메뉴 건너뛰기




Volumn 31, Issue 16, 2011, Pages 3396-3409

Molecular chaperone Hsp90 regulates REV1-mediated mutagenesis

Author keywords

[No Author keywords available]

Indexed keywords

CYCLINE; DNA POLYMERASE REV1; HEAT SHOCK PROTEIN 90; PROTEASOME;

EID: 79961165129     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.05117-11     Document Type: Article
Times cited : (32)

References (66)
  • 1
    • 63249113718 scopus 로고    scopus 로고
    • Interaction with DNA polymerase η is required for nuclear accumulation of REV1 and suppression of spontaneous mutations in human cells
    • Akagi, J., et al. 2009. Interaction with DNA polymerase η is required for nuclear accumulation of REV1 and suppression of spontaneous mutations in human cells. DNA Repair (Amst.) 8:585-599.
    • (2009) DNA Repair (Amst.) , vol.8 , pp. 585-599
    • Akagi, J.1
  • 2
    • 0347993069 scopus 로고    scopus 로고
    • Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress
    • Arlander, S. J., et al. 2003. Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress. J. Biol. Chem. 278:52572-52577.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52572-52577
    • Arlander, S.J.1
  • 3
    • 29144499065 scopus 로고    scopus 로고
    • Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis
    • Bienko, M., et al. 2005. Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis. Science 310:1821-1824.
    • (2005) Science , vol.310 , pp. 1821-1824
    • Bienko, M.1
  • 4
    • 75949122886 scopus 로고    scopus 로고
    • Regulation of translesion synthesis DNA polymerase η by monoubiquitination
    • Bienko, M., et al. 2010. Regulation of translesion synthesis DNA polymerase η by monoubiquitination. Mol. Cell 37:396-407.
    • (2010) Mol. Cell , vol.37 , pp. 396-407
    • Bienko, M.1
  • 5
    • 34547684065 scopus 로고    scopus 로고
    • HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination
    • Boyault, C., K. Sadoul, M. Pabion, and S. Khochbin. 2007. HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination. Oncogene 26:5468-5476.
    • (2007) Oncogene , vol.26 , pp. 5468-5476
    • Boyault, C.1    Sadoul, K.2    Pabion, M.3    Khochbin, S.4
  • 6
    • 55949125726 scopus 로고    scopus 로고
    • Human DNA polymerase η activity and translocation is regulated by phosphorylation
    • Chen, Y. W., et al. 2008. Human DNA polymerase η activity and translocation is regulated by phosphorylation. Proc. Natl. Acad. Sci. U. S. A. 105: 16578-16583.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 16578-16583
    • Chen, Y.W.1
  • 7
    • 10044275174 scopus 로고    scopus 로고
    • The role of DNA polymerase η in UV mutational spectra
    • Choi, J. H., and G. P. Pfeifer. 2005. The role of DNA polymerase η in UV mutational spectra. DNA Repair (Amst.) 4:211-220.
    • (2005) DNA Repair (Amst.) , vol.4 , pp. 211-220
    • Choi, J.H.1    Pfeifer, G.P.2
  • 8
    • 0344875492 scopus 로고    scopus 로고
    • Ribozyme-mediated REV1 inhibition reduces the frequency of UV-induced mutations in the human HPRT gene
    • Clark, D. R., W. Zacharias, L. Panaitescu, and W. G. McGregor. 2003. Ribozyme-mediated REV1 inhibition reduces the frequency of UV-induced mutations in the human HPRT gene. Nucleic Acids Res. 31:4981-4988.
    • (2003) Nucleic Acids Res , vol.31 , pp. 4981-4988
    • Clark, D.R.1    Zacharias, W.2    Panaitescu, L.3    McGregor, W.G.4
  • 10
    • 19444383801 scopus 로고    scopus 로고
    • Trading places: how do DNA polymerases switch during translesion DNA synthesis?
    • Friedberg, E. C., A. R. Lehmann, and R. P. Fuchs. 2005. Trading places: how do DNA polymerases switch during translesion DNA synthesis? Mol. Cell 18:499-505.
