메뉴 건너뛰기




Volumn 41, Issue 12, 2013, Pages 6098-6108

The 26S proteasome drives trinucleotide repeat expansions

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; PROTEASOME; REGULATOR PROTEIN; SEM1 PROTEIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 84880215877     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkt295     Document Type: Article
Times cited : (7)

References (77)
  • 1
    • 34547692622 scopus 로고    scopus 로고
    • Trinucleotide repeat disorders
    • Orr, H.T. and Zoghbi, H.Y. (2007) Trinucleotide repeat disorders. Annu. Rev. Neurosci., 30, 575-621.
    • (2007) Annu. Rev. Neurosci. , vol.30 , pp. 575-621
    • Orr, H.T.1    Zoghbi, H.Y.2
  • 2
    • 34250878426 scopus 로고    scopus 로고
    • Expandable DNA repeats and human disease
    • Mirkin, S.M. (2007) Expandable DNA repeats and human disease. Nature, 447, 932-940.
    • (2007) Nature , vol.447 , pp. 932-940
    • Mirkin, S.M.1
  • 3
    • 77649144557 scopus 로고    scopus 로고
    • Repeat instability as the basis for human diseases and as a potential target for therapy
    • Lopez Castel, A., Cleary, J.D. and Pearson, C.E. (2010) Repeat instability as the basis for human diseases and as a potential target for therapy. Nat. Rev. Mol. Cell. Biol., 11, 165-170.
    • (2010) Nat. Rev. Mol. Cell. Biol. , vol.11 , pp. 165-170
    • Lopez Castel, A.1    Cleary, J.D.2    Pearson, C.E.3
  • 4
    • 77958109197 scopus 로고    scopus 로고
    • Mechanisms of trinucleotide repeat instability during human development
    • McMurray, C.T. (2010) Mechanisms of trinucleotide repeat instability during human development. Nat. Rev. Genet., 11, 786-799.
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 786-799
    • McMurray, C.T.1
  • 5
    • 0029968460 scopus 로고    scopus 로고
    • Trinucleotide repeats in neurogenetic disorders
    • Paulson, H.L. and Fischbeck, K.H. (1996) Trinucleotide repeats in neurogenetic disorders. Annu. Rev. Neurosci., 19, 79-107.
    • (1996) Annu. Rev. Neurosci. , vol.19 , pp. 79-107
    • Paulson, H.L.1    Fischbeck, K.H.2
  • 6
    • 0242549824 scopus 로고    scopus 로고
    • DNA repair and trinucleotide repeat instability
    • Lahue, R.S. and Slater, D.L. (2003) DNA repair and trinucleotide repeat instability. Front. Biosci., 8, s553-s565.
    • (2003) Front. Biosci. , vol.8
    • Lahue, R.S.1    Slater, D.L.2
  • 7
    • 44949205290 scopus 로고    scopus 로고
    • Hijacking of the mismatch repair system to cause CAG expansion and cell death in neurodegenerative disease
    • McMurray, C.T. (2008) Hijacking of the mismatch repair system to cause CAG expansion and cell death in neurodegenerative disease. DNA Repair, 7, 1121-1134.
    • (2008) DNA Repair , vol.7 , pp. 1121-1134
    • McMurray, C.T.1
  • 8
    • 0032708840 scopus 로고    scopus 로고
    • Msh2 deficiency prevents in vivo somatic instability of the CAG repeat in Huntington disease transgenic mice
    • Manley, K., Shirley, T.L., Flaherty, L. and Messer, A. (1999) Msh2 deficiency prevents in vivo somatic instability of the CAG repeat in Huntington disease transgenic mice. Nat. Genet., 23, 471-473.
    • (1999) Nat. Genet. , vol.23 , pp. 471-473
    • Manley, K.1    Shirley, T.L.2    Flaherty, L.3    Messer, A.4
  • 9
    • 0035065524 scopus 로고    scopus 로고
    • Trinucleotide expansion in haploid germ cells by gap repair
    • Kovtun, I.V. and McMurray, C.T. (2001) Trinucleotide expansion in haploid germ cells by gap repair. Nat. Genet., 27, 407-411.
