메뉴 건너뛰기




Volumn 3, Issue SEP, 2013, Pages

Ubiquitination site preferences in anaphase promoting complex/cyclosome (APC/C) substrates

Author keywords

(APC C); Aurora A; Degron; KEN; Ubiquitin acceptor; Ubiquitination

Indexed keywords

ANAPHASE PROMOTING COMPLEX; AURORA A KINASE; DEGRON; PROTEIN BINDING;

EID: 84885588582     PISSN: None     EISSN: 20462441     Source Type: Journal    
DOI: 10.1098/rsob.130097     Document Type: Article
Times cited : (36)

References (58)
  • 1
    • 0035235736 scopus 로고    scopus 로고
    • Mitotic kinases as regulators of cell division and its checkpoints
    • DOI 10.1038/35048096
    • Nigg EA. 2001 Mitotic kinases as regulators of cell division and its checkpoints. Nat. Rev. Mol. Cell Biol. 2, 21-32. (doi:10.1038/35048096) (Pubitemid 33676958)
    • (2001) Nature Reviews Molecular Cell Biology , vol.2 , Issue.1 , pp. 21-32
    • Nigg, E.A.1
  • 2
    • 35448956881 scopus 로고    scopus 로고
    • Finishing mitosis, one step at a time
    • DOI 10.1038/nrm2276, PII NRM2276
    • Sullivan M, Morgan DO. 2007 Finishing mitosis, one step at a time. Nat. Rev. Mol. Cell Biol. 8, 894-903. (doi:10.1038/nrm2276) (Pubitemid 47622563)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.11 , pp. 894-903
    • Sullivan, M.1    Morgan, D.O.2
  • 3
    • 79959555511 scopus 로고    scopus 로고
    • Cubism and the cell cycle: The many faces of the APC/C
    • doi:10.1038/nrm3132
    • Pines J. 2011 Cubism and the cell cycle: the many faces of the APC/C. Nat. Rev. Mol. Cell Biol. 12, 427-438. (doi:10.1038/nrm3132)
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 427-438
    • Pines, J.1
  • 4
    • 84861877407 scopus 로고    scopus 로고
    • 2012 the ubiquitin code
    • doi:10.1146/ annurev-biochem-060310-170328
    • Komander D, Rape M. 2012 The ubiquitin code. Annu. Rev. Biochem. 81, 203-229. (doi:10.1146/ annurev-biochem-060310-170328)
    • Annu. Rev. Biochem. , vol.81 , pp. 203-229
    • Komander, D.1    Rape, M.2
  • 5
    • 79955982521 scopus 로고    scopus 로고
    • Structure, function and mechanism of the anaphase promoting complex (APC/C)
    • doi:10.1017/ S0033583510000259
    • Barford D. 2011 Structure, function and mechanism of the anaphase promoting complex (APC/C). Q. Rev. Biophys. 44, 153-190. (doi:10.1017/ S0033583510000259)
    • (2011) Q. Rev. Biophys. , vol.44 , pp. 153-190
    • Barford, D.1
  • 6
    • 84863867994 scopus 로고    scopus 로고
    • Substrate targeting by the ubiquitin-proteasome system in mitosis. Semin
    • doi:10.1016/j.semcdb. 2012.01.015
    • Min M, Lindon C. 2012 Substrate targeting by the ubiquitin-proteasome system in mitosis. Semin. Cell Dev. Biol. 23, 482-491. (doi:10.1016/j.semcdb. 2012.01.015)
    • (2012) Cell Dev. Biol. , vol.23 , pp. 482-491
    • Min, M.1    Lindon, C.2
  • 7
    • 0016512443 scopus 로고
    • Formate assay in body fluids: Application in methanol poisoning
    • doi:10.1016/j.semcdb.2011.03.009
    • Makar AB, McMartin KE, Palese M, Tephly TR. 1975 Formate assay in body fluids: application in methanol poisoning. Biochem. Med. 13, 117-126. (doi:10.1016/j.semcdb.2011.03.009)
    • (1975) Biochem. Med. , vol.13 , pp. 117-126
    • Makar, A.B.1    McMartin, K.E.2    Palese, M.3    Tephly, T.R.4
  • 8
    • 1642458099 scopus 로고    scopus 로고
    • Ordered proteolysis in anaphase inactivates Plk1 to contribute to proper mitotic exit in human cells
