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Volumn 154, Issue 5, 2013, Pages

XProteasome-mediated processing of Def1, a critical step in the cellular response to transcription stress

Author keywords

[No Author keywords available]

Indexed keywords

CULLIN; ELA1 PROTEIN; ELONGIN; PROTEASOME; PROTEIN; PROTEIN DEF1; RNA POLYMERASE II; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84883405887     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2013.07.028     Document Type: Article
Times cited : (65)

References (70)
  • 1
    • 35748950163 scopus 로고    scopus 로고
    • Damage-induced ubiquitylation of human RNA polymerase II by the ubiquitin ligase Nedd4, but not Cockayne syndrome proteins or BRCA1
    • R. Anindya, O. Aygün, and J.Q. Svejstrup Damage-induced ubiquitylation of human RNA polymerase II by the ubiquitin ligase Nedd4, but not Cockayne syndrome proteins or BRCA1 Mol. Cell 28 2007 386 397
    • (2007) Mol. Cell , vol.28 , pp. 386-397
    • Anindya, R.1    Aygün, O.2    Svejstrup, J.Q.3
  • 3
    • 0029084914 scopus 로고
    • Elongin (SIII): A multisubunit regulator of elongation by RNA polymerase II
    • T. Aso, W.S. Lane, J.W. Conaway, and R.C. Conaway Elongin (SIII): a multisubunit regulator of elongation by RNA polymerase II Science 269 1995 1439 1443
    • (1995) Science , vol.269 , pp. 1439-1443
    • Aso, T.1    Lane, W.S.2    Conaway, J.W.3    Conaway, R.C.4
  • 4
    • 84890243576 scopus 로고    scopus 로고
    • The ubiquitin proteasome system - Implications for cell cycle control and the targeted treatment of cancer
    • 10.1016/j.bbamcr.2013.02.028
    • F. Bassermann, R. Eichner, and M. Pagano The ubiquitin proteasome system - implications for cell cycle control and the targeted treatment of cancer Biochim. Biophys. Acta 2013 10.1016/j.bbamcr.2013.02.028
    • (2013) Biochim. Biophys. Acta
    • Bassermann, F.1    Eichner, R.2    Pagano, M.3
  • 5
    • 0032827035 scopus 로고    scopus 로고
    • Rsp5 ubiquitin-protein ligase mediates DNA damage-induced degradation of the large subunit of RNA polymerase II in Saccharomyces cerevisiae
    • S.L. Beaudenon, M.R. Huacani, G. Wang, D.P. McDonnell, and J.M. Huibregtse Rsp5 ubiquitin-protein ligase mediates DNA damage-induced degradation of the large subunit of RNA polymerase II in Saccharomyces cerevisiae Mol. Cell. Biol. 19 1999 6972 6979
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6972-6979
    • Beaudenon, S.L.1    Huacani, M.R.2    Wang, G.3    McDonnell, D.P.4    Huibregtse, J.M.5
  • 6
    • 77649165394 scopus 로고    scopus 로고
    • Maintaining genome stability at the replication fork
    • D. Branzei, and M. Foiani Maintaining genome stability at the replication fork Nat. Rev. Mol. Cell Biol. 11 2010 208 219
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 208-219
    • Branzei, D.1    Foiani, M.2
  • 8
    • 36749039152 scopus 로고    scopus 로고
    • Analysis of a predicted nuclear localization signal: Implications for the intracellular localization and function of the Saccharomyces cerevisiae RNA-binding protein Scp160
    • M.A. Brykailo, L.M. McLane, J. Fridovich-Keil, and A.H. Corbett Analysis of a predicted nuclear localization signal: implications for the intracellular localization and function of the Saccharomyces cerevisiae RNA-binding protein Scp160 Nucleic Acids Res. 35 2007 6862 6869
    • (2007) Nucleic Acids Res. , vol.35 , pp. 6862-6869
    • Brykailo, M.A.1    McLane, L.M.2    Fridovich-Keil, J.3    Corbett, A.H.4
  • 9
    • 79954464577 scopus 로고    scopus 로고
    • Expanded polyglutamine domain possesses nuclear export activity which modulates subcellular localization and toxicity of polyQ disease protein via exportin-1