    • (2001) Nat. Genet. , vol.27 , pp. 407-411
    • Kovtun, I.V.1    McMurray, C.T.2
  • 10
    • 0037081784 scopus 로고    scopus 로고
    • Somatic expansion behaviour of the (CTG)n repeat in myotonic dystrophy knock-in mice is differentially affected by Msh3 and Msh6 mismatch-repair proteins
    • van den Broek, W.J., Nelen, M.R., Wansink, D.G., Coerwinkel, M.M., te Riele, H., Groenen, P.J. and Wieringa, B. (2002) Somatic expansion behaviour of the (CTG)n repeat in myotonic dystrophy knock-in mice is differentially affected by Msh3 and Msh6 mismatch-repair proteins. Hum. Mol. Genet., 11, 191-198.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 191-198
    • Van Den Broek, W.J.1    Nelen, M.R.2    Wansink, D.G.3    Coerwinkel, M.M.4    Te Riele, H.5    Groenen, P.J.6    Wieringa, B.7
  • 14
    • 4444323468 scopus 로고    scopus 로고
    • Pms2 is a genetic enhancer of trinucleotide CAG"CTG repeat somatic mosaicism: Implications for the mechanism of triplet repeat expansion
    • Gomes-Pereira, M., Fortune, M.T., Ingram, L., McAbney, J.P. and Monckton, D.G (2004) Pms2 is a genetic enhancer of trinucleotide CAG"CTG repeat somatic mosaicism: implications for the mechanism of triplet repeat expansion. Hum. Mol. Genet., 13, 1815-1825.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1815-1825
    • Gomes-Pereira, M.1    Fortune, M.T.2    Ingram, L.3    McAbney, J.P.4    Monckton, D.G.5
  • 15
    • 34249337762 scopus 로고    scopus 로고
    • OGG1 initiates age-dependent CAG trinucleotide expansion in somatic cells
    • Kovtun, I.V., Liu, Y., Bjoras, M., Klungland, A., Wilson, S.H. and McMurray, CT. (2007) OGG1 initiates age-dependent CAG trinucleotide expansion in somatic cells. Nature, 447, 447-452.
    • (2007) Nature , vol.447 , pp. 447-452
    • Kovtun, I.V.1    Liu, Y.2    Bjoras, M.3    Klungland, A.4    Wilson, S.H.5    McMurray, C.T.6
  • 16
    • 81855206487 scopus 로고    scopus 로고
    • Xpa deficiency reduces CAG trinucleotide repeat instability in neuronal tissues in a mouse model of SCA1
    • Hubert, L. Jr, Lin, Y., Dion, V. and Wilson, J.H. (2011) Xpa deficiency reduces CAG trinucleotide repeat instability in neuronal tissues in a mouse model of SCA1. Hum. Mol. Genet., 20, 4822-4830.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 4822-4830
    • Hubert, Jr.L.1    Lin, Y.2    Dion, V.3    Wilson, J.H.4
  • 18
    • 84869005181 scopus 로고    scopus 로고
    • MutSß and histone deacetylase complexes promote expansions of trinucleotide repeats in human cells
    • Gannon, A.M., Frizzell, A., Healy, E. and Lahue, R.S. (2012) MutSß and histone deacetylase complexes promote expansions of trinucleotide repeats in human cells. Nucleic Acids Res., 40, 10324-10333.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 10324-10333
    • Gannon, A.M.1    Frizzell, A.2    Healy, E.3    Lahue, R.S.4
  • 19
    • 84864687923 scopus 로고    scopus 로고
    • Histone deacetylase complexes as caretakers of genome stability
    • Lahue, R.S. and Frizzell, A. (2012) Histone deacetylase complexes as caretakers of genome stability. Epigenetics, 7, 806-810.