    • DOI 10.1083/jcb.200309035
    • Lindon C, Pines J. 2004 Ordered proteolysis in anaphase inactivates Plk1 to contribute to proper mitotic exit in human cells. J. Cell Biol. 164, 233-241. (doi:10.1083/jcb.200309035) (Pubitemid 38133943)
    • (2004) Journal of Cell Biology , vol.164 , Issue.2 , pp. 233-241
    • Lindon, C.1    Pines, J.2
  • 9
    • 0026089183 scopus 로고
    • Cyclin is degraded by the ubiquitin pathway
    • Glotzer M, Murray AW, Kirschner MW. 1991 Cyclin is degraded by the ubiquitin pathway. Nature 349, 132-138. (doi:10.1038/349132a0) (Pubitemid 21912025)
    • (1991) Nature , vol.349 , Issue.6305 , pp. 132-138
    • Glotzer, M.1    Murray, A.W.2    Kirschner, M.W.3
  • 10
    • 0034654399 scopus 로고    scopus 로고
    • The KEN box: An APC recognition signal distinct from the D box targeted by Cdh1
    • Pfleger CM, Kirschner MW. 2000 The KEN box: an APC recognition signal distinct from the D box targeted by Cdh1. Genes Dev. 14, 655-665. (doi:10.1101/gad.14.6.655) (Pubitemid 30176820)
    • (2000) Genes and Development , vol.14 , Issue.6 , pp. 655-665
    • Pfleger, C.M.1    Kirschner, M.W.2
  • 11
    • 0030693087 scopus 로고    scopus 로고
    • CDC20 and CDH1: A family of substrate-specific activators of APC- dependent proteolysis
    • DOI 10.1126/science.278.5337.460
    • Visintin R, Prinz S, Amon A. 1997 CDC20 and CDH1: a family of substrate-specific activators of APCdependent proteolysis. Science 278, 460-463. (doi:10.1126/science.278.5337.460) (Pubitemid 27454429)
    • (1997) Science , vol.278 , Issue.5337 , pp. 460-463
    • Visintin, R.1    Prinz, S.2    Amon, A.3
  • 12
    • 79951491055 scopus 로고    scopus 로고
    • Structures of APC/C(Cdh1) with substrates identify Cdh1 and Apc10 as the D-box co-receptor
    • doi:10.1038/nature09625
    • da Fonseca PC, Kong EH, Zhang Z, Schreiber A, Williams MA, Morris EP, Barford D. 2011 Structures of APC/C(Cdh1) with substrates identify Cdh1 and Apc10 as the D-box co-receptor. Nature 470, 274-278. (doi:10.1038/nature09625)
    • (2011) Nature , vol.470 , pp. 274-278
    • Da Fonseca, P.C.1    Kong, E.H.2    Zhang, Z.3    Schreiber, A.4    Williams, M.A.5    Morris, E.P.6    Barford, D.7
  • 13
    • 84878881252 scopus 로고    scopus 로고
    • Insights into degron recognition by APC/C coactivators from the structure of an Acm1-Cdh1 complex
    • doi:10.1016/j. molcel.2013.04.024
    • He J, Chao WC, Zhang Z, Yang J, Cronin N, Barford D. 2013 Insights into degron recognition by APC/C coactivators from the structure of an Acm1-Cdh1 complex. Mol. Cell 50, 649-660. (doi:10.1016/j. molcel.2013.04.024)
    • (2013) Mol. Cell , vol.50 , pp. 649-660
    • He, J.1    Chao, W.C.2    Zhang, Z.3    Yang, J.4    Cronin, N.5    Barford, D.6
  • 14
    • 34447097834 scopus 로고    scopus 로고
    • Sequential E2s drive polyubiquitin chain assembly on APC targets
    • DOI 10.1016/j.cell.2007.05.027, PII S0092867407006654
    • Rodrigo-Brenni MC, Morgan DO. 2007 Sequential E2 s drive polyubiquitin chain assembly on APC targets. Cell 130, 127-139. (doi:10.1016/j.cell. 2007.05.027) (Pubitemid 47031321)
    • (2007) Cell , vol.130 , Issue.1 , pp. 127-139
    • Rodrigo-Brenni, M.C.1    Morgan, D.O.2
  • 15
    • 79959347898 scopus 로고    scopus 로고
    • Regulation of ubiquitin chain initiation to control the timing of substrate degradation