    • W.M. Chan, H. Tsoi, C.C. Wu, C.H. Wong, T.C. Cheng, H.Y. Li, K.F. Lau, P.C. Shaw, N. Perrimon, and H.Y. Chan Expanded polyglutamine domain possesses nuclear export activity which modulates subcellular localization and toxicity of polyQ disease protein via exportin-1 Hum. Mol. Genet. 20 2011 1738 1750
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 1738-1750
    • Chan, W.M.1    Tsoi, H.2    Wu, C.C.3    Wong, C.H.4    Cheng, T.C.5    Li, H.Y.6    Lau, K.F.7    Shaw, P.C.8    Perrimon, N.9    Chan, H.Y.10
  • 10
    • 21644449682 scopus 로고    scopus 로고
    • Def1p is involved in telomere maintenance in budding yeast
    • Y.B. Chen, C.P. Yang, R.X. Li, R. Zeng, and J.Q. Zhou Def1p is involved in telomere maintenance in budding yeast J. Biol. Chem. 280 2005 24784 24791
    • (2005) J. Biol. Chem. , vol.280 , pp. 24784-24791
    • Chen, Y.B.1    Yang, C.P.2    Li, R.X.3    Zeng, R.4    Zhou, J.Q.5
  • 11
    • 78149313167 scopus 로고    scopus 로고
    • Combined chemical and genetic approach to inhibit proteolysis by the proteasome
    • G.A. Collins, T.A. Gomez, R.J. Deshaies, and W.P. Tansey Combined chemical and genetic approach to inhibit proteolysis by the proteasome Yeast 27 2010 965 974
    • (2010) Yeast , vol.27 , pp. 965-974
    • Collins, G.A.1    Gomez, T.A.2    Deshaies, R.J.3    Tansey, W.P.4
  • 12
  • 13
    • 84872422245 scopus 로고    scopus 로고
    • Transcription coupled repair at the interface between transcription elongation and mRNP biogenesis
    • H. Gaillard, and A. Aguilera Transcription coupled repair at the interface between transcription elongation and mRNP biogenesis Biochim. Biophys. Acta 1829 2013 141 150
    • (2013) Biochim. Biophys. Acta , vol.1829 , pp. 141-150
    • Gaillard, H.1    Aguilera, A.2
  • 15
    • 0029121296 scopus 로고
    • Nuclear export signals and the fast track to the cytoplasm
    • L. Gerace Nuclear export signals and the fast track to the cytoplasm Cell 82 1995 341 344
    • (1995) Cell , vol.82 , pp. 341-344
    • Gerace, L.1
  • 17
    • 84869083002 scopus 로고    scopus 로고
    • RNA polymerase II collision interrupts convergent transcription
    • D.J. Hobson, W. Wei, L.M. Steinmetz, and J.Q. Svejstrup RNA polymerase II collision interrupts convergent transcription Mol. Cell 48 2012 365 374
    • (2012) Mol. Cell , vol.48 , pp. 365-374
    • Hobson, D.J.1    Wei, W.2    Steinmetz, L.M.3    Svejstrup, J.Q.4
  • 18
    • 63049096813 scopus 로고    scopus 로고
    • Ubiquitin-binding domains and their role in the DNA damage response
    • K. Hofmann Ubiquitin-binding domains and their role in the DNA damage response DNA Repair (Amst.) 8 2009 544 556
    • (2009) DNA Repair (Amst.) , vol.8 , pp. 544-556
    • Hofmann, K.1
  • 19
    • 0034268493 scopus 로고    scopus 로고
    • Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing
    • T. Hoppe, K. Matuschewski, M. Rape, S. Schlenker, H.D. Ulrich, and S. Jentsch Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing Cell 102 2000 577 586
    • (2000) Cell , vol.102 , pp. 577-586
    • Hoppe, T.1    Matuschewski, K.2    Rape, M.3    Schlenker, S.4    Ulrich, H.D.5    Jentsch, S.6
  • 21
    • 0030888109 scopus 로고    scopus 로고
    • The large subunit of RNA polymerase II is a substrate of the Rsp5 ubiquitin-protein ligase
    • J.M. Huibregtse, J.C. Yang, and S.L. Beaudenon The large subunit of RNA polymerase II is a substrate of the Rsp5 ubiquitin-protein ligase Proc. Natl. Acad. Sci. USA 94 1997 3656 3661
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3656-3661