    • (2012) Epigenetics , vol.7 , pp. 806-810
    • Lahue, R.S.1    Frizzell, A.2
  • 20
    • 34548204316 scopus 로고    scopus 로고
    • Transcription-induced CAG repeat contraction in human cells is mediated in part by transcription-coupled nucleotide excision repair
    • Lin, Y. and Wilson, J.H. (2007) Transcription-induced CAG repeat contraction in human cells is mediated in part by transcription-coupled nucleotide excision repair. Mol. Cell. Biol., 27, 6209-6217.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 6209-6217
    • Lin, Y.1    Wilson, J.H.2
  • 21
    • 84867176120 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system of Saccharomyces cerevisiae
    • Finley, D., Ullrich, H.D., Sommer, T. and Kaiser, P. (2012) The ubiquitin-proteasome system of Saccharomyces cerevisiae. Genetics, 192, 319-360.
    • (2012) Genetics , vol.192 , pp. 319-360
    • Finley, D.1    Ullrich, H.D.2    Sommer, T.3    Kaiser, P.4
  • 22
    • 33846042439 scopus 로고    scopus 로고
    • Nucleotide excision repair and the ubiquitin proteasome pathway-do all roads lead to Rome?
    • Reed, S.H. and Gillette, T.G (2007) Nucleotide excision repair and the ubiquitin proteasome pathway-do all roads lead to Rome? DNA Repair, 6, 149-156.
    • (2007) DNA Repair , vol.6 , pp. 149-156
    • Reed, S.H.1    Gillette, T.G.2
  • 23
    • 0035947238 scopus 로고    scopus 로고
    • The 19S regulatory particle of the proteasome is required for efficient transcription elongation by RNA polymerase II
    • Ferdous, A., Gonzalez, F., Sun, L., Kodadek, T. and Johnston, SA. (2001) The 19S regulatory particle of the proteasome is required for efficient transcription elongation by RNA polymerase II. Mol. Cell, 7, 981-991.
    • (2001) Mol. Cell , vol.7 , pp. 981-991
    • Ferdous, A.1    Gonzalez, F.2    Sun, L.3    Kodadek, T.4    Johnston, S.A.5
  • 24
    • 77449127817 scopus 로고    scopus 로고
    • No Splicing, no dicing: Non-proteolytic roles of the ubiquitin-proteasome system in transcription
    • Kodadek, T. (2010) No Splicing, no dicing: non-proteolytic roles of the ubiquitin-proteasome system in transcription. J. Biol. Chem., 285, 2221-2226.
    • (2010) J. Biol. Chem. , vol.285 , pp. 2221-2226
    • Kodadek, T.1
  • 25
    • 79151480945 scopus 로고    scopus 로고
    • The proteasome and its regulatory roles in gene expression
    • Kwak, J., Workman, J.L. and Lee, D. (2011) The proteasome and its regulatory roles in gene expression. Biochim. Biophys. Acta, 1809, 88-96.
    • (2011) Biochim. Biophys. Acta , pp. 88-96
    • Kwak, J.1    Workman, J.L.2    Lee, D.3
  • 26
    • 27544486193 scopus 로고    scopus 로고
    • The proteasome regulatory particle alters the SAGA coactivator to enhance its interactions with transcriptional activators
    • Lee, D., Ezhkova, E., Li, B., Pattenden, S.G, Tansey, W.P. and Workman, J.L. (2005) The proteasome regulatory particle alters the SAGA coactivator to enhance its interactions with transcriptional activators. Cell, 123, 423-436.
    • (2005) Cell , vol.123 , pp. 423-436
    • Lee, D.1    Ezhkova, E.2    Li, B.3    Pattenden, S.G.4    Tansey, W.P.5    Workman, J.L.6
  • 27
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • Brachmann, C.B., Davies, A., Cost, GJ., Caputo, E., Li, J., Hieter, P. and Boeke, J.D. (1998) Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast, 14, 115-132.
