메뉴 건너뛰기




Volumn 12, Issue 2, 2013, Pages 365-378

REV7 is required for anaphase-promoting complex-dependent ubiquitination and degradation of translesion DNA polymerase REV1

Author keywords

Anaphase promoting complex; DNA damage tolerance; REV1; REV7; Translesion DNA synthesis

Indexed keywords

ANAPHASE PROMOTING COMPLEX; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; CELL CYCLE PROTEIN 20; DNA POLYMERASE; DNA POLYMERASE REV1; DNA POLYMERASE REV7; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; UVOMORULIN;

EID: 84873619237     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.23214     Document Type: Article
Times cited : (25)

References (75)
  • 1
    • 38049125552 scopus 로고    scopus 로고
    • The fidelity of DNA synthesis by eukaryotic replicative and translesion synthesis polymerases
    • PMID:18166979
    • McCulloch SD, Kunkel TA. The fidelity of DNA synthesis by eukaryotic replicative and translesion synthesis polymerases. Cell Res 2008; 18:148-61; PMID:18166979; http://dx.doi.org/10.1038/cr.2008.4.
    • (2008) Cell Res , vol.18 , pp. 148-161
    • McCulloch, S.D.1    Kunkel, T.A.2
  • 2
    • 21244506437 scopus 로고    scopus 로고
    • Eukaryotic translesion synthesis DNA polymerases: Specificity of structure and function
    • PMID:15952890
    • Prakash S, Johnson RE, Prakash L. Eukaryotic translesion synthesis DNA polymerases: specificity of structure and function. Annu Rev Biochem 2005; 74:317- 53; PMID:15952890; http://dx.doi.org/10.1146/annurev.biochem.74.082803. 133250.
    • (2005) Annu Rev Biochem , vol.74 , pp. 317-353
    • Prakash, S.1    Johnson, R.E.2    Prakash, L.3
  • 3
    • 79251481487 scopus 로고    scopus 로고
    • DNA polymerases and cancer
    • PMID:21258395
    • Lange SS, Takata K, Wood RD. DNA polymerases and cancer. Nat Rev Cancer 2011; 11:96-110; PMID:21258395; http://dx.doi.org/10.1038/nrc2998.
    • (2011) Nat Rev Cancer , vol.11 , pp. 96-110
    • Lange, S.S.1    Takata, K.2    Wood, R.D.3
  • 4
    • 63849131910 scopus 로고    scopus 로고
    • Eukaryotic translesion polymerases and their roles and regulation in DNA damage tolerance
    • PMID:19258535
    • Waters LS, Minesinger BK, Wiltrout ME, D'Souza S, Woodruff RV, Walker GC. Eukaryotic translesion polymerases and their roles and regulation in DNA damage tolerance. Microbiol Mol Biol Rev 2009; 73:134- 54; PMID:19258535; http://dx.doi.org/10.1128/MMBR.00034-08.
    • (2009) Microbiol Mol Biol Rev , vol.73 , pp. 134-154
    • Waters, L.S.1    Minesinger, B.K.2    Wiltrout, M.E.3    D'souza, S.4    Woodruff, R.V.5    Walker, G.C.6
  • 5
    • 77950805150 scopus 로고    scopus 로고
    • Loss of DNA polymerase ζ enhances spontaneous tumorigenesis
    • PMID:20215524
    • Wittschieben JP, Patil V, Glushets V, Robinson LJ, Kusewitt DF, Wood RD. Loss of DNA polymerase ζ enhances spontaneous tumorigenesis. Cancer Res 2010; 70:2770-8; PMID:20215524; http://dx.doi.org/10.1158/0008-5472.CAN-09-4267.
    • (2010) Cancer Res , vol.70 , pp. 2770-2778
    • Wittschieben, J.P.1    Patil, V.2    Glushets, V.3    Robinson, L.J.4    Kusewitt, D.F.5    Wood, R.D.6
  • 6
    • 78650575542 scopus 로고    scopus 로고
    • Suppression of Rev3, the catalytic subunit of Polζ, sensitizes drug-resistant lung tumors to chemotherapy
    • PMID:21068376
    • Doles J, Oliver TG, Cameron ER, Hsu G, Jacks T, Walker GC, et al. Suppression of Rev3, the catalytic subunit of Polζ, sensitizes drug-resistant lung tumors to chemotherapy. Proc Natl Acad Sci USA 2010; 107:20786-91; PMID:21068376; http://dx.doi.org/10.1073/pnas.1011409107.
    • (2010) Proc Natl Acad Sci. USA , vol.107 , pp. 20786-20791
    • Doles, J.1    Oliver, T.G.2    Cameron, E.R.3    Hsu, G.4    Jacks, T.5    Walker, G.C.6
  • 7
    • 84862777927 scopus 로고    scopus 로고
    • Regulation of rev1 by the fanconi anemia core complex
    • PMID:22266823
    • Kim H, Yang K, Dejsuphong D, D'Andrea AD. Regulation of Rev1 by the Fanconi anemia core complex. Nat Struct Mol Biol 2012; 19:164-70; PMID:22266823; http://dx.doi.org/10.1038/nsmb.2222.
    • (2012) Nat Struct Mol Biol. , vol.19 , pp. 164-170
    • Kim, H.1    Yang, K.2    Dejsuphong, D.3    D'andrea, A.D.4
  • 8
    • 82555187816 scopus 로고    scopus 로고
    • The dCMP transferase activity of yeast Rev1 is biologically relevant during the bypass of endogenously generated AP sites
    • PMID:22024240
    • Kim N, Mudrak SV, Jinks-Robertson S. The dCMP transferase activity of yeast Rev1 is biologically relevant during the bypass of endogenously generated AP sites. DNA Repair (Amst) 2011; 10:1262-71; PMID:22024240; http://dx.doi.org/10.1016/j.dnarep.2011.09.017.
    • (2011) DNA Repair (Amst) , vol.10 , pp. 1262-1271
    • Kim, N.1    Mudrak, S.V.2    Jinks-Robertson, S.3
  • 9
    • 78951481539 scopus 로고    scopus 로고
    • The DNA polymerase activity of Saccharomyces cerevisiae Rev1 is biologically significant
    • PMID:20980236
    • Wiltrout ME, Walker GC. The DNA polymerase activity of Saccharomyces cerevisiae Rev1 is biologically significant. Genetics 2011; 187:21-35; PMID:20980236; http://dx.doi.org/10.1534/genetics.110.124172.