    • (2005) Mol. Cell , vol.18 , pp. 499-505
    • Friedberg, E.C.1    Lehmann, A.R.2    Fuchs, R.P.3
  • 11
    • 0141960298 scopus 로고    scopus 로고
    • Human proliferating cell nuclear antigen, poly(ADPribose) polymerase-1, and p21waf1/cip1
    • Frouin, I., et al. 2003. Human proliferating cell nuclear antigen, poly(ADPribose) polymerase-1, and p21waf1/cip1. A dynamic exchange of partners. J. Biol. Chem. 278:39265-39268.
    • (2003) A dynamic exchange of partners. J. Biol. Chem. , vol.278 , pp. 39265-39268
    • Frouin, I.1
  • 12
    • 0034636106 scopus 로고    scopus 로고
    • The function of the human homolog of Saccharomyces cerevisiae REV1 is required for mutagenesis induced by UV light
    • Gibbs, P. E., et al. 2000. The function of the human homolog of Saccharomyces cerevisiae REV1 is required for mutagenesis induced by UV light. Proc. Natl. Acad. Sci. U. S. A. 97:4186-4191.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 4186-4191
    • Gibbs, P.E.1
  • 13
    • 0345732688 scopus 로고    scopus 로고
    • Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis
    • Guo, C., et al. 2003. Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis. EMBO J. 22:6621-6630.
    • (2003) EMBO J , vol.22 , pp. 6621-6630
    • Guo, C.1
  • 15
    • 33746162368 scopus 로고    scopus 로고
    • REV1 protein interacts with PCNA: significance of the REV1 BRCT domain in vitro and in vivo
    • Guo, C., et al. 2006. REV1 protein interacts with PCNA: significance of the REV1 BRCT domain in vitro and in vivo. Mol. Cell 23:265-271.
    • (2006) Mol. Cell , vol.23 , pp. 265-271
    • Guo, C.1
  • 16
    • 33845223494 scopus 로고    scopus 로고
    • Ubiquitin-binding motifs in REV1 protein are required for its role in the tolerance of DNA damage
    • Guo, C., et al. 2006. Ubiquitin-binding motifs in REV1 protein are required for its role in the tolerance of DNA damage. Mol. Cell. Biol. 26:8892-8900.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 8892-8900
    • Guo, C.1
  • 17
    • 0037013287 scopus 로고    scopus 로고
    • Yeast Rev1 protein is a G template-specific DNA polymerase
    • Haracska, L., S. Prakash, and L. Prakash. 2002. Yeast Rev1 protein is a G template-specific DNA polymerase. J. Biol. Chem. 277:15546-15551.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15546-15551
    • Haracska, L.1    Prakash, S.2    Prakash, L.3
  • 18
    • 0035871360 scopus 로고    scopus 로고
    • Roles of yeast DNA polymerases δ and ζ and of Rev1 in the bypass of abasic sites
    • Haracska, L., et al. 2001. Roles of yeast DNA polymerases δ and ζ and of Rev1 in the bypass of abasic sites. Genes Dev. 15:945-954.
    • (2001) Genes Dev , vol.15 , pp. 945-954
    • Haracska, L.1
  • 19
    • 76749108600 scopus 로고    scopus 로고
    • Differential roles for DNA polymerases eta, zeta, and REV1 in lesion bypass of intrastrand versus interstrand DNA crosslinks
    • Hicks, J. K., et al. 2010. Differential roles for DNA polymerases eta, zeta, and REV1 in lesion bypass of intrastrand versus interstrand DNA crosslinks. Mol. Cell. Biol. 30:1217-1230.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 1217-1230
    • Hicks, J.K.1
  • 20
    • 33645008019 scopus 로고    scopus 로고
    • ATR homolog Mec1 controls association of DNA polymerase ζ-Rev1 complex with regions near a double-strand break
    • Hirano, Y., and K. Sugimoto. 2006. ATR homolog Mec1 controls association of DNA polymerase ζ-Rev1 complex with regions near a double-strand break. Curr. Biol. 16:586-590.