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 28
    • 0028597439 scopus 로고
    • Analysis of Saccharomyces cerevisiae proteins induced by peroxide and superoxide stress
    • Jamieson, D.J., Rivers, S.L. and Stephen, D.W. (1995) Analysis of Saccharomyces cerevisiae proteins induced by peroxide and superoxide stress. Microbiology, 140, 3277-3283.
    • (1995) Microbiology , vol.140 , pp. 3277-3283
    • Jamieson, D.J.1    Rivers, S.L.2    Stephen, D.W.3
  • 29
    • 3042799223 scopus 로고    scopus 로고
    • Sem1p is a novel subunit of the 26 S proteasome from Saccharomyces cerevisiae
    • Sone, T., Saeki, Y., Toh-e, A. and Yokosawa, H. (2004) Sem1p is a novel subunit of the 26 S proteasome from Saccharomyces cerevisiae. J. Biol. Chem., 279, 28807-28816.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28807-28816
    • Sone, T.1    Saeki, Y.2    Toh-E, A.3    Yokosawa, H.4
  • 31
    • 4544305959 scopus 로고    scopus 로고
    • Genetic assays for triplet repeat instability in yeast
    • Dixon, M.J., Bhattacharyya, S. and Lahue, R.S. (2004) Genetic assays for triplet repeat instability in yeast. Methods Mol. Biol., 277, 29-45.
    • (2004) Methods Mol. Biol. , vol.277 , pp. 29-45
    • Dixon, M.J.1    Bhattacharyya, S.2    Lahue, R.S.3
  • 32
    • 0000870917 scopus 로고    scopus 로고
    • Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Saccharomyces cerevisiae J
    • Lee, D.H. and Goldberg, A.L. (1996) Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Saccharomyces cerevisiae J. Biol. Chem., 271, 27280-27284.
    • (1996) Biol. Chem. , vol.271 , pp. 27280-27284
    • Lee, D.H.1    Goldberg, A.L.2
  • 33
    • 0033026065 scopus 로고    scopus 로고
    • Interaction between the product of the breast cancer susceptibility gene BRCA2 and DSS1, a protein functionally conserved from yeast to mammals
    • Marston, N.J., Richards, W.J., Hughes, D., Bertwistle, D., Marshall, C.J. and Ashworth, A. (1999) Interaction between the product of the breast cancer susceptibility gene BRCA2 and DSS1, a protein functionally conserved from yeast to mammals. Mol. Cell. Biol., 19, 4633-4642.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4633-4642
    • Marston, N.J.1    Richards, W.J.2    Hughes, D.3    Bertwistle, D.4    Marshall, C.J.5    Ashworth, A.6
  • 36
    • 78649433314 scopus 로고    scopus 로고
    • Depletion of DSS1 protein disables homologous recombinational repair in human cells
    • Kristensen, C.N., Bystol, K.M., Serrano, L. and Brenneman, M.A. (2010) Depletion of DSS1 protein disables homologous recombinational repair in human cells. Mutat. Res., 694, 60-64.
    • (2010) Mutat. Res. , vol.694 , pp. 60-64
    • Kristensen, C.N.1    Bystol, K.M.2    Serrano, L.3    Brenneman, M.A.4
  • 38
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-delta delta C(T)) method
    • Livak, K.J. and Schmittgen, T.D. (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2(-delta delta C(T)) method. Methods, 25, 402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 39
    • 13544259975 scopus 로고    scopus 로고
    • Sem1, the yeast ortholog of a human BRCA2-binding protein, is a component of the proteasome regulatory particle that enhances proteasome stability
    • Funakoshi, M., Li, X., Velichutina, I., Hochstrasser, M. and Kobayashi, H. (2004) Sem1, the yeast ortholog of a human BRCA2-binding protein, is a component of the proteasome regulatory particle that enhances proteasome stability. J. Cell. Sci., 117, 6447-7457.
    • (2004) J. Cell. Sci. , vol.117 , pp. 6447-7457
    • Funakoshi, M.1    Li, X.2    Velichutina, I.3    Hochstrasser, M.4    Kobayashi, H.5
  • 43
    • 68349157358 scopus 로고    scopus 로고
    • PCI complexes: Beyond the proteasome, CNS, and eIF3 troika
    • Pick, E., Hoffman, K. and Glickman, M.H. (2009) PCI complexes: beyond the proteasome, CNS, and eIF3 troika. Mol. Cell, 35, 260-264.