    • (2011) Genetics , vol.187 , pp. 21-35
    • Wiltrout, M.E.1    Walker, G.C.2
  • 10
    • 33746162368 scopus 로고    scopus 로고
    • REV1 protein interacts with PCNA: Significance of the REV1 BRCT domain in vitro and in vivo
    • PMID:16857592
    • Guo C, Sonoda E, Tang TS, Parker JL, Bielen AB, Takeda S, et al. REV1 protein interacts with PCNA: significance of the REV1 BRCT domain in vitro and in vivo. Mol Cell 2006; 23:265-71; PMID:16857592; http://dx.doi.org/10.1016/j. molcel.2006.05.038.
    • (2006) Mol Cell , vol.23 , pp. 265-271
    • Guo, C.1    Sonoda, E.2    Tang, T.S.3    Parker, J.L.4    Bielen, A.B.5    Takeda, S.6
  • 11
    • 34547117417 scopus 로고    scopus 로고
    • A ubiquitin-binding motif in the translesion DNA polymerase Rev1 mediates its essential functional interaction with ubiquitinated proliferating cell nuclear antigen in response to DNA damage
    • PMID:17517887
    • Wood A, Garg P, Burgers PM. A ubiquitin-binding motif in the translesion DNA polymerase Rev1 mediates its essential functional interaction with ubiquitinated proliferating cell nuclear antigen in response to DNA damage. J Biol Chem 2007; 282:20256- 63; PMID:17517887; http://dx.doi.org/10.1074/jbc. M702366200.
    • (2007) J Biol Chem , vol.282 , pp. 20256-20263
    • Wood, A.1    Garg, P.2    Burgers, P.M.3
  • 12
    • 0345732688 scopus 로고    scopus 로고
    • Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis
    • PMID:14657033
    • Guo C, Fischhaber PL, Luk-Paszyc MJ, Masuda Y, Zhou J, Kamiya K, et al. Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis. EMBO J 2003; 22:6621-30; PMID:14657033; http://dx.doi.org/10.1093/emboj/cdg626.
    • (2003) EMBO J , vol.22 , pp. 6621-6630
    • Guo, C.1    Fischhaber, P.L.2    Luk-Paszyc, M.J.3    Masuda, Y.4    Zhou, J.5    Kamiya, K.6
  • 13
    • 60849084453 scopus 로고    scopus 로고
    • Identification of a novel REV1-interacting motif necessary for DNA polymerase κ function
    • PMID:19170759
    • Ohashi E, Hanafusa T, Kamei K, Song I, Tomida J, Hashimoto H, et al. Identification of a novel REV1-interacting motif necessary for DNA polymerase κ function. Genes Cells 2009; 14:101-11; PMID:19170759; http://dx.doi.org/10.1111/j.1365-2443.2008.01255.x.
    • (2009) Genes Cells , vol.14 , pp. 101-111
    • Ohashi, E.1    Hanafusa, T.2    Kamei, K.3    Song, I.4    Tomida, J.5    Hashimoto, H.6
  • 14
    • 14844362615 scopus 로고    scopus 로고
    • Vertebrate DNA damage tolerance requires the C-terminus but not BRCT or transferase domains of REV1
    • PMID:15741181
    • Ross AL, Simpson LJ, Sale JE. Vertebrate DNA damage tolerance requires the C-terminus but not BRCT or transferase domains of REV1. Nucleic Acids Res 2005; 33:1280-9; PMID:15741181; http://dx.doi.org/10.1093/nar/gki279.
    • (2005) Nucleic Acids Res , vol.33 , pp. 1280-1289
    • Ross, A.L.1    Simpson, L.J.2    Sale, J.E.3
  • 15
    • 33845427432 scopus 로고    scopus 로고
    • Complex formation with Rev1 enhances the proficiency of saccharomyces cerevisiae DNA polymerase ζ for mismatch extension and for extension opposite from DNA lesions
    • PMID:17030609
    • Acharya N, Johnson RE, Prakash S, Prakash L. Complex formation with Rev1 enhances the proficiency of Saccharomyces cerevisiae DNA polymerase ζ for mismatch extension and for extension opposite from DNA lesions. Mol Cell Biol 2006; 26:9555- 63; PMID:17030609; http://dx.doi.org/10.1128/MCB.01671-06.
    • (2006) Mol Cell Biol , vol.26 , pp. 9555-9563
    • Acharya, N.1    Johnson, R.E.2    Prakash, S.3    Prakash, L.4
  • 16
    • 27144521116 scopus 로고    scopus 로고
    • Complex formation of yeast Rev1 and Rev7 proteins: A novel role for the polymeraseassociated domain
    • PMID:16227619
    • Acharya N, Haracska L, Johnson RE, Unk I, Prakash S, Prakash L. Complex formation of yeast Rev1 and Rev7 proteins: a novel role for the polymeraseassociated domain. Mol Cell Biol 2005; 25:9734- 40; PMID:16227619; http://dx.doi.org/10.1128/MCB.25.21.9734-9740.2005.
    • (2005) Mol Cell Biol. , vol.25 , pp. 9734-9740
    • Acharya, N.1    Haracska, L.2    Johnson, R.E.3    Unk, I.4    Prakash, S.5    Prakash, L.6
  • 17
    • 33750304863 scopus 로고    scopus 로고
    • Novel role for the C terminus of Saccharomyces cerevisiae Rev1 in mediating proteinprotein interactions
    • PMID:16923957
    • D'Souza S, Walker GC. Novel role for the C terminus of Saccharomyces cerevisiae Rev1 in mediating proteinprotein interactions. Mol Cell Biol 2006; 26:8173- 82; PMID:16923957; http://dx.doi.org/10.1128/MCB.00202-06.