    • doi:10.1016/j. molcel.2011.04.022
    • Williamson A, Banerjee S, Zhu X, Philipp I, Iavarone AT, Rape M. 2011 Regulation of ubiquitin chain initiation to control the timing of substrate degradation. Mol. Cell 42, 744-757. (doi:10.1016/j. molcel.2011.04.022)
    • (2011) Mol. Cell 42 , pp. 744-757
    • Williamson, A.1    Banerjee, S.2    Zhu, X.3    Philipp, I.4    Iavarone, A.T.5    Rape, M.6
  • 17
    • 43049162227 scopus 로고    scopus 로고
    • Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex
    • DOI 10.1016/j.cell.2008.04.012, PII S0092867408005035
    • Jin L, Williamson A, Banerjee S, Philipp I, Rape M. 2008 Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex. Cell 133, 653-665. (doi:10.1016/j.cell.2008.04.012) (Pubitemid 351636306)
    • (2008) Cell , vol.133 , Issue.4 , pp. 653-665
    • Jin, L.1    Williamson, A.2    Banerjee, S.3    Philipp, I.4    Rape, M.5
  • 19
    • 80054694510 scopus 로고    scopus 로고
    • Global identification of modular cullin-RING ligase substrates
    • doi:10.1016/j.cell.2011.09.019
    • Emanuele MJ et al. 2011 Global identification of modular cullin-RING ligase substrates. Cell 147, 459-474. (doi:10.1016/j.cell.2011.09.019)
    • (2011) Cell , vol.147 , pp. 459-474
    • Emanuele, M.J.1
  • 20
    • 82455179484 scopus 로고    scopus 로고
    • Systematic and quantitative assessment of the ubiquitin-modified proteome
    • doi:10.1016/j.molcel.2011.08.025
    • Kim W et al. 2011 Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol. Cell 44, 325-340. (doi:10.1016/j.molcel.2011. 08.025)
    • (2011) Mol. Cell , vol.44 , pp. 325-340
    • Kim, W.1
  • 21
    • 82355164206 scopus 로고    scopus 로고
    • Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels
    • doi:10.1074/jbc.M111.248856
    • Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR. 2011 Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels. J. Biol. Chem. 286, 41 530-41 538. (doi:10.1074/jbc.M111.248856)
    • (2011) J. Biol. Chem. , vol.286 , pp. 41530-41538
    • Lee, K.A.1    Hammerle, L.P.2    Andrews, P.S.3    Stokes, M.P.4    Mustelin, T.5    Silva, J.C.6    Black, R.A.7    Doedens, J.R.8
  • 22
    • 84861151032 scopus 로고    scopus 로고
    • Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition
    • doi:10.1074/mcp.M111.016857
    • Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA. 2012 Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition. Mol. Cell. Proteomics 11, 148-159. (doi:10.1074/mcp.M111.016857)
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 148-159
    • Udeshi, N.D.1    Mani, D.R.2    Eisenhaure, T.3    Mertins, P.4    Jaffe, J.D.5    Clauser, K.R.6    Hacohen, N.7    Carr, S.A.8
  • 23
    • 80054033461 scopus 로고    scopus 로고
    • A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles
    • doi:10.1074/mcp. M111.013284
    • Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C. 2011 A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Mol. Cell. Proteomics 10, M111.013284. (doi:10.1074/mcp. M111.013284)
    • (2011) Mol. Cell. Proteomics , vol.10
    • Wagner, S.A.1    Beli, P.2    Weinert, B.T.3    Nielsen, M.L.4    Cox, J.5    Mann, M.6    Choudhary, C.7
  • 24
    • 84867101049 scopus 로고    scopus 로고
    • Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass
    • doi:10.1038/ncb2579