    • (2006) Curr. Biol. , vol.16 , pp. 586-590
    • Hirano, Y.1    Sugimoto, K.2
  • 21
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege, C., B. Pfander, G. L. Moldovan, G. Pyrowolakis, and S. Jentsch. 2002. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419:135-141.
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 22
    • 66349089259 scopus 로고    scopus 로고
    • Separate domains of Rev1 mediate two modes of DNA damage bypass in mammalian cells
    • Jansen, J. G., et al. 2009. Separate domains of Rev1 mediate two modes of DNA damage bypass in mammalian cells. Mol. Cell. Biol. 29:3113-3123.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 3113-3123
    • Jansen, J.G.1
  • 23
    • 13744257910 scopus 로고    scopus 로고
    • The BRCT domain of mammalian Rev1 is involved in regulating DNA translesion synthesis
    • Jansen, J. G., et al. 2005. The BRCT domain of mammalian Rev1 is involved in regulating DNA translesion synthesis. Nucleic Acids Res. 33:356-365.
    • (2005) Nucleic Acids Res , vol.33 , pp. 356-365
    • Jansen, J.G.1
  • 24
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
    • Kamal, A., et al. 2003. A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 425:407-410.
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1
  • 25
    • 2442417331 scopus 로고    scopus 로고
    • Interaction of human DNA polymerase η with monoubiquitinated PCNA: a possible mechanism for the polymerase switch in response to DNA damage
    • Kannouche, P. L., J. Wing, and A. R. Lehmann. 2004. Interaction of human DNA polymerase η with monoubiquitinated PCNA: a possible mechanism for the polymerase switch in response to DNA damage. Mol. Cell 14:491-500.
    • (2004) Mol. Cell , vol.14 , pp. 491-500
    • Kannouche, P.L.1    Wing, J.2    Lehmann, A.R.3
  • 26
    • 57749101303 scopus 로고    scopus 로고
    • Regulated proteolysis of DNA polymerase η during the DNA-damage response in C. elegans
    • Kim, S. H., and W. M. Michael. 2008. Regulated proteolysis of DNA polymerase _ during the DNA-damage response in C. elegans. Mol. Cell 32:757-766.
    • (2008) Mol. Cell , vol.32 , pp. 757-766
    • Kim, S.H.1    Michael, W.M.2
  • 27
    • 39149104625 scopus 로고    scopus 로고
    • Comparative analysis of in vivo interactions between Rev1 protein and other Y-family DNA polymerases in animals and yeasts
    • Kosarek, J. N., et al. 2008. Comparative analysis of in vivo interactions between Rev1 protein and other Y-family DNA polymerases in animals and yeasts. DNA Repair (Amst.) 7:439-451.
    • (2008) DNA Repair (Amst.) , vol.7 , pp. 439-451
    • Kosarek, J.N.1
  • 28
    • 34249941966 scopus 로고    scopus 로고
    • Translesion synthesis: Y-family polymerases and the polymerase switch
    • Lehmann, A. R., et al. 2007. Translesion synthesis: Y-family polymerases and the polymerase switch. DNA Repair (Amst.) 6:891-899.
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 891-899
    • Lehmann, A.R.1
  • 29
    • 33645812751 scopus 로고    scopus 로고
    • Human REV1 modulates the cytotoxicity and mutagenicity of cisplatin in human ovarian carcinoma cells
    • Lin, X., T. Okuda, J. Trang, and S. B. Howell. 2006. Human REV1 modulates the cytotoxicity and mutagenicity of cisplatin in human ovarian carcinoma cells. Mol. Pharmacol. 69:1748-1754.