    • (2009) Mol. Cell , vol.35 , pp. 260-264
    • Pick, E.1    Hoffman, K.2    Glickman, M.H.3
  • 44
    • 64549083597 scopus 로고    scopus 로고
    • Sem1p and Ubp6p orchestrate telomeric silencing by modulating histone H2B ubiquitination and H3 acetylation
    • Qin, S., Wang, Q., Ray, A., Wani, G., Zhao, Q., Bhaumik, S.R. and Wani, A.A. (2009) Sem1p and Ubp6p orchestrate telomeric silencing by modulating histone H2B ubiquitination and H3 acetylation. Nucleic Acids Res., 37, 1843-1853.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 1843-1853
    • Qin, S.1    Wang, Q.2    Ray, A.3    Wani, G.4    Zhao, Q.5    Bhaumik, S.R.6    Wani, A.A.7
  • 46
    • 64049087859 scopus 로고    scopus 로고
    • Sem1 is a functional component of the nuclear pore complex-associated messenger RNA export machinery
    • Faza, M.B., Kemmler, S., Jimeno, S., Gonzalez-Aguilera, C, Aguilera, A., Hurt, E. and Panse, V.G. (2009) Sem1 is a functional component of the nuclear pore complex-associated messenger RNA export machinery. J. Cell Biol., 184, 833-846.
    • (2009) J. Cell Biol. , vol.184 , pp. 833-846
    • Faza, M.B.1    Kemmler, S.2    Jimeno, S.3    Gonzalez-Aguilera, C.4    Aguilera, A.5    Hurt, E.6    Panse, V.G.7
  • 47
    • 1442264792 scopus 로고    scopus 로고
    • Plasticity in eucaryotic 20S proteasome ring assembly revealed by a subunit deletion in yeast
    • Velichutina, I., Connerly, P.L., Arendt, C.S., Li, X. and Hochstrasser, M. (2004) Plasticity in eucaryotic 20S proteasome ring assembly revealed by a subunit deletion in yeast. EMBO J., 23, 500-510.
    • (2004) EMBO J. , vol.23 , pp. 500-510
    • Velichutina, I.1    Connerly, P.L.2    Arendt, C.S.3    Li, X.4    Hochstrasser, M.5
  • 49
    • 0141680281 scopus 로고    scopus 로고
    • Derivation of a JC virus-resistant human glial cell line: Implications for the identification of host cell factors that determine viral tropism
    • Gee, GV., Manley, K. and Atwood, W.J. (2003) Derivation of a JC virus-resistant human glial cell line: implications for the identification of host cell factors that determine viral tropism. Virology, 314, 101-109.
    • (2003) Virology , vol.314 , pp. 101-109
    • Gee, G.V.1    Manley, K.2    Atwood, W.J.3
  • 50
    • 36248939736 scopus 로고    scopus 로고
    • Expansions of CAG"CTG repeats in immortalized human astrocytes
    • Claassen, DA. and Lahue, R.S. (2007) Expansions of CAG"CTG repeats in immortalized human astrocytes. Hum. Mol. Genet., 16, 3088-3096.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 3088-3096
    • Claassen, D.A.1    Lahue, R.S.2
  • 51
    • 34547628200 scopus 로고    scopus 로고
    • Proteasome function is required for DNA damage response and fanconi anemia pathway activation
    • Jacquemont, C. and Taniguchi, T. (2007) Proteasome function is required for DNA damage response and fanconi anemia pathway activation. Cancer Res., 67, 7395-7405.