    • (2006) Mol Cell Biol. , vol.26 , pp. 8173-8182
    • D'souza, S.1    Walker, G.C.2
  • 18
    • 39149104625 scopus 로고    scopus 로고
    • Comparative analysis of in vivo interactions between Rev1 protein and other Y-family DNA polymerases in animals and yeasts
    • PMID:18242152
    • Kosarek JN, Woodruff RV, Rivera-Begeman A, Guo C, D'Souza S, Koonin EV, et al. Comparative analysis of in vivo interactions between Rev1 protein and other Y-family DNA polymerases in animals and yeasts. DNA Repair (Amst) 2008; 7:439-51; PMID:18242152; http://dx.doi.org/10.1016/j.dnarep.2007.11.016.
    • (2008) DNA Repair (Amst) , vol.7 , pp. 439-451
    • Kosarek, J.N.1    Woodruff, R.V.2    Rivera-Begeman, A.3    Guo, C.4    D'souza, S.5    Koonin, E.V.6
  • 19
    • 84863393545 scopus 로고    scopus 로고
    • REV1 and polymerase ζ facilitate homologous recombination repair
    • PMID:21926160
    • Sharma S, Hicks JK, Chute CL, Brennan JR, Ahn JY, Glover TW, et al. REV1 and polymerase ζ facilitate homologous recombination repair. Nucleic Acids Res 2012; 40:682-91; PMID:21926160; http://dx.doi.org/10.1093/nar/gkr769.
    • (2012) Nucleic Acids Res , vol.40 , pp. 682-691
    • Sharma, S.1    Hicks, J.K.2    Chute, C.L.3    Brennan, J.R.4    Ahn, J.Y.5    Glover, T.W.6
  • 20
    • 77951218269 scopus 로고    scopus 로고
    • Crystal structure of human REV7 in complex with a human REV3 fragment and structural implication of the interaction between DNA polymerase ζ and REV1
    • PMID:20164194
    • Hara K, Hashimoto H, Murakumo Y, Kobayashi S, Kogame T, Unzai S, et al. Crystal structure of human REV7 in complex with a human REV3 fragment and structural implication of the interaction between DNA polymerase ζ and REV1. J Biol Chem 2010; 285:12299-307; PMID:20164194; http://dx.doi.org/10.1074/ jbc.M109.092403.
    • (2010) J Biol Chem. , vol.285 , pp. 12299-12307
    • Hara, K.1    Hashimoto, H.2    Murakumo, Y.3    Kobayashi, S.4    Kogame, T.5    Unzai, S.6
  • 21
    • 38049150571 scopus 로고    scopus 로고
    • DNA polymerase zeta (pol zeta) in higher eukaryotes
    • PMID:18157155
    • Gan GN, Wittschieben JP, Wittschieben BO, Wood RD. DNA polymerase zeta (pol zeta) in higher eukaryotes. Cell Res 2008; 18:174-83; PMID:18157155; http://dx.doi.org/10.1038/cr.2007.117.
    • (2008) Cell Res , vol.18 , pp. 174-183
    • Gan, G.N.1    Wittschieben, J.P.2    Wittschieben, B.O.3    Wood, R.D.4
  • 22
    • 0029952294 scopus 로고    scopus 로고
    • Thyminethymine dimer bypass by yeast DNA polymerase
    • PMID:8658138
    • Nelson JR, Lawrence CW, Hinkle DC. Thyminethymine dimer bypass by yeast DNA polymerase ζ. Science 1996; 272:1646-9; PMID:8658138; http://dx.doi.org/10.1126/science.272.5268.1646.
    • (1996) Science , vol.272 , pp. 1646-1649
    • Nelson, J.R.1    Lawrence, C.W.2    Hinkle, D.C.3
  • 23
    • 4544350294 scopus 로고    scopus 로고
    • Purification of Drosophila DNA polymerase ζ by REV1 proteinaffinity chromatography
    • PMID:15175013
    • Takeuchi R, Oshige M, Uchida M, Ishikawa G, Takata K, Shimanouchi K, et al. Purification of Drosophila DNA polymerase ζ by REV1 proteinaffinity chromatography. Biochem J 2004; 382:535- 43; PMID:15175013; http://dx.doi.org/ 10.1042/BJ20031833.
    • (2004) Biochem J. , vol.382 , pp. 535-543
    • Takeuchi, R.1    Oshige, M.2    Uchida, M.3    Ishikawa, G.4    Takata, K.5    Shimanouchi, K.6
  • 24
    • 33646240593 scopus 로고    scopus 로고
    • Inactivation of human MAD2B in nasopharyngeal carcinoma cells leads to chemosensitization to DNA-damaging agents
    • PMID:16618761
    • Cheung HW, Chun AC, Wang Q, Deng W, Hu L, Guan XY, et al. Inactivation of human MAD2B in nasopharyngeal carcinoma cells leads to chemosensitization to DNA-damaging agents. Cancer Res 2006; 66:4357-67; PMID:16618761; http://dx.doi.org/10.1158/0008-5472.CAN-05-3602.
    • (2006) Cancer Res , vol.66 , pp. 4357-4367
    • Cheung, H.W.1    Chun, A.C.2    Wang, Q.3    Deng, W.4    Hu, L.5    Guan, X.Y.6
  • 25
    • 21744447035 scopus 로고    scopus 로고
    • Multiple roles of vertebrate REV genes in DNA repair and recombination
    • PMID:15988022
    • Okada T, Sonoda E, Yoshimura M, Kawano Y, Saya H, Kohzaki M, et al. Multiple roles of vertebrate REV genes in DNA repair and recombination. Mol Cell Biol 2005; 25:6103-11; PMID:15988022; http://dx.doi.org/10.1128/MCB.25.14.6103- 6111.2005.
    • (2005) Mol Cell Biol. , vol.25 , pp. 6103-6111
    • Okada, T.1    Sonoda, E.2    Yoshimura, M.3    Kawano, Y.4    Saya, H.5    Kohzaki, M.6
  • 26
    • 40849087740 scopus 로고    scopus 로고
    • HRev7, putative subunit of hPolzeta, plays a critical role in survival, induction of mutations, and progression through S-phase, of UV((254nm))- irradiated human fibroblasts
    • PMID:18295554
    • McNally K, Neal JA, McManus TP, McCormick JJ, Maher VM. hRev7, putative subunit of hPolzeta, plays a critical role in survival, induction of mutations, and progression through S-phase, of UV((254nm))- irradiated human fibroblasts. DNA Repair (Amst) 2008; 7:597-604; PMID:18295554; http://dx.doi.org/10.1016/j. dnarep.2007.12.013.