    • (2006) Mol. Pharmacol. , vol.69 , pp. 1748-1754
    • Lin, X.1    Okuda, T.2    Trang, J.3    Howell, S.B.4
  • 30
    • 0037169495 scopus 로고    scopus 로고
    • Mechanisms of dCMP transferase reactions catalyzed by mouse Rev1 protein
    • Masuda, Y., M. Takahashi, S. Fukuda, M. Sumii, and K. Kamiya. 2002. Mechanisms of dCMP transferase reactions catalyzed by mouse Rev1 protein. J. Biol. Chem. 277:3040-3046.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3040-3046
    • Masuda, Y.1    Takahashi, M.2    Fukuda, S.3    Sumii, M.4    Kamiya, K.5
  • 31
    • 1242291789 scopus 로고    scopus 로고
    • CHIP: a link between the chaperone and proteasome systems
    • McDonough, H., and C. Patterson. 2003. CHIP: a link between the chaperone and proteasome systems. Cell Stress Chaperones 8:303-308.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 303-308
    • McDonough, H.1    Patterson, C.2
  • 32
    • 43849098620 scopus 로고    scopus 로고
    • The Fanconi anemia core complex is required for efficient point mutagenesis and Rev1 foci assembly
    • Mirchandani, K. D., R. M. McCaffrey, and A. D. D'Andrea. 2008. The Fanconi anemia core complex is required for efficient point mutagenesis and Rev1 foci assembly. DNA Repair (Amst.) 7:902-911.
    • (2008) DNA Repair (Amst.) , vol.7 , pp. 902-911
    • Mirchandani, K.D.1    McCaffrey, R.M.2    D'Andrea, A.D.3
  • 33
    • 10244232940 scopus 로고    scopus 로고
    • REV1 accumulates in DNA damage-induced nuclear foci in human cells and is implicated in mutagenesis by benzo[a]pyrenediolepoxide
    • Mukhopadhyay, S., D. R. Clark, N. B. Watson, W. Zacharias, and W. G. McGregor. 2004. REV1 accumulates in DNA damage-induced nuclear foci in human cells and is implicated in mutagenesis by benzo[a]pyrenediolepoxide. Nucleic Acids Res. 32:5820-5826.
    • (2004) Nucleic Acids Res , vol.32 , pp. 5820-5826
    • Mukhopadhyay, S.1    Clark, D.R.2    Watson, N.B.3    Zacharias, W.4    McGregor, W.G.5
  • 35
    • 0035929659 scopus 로고    scopus 로고
    • Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7
    • Murakumo, Y., et al. 2001. Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7. J. Biol. Chem. 276:35644-35651.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35644-35651
    • Murakumo, Y.1
  • 36
    • 0034635445 scopus 로고    scopus 로고
    • A human REV7 homolog that interacts with the polymerase η catalytic subunit hREV3 and the spindle assembly checkpoint protein hMAD2
    • Murakumo, Y., et al. 2000. A human REV7 homolog that interacts with the polymerase η catalytic subunit hREV3 and the spindle assembly checkpoint protein hMAD2. J. Biol. Chem. 275:4391-4397.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4391-4397
    • Murakumo, Y.1
  • 38
    • 0029787108 scopus 로고    scopus 로고
    • Deoxycytidyl transferase activity of yeast REV1 protein
    • Nelson, J. R., C. W. Lawrence, and D. C. Hinkle. 1996. Deoxycytidyl transferase activity of yeast REV1 protein. Nature 382:729-731.
    • (1996) Nature , vol.382 , pp. 729-731
    • Nelson, J.R.1    Lawrence, C.W.2    Hinkle, D.C.3
  • 39
    • 34249727193 scopus 로고    scopus 로고
    • Hsp90 regulates the Fanconi anemia DNA damage response pathway
    • Oda, T., T. Hayano, H. Miyaso, N. Takahashi, and T. Yamashita. 2007. Hsp90 regulates the Fanconi anemia DNA damage response pathway. Blood 109:5016-5026.
    • (2007) Blood , vol.109 , pp. 5016-5026
    • Oda, T.1    Hayano, T.2    Miyaso, H.3    Takahashi, N.4    Yamashita, T.5
  • 40
    • 41149103625 scopus 로고    scopus 로고
    • Rines/RNF180, a novel RING finger gene-encoded product, is a membrane-bound ubiquitin ligase
    • Ogawa, M., et al. 2008. Rines/RNF180, a novel RING finger gene-encoded product, is a membrane-bound ubiquitin ligase. Genes Cells 13:397-409.