    • Huibregtse, J.M.1    Yang, J.C.2    Beaudenon, S.L.3
  • 22
    • 33947726050 scopus 로고    scopus 로고
    • CRM1-mediated nuclear export: To the pore and beyond
    • S. Hutten, and R.H. Kehlenbach CRM1-mediated nuclear export: to the pore and beyond Trends Cell Biol. 17 2007 193 201
    • (2007) Trends Cell Biol. , vol.17 , pp. 193-201
    • Hutten, S.1    Kehlenbach, R.H.2
  • 23
    • 56249108370 scopus 로고    scopus 로고
    • Ubiquitin-independent degradation of proteins by the proteasome
    • I. Jariel-Encontre, G. Bossis, and M. Piechaczyk Ubiquitin-independent degradation of proteins by the proteasome Biochim. Biophys. Acta 1786 2008 153 177
    • (2008) Biochim. Biophys. Acta , vol.1786 , pp. 153-177
    • Jariel-Encontre, I.1    Bossis, G.2    Piechaczyk, M.3
  • 24
    • 37749054981 scopus 로고    scopus 로고
    • Novel roles for selected genes in meiotic DNA processing
    • P.W. Jordan, F. Klein, and D.R. Leach Novel roles for selected genes in meiotic DNA processing PLoS Genet. 3 2007 e222
    • (2007) PLoS Genet. , vol.3 , pp. 222
    • Jordan, P.W.1    Klein, F.2    Leach, D.R.3
  • 25
    • 22744456248 scopus 로고    scopus 로고
    • The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme
    • Y. Kee, N. Lyon, and J.M. Huibregtse The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme EMBO J. 24 2005 2414 2424
    • (2005) EMBO J. , vol.24 , pp. 2414-2424
    • Kee, Y.1    Lyon, N.2    Huibregtse, J.M.3
  • 27
    • 60849126138 scopus 로고    scopus 로고
    • Modification by single ubiquitin moieties rather than polyubiquitination is sufficient for proteasomal processing of the p105 NF-kappaB precursor
    • Y. Kravtsova-Ivantsiv, S. Cohen, and A. Ciechanover Modification by single ubiquitin moieties rather than polyubiquitination is sufficient for proteasomal processing of the p105 NF-kappaB precursor Mol. Cell 33 2009 496 504
    • (2009) Mol. Cell , vol.33 , pp. 496-504
    • Kravtsova-Ivantsiv, Y.1    Cohen, S.2    Ciechanover, A.3
  • 28
    • 0034733591 scopus 로고    scopus 로고
    • Rapid and reliable protein extraction from yeast
    • V.V. Kushnirov Rapid and reliable protein extraction from yeast Yeast 16 2000 857 860
    • (2000) Yeast , vol.16 , pp. 857-860
    • Kushnirov, V.V.1
  • 29
    • 0029994329 scopus 로고    scopus 로고
    • A protein that shuttles between the nucleus and the cytoplasm is an important mediator of RNA export
    • M.S. Lee, M. Henry, and P.A. Silver A protein that shuttles between the nucleus and the cytoplasm is an important mediator of RNA export Genes Dev. 10 1996 1233 1246
    • (1996) Genes Dev. , vol.10 , pp. 1233-1246
    • Lee, M.S.1    Henry, M.2    Silver, P.A.3
  • 30
    • 0034630317 scopus 로고    scopus 로고
    • Apoptotic DNA fragmentation
    • S. Nagata Apoptotic DNA fragmentation Exp. Cell Res. 256 2000 12 18
    • (2000) Exp. Cell Res. , vol.256 , pp. 12-18
    • Nagata, S.1
  • 32
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B
    • V.J. Palombella, O.J. Rando, A.L. Goldberg, and T. Maniatis The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B Cell 78 1994 773 785
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 33
    • 33646270662 scopus 로고    scopus 로고
    • Sonic hedgehog signaling regulates Gli2 transcriptional activity by suppressing its processing and degradation
    • Y. Pan, C.B. Bai, A.L. Joyner, and B. Wang Sonic hedgehog signaling regulates Gli2 transcriptional activity by suppressing its processing and degradation Mol. Cell. Biol. 26 2006 3365 3377
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3365-3377
    • Pan, Y.1    Bai, C.B.2    Joyner, A.L.3    Wang, B.4
  • 34
    • 33746786326 scopus 로고    scopus 로고