    • Povlsen LK et al. 2012 Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass. Nat. Cell Biol. 14, 1089-1098. (doi:10.1038/ncb2579)
    • (2012) Nat. Cell Biol. , vol.14 , pp. 1089-1098
    • Povlsen, L.K.1
  • 25
    • 78651225388 scopus 로고    scopus 로고
    • Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling
    • doi:10.1038/nbt.1654
    • Xu G, Paige JS, Jaffrey SR. 2010 Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling. Nat. Biotechnol. 28, 868-873. (doi:10.1038/nbt.1654)
    • (2010) Nat. Biotechnol. , vol.28 , pp. 868-873
    • Xu, G.1    Paige, J.S.2    Jaffrey, S.R.3
  • 27
    • 0037199968 scopus 로고    scopus 로고
    • Hierarchical organization of modularity in metabolic networks
    • DOI 10.1126/science.1073374
    • Ravasz E, Somera AL, Mongru DA, Oltvai ZN, Barabasi AL. 2002 Hierarchical organization of modularity in metabolic networks. Science 297, 1551-1555. (doi:10.1126/science.1073374) (Pubitemid 34971002)
    • (2002) Science , vol.297 , Issue.5586 , pp. 1551-1555
    • Ravasz, E.1    Somera, A.L.2    Mongru, D.A.3    Oltvai, Z.N.4    Barabasi, A.-L.5
  • 28
    • 67449104195 scopus 로고    scopus 로고
    • In silico analysis of phosphoproteome data suggests a rich-get-richer process of phosphosite accumulation over evolution
    • doi:10.1074/mcp.M800466-MCP200
    • Yachie N, Saito R, Sugahara J, Tomita M, Ishihama Y. 2009 In silico analysis of phosphoproteome data suggests a rich-get-richer process of phosphosite accumulation over evolution. Mol. Cell. Proteomics 8, 1061-1071. (doi:10.1074/mcp.M800466-MCP200)
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 1061-1071
    • Yachie, N.1    Saito, R.2    Sugahara, J.3    Tomita, M.4    Ishihama, Y.5
  • 29
    • 3242891318 scopus 로고    scopus 로고
    • The DISOPRED server for the prediction of protein disorder
    • DOI 10.1093/bioinformatics/bth195
    • Ward JJ, McGuffin LJ, Bryson K, Buxton BF, Jones DT. 2004 The DISOPRED server for the prediction of protein disorder. Bioinformatics 20, 2138-2139. (doi:10.1093/bioinformatics/bth195) (Pubitemid 39236567)
    • (2004) Bioinformatics , vol.20 , Issue.13 , pp. 2138-2139
    • Ward, J.J.1    McGuffin, L.J.2    Bryson, K.3    Buxton, B.F.4    Jones, D.T.5
  • 30
    • 84872102009 scopus 로고    scopus 로고
    • Design principles of a universal protein degradation machine
    • doi:10.1016/j.jmb.2012.11.001
    • Matyskiela ME, Martin A. 2013 Design principles of a universal protein degradation machine. J. Mol. Biol. 425, 199-213. (doi:10.1016/j.jmb.2012.11.001)
    • (2013) J. Mol. Biol. , vol.425 , pp. 199-213
    • Matyskiela, M.E.1    Martin, A.2
  • 31
    • 84864213113 scopus 로고    scopus 로고
    • Systematic functional prioritization of protein posttranslational modifications
    • doi:10.1016/j. cell.2012.05.036
    • Beltrao P et al. 2012 Systematic functional prioritization of protein posttranslational modifications. Cell 150, 413-425. (doi:10.1016/j. cell.2012.05.036)
    • (2012) Cell , vol.150 , pp. 413-425
    • Beltrao, P.1
  • 33
    • 77951644400 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis
    • doi:10.1126/scisignal.2000475
    • Olsen JV et al. 2010 Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci. Signal. 3, ra3. (doi:10.1126/scisignal.2000475)
    • (2010) Sci. Signal. , vol.3
    • Olsen, J.V.1
  • 34
    • 84873521371 scopus 로고    scopus 로고