    • (2007) Cancer Res. , vol.67 , pp. 7395-7405
    • Jacquemont, C.1    Taniguchi, T.2
  • 52
    • 0029739021 scopus 로고    scopus 로고
    • Mammalian Sug1 and c-Fos in the nuclear 26S proteasome
    • Wang, W., Chevray, P.M. and Nathans, D. (1996) Mammalian Sug1 and c-Fos in the nuclear 26S proteasome. Proc. Natl Acad. Sci. USA, 93, 8236-8240.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 8236-8240
    • Wang, W.1    Chevray, P.M.2    Nathans, D.3
  • 53
    • 0030061512 scopus 로고    scopus 로고
    • Identification of the gal4 suppressor Sug1 as a subunit of the yeast 26S proteasome
    • Rubin, D.M., Coux, O., Wefes, I., Hengartner, C, Young, RA., Goldberg, A.L. and Finley, D. (1996) Identification of the gal4 suppressor Sug1 as a subunit of the yeast 26S proteasome. Nature, 379, 655-657.
    • (1996) Nature , vol.379 , pp. 655-657
    • Rubin, D.M.1    Coux, O.2    Wefes, I.3    Hengartner, C.4    Young, R.A.5    Goldberg, A.L.6    Finley, D.7
  • 54
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux, O., Tanaka, K. and Goldberg, A.L. (1996) Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem., 65, 801-847.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 55
    • 33644854741 scopus 로고    scopus 로고
    • Inhibition of TRIP1/S8/hSug1, a component of the human 19S proteasome, enhances mitotic apoptosis induced by spindle poisons
    • Yamada, H.Y. and Gorbsky, GJ. (2006) Inhibition of TRIP1/S8/hSug1, a component of the human 19S proteasome, enhances mitotic apoptosis induced by spindle poisons. Mol. Cancer Ther., 5, 29-38.
    • (2006) Mol. Cancer Ther. , vol.5 , pp. 29-38
    • Yamada, H.Y.1    Gorbsky, G.J.2
  • 56
    • 73149110451 scopus 로고    scopus 로고
    • The 19S proteasome positively regulates histone methylation at cytokine inducible genes
    • Koues, O.I., Dudley, R.K., Mehta, N.T. and Greer, S.F. (2009) The 19S proteasome positively regulates histone methylation at cytokine inducible genes. Biochim. Biophys. Acta, 1789, 691-701.
    • (2009) Biochim. Biophys. Acta , vol.1789 , pp. 691-701
    • Koues, O.I.1    Dudley, R.K.2    Mehta, N.T.3    Greer, S.F.4
  • 57
    • 34249007126 scopus 로고    scopus 로고
    • A ubiquitin stress response induces altered proteasome composition
    • Hanna, J., Meides, A., Zhang, D.P. and Finley, D. (2007) A ubiquitin stress response induces altered proteasome composition. Cell, 129, 747-759.
    • (2007) Cell , vol.129 , pp. 747-759
    • Hanna, J.1    Meides, A.2    Zhang, D.P.3    Finley, D.4
  • 59
    • 0344629427 scopus 로고    scopus 로고
    • Ubiquitin depletion as a key mediator of toxicity by translational inhibitors
    • Hanna, J., Leggett, D.S. and Finley, D. (2003) Ubiquitin depletion as a key mediator of toxicity by translational inhibitors. Mol. Cell. Biol., 23, 9251-9261.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 9251-9261
    • Hanna, J.1    Leggett, D.S.2    Finley, D.3
  • 60
    • 2942620845 scopus 로고    scopus 로고
    • Regulatory mechanisms controlling biogenesis of ubiquitin and the proteasome
    • London, M.K., Keck, B.I., Ramos, P.C. and Dohmen, R.J. (2004) Regulatory mechanisms controlling biogenesis of ubiquitin and the proteasome. FEBS Lett., 567, 259-264.
    • (2004) FEBS Lett. , vol.567 , pp. 259-264
    • London, M.K.1    Keck, B.I.2    Ramos, P.C.3    Dohmen, R.J.4
  • 61
    • 0036295955 scopus 로고    scopus 로고
    • Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis
    • Saeki, Y., Saitoh, A., Toh-e, A. and Yokosawa, H. (2002) Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis. Biochem. Biophys. Res. Commun., 293, 986-992.