    • (2008) Genes Cells , vol.13 , pp. 397-409
    • Ogawa, M.1
  • 41
    • 60849084453 scopus 로고    scopus 로고
    • Identification of a novel REV1-interacting motif necessary for DNA polymerase η function
    • Ohashi, E., et al. 2009. Identification of a novel REV1-interacting motif necessary for DNA polymerase η function. Genes Cells 14:101-111.
    • (2009) Genes Cells , vol.14 , pp. 101-111
    • Ohashi, E.1
  • 42
    • 3042812439 scopus 로고    scopus 로고
    • Interaction of hREV1 with three human Y-family DNA polymerases
    • Ohashi, E., et al. 2004. Interaction of hREV1 with three human Y-family DNA polymerases. Genes Cells 9:523-531.
    • (2004) Genes Cells , vol.9 , pp. 523-531
    • Ohashi, E.1
  • 43
    • 78049441698 scopus 로고    scopus 로고
    • Separate roles of structured and unstructured regions of Y-family DNA polymerases
    • Ohmori, H., T. Hanafusa, E. Ohashi, and C. Vaziri. 2009. Separate roles of structured and unstructured regions of Y-family DNA polymerases. Adv. Protein Chem. Struct. Biol. 78:99-146.
    • (2009) Adv. Protein Chem. Struct. Biol. , vol.78 , pp. 99-146
    • Ohmori, H.1    Hanafusa, T.2    Ohashi, E.3    Vaziri, C.4
  • 44
    • 67149110241 scopus 로고    scopus 로고
    • Role of DNA damage-induced replication checkpoint in promoting lesion bypass by translesion synthesis in yeast
    • Pages, V., S. R. Santa Maria, L. Prakash, and S. Prakash. 2009. Role of DNA damage-induced replication checkpoint in promoting lesion bypass by translesion synthesis in yeast. Genes Dev. 23:1438-1449.
    • (2009) Genes Dev , vol.23 , pp. 1438-1449
    • Pages, V.1    Santa Maria, S.R.2    Prakash, L.3    Prakash, S.4
  • 45
    • 0026637161 scopus 로고
    • A signature element distinguishes sibling and independent mutations in a shuttle vector plasmid
    • Parris, C. N., and M. M. Seidman. 1992. A signature element distinguishes sibling and independent mutations in a shuttle vector plasmid. Gene 117:1-5.
    • (1992) Gene , vol.117 , pp. 1-5
    • Parris, C.N.1    Seidman, M.M.2
  • 46
    • 41149111451 scopus 로고    scopus 로고
    • The Hsp90 molecular chaperone: an open and shut case for treatment
    • Pearl, L. H., C. Prodromou, and P. Workman. 2008. The Hsp90 molecular chaperone: an open and shut case for treatment. Biochem. J. 410:439-453.
    • (2008) Biochem. J. , vol.410 , pp. 439-453
    • Pearl, L.H.1    Prodromou, C.2    Workman, P.3
  • 47
    • 74449093973 scopus 로고    scopus 로고
    • A comprehensive catalogue of somatic mutations from a human cancer genome
    • Pleasance, E. D., et al. 2010. A comprehensive catalogue of somatic mutations from a human cancer genome. Nature 463:191-196.
    • (2010) Nature , vol.463 , pp. 191-196
    • Pleasance, E.D.1
  • 48
    • 74449085934 scopus 로고    scopus 로고
    • A small-cell lung cancer genome with complex signatures of tobacco exposure
    • Pleasance, E. D., et al. 2010. A small-cell lung cancer genome with complex signatures of tobacco exposure. Nature 463:184-190.