    • Phosphorylation variation during the cell cycle scales with structural propensities of proteins
    • doi:10.1371/journal.pcbi. 1002842
    • Tyanova S, Cox J, Olsen J, Mann M, Frishman D. 2013 Phosphorylation variation during the cell cycle scales with structural propensities of proteins. PLoS Comp. Biol. 9, e1002842. (doi:10.1371/journal.pcbi. 1002842)
    • (2013) PLoS Comp. Biol. , vol.9
    • Tyanova, S.1    Cox, J.2    Olsen, J.3    Mann, M.4    Frishman, D.5
  • 35
    • 55849133733 scopus 로고    scopus 로고
    • Identification of SCF ubiquitin ligase substrates by global protein stability profiling
    • doi:10. 1126/science.1160462
    • Yen HC, Elledge SJ. 2008 Identification of SCF ubiquitin ligase substrates by global protein stability profiling. Science 322, 923-929. (doi:10. 1126/science.1160462)
    • (2008) Science , vol.322 , pp. 923-929
    • Yen, H.C.1    Elledge, S.J.2
  • 36
    • 84857047339 scopus 로고    scopus 로고
    • PhosphoSitePlus: A comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
    • doi:10.1093/nar/gkr1122
    • Hornbeck PV, Kornhauser JM, Tkachev S, Zhang B, Skrzypek E, Murray B, Latham V, Sullivan M. 2012 PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Res. 40, D261-D270. (doi:10.1093/nar/gkr1122)
    • (2012) Nucleic Acids Res. , vol.40
    • Hornbeck, P.V.1    Kornhauser, J.M.2    Tkachev, S.3    Zhang, B.4    Skrzypek, E.5    Murray, B.6    Latham, V.7    Sullivan, M.8
  • 38
    • 55249088712 scopus 로고    scopus 로고
    • APC/C Cdh1 targets aurora kinase to control reorganization of the mitotic spindle at anaphase
    • doi:10.1016/j.cub.2008.09.058
    • Floyd S, Pines J, Lindon C. 2008 APC/C Cdh1 targets aurora kinase to control reorganization of the mitotic spindle at anaphase. Curr. Biol. 18, 1649-1658. (doi:10.1016/j.cub.2008.09.058)
    • (2008) Curr. Biol. , vol.18 , pp. 1649-1658
    • Floyd, S.1    Pines, J.2    Lindon, C.3
  • 39
    • 33744813542 scopus 로고    scopus 로고
    • Early mitotic degradation of Nek2A depends on Cdc20-independent interaction with the APC/C
    • DOI 10.1038/ncb1410, PII N1410
    • Hayes MJ, Kimata Y, Wattam SL, Lindon C, Mao G, Yamano H, Fry AM. 2006 Early mitotic degradation of Nek2A depends on Cdc20-independent interaction with the APC/C. Nat. Cell Biol. 8, 607-614. (doi:10.1038/ncb1410) (Pubitemid 43827354)
    • (2006) Nature Cell Biology , vol.8 , Issue.6 , pp. 607-614
    • Hayes, M.J.1    Kimata, Y.2    Wattam, S.L.3    Lindon, C.4    Mao, G.5    Yamano, H.6    Fry, A.M.7
  • 40
    • 84872849589 scopus 로고    scopus 로고
    • Mechanisms controlling the temporal degradation of Nek2A and Kif18A by the APC/C-Cdc20 complex
    • doi:10.1038/emboj.2012.335
    • Sedgwick GG, Hayward DG, Di Fiore B, Pardo M, Yu L, Pines J, Nilsson J. 2013 Mechanisms controlling the temporal degradation of Nek2A and Kif18A by the APC/C-Cdc20 complex. EMBO J. 32, 303-314. (doi:10.1038/emboj.2012.335)
    • (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
  • 41
    • 0036714512 scopus 로고    scopus 로고
    • Identification of a new APC/C recognition domain, the A box, which is required for the Cdh1-dependent destruction of the kinase Aurora-A during mitotic exit
    • DOI 10.1101/gad.1007302
    • Littlepage LE, Ruderman JV. 2002 Identification of a new APC/C recognition domain, the A box, which is required for the Cdh1-dependent destruction of the kinase Aurorα-A during mitotic exit. Genes Dev. 16, 2274-2285. (doi:10.1101/gad.1007302) (Pubitemid 35013090)