    • (2008) DNA Repair (Amst) , vol.7 , pp. 597-604
    • McNally, K.1    Neal, J.A.2    Mcmanus, T.P.3    McCormick, J.J.4    Maher, V.M.5
  • 28
    • 0034635445 scopus 로고    scopus 로고
    • A human REV7 homolog that interacts with the polymerase ζ catalytic subunit hREV3 and the spindle assembly checkpoint protein hMAD2
    • PMID:10660610
    • Murakumo Y, Roth T, Ishii H, Rasio D, Numata S, Croce CM, et al. A human REV7 homolog that interacts with the polymerase ζ catalytic subunit hREV3 and the spindle assembly checkpoint protein hMAD2. J Biol Chem 2000; 275:4391-7; PMID:10660610; http://dx.doi.org/10.1074/jbc.275.6.439129.
    • (2000) J Biol Chem. , vol.275 , pp. 4391-4397
    • Murakumo, Y.1    Roth, T.2    Ishii, H.3    Rasio, D.4    Numata, S.5    Croce, C.M.6
  • 29
    • 0035878111 scopus 로고    scopus 로고
    • MAD2B is an inhibitor of the anaphase- promoting complex
    • PMID:11459826
    • Chen J, Fang G. MAD2B is an inhibitor of the anaphase- promoting complex. Genes Dev 2001; 15:1765- 70; PMID:11459826; http://dx.doi.org/10.1101/gad. 898701.
    • (2001) Genes Dev , vol.15 , pp. 1765-1770
    • Chen, J.1    Fang, G.2
  • 30
    • 0035878126 scopus 로고    scopus 로고
    • Inhibition of Cdh1-APC by the MAD2-related protein MAD2L2: A novel mechanism for regulating Cdh1
    • PMID:11459825
    • Pfleger CM, Salic A, Lee E, Kirschner MW. Inhibition of Cdh1-APC by the MAD2-related protein MAD2L2: a novel mechanism for regulating Cdh1. Genes Dev 2001; 15:1759-64; PMID:11459825; http://dx.doi.org/10.1101/gad.897901.
    • (2001) Genes Dev , vol.15 , pp. 1759-1764
    • Pfleger, C.M.1    Salic, A.2    Lee, E.3    Kirschner, M.W.4
  • 31
    • 33144478094 scopus 로고    scopus 로고
    • Roles of the anaphase-promoting complex/cyclosome and of its activator Cdc20 in functional substrate binding
    • PMID:16455800
    • Eytan E, Moshe Y, Braunstein I, Hershko A. Roles of the anaphase-promoting complex/cyclosome and of its activator Cdc20 in functional substrate binding. Proc Natl Acad Sci USA 2006; 103:2081-6; PMID:16455800; http://dx.doi.org/10.1073/pnas.0510695103.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 2081-2086
    • Eytan, E.1    Moshe, Y.2    Braunstein, I.3    Hershko, A.4
  • 32
    • 34250799719 scopus 로고    scopus 로고
    • Cdc20: A WD40 activator for a cell cycle degradation machine
    • PMID:17612486
    • Yu H. Cdc20: a WD40 activator for a cell cycle degradation machine. Mol Cell 2007; 27:3-16; PMID:17612486; http://dx.doi.org/10.1016/j.molcel.2007.06. 009.
    • (2007) Mol Cell , vol.27 , pp. 3-16
    • Yu, H.1
  • 33
    • 77958465476 scopus 로고    scopus 로고
    • APC/C-Cdh1: From cell cycle to cellular differentiation and genomic integrity
    • PMID:20935501
    • Qiao X, Zhang L, Gamper AM, Fujita T, Wan Y. APC/C-Cdh1: from cell cycle to cellular differentiation and genomic integrity. Cell Cycle 2010; 9:3904- 12; PMID:20935501; http://dx.doi.org/10.4161/cc.9.19.13585.
    • (2010) Cell Cycle , vol.9 , pp. 3904-3912
    • Qiao, X.1    Zhang, L.2    Gamper, A.M.3    Fujita, T.4    Wan, Y.5
  • 34
    • 0026089183 scopus 로고
    • Cyclin is degraded by the ubiquitin pathway
    • PMID:1846030
    • Glotzer M, Murray AW, Kirschner MW. Cyclin is degraded by the ubiquitin pathway. Nature 1991; 349:132-8; PMID:1846030; http://dx.doi.org/10.1038/ 349132a0.
    • (1991) Nature , vol.349 , pp. 132-138
    • Glotzer, M.1    Murray, A.W.2    Kirschner, M.W.3
  • 35
    • 0034654399 scopus 로고    scopus 로고
    • The KEN box: An APC recognition signal distinct from the D box targeted by Cdh1
    • PMID:10733526
    • Pfleger CM, Kirschner MW. The KEN box: an APC recognition signal distinct from the D box targeted by Cdh1. Genes Dev 2000; 14:655-65; PMID:10733526.
    • (2000) Genes Dev , vol.14 , pp. 655-665
    • Pfleger, C.M.1    Kirschner, M.W.2
  • 36
    • 34547092698 scopus 로고    scopus 로고
    • Cell cycle-dependent expression of centrosomal ninein-like protein in human cells is regulated by the anaphase-promoting complex
    • PMID:17403670
    • Wang Y, Zhan Q. Cell cycle-dependent expression of centrosomal ninein-like protein in human cells is regulated by the anaphase-promoting complex. J Biol Chem 2007; 282:17712-9; PMID:17403670; http://dx.doi.org/10. 1074/jbc.M701350200.
    • (2007) J Biol Chem. , vol.282 , pp. 17712-17719
    • Wang, Y.1    Zhan, Q.2
  • 37
    • 50249083985 scopus 로고    scopus 로고
    • Anaphase-promoting complex/cyclosome-CDH1- mediated proteolysis of the forkhead box M1 transcription factor is critical for regulated entry into S phase
    • PMID:18573889
    • Park HJ, Costa RH, Lau LF, Tyner AL, Raychaudhuri P. Anaphase-promoting complex/cyclosome-CDH1- mediated proteolysis of the forkhead box M1 transcription factor is critical for regulated entry into S phase. Mol Cell Biol 2008; 28:5162-71; PMID:18573889; http://dx.doi.org/10.1128/MCB.00387-08.
