation in yeast
    • Rothstein R (1991). Targeting, disruption, replacement, and allele rescue: integrative DNA transformation in yeast. Methods Enzymol 194, 281-301.
    • (1991) Methods Enzymol , vol.194 , pp. 281-301
    • Rothstein, R.1
  • 49
    • 34548822685 scopus 로고    scopus 로고
    • A process independent of the anaphasepromoting complex contributes to instability of the yeast S phase cyclin clb5
    • Sari F, Braus GH, Irniger S. (2007). A process independent of the anaphasepromoting complex contributes to instability of the yeast S phase cyclin Clb5. J Biol Chem 282, 26614-26622.
    • (2007) J Biol Chem , vol.282 , pp. 26614-26622
    • Sari, F.1    Braus, G.H.2    Irniger, S.3
  • 50
    • 77957220495 scopus 로고    scopus 로고
    • Further insight into substrate recognition by USP7: Structural and biochemical analysis of the HdmX and hdm2 interactions with USP7
    • Sarkari F, La Delfa A, Arrowsmith CH, Frappier L, Sheng Y., Saridakis V. (2010). Further insight into substrate recognition by USP7: structural and biochemical analysis of the HdmX and Hdm2 interactions with USP7. J Mol Biol 402, 825-837.
    • (2010) J Mol Biol , vol.402 , pp. 825-837
    • Sarkari, F.1    La Delfa, A.2    Arrowsmith, C.H.3    Frappier, L.4    Sheng, Y.5    Saridakis, V.6
  • 51
    • 84455173201 scopus 로고    scopus 로고
    • Protein-linked ubiquitin chain structure restricts activity of deubiquitinating enzymes
    • Schaefer JB, Morgan D.O. (2011). Protein-linked ubiquitin chain structure restricts activity of deubiquitinating enzymes. J Biol Chem 286, 45186-45196.
    • (2011) J Biol Chem , vol.286 , pp. 45186-45196
    • Schaefer, J.B.1    Morgan, D.O.2
  • 52
    • 0027220020 scopus 로고
    • CLB5 and CLB6, a new pair of B cyclins involved in DNA replication in saccharomyces cerevisiae
    • Schwob E, Nasmyth K. (1993). CLB5 and CLB6, a new pair of B cyclins involved in DNA replication in Saccharomyces cerevisiae. Genes Dev 7, 1160-1175.
    • (1993) Genes Dev , vol.7 , pp. 1160-1175
    • Schwob, E.1    Nasmyth, K.2
  • 54
    • 0032473568 scopus 로고    scopus 로고
    • The polo-like kinase cdc5p and the WD-repeat protein cdc20p/fizzy are regulators and substrates of the anaphase promoting complex in saccharomyces cerevisiae
    • Shirayama M, Zachariae W, Ciosk R., Nasmyth K. (1998). The Polo-like kinase Cdc5p and the WD-repeat protein Cdc20p/fizzy are regulators and substrates of the anaphase promoting complex in Saccharomyces cerevisiae. EMBO J 17, 1336-1349.
    • (1998) EMBO J , vol.17 , pp. 1336-1349
    • Shirayama, M.1    Zachariae, W.2    Ciosk, R.3    Nasmyth, K.4
  • 55
    • 0027007963 scopus 로고
    • Role of phosphorylation in p34cdc2 activation: Identification of an activating kinase
    • Solomon MJ, Lee T, Kirschner M.W. (1992). Role of phosphorylation in p34cdc2 activation: identification of an activating kinase. Mol Biol Cell 3, 13-27.
    • (1992) Mol Biol Cell , vol.3 , pp. 13-27
    • Solomon, M.J.1    Lee, T.2    Kirschner, M.W.3
  • 56
    • 41549142601 scopus 로고    scopus 로고
    • Reverse the curse - The role of deubiquitination in cell cycle control
    • Song L, Rape M. (2008). Reverse the curse-the role of deubiquitination in cell cycle control. Curr Opin Cell Biol 20, 156-163.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 156-163
    • Song, L.1    Rape, M.2
  • 58
    • 0001616078 scopus 로고    scopus 로고
    • A conserved cyclin-binding domain determines functional interplay between anaphase-promoting complex-cdh1 and cyclin A-cdk2 during cell cycle progression
    • Sorensen CS, Lukas C, Kramer E.R., Peters JM, Bartek J, Lukas J. (2001). A conserved cyclin-binding domain determines functional interplay between anaphase-promoting complex-Cdh1 and cyclin A-Cdk2 during cell cycle progression. Mol Cell Biol 21, 3692-3703.