    • (2010) Nature , vol.463 , pp. 184-190
    • Pleasance, E.D.1
  • 49
    • 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
    • Sabbioneda, S., I. Bortolomai, M. Giannattasio, P. Plevani, and M. Muzi-Falconi. 2007. Yeast Rev1 is cell cycle regulated, phosphorylated in response to DNA damage and its binding to chromosomes is dependent upon MEC1. DNA Repair (Amst.) 6:121-127.
    • (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
  • 50
    • 74049129007 scopus 로고    scopus 로고
    • The molecular chaperone Hsp90 regulates accumulation of DNA polymerase η at replication stalling sites in UV-irradiated cells
    • Sekimoto, T., et al. 2010. The molecular chaperone Hsp90 regulates accumulation of DNA polymerase _ at replication stalling sites in UV-irradiated cells. Mol. Cell 37:79-89.
    • (2010) Mol. Cell , vol.37 , pp. 79-89
    • Sekimoto, T.1
  • 51
    • 60549096252 scopus 로고    scopus 로고
    • Two-polymerase mechanisms dictate error-free and error-prone translesion DNA synthesis in mammals
    • Shachar, S., et al. 2009. Two-polymerase mechanisms dictate error-free and error-prone translesion DNA synthesis in mammals. EMBO J. 28:383-393.
    • (2009) EMBO J , vol.28 , pp. 383-393
    • Shachar, S.1
  • 52
    • 33846640580 scopus 로고    scopus 로고
    • Polymerase eta is a short-lived, proteasomally degraded protein that is temporarily stabilized following UV irradiation in Saccharomyces cerevisiae
    • Skoneczna, A., J. McIntyre, M. Skoneczny, Z. Policinska, and E. Sledziewska-Gojska. 2007. Polymerase eta is a short-lived, proteasomally degraded protein that is temporarily stabilized following UV irradiation in Saccharomyces cerevisiae. J. Mol. Biol. 366:1074-1086.
    • (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
  • 53
    • 77953916528 scopus 로고    scopus 로고
    • HSP90 at the hub of protein homeostasis: emerging mechanistic insights
    • Taipale, M., D. F. Jarosz, and S. Lindquist. 2010. HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat. Rev. Mol. Cell Biol. 11:515-528.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 515-528
    • Taipale, M.1    Jarosz, D.F.2    Lindquist, S.3
  • 54
    • 73649125005 scopus 로고    scopus 로고
    • CRL4Cdt2 E3 ubiquitin ligase monoubiquitinates PCNA to promote translesion DNA synthesis
    • Terai, K., T. Abbas, A. A. Jazaeri, and A. Dutta. 2010. CRL4Cdt2 E3 ubiquitin ligase monoubiquitinates PCNA to promote translesion DNA synthesis. Mol. Cell 37:143-149.
    • (2010) Mol. Cell , vol.37 , pp. 143-149
    • Terai, K.1    Abbas, T.2    Jazaeri, A.A.3    Dutta, A.4
  • 55
    • 4544251295 scopus 로고    scopus 로고
    • Co-localization in replication foci and interaction of human Y-family members. DNA polymerase pol η and REVl protein
    • Tissier, A., et al. 2004. Co-localization in replication foci and interaction of human Y-family members, DNA polymerase pol η and REVl protein. DNA Repair (Amst.) 3:1503-1514.
    • (2004) DNA Repair (Amst.) , vol.3 , pp. 1503-1514
    • Tissier, A.1
  • 57
    • 6344288785 scopus 로고    scopus 로고
    • Rad18 guides polη to replication stalling sites through physical interaction and PCNA monoubiquitination
    • Watanabe, K., et al. 2004. Rad18 guides polη to replication stalling sites through physical interaction and PCNA monoubiquitination. EMBO J. 23: 3886-3896.
    • (2004) EMBO J , vol.23 , pp. 3886-3896
    • Watanabe, K.1
  • 58
    • 63849131910 scopus 로고    scopus 로고
    • Eukaryotic translesion polymerases and their roles and regulation in DNA damage tolerance
    • Waters, L. S., et al. 2009. Eukaryotic translesion polymerases and their roles and regulation in DNA damage tolerance. Microbiol. Mol. Biol. Rev. 73: 134-154.