    • (2008) Mol Cell Biol , vol.28 , pp. 5162-5171
    • Park, H.J.1    Costa, R.H.2    Lau, L.F.3    Tyner, A.L.4    Raychaudhuri, P.5
  • 38
    • 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
    • PMID:12208850
    • Littlepage LE, Ruderman JV. 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. Genes Dev 2002; 16:2274-85; PMID:12208850; http://dx.doi.org/10.1101/gad.1007302.
    • (2002) Genes Dev , vol.16 , pp. 2274-2285
    • Littlepage, L.E.1    Ruderman, J.V.2
  • 39
    • 33749243774 scopus 로고    scopus 로고
    • The CRY box: A second apccdh1-dependent degron in mammalian cdc20
    • PMID:16878123
    • Reis A, Levasseur M, Chang HY, Elliott DJ, Jones KT. The CRY box: a second APCcdh1-dependent degron in mammalian cdc20. EMBO Rep 2006; 7:1040- 5; PMID:16878123; http://dx.doi.org/10.1038/sj.embor.7400772.
    • (2006) EMBO Rep , vol.7 , pp. 1040-1045
    • Reis, A.1    Levasseur, M.2    Chang, H.Y.3    Elliott, D.J.4    Jones, K.T.5
  • 40
    • 34547937914 scopus 로고    scopus 로고
    • A bacterial effector targets mad2L2, an APC inhibitor, to modulate host cell cycling
    • PMID:17719540
    • Iwai H, Kim M, Yoshikawa Y, Ashida H, Ogawa M, Fujita Y, et al. A bacterial effector targets Mad2L2, an APC inhibitor, to modulate host cell cycling. Cell 2007; 130:611-23; PMID:17719540; http://dx.doi.org/10.1016/j.cell. 2007.06.043.
    • (2007) Cell , vol.130 , pp. 611-623
    • Iwai, H.1    Kim, M.2    Yoshikawa, Y.3    Ashida, H.4    Ogawa, M.5    Fujita, Y.6
  • 41
    • 0042889587 scopus 로고    scopus 로고
    • Adenovirus ADP protein (E3-11.6K), which is required for efficient cell lysis and virus release, interacts with human MAD2B
    • PMID:12951035
    • Ying B, Wold WS. Adenovirus ADP protein (E3-11.6K), which is required for efficient cell lysis and virus release, interacts with human MAD2B. Virology 2003; 313:224-34; PMID:12951035; http://dx.doi.org/10.1016/S0042-6822(03)00287- 3.
    • (2003) Virology , vol.313 , pp. 224-234
    • Ying, B.1    Wold, W.S.2
  • 42
    • 29444454665 scopus 로고    scopus 로고
    • Ubiquitinated proliferating cell nuclear antigen activates translesion DNA polymerases η and REV1
    • PMID:16344468
    • Garg P, Burgers PM. Ubiquitinated proliferating cell nuclear antigen activates translesion DNA polymerases η and REV1. Proc Natl Acad Sci USA 2005; 102:18361-6; PMID:16344468; http://dx.doi.org/10.1073/pnas.0505949102.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 18361-18366
    • Garg, P.1    Burgers, P.M.2
  • 43
    • 33846640580 scopus 로고    scopus 로고
    • Polymerase η is a short-lived, proteasomally degraded protein that is temporarily stabilized following UV irradiation in Saccharomyces cerevisiae
    • PMID:17198712
    • Skoneczna A, McIntyre J, Skoneczny M, Policinska Z, Sledziewska-Gojska E. Polymerase η is a short-lived, proteasomally degraded protein that is temporarily stabilized following UV irradiation in Saccharomyces cerevisiae. J Mol Biol 2007; 366:1074-86; PMID:17198712; http://dx.doi.org/10.1016/j.jmb.2006. 11.093.
    • (2007) J Mol Biol , vol.366 , pp. 1074-1086
    • Skoneczna, A.1    McIntyre, J.2    Skoneczny, M.3    Policinska, Z.4    Sledziewska-Gojska, E.5
  • 44
    • 75749108557 scopus 로고    scopus 로고
    • Pirh2 E3 ubiquitin ligase targets DNA polymerase η for 20S proteasomal degradation
    • PMID:20008555
    • Jung YS, Liu G, Chen X. Pirh2 E3 ubiquitin ligase targets DNA polymerase η for 20S proteasomal degradation. Mol Cell Biol 2010; 30:1041-8; PMID:20008555; http://dx.doi.org/10.1128/MCB.01198-09.
    • (2010) Mol Cell Biol , vol.30 , pp. 1041-1048
    • Jung, Y.S.1    Liu, G.2    Chen, X.3
  • 45
    • 84855850825 scopus 로고    scopus 로고
    • DNA polymerase η is targeted by mdm2 for polyubiquitination and proteasomal degradation in response to ultraviolet irradiation
    • PMID:22056306
    • Jung YS, Qian Y, Chen X. DNA polymerase η is targeted by Mdm2 for polyubiquitination and proteasomal degradation in response to ultraviolet irradiation. DNA Repair (Amst) 2012; 11:177-84; PMID:22056306; http://dx.doi.org/10.1016/j.dnarep.2011.10.017.
    • (2012) DNA Repair (Amst) , vol.11 , pp. 177-184
    • Jung, Y.S.1    Qian, Y.2    Chen, X.3
  • 46
    • 53249097348 scopus 로고    scopus 로고
    • Control of DNA polymerase λ stability by phosphorylation and ubiquitination during the cell cycle
    • PMID:18688254
    • Wimmer U, Ferrari E, Hunziker P, Hübscher U. Control of DNA polymerase λ stability by phosphorylation and ubiquitination during the cell cycle. EMBO Rep 2008; 9:1027-33; PMID:18688254; http://dx.doi.org/10.1038/ embor.2008.148.