    • (2001) Mol Cell Biol , vol.21 , pp. 3692-3703
    • Sorensen, C.S.1    Lukas, C.2    Kramer, E.R.3    Peters, J.M.4    Bartek, J.5    Lukas, J.6
  • 60
    • 0344668551 scopus 로고    scopus 로고
    • Securin and B-cyclin/CDK are the only essential targets of the APC
    • Thornton BR, Toczyski D.P. (2003). Securin and B-cyclin/CDK are the only essential targets of the APC. Nat Cell Biol 5, 1090-1094.
    • (2003) Nat Cell Biol , vol.5 , pp. 1090-1094
    • Thornton, B.R.1    Toczyski, D.P.2
  • 61
    • 33751213571 scopus 로고    scopus 로고
    • Precise destruction: An emerging picture of the APC
    • Thornton BR, Toczyski D.P. (2006). Precise destruction: an emerging picture of the APC. GenesDev 20, 3069-3078.
    • (2006) GenesDev , vol.20 , pp. 3069-3078
    • Thornton, B.R.1    Toczyski, D.P.2
  • 63
    • 0030693087 scopus 로고    scopus 로고
    • CDC20 and CDH1: A family of substrate-specific activators of APC-dependent proteolysis
    • Visintin R, Prinz S, Amon A. (1997). CDC20 and CDH1: a family of substrate-specific activators of APC-dependent proteolysis. Science 278, 460-463.
    • (1997) Science , vol.278 , pp. 460-463
    • Visintin, R.1    Prinz, S.2    Amon, A.3
  • 65
    • 33845893585 scopus 로고    scopus 로고
    • Cdk and APC activities limit the spindlestabilizing function of fin1 to anaphase
    • Woodbury EL, Morgan D.O. (2007). Cdk and APC activities limit the spindlestabilizing function of Fin1 to anaphase. Nat Cell Biol 9, 106-112.
    • (2007) Nat Cell Biol , vol.9 , pp. 106-112
    • Woodbury, E.L.1    Morgan, D.O.2
  • 66
    • 0032573374 scopus 로고    scopus 로고
    • Control of cyclin ubiquitination by CDK-regulated binding of hct1 to the anaphase promoting complex
    • Zachariae W, Schwab M, Nasmyth K., Seufert W. (1998). Control of cyclin ubiquitination by CDK-regulated binding of Hct1 to the anaphase promoting complex. Science 282, 1721-1724.
    • (1998) Science , vol.282 , pp. 1721-1724
    • Zachariae, W.1    Schwab, M.2    Nasmyth, K.3    Seufert, W.4
  • 67
    • 33746766974 scopus 로고    scopus 로고
    • A role for the deubiquitinating enzyme USP28 in control of the DNA-damage response
    • Zhang D, Zaugg K, Mak T.W., Elledge S.J. (2006). A role for the deubiquitinating enzyme USP28 in control of the DNA-damage response. Cell 126, 529-542.
    • (2006) Cell , vol.126 , pp. 529-542
    • Zhang, D.1    Zaugg, K.2    Mak, T.W.3    Elledge, S.J.4
  • 68
    • 0038485578 scopus 로고    scopus 로고
    • Nuclear localization of the cell cycle regulator CDH1 and its regulation by phosphorylation
    • Zhou Y, Ching Y P, Chun AC, Jin D.Y. (2003). Nuclear localization of the cell cycle regulator CDH1 and its regulation by phosphorylation. J Biol Chem 278, 12530-12536.
    • (2003) J Biol Chem , vol.278 , pp. 12530-12536
    • Zhou, Y.1    Ching, Y.P.2    Chun, A.C.3    Jin, D.Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.