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 986-992
    • Saeki, Y.1    Saitoh, A.2    Toh-E, A.3    Yokosawa, H.4
  • 62
    • 3142566639 scopus 로고    scopus 로고
    • Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system
    • Verma, R., Oania, R., Graumann, J. and Deshaies, R.J. (2004) Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system. Cell, 118, 99-110.
    • (2004) Cell , vol.118 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 63
    • 77952741384 scopus 로고    scopus 로고
    • Functional differences between two major ubiquitin receptors in the proteasome; S5a and hRpn13
    • Elangovan, M., Oh, C, Sukumaran, L., Wojcik, C. and Yoo, Y.J. (2010) Functional differences between two major ubiquitin receptors in the proteasome; S5a and hRpn13. Biochem. Biophys. Res. Commun., 396, 425-428.
    • (2010) Biochem. Biophys. Res. Commun. , vol.396 , pp. 425-428
    • Elangovan, M.1    Oh, C.2    Sukumaran, L.3    Wojcik, C.4    Yoo, Y.J.5
  • 64
    • 52649175449 scopus 로고    scopus 로고
    • Regulation of acetylation at the major histocompatibility complex class II proximal promoter by the 19S proteasomal ATPase Sug1
    • Koues, O.I., Dudley, R.K., Truax, A.D., Gerhardt, D., Bhat, K.P., McNeal, S. and Greer, S.F. (2008) Regulation of acetylation at the major histocompatibility complex class II proximal promoter by the 19S proteasomal ATPase Sug1. Mol. Cell. Biol., 28, 5837-5850.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 5837-5850
    • Koues, O.I.1    Dudley, R.K.2    Truax, A.D.3    Gerhardt, D.4    Bhat, K.P.5    McNeal, S.6    Greer, S.F.7
  • 66
    • 33644521786 scopus 로고    scopus 로고
    • DSS1 is required for the stability of BRCA2
    • Li, J., Zou, C, Bai, Y., Wazer, D.E., Band, V. and Gao, Q. (2006) DSS1 is required for the stability of BRCA2. Oncogene, 25, 1186-1194.
    • (2006) Oncogene , vol.25 , pp. 1186-1194
    • Li, J.1    Zou, C.2    Bai, Y.3    Wazer, D.E.4    Band, V.5    Gao, Q.6
  • 67
    • 67650463334 scopus 로고    scopus 로고
    • The vital link between the ubiquitin-proteasome pathway and DNA repair: Impact on cancer therapy
    • Motegi, A., Murakawa, Y. and Takeda, S. (2009) The vital link between the ubiquitin-proteasome pathway and DNA repair: impact on cancer therapy. Cancer Lett., 283, 1-9.
    • (2009) Cancer Lett. , vol.283 , pp. 1-9
    • Motegi, A.1    Murakawa, Y.2    Takeda, S.3
  • 68
    • 84863872306 scopus 로고    scopus 로고
    • Protein degradation in DNA damage response
    • Kouranti, I. and Peyroche, A. (2012) Protein degradation in DNA damage response. Semin. Cell Dev. Biol., 23, 538-545.
    • (2012) Semin. Cell Dev. Biol. , vol.23 , pp. 538-545
    • Kouranti, I.1    Peyroche, A.2
  • 69
    • 34548775695 scopus 로고    scopus 로고
    • A persistent RNA.DNA hybrid formed by transcription of the Friedreich ataxia triplet repeat in live bacteria, and by T7 RNAP in vitro
    • Grabczyk, E., Mancuso, M. and Sammarco, M.C. (2007) A persistent RNA.DNA hybrid formed by transcription of the Friedreich ataxia triplet repeat in live bacteria, and by T7 RNAP in vitro. Nucleic Acids Res., 35, 5351-5359.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 5351-5359
    • Grabczyk, E.1    Mancuso, M.2    Sammarco, M.C.3
  • 72
    • 84860745933 scopus 로고    scopus 로고
    • The nucleotide sequence, DNA damage location, and protein stoichiometry influence the base excision repair outcome at CAG/CTG repeats
    • Goula, A.V., Pearson, C.E., Della Maria, J., Trottier, Y., Tomkinson, A.E., Wilson, D.M.III and Merienne, K. (2012) The nucleotide sequence, DNA damage location, and protein stoichiometry influence the base excision repair outcome at CAG/CTG repeats. Biochemistry, 51, 3919-3932.