    • (2008) EMBO Rep , vol.9 , pp. 1027-1033
    • Wimmer, U.1    Ferrari, E.2    Hunziker, P.3    Hübscher, U.4
  • 47
    • 33745141184 scopus 로고    scopus 로고
    • The critical mutagenic translesion DNA polymerase Rev1 is highly expressed during G(2)/M phase rather than S phase
    • PMID:16751278
    • Waters LS, Walker GC. The critical mutagenic translesion DNA polymerase Rev1 is highly expressed during G(2)/M phase rather than S phase. Proc Natl Acad Sci USA 2006; 103:8971-6; PMID:16751278; http://dx.doi.org/10.1073/pnas. 0510167103.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 8971-8976
    • Waters, L.S.1    Walker, G.C.2
  • 48
    • 33845801753 scopus 로고    scopus 로고
    • Yeast Rev1 is cell cycle regulated, phosphorylated in response to DNA damage and its binding to chromosomes is dependent upon MEC1
    • PMID:17035102
    • Sabbioneda S, Bortolomai I, Giannattasio M, Plevani P, Muzi-Falconi M. Yeast Rev1 is cell cycle regulated, phosphorylated in response to DNA damage and its binding to chromosomes is dependent upon MEC1. DNA Repair (Amst) 2007; 6:121-7; PMID:17035102; http://dx.doi.org/10.1016/j.dnarep.2006.09.002.
    • (2007) DNA Repair (Amst) , vol.6 , pp. 121-127
    • Sabbioneda, S.1    Bortolomai, I.2    Giannattasio, M.3    Plevani, P.4    Muzi-Falconi, M.5
  • 49
    • 79961165129 scopus 로고    scopus 로고
    • Molecular chaperone Hsp90 regulates REV1-mediated mutagenesis
    • PMID:21690293
    • Pozo FM, Oda T, Sekimoto T, Murakumo Y, Masutani C, Hanaoka F, et al. Molecular chaperone Hsp90 regulates REV1-mediated mutagenesis. Mol Cell Biol 2011; 31:3396-409; PMID:21690293; http://dx.doi.org/10.1128/MCB.05117-11.
    • (2011) Mol Cell Biol , vol.31 , pp. 3396-3409
    • Pozo, F.M.1    Oda, T.2    Sekimoto, T.3    Murakumo, Y.4    Masutani, C.5    Hanaoka, F.6
  • 50
    • 79451475938 scopus 로고    scopus 로고
    • Proteasomal regulation of the mutagenic translesion DNA polymerase, Saccharomyces cerevisiae Rev1
    • PMID:21227758
    • Wiltrout ME, Walker GC. Proteasomal regulation of the mutagenic translesion DNA polymerase, Saccharomyces cerevisiae Rev1. DNA Repair (Amst) 2011; 10:169-75; PMID:21227758; http://dx.doi.org/10.1016/j.dnarep.2010.10.008.
    • (2011) DNA Repair (Amst) , vol.10 , pp. 169-175
    • Wiltrout, M.E.1    Walker, G.C.2
  • 51
    • 33845223494 scopus 로고    scopus 로고
    • Ubiquitin-binding motifs in REV1 protein are required for its role in the tolerance of DNA damage
    • PMID:16982685
    • Guo C, Tang TS, Bienko M, Parker JL, Bielen AB, Sonoda E, et al. Ubiquitin-binding motifs in REV1 protein are required for its role in the tolerance of DNA damage. Mol Cell Biol 2006; 26:8892- 900; PMID:16982685; http://dx.doi.org/10.1128/MCB.01118-06.
    • (2006) Mol Cell Biol , vol.26 , pp. 8892-8900
    • Guo, C.1    Tang, T.S.2    Bienko, M.3    Parker, J.L.4    Bielen, A.B.5    Sonoda, E.6
  • 52
    • 48149104225 scopus 로고    scopus 로고
    • Novel conserved motifs in Rev1 C-terminus are required for mutagenic DNA damage tolerance
    • PMID:18603483
    • D'Souza S, Waters LS, Walker GC. Novel conserved motifs in Rev1 C-terminus are required for mutagenic DNA damage tolerance. DNA Repair (Amst) 2008; 7:1455-70; PMID:18603483; http://dx.doi.org/10.1016/j.dnarep.2008.05.009.
    • (2008) DNA Repair (Amst) , vol.7 , pp. 1455-1470
    • D'souza, S.1    Waters, L.S.2    Walker, G.C.3
  • 53
    • 76449099936 scopus 로고    scopus 로고
    • Ubiquitin-dependent regulation of translesion polymerases
    • PMID:20074045
    • Chun AC, Jin DY. Ubiquitin-dependent regulation of translesion polymerases. Biochem Soc Trans 2010; 38:110-5; PMID:20074045; http://dx.doi.org/10.1042/BST0380110.
    • (2010) Biochem Soc Trans , vol.38 , pp. 110-115
    • Chun, A.C.1    Jin, D.Y.2
  • 54
    • 0035930333 scopus 로고    scopus 로고
    • The anaphase-promoting complex mediates TGF-β signaling by targeting SnoN for destruction
    • PMID:11741538
    • Wan Y, Liu X, Kirschner MW. The anaphase-promoting complex mediates TGF-β signaling by targeting SnoN for destruction. Mol Cell 2001; 8:1027-39; PMID:11741538; http://dx.doi.org/10.1016/S1097-2765(01)00382-3.
    • (2001) Mol Cell , vol.8 , pp. 1027-1039
    • Wan, Y.1    Liu, X.2    Kirschner, M.W.3
  • 55
    • 77954243203 scopus 로고    scopus 로고
    • Interplay between Cdh1 and JNK activity during the cell cycle
    • PMID:20581839
    • Gutierrez GJ, Tsuji T, Chen M, Jiang W, Ronai ZA. Interplay between Cdh1 and JNK activity during the cell cycle. Nat Cell Biol 2010; 12:686-95; PMID:20581839; http://dx.doi.org/10.1038/ncb2071.
    • (2010) Nat Cell Biol , vol.12 , pp. 686-695
    • Gutierrez, G.J.1    Tsuji, T.2    Chen, M.3    Jiang, W.4    Ronai, Z.A.5
  • 56
    • 79954569219 scopus 로고    scopus 로고
    • Regulation of mitochondrial morphology by APC/CCdh1-mediated control of Drp1 stability
    • PMID:21325626
    • Horn SR, Thomenius MJ, Johnson ES, Freel CD, Wu JQ, Coloff JL, et al. Regulation of mitochondrial morphology by APC/CCdh1-mediated control of Drp1 stability. Mol Biol Cell 2011; 22:1207-16; PMID:21325626; http://dx.doi.org/10. 1091/mbc.E10-07-0567.