    • (2009) Microbiol. Mol. Biol. Rev. , vol.73 , pp. 134-154
    • Waters, L.S.1
  • 59
    • 33745141184 scopus 로고    scopus 로고
    • The critical mutagenic translesion DNA polymerase Rev1 is highly expressed during G(2)/M phase rather than S phase
    • Waters, L. S., and G. C. Walker. 2006. The critical mutagenic translesion DNA polymerase Rev1 is highly expressed during G(2)/M phase rather than S phase. Proc. Natl. Acad. Sci. U. S. A. 103:8971-8976.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 8971-8976
    • Waters, L.S.1    Walker, G.C.2
  • 60
    • 79451475938 scopus 로고    scopus 로고
    • Proteasomal regulation of the mutagenic translesion DNA polymerase. Saccharomyces cerevisiae Rev1
    • Wiltrout, M. E., and G. C. Walker. 2011. Proteasomal regulation of the mutagenic translesion DNA polymerase, Saccharomyces cerevisiae Rev1. DNA Repair (Amst.) 10:169-175.
    • (2011) DNA Repair (Amst.) , vol.10 , pp. 169-175
    • Wiltrout, M.E.1    Walker, G.C.2
  • 61
    • 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
    • Wood, A., P. Garg, and P. M. Burgers. 2007. 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. 282:20256-20263.
    • (2007) J. Biol. Chem. , vol.282 , pp. 20256-20263
    • Wood, A.1    Garg, P.2    Burgers, P.M.3
  • 62
    • 78650580818 scopus 로고    scopus 로고
    • Error-prone translesion synthesis mediates acquired chemoresistance
    • Xie, K., J. Doles, M. T. Hemann, and G. C. Walker. 2010. Error-prone translesion synthesis mediates acquired chemoresistance. Proc. Natl. Acad. Sci. U. S. A. 107:20792-20797.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 20792-20797
    • Xie, K.1    Doles, J.2    Hemann, M.T.3    Walker, G.C.4
  • 63
    • 0036789884 scopus 로고    scopus 로고
    • Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu
    • Xu, W., et al. 2002. Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu. Proc. Natl. Acad. Sci. U. S. A. 99:12847-12852.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 12847-12852
    • Xu, W.1
  • 64
    • 35148815984 scopus 로고    scopus 로고
    • Hsp90 and the Fanconi anemia pathway: a molecular link between protein quality control and the DNA damage response
    • Yamashita, T., T. Oda, and T. Sekimoto. 2007. Hsp90 and the Fanconi anemia pathway: a molecular link between protein quality control and the DNA damage response. Cell Cycle 6:2232-2235.
    • (2007) Cell Cycle , vol.6 , pp. 2232-2235
    • Yamashita, T.1    Oda, T.2    Sekimoto, T.3
  • 65
    • 0036529562 scopus 로고    scopus 로고
    • Response of human REV1 to different DNA damage: preferential dCMP insertion opposite the lesion
    • Zhang, Y., et al. 2002. Response of human REV1 to different DNA damage: preferential dCMP insertion opposite the lesion. Nucleic Acids Res. 30: 1630-1638.
    • (2002) Nucleic Acids Res , vol.30 , pp. 1630-1638
    • Zhang, Y.1
  • 66
    • 67650928194 scopus 로고    scopus 로고
    • DNA polymerase ζ cooperates with polymerases k and ι in translesion DNA synthesis across pyrimidine photodimers in cells from XPV patients
    • Ziv, O., N. Geacintov, S. Nakajima, A. Yasui, and Z. Livneh. 2009. DNA polymerase ζ cooperates with polymerases k and ι in translesion DNA synthesis across pyrimidine photodimers in cells from XPV patients. Proc. Natl. Acad. Sci. U. S. A. 106:11552-11557.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 11552-11557
    • Ziv, O.1    Geacintov, N.2    Nakajima, S.3    Yasui, A.4    Livneh, Z.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.