    • (2002) Genes and Development , vol.16 , Issue.17 , pp. 2274-2285
    • Littlepage, L.E.1    Ruderman, J.V.2
  • 42
    • 12344309497 scopus 로고    scopus 로고
    • Requirements for the destruction of human Aurora-A
    • DOI 10.1242/jcs.01418
    • Crane R, Kloepfer A, Ruderman JV. 2004 Requirements for the destruction of human Aurorα-A. J. Cell Sci. 117, 5975-5983. (doi:10.1242/jcs.01418) (Pubitemid 40123964)
    • (2004) Journal of Cell Science , vol.117 , Issue.25 , pp. 5975-5983
    • Crane, R.1    Kloepfer, A.2    Ruderman, J.V.3
  • 43
    • 0037157197 scopus 로고    scopus 로고
    • Degradation of human Aurora-A protein kinase is mediated by hCdh1
    • DOI 10.1016/S0014-5793(02)02711-4, PII S0014579302027114
    • Taguchi S, Honda K, Sugiura K, Yamaguchi A, Furukawa K, Urano T. 2002 Degradation of human Aurorα-A protein kinase is mediated by hCdh1. FEBS Lett. 519, 59-65. (doi:10.1016/S0014-5793(02) 02711-4) (Pubitemid 34521992)
    • (2002) FEBS Letters , vol.519 , Issue.1-3 , pp. 59-65
    • Taguchi, S.-I.1    Honda, K.2    Sugiura, K.3    Yamaguchi, A.4    Furukawa, K.5    Urano, T.6
  • 45
    • 79955780605 scopus 로고    scopus 로고
    • A novel strategy to isolate ubiquitin conjugates reveals wide role for ubiquitination during neural development
    • doi:10.1074/mcp. M110.002188
    • Franco M, Seyfried NT, Brand AH, Peng J, Mayor U. 2011 A novel strategy to isolate ubiquitin conjugates reveals wide role for ubiquitination during neural development. Mol. Cell. Proteomics 10, M110.002188. (doi:10.1074/mcp. M110.002188)
    • (2011) Mol. Cell. Proteomics , vol.10
    • Franco, M.1    Seyfried, N.T.2    Brand, A.H.3    Peng, J.4    Mayor, U.5
  • 46
    • 33744911377 scopus 로고    scopus 로고
    • Lysine activation and functional analysis of E2-mediated conjugation in the SUMO pathway
    • DOI 10.1038/nsmb1104, PII N1104
    • Yunus AA, Lima CD. 2006 Lysine activation and functional analysis of E2-mediated conjugation in the SUMO pathway. Nat. Struct. Mol. Biol. 13, 491-499. (doi:10.1038/nsmb1104) (Pubitemid 43848903)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.6 , pp. 491-499
    • Yunus, A.A.1    Lima, C.D.2
  • 47
    • 77953158465 scopus 로고    scopus 로고
    • Quantitative site-specific phosphorylation dynamics of human protein kinases during mitotic progression
    • doi:10.1074/mcp.M900335-MCP200
    • Dulla K, Daub H, Hornberger R, Nigg EA, Korner R. 2010 Quantitative site-specific phosphorylation dynamics of human protein kinases during mitotic progression. Mol. Cell. Proteomics 9, 1167-1181. (doi:10.1074/mcp.M900335- MCP200)
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1167-1181
    • Dulla, K.1    Daub, H.2    Hornberger, R.3    Nigg, E.A.4    Korner, R.5
  • 48
    • 84859051901 scopus 로고    scopus 로고
    • ELM - The database of eukaryotic linear motifs
    • doi:10.1093/ nar/gkr1064
    • Dinkel H et al. 2012 ELM-the database of eukaryotic linear motifs. Nucleic Acids Res. 40, D242-D251. (doi:10.1093/ nar/gkr1064)
    • (2012) Nucleic Acids Res. , vol.40
    • Dinkel, H.1
  • 49
    • 33947310066 scopus 로고    scopus 로고
    • Cdc20 in the spindle assembly checkpoint
    • DOI 10.1101/gad.1511107