    • (2011) Mol Biol Cell , vol.22 , pp. 1207-1216
    • Horn, S.R.1    Thomenius, M.J.2    Johnson, E.S.3    Freel, C.D.4    Wu, J.Q.5    Coloff, J.L.6
  • 57
    • 77952586024 scopus 로고    scopus 로고
    • Proteolysis of rad17 by cdh1/APC regulates checkpoint termination and recovery from genotoxic stress
    • PMID:20424596
    • Zhang L, Park CH, Wu J, Kim H, Liu W, Fujita T, et al. Proteolysis of Rad17 by Cdh1/APC regulates checkpoint termination and recovery from genotoxic stress. EMBO J 2010; 29:1726-37; PMID:20424596; http://dx.doi.org/10.1038/emboj. 2010.55.
    • (2010) EMBO J , vol.29 , pp. 1726-1737
    • Zhang, L.1    Park, C.H.2    Wu, J.3    Kim, H.4    Liu, W.5    Fujita, T.6
  • 58
    • 77958484246 scopus 로고    scopus 로고
    • Degradation of the human mitotic checkpoint kinase mps1 is cell cycle-regulated by apcccdc20 and apc-ccdh1 ubiquitin ligases
    • PMID:20729194
    • Cui Y, Cheng X, Zhang C, Zhang Y, Li S, Wang C, et al. Degradation of the human mitotic checkpoint kinase Mps1 is cell cycle-regulated by APCcCdc20 and APC-cCdh1 ubiquitin ligases. J Biol Chem 2010; 285:32988-98; PMID:20729194; http://dx.doi.org/10.1074/jbc.M110.140905.
    • (2010) J Biol Chem , vol.285 , pp. 32988-32998
    • Cui, Y.1    Cheng, X.2    Zhang, C.3    Zhang, Y.4    Li, S.5    Wang, C.6
  • 59
    • 79952282492 scopus 로고    scopus 로고
    • How APC/C-Cdc20 changes its substrate specificity in mitosis
    • PMID:21336306
    • Izawa D, Pines J. How APC/C-Cdc20 changes its substrate specificity in mitosis. Nat Cell Biol 2011; 13:223-33; PMID:21336306; http://dx.doi.org/10. 1038/ncb2165.
    • (2011) Nat Cell Biol , vol.13 , pp. 223-233
    • Izawa, D.1    Pines, J.2
  • 60
    • 79961109743 scopus 로고    scopus 로고
    • APC/CCdh1-dependent proteolysis of USP1 regulates the response to UV-mediated DNA damage
    • PMID:21768287
    • Cotto-Rios XM, Jones MJ, Busino L, Pagano M, Huang TT. APC/CCdh1-dependent proteolysis of USP1 regulates the response to UV-mediated DNA damage. J Cell Biol 2011; 194:177-86; PMID:21768287; http://dx.doi.org/10. 1083/jcb.201101062.
    • (2011) J Cell Biol , vol.194 , pp. 177-186
    • Cotto-Rios, X.M.1    Jones, M.J.2    Busino, L.3    Pagano, M.4    Huang, T.T.5
  • 61
    • 0038317575 scopus 로고    scopus 로고
    • Xkid is degraded in a D-box, KEN-box, and A-boxindependent pathway
    • PMID:12773557
    • Castro A, Vigneron S, Bernis C, Labbé JC, Lorca T. Xkid is degraded in a D-box, KEN-box, and A-boxindependent pathway. Mol Cell Biol 2003; 23:4126- 38; PMID:12773557; http://dx.doi.org/10.1128/MCB.23.12.4126-4138.2003.
    • (2003) Mol Cell Biol , vol.23 , pp. 4126-4138
    • Castro, A.1    Vigneron, S.2    Bernis, C.3    Labbé, J.C.4    Lorca, T.5
  • 62
    • 26944487640 scopus 로고    scopus 로고
    • A novel motif governs APC-dependent degradation of Drosophila ORC1 in vivo
    • PMID:16195415
    • Araki M, Yu H, Asano M. A novel motif governs APC-dependent degradation of Drosophila ORC1 in vivo. Genes Dev 2005; 19:2458-65; PMID:16195415; http://dx.doi.org/10.1101/gad.1361905.
    • (2005) Genes Dev , vol.19 , pp. 2458-2465
    • Araki, M.1    Yu, H.2    Asano, M.3
  • 63
    • 43049162227 scopus 로고    scopus 로고
    • Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex
    • PMID:18485873
    • Jin L, Williamson A, Banerjee S, Philipp I, Rape M. Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex. Cell 2008; 133:653- 65; PMID:18485873; http://dx.doi.org/10.1016/j.cell.2008.04.012.
    • (2008) Cell , vol.133 , pp. 653-665
    • Jin, L.1    Williamson, A.2    Banerjee, S.3    Philipp, I.4    Rape, M.5
  • 64
    • 19444378969 scopus 로고    scopus 로고
    • The WD40 propeller domain of Cdh1 functions as a destruction box receptor for APC/C substrates
    • PMID:15916961
    • Kraft C, Vodermaier HC, Maurer-Stroh S, Eisenhaber F, Peters JM. The WD40 propeller domain of Cdh1 functions as a destruction box receptor for APC/C substrates. Mol Cell 2005; 18:543-53; PMID:15916961; http://dx.doi.org/10.1016/ j.molcel.2005.04.023.
    • (2005) Mol Cell , vol.18 , pp. 543-553
    • Kraft, C.1    Vodermaier, H.C.2    Maurer-Stroh, S.3    Eisenhaber, F.4    Peters, J.M.5
  • 65
    • 84859750018 scopus 로고    scopus 로고
    • Regulation of APC/CCdc20 activity by RASSF1A-APC/CCdc20 circuitry
    • PMID:21874044
    • Chow C, Wong N, Pagano M, Lun SW, Nakayama KI, Nakayama K, et al. Regulation of APC/CCdc20 activity by RASSF1A-APC/CCdc20 circuitry. Oncogene 2012; 31:1975-87; PMID:21874044; http://dx.doi.org/10.1038/onc.2011.372.