    • (2012) Biochemistry , vol.51 , pp. 3919-3932
    • Goula, A.V.1    Pearson, C.E.2    Della Maria, J.3    Trottier, Y.4    Tomkinson, A.E.5    Wilson III, D.M.6    Merienne, K.7
  • 73
    • 20444428382 scopus 로고    scopus 로고
    • Multiple mechanisms confining RNA polymerase II ubiquitylation to polymerases undergoing transcriptional arrest
    • Somesh, B.P., Reid, J., Liu, W.F., Sogaard, T.M., Erdjument-Bromage, H., Tempst, P. and Svejstrup, J.Q. (2005) Multiple mechanisms confining RNA polymerase II ubiquitylation to polymerases undergoing transcriptional arrest. Cell, 121, 913-923.
    • (2005) Cell , vol.121 , pp. 913-923
    • Somesh, B.P.1    Reid, J.2    Liu, W.F.3    Sogaard, T.M.4    Erdjument-Bromage, H.5    Tempst, P.6    Svejstrup, J.Q.7
  • 74
    • 84867052175 scopus 로고    scopus 로고
    • Nucleotide excision repair, mismatch repair, and R-loops modulate convergent transcription-induced cell death and repeat instability
    • Lin, Y. and Wilson, J.H. (2012) Nucleotide excision repair, mismatch repair, and R-loops modulate convergent transcription-induced cell death and repeat instability. PLoS One, 7, e46807.
    • (2012) PLoS One , vol.7
    • Lin, Y.1    Wilson, J.H.2
  • 75
    • 84867386032 scopus 로고    scopus 로고
    • The Ubiquitin-Proteasome System in Huntington's disease: Are proteasomes impaired, initiators of disease, or coming to the rescue?
    • Article ID: 837015
    • Schipper-Krom, S., Juenemann, K. and Reits, E.A. (2012) The Ubiquitin-Proteasome System in Huntington's disease: are proteasomes impaired, initiators of disease, or coming to the rescue? Biochem. Res. Int., 2012, Article ID: 837015.
    • (2012) Biochem. Res. Int. , vol.2012
    • Schipper-Krom, S.1    Juenemann, K.2    Reits, E.A.3
  • 76
    • 84874713556 scopus 로고    scopus 로고
    • Regulation of feedback between protein kinase a and the proteasome system worsens Huntington's disease Mol
    • Lin, J.T., Chang, W.C., Chen, H.M., Lai, H.L., Chen, C.Y., Tao, M.H. and Chern, Y. (2013) Regulation of feedback between protein kinase a and the proteasome system worsens Huntington's disease Mol. Cell. Biol., 33, 1073-1084.
    • (2013) Cell. Biol. , vol.33 , pp. 1073-1084
    • Lin, J.T.1    Chang, W.C.2    Chen, H.M.3    Lai, H.L.4    Chen, C.Y.5    Tao, M.H.6    Chern, Y.7
  • 77
    • 84866988499 scopus 로고    scopus 로고
    • Ubiquitin-based anticancer therapy: Carpet bombing with proteasome inhibitors vs surgical strikes with E1, E2, E3, or DUB inhibitors
    • Mattern, M.R., Wu, J. and Nicholson, B. (2012) Ubiquitin-based anticancer therapy: carpet bombing with proteasome inhibitors vs surgical strikes with E1, E2, E3, or DUB inhibitors. Biochim. Biophys. Acta, 1823, 2014-2021.
    • (2012) Biochim. Biophys. Acta , pp. 2014-2021
    • Mattern, M.R.1    Wu, J.2    Nicholson, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.