    • Burton JL, Solomon MJ. 2007 Mad3p, a pseudosubstrate inhibitor of APCCdc20 in thespindle assembly checkpoint. Genes Dev. 21, 655-667. (doi:10.1101/gad.1511107) (Pubitemid 46440288)
    • (2007) Genes and Development , vol.21 , Issue.6 , pp. 655-667
    • Burton, J.L.1    Solomon, M.J.2
  • 50
    • 79955581195 scopus 로고    scopus 로고
    • Mechanisms of pseudosubstrate inhibition of the anaphase promoting complex by Acm1
    • doi:10.1038/emboj. 2011.90
    • Burton JL, Xiong Y, Solomon MJ. 2011 Mechanisms of pseudosubstrate inhibition of the anaphase promoting complex by Acm1. EMBO J. 30, 1818-1829. (doi:10.1038/emboj. 2011.90)
    • (2011) EMBO J. , vol.30 , pp. 1818-1829
    • Burton, J.L.1    Xiong, Y.2    Solomon, M.J.3
  • 51
    • 53049108497 scopus 로고    scopus 로고
    • Unique D box and KEN box sequences limit ubiquitination of Acm 1 and promote pseudosubstrate inhibition of the anaphase-promoting complex
    • doi:10.1074/jbc. M803695200
    • Choi E, Dial JM, Jeong DE, Hall MC. 2008 Unique D box and KEN box sequences limit ubiquitination of Acm1 and promote pseudosubstrate inhibition of the anaphase-promoting complex. J. Biol. Chem. 283, 23 701-23 710. (doi:10.1074/jbc. M803695200)
    • (2008) J. Biol. Chem. , vol.283 , pp. 23701-23710
    • Choi, E.1    Dial, J.M.2    Jeong, D.E.3    Hall, M.C.4
  • 52
    • 43449139689 scopus 로고    scopus 로고
    • Modulation of the mitotic regulatory network by APC-dependent destruction of the Cdh1 inhibitor Acm1
    • DOI 10.1016/j.molcel.2008.04.004, PII S1097276508002645
    • Enquist-Newman M, Sullivan M, Morgan DO. 2008 Modulation of the mitotic regulatory network by APC-dependent destruction of the Cdh1 inhibitor Acm1. Mol. Cell. 30, 437-446. (doi:10.1016/j molcel.2008.04.004) (Pubitemid 351672373)
    • (2008) Molecular Cell , vol.30 , Issue.4 , pp. 437-446
    • Enquist-Newman, M.1    Sullivan, M.2    Morgan, D.O.3
  • 53
    • 42049120523 scopus 로고    scopus 로고
    • A mutual inhibition between APC/C and its substrate Mes1 required for meiotic progression in fission yeast
    • doi:10.1016/j.devcel.2007.12.010
    • Kimata Y, Trickey M, Izawa D, Gannon J, Yamamoto M, Yamano H. 2008 A mutual inhibition between APC/C and its substrate Mes1 required for meiotic progression in fission yeast. Dev. Cell 14, 446-454. (doi:10.1016/j.devcel.2007. 12.010)
    • (2008) Dev. Cell , vol.14 , pp. 446-454
    • Kimata, Y.1    Trickey, M.2    Izawa, D.3    Gannon, J.4    Yamamoto, M.5    Yamano, H.6
  • 54
    • 47549083849 scopus 로고    scopus 로고
    • Positive feedback sharpens the anaphase switch
    • doi:10.1038/nature07050
    • Holt LJ, Krutchinsky AN, Morgan DO. 2008 Positive feedback sharpens the anaphase switch. Nature 454, 353-357. (doi:10.1038/nature07050)
    • (2008) Nature , vol.454 , pp. 353-357
    • Holt, L.J.1    Krutchinsky, A.N.2    Morgan, D.O.3
  • 56
    • 25144525540 scopus 로고    scopus 로고
    • CDKs promote DNA replication origin licensing in human cells by protecting Cdc6 from APC/C-dependent proteolysis
    • DOI 10.1016/j.cell.2005.08.013, PII S0092867405008172
    • Mailand N, Diffley JFX. 2005 CDKs promote DNA replication origin licensing in human cells by protecting Cdc6 from APC/C-dependent proteolysis. Cell 122, 915-926. (doi:10.1016/j.cell.2005.08.013) (Pubitemid 41345208)
    • (2005) Cell , vol.122 , Issue.6 , pp. 915-926
    • Mailand, N.1    Diffley, J.F.X.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.