    • (2012) Oncogene , vol.31 , pp. 1975-1987
    • Chow, C.1    Wong, N.2    Pagano, M.3    Lun, S.W.4    Nakayama, K.I.5    Nakayama, K.6
  • 66
    • 0038823615 scopus 로고    scopus 로고
    • Structure and enzymatic properties of a stable complex of the human REV1 and REV7 proteins
    • PMID:12529368
    • Masuda Y, Ohmae M, Masuda K, Kamiya K. Structure and enzymatic properties of a stable complex of the human REV1 and REV7 proteins. J Biol Chem 2003; 278:12356-60; PMID:12529368; http://dx.doi.org/10.1074/jbc.M211765200.
    • (2003) J Biol Chem , vol.278 , pp. 12356-12360
    • Masuda, Y.1    Ohmae, M.2    Masuda, K.3    Kamiya, K.4
  • 67
    • 0035929659 scopus 로고    scopus 로고
    • Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7
    • PMID:11485998
    • Murakumo Y, Ogura Y, Ishii H, Numata S, Ichihara M, Croce CM, et al. Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7. J Biol Chem 2001; 276:35644-51; PMID:11485998; http://dx.doi.org/10. 1074/jbc.M102051200.
    • (2001) J Biol Chem , vol.276 , pp. 35644-35651
    • Murakumo, Y.1    Ogura, Y.2    Ishii, H.3    Numata, S.4    Ichihara, M.5    Croce, C.M.6
  • 68
    • 84858608663 scopus 로고    scopus 로고
    • The vital role of polymerase ζ and REV1 in mutagenic, but not correct, DNA synthesis across benzo[a]pyrene-dG and recruitment of polymerase ζ by REV1 to replication-stalled site
    • PMID:22303021
    • Hashimoto K, Cho Y, Yang IY, Akagi J, Ohashi E, Tateishi S, et al. The vital role of polymerase ζ and REV1 in mutagenic, but not correct, DNA synthesis across benzo[a]pyrene-dG and recruitment of polymerase ζ by REV1 to replication-stalled site. J Biol Chem 2012; 287:9613-22; PMID:22303021; http://dx.doi.org/10.1074/jbc.M111.331728.
    • (2012) J Biol Chem , vol.287 , pp. 9613-9622
    • Hashimoto, K.1    Cho, Y.2    Yang, I.Y.3    Akagi, J.4    Ohashi, E.5    Tateishi, S.6
  • 69
    • 0021869226 scopus 로고
    • REV7, a new gene concerned with UV mutagenesis in yeast
    • PMID:3897794
    • Lawrence CW, Das G, Christensen RB. REV7, a new gene concerned with UV mutagenesis in yeast. Mol Gen Genet 1985; 200:80-5; PMID:3897794; http://dx.doi.org/10.1007/BF00383316.
    • (1985) Mol Gen Genet , vol.200 , pp. 80-85
    • Lawrence, C.W.1    Das, G.2    Christensen, R.B.3
  • 70
    • 0034676229 scopus 로고    scopus 로고
    • Alteration of ultravioletinduced mutagenesis in yeast through molecular modulation of the REV3 and REV7 gene expression
    • PMID:11018586
    • Rajpal DK, Wu X, Wang Z. Alteration of ultravioletinduced mutagenesis in yeast through molecular modulation of the REV3 and REV7 gene expression. Mutat Res 2000; 461:133-43; PMID:11018586; http://dx.doi.org/10.1016/S0921-8777(00) 00047-1.
    • (2000) Mutat Res , vol.461 , pp. 133-143
    • Rajpal, D.K.1    Wu, X.2    Wang, Z.3
  • 71
    • 0028027308 scopus 로고
    • Ubiquitindependent c-Jun degradation in vivo is mediated by the δ domain
    • PMID:8087846
    • Treier M, Staszewski LM, Bohmann D. Ubiquitindependent c-Jun degradation in vivo is mediated by the δ domain. Cell 1994; 78:787-98; PMID:8087846; http://dx.doi.org/10.1016/S0092-8674(94)90502-9.
    • (1994) Cell , vol.78 , pp. 787-798
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3
  • 72
    • 0038485578 scopus 로고    scopus 로고
    • Nuclear localization of the cell cycle regulator CDH1 and its regulation by phosphorylation
    • PMID:12560341
    • Zhou Y, Ching YP, Chun AC, Jin DY. Nuclear localization of the cell cycle regulator CDH1 and its regulation by phosphorylation. J Biol Chem 2003; 278:12530- 6; PMID:12560341; http://dx.doi.org/10.1074/jbc.M212853200.
    • (2003) J Biol Chem , vol.278 , pp. 12530-12536
    • Zhou, Y.1    Ching, Y.P.2    Chun, A.C.3    Jin, D.Y.4
  • 73
    • 0028306459 scopus 로고
    • Expression of achaete-scute homolog 3 in Xenopus embryos converts ectodermal cells to a neural fate
    • PMID:7926743
    • Turner DL, Weintraub H. Expression of achaete-scute homolog 3 in Xenopus embryos converts ectodermal cells to a neural fate. Genes Dev 1994; 8:1434- 47; PMID:7926743; http://dx.doi.org/10.1101/gad.8.12.1434.
    • (1994) Genes Dev , vol.8 , pp. 1434-1447
    • Turner, D.L.1    Weintraub, H.2
  • 74
    • 77951722696 scopus 로고    scopus 로고
    • N-linked glycosylation is required for optimal proteolytic activation of membrane-bound transcription factor CREB-H
    • PMID:20356926
    • Chan CP, Mak TY, Chin KT, Ng IOL, Jin DY. N-linked glycosylation is required for optimal proteolytic activation of membrane-bound transcription factor CREB-H. J Cell Sci 2010; 123:1438- 48; PMID:20356926; http://dx.doi.org/10.1242/jcs.067819.
    • (2010) J Cell Sci , vol.123 , pp. 1438-1448
    • Chan, C.P.1    Mak, T.Y.2    Chin, K.T.3    Ng, I.O.L.4    Jin, D.Y.5
  • 75
    • 0023003380 scopus 로고
    • Vivo half-life of a protein is a function of its amino-terminal residue
    • PMID:3018930
    • Bachmair A, Finley D, Varshavsky A. In vivo half-life of a protein is a function of its amino-terminal residue. Science 1986; 234:179-86; PMID:3018930; http://dx.doi.org/10.1126/science.3018930.
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.