    • Proteasome-mediated protein processing by bidirectional degradation initiated from an internal site
    • W. Piwko, and S. Jentsch Proteasome-mediated protein processing by bidirectional degradation initiated from an internal site Nat. Struct. Mol. Biol. 13 2006 691 697
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 691-697
    • Piwko, W.1    Jentsch, S.2
  • 35
    • 0036713442 scopus 로고    scopus 로고
    • Novel domains and orthologues of eukaryotic transcription elongation factors
    • C.P. Ponting Novel domains and orthologues of eukaryotic transcription elongation factors Nucleic Acids Res. 30 2002 3643 3652
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3643-3652
    • Ponting, C.P.1
  • 36
    • 0036091848 scopus 로고    scopus 로고
    • Taking a bite: Proteasomal protein processing
    • M. Rape, and S. Jentsch Taking a bite: proteasomal protein processing Nat. Cell Biol. 4 2002 E113 E116
    • (2002) Nat. Cell Biol. , vol.4
    • Rape, M.1    Jentsch, S.2
  • 37
    • 0035977095 scopus 로고    scopus 로고
    • Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone
    • M. Rape, T. Hoppe, I. Gorr, M. Kalocay, H. Richly, and S. Jentsch Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone Cell 107 2001 667 677
    • (2001) Cell , vol.107 , pp. 667-677
    • Rape, M.1    Hoppe, T.2    Gorr, I.3    Kalocay, M.4    Richly, H.5    Jentsch, S.6
  • 38
    • 3142691854 scopus 로고    scopus 로고
    • DNA damage-induced Def1-RNA polymerase II interaction and Def1 requirement for polymerase ubiquitylation in vitro
    • J. Reid, and J.Q. Svejstrup DNA damage-induced Def1-RNA polymerase II interaction and Def1 requirement for polymerase ubiquitylation in vitro J. Biol. Chem. 279 2004 29875 29878
    • (2004) J. Biol. Chem. , vol.279 , pp. 29875-29878
    • Reid, J.1    Svejstrup, J.Q.2
  • 39
    • 33646883307 scopus 로고    scopus 로고
    • Requirement of ELC1 for RNA polymerase II polyubiquitylation and degradation in response to DNA damage in Saccharomyces cerevisiae
    • B. Ribar, L. Prakash, and S. Prakash Requirement of ELC1 for RNA polymerase II polyubiquitylation and degradation in response to DNA damage in Saccharomyces cerevisiae Mol. Cell. Biol. 26 2006 3999 4005
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3999-4005
    • Ribar, B.1    Prakash, L.2    Prakash, S.3
  • 40
    • 34147193817 scopus 로고    scopus 로고
    • ELA1 and CUL3 are required along with ELC1 for RNA polymerase II polyubiquitylation and degradation in DNA-damaged yeast cells
    • B. Ribar, L. Prakash, and S. Prakash ELA1 and CUL3 are required along with ELC1 for RNA polymerase II polyubiquitylation and degradation in DNA-damaged yeast cells Mol. Cell. Biol. 27 2007 3211 3216
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 3211-3216
    • Ribar, B.1    Prakash, L.2    Prakash, S.3
  • 41
    • 34250900335 scopus 로고    scopus 로고
    • Lessons from 50 years of SOS DNA-damage-induced mutagenesis
    • K. Schlacher, and M.F. Goodman Lessons from 50 years of SOS DNA-damage-induced mutagenesis Nat. Rev. Mol. Cell Biol. 8 2007 587 594
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 587-594
    • Schlacher, K.1    Goodman, M.F.2
  • 42
    • 0345616428 scopus 로고    scopus 로고
    • A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain
    • S.C. Shih, G. Prag, S.A. Francis, M.A. Sutanto, J.H. Hurley, and L. Hicke A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain EMBO J. 22 2003 1273 1281
    • (2003) EMBO J. , vol.22 , pp. 1273-1281
    • Shih, S.C.1    Prag, G.2    Francis, S.A.3    Sutanto, M.A.4    Hurley, J.H.5    Hicke, L.6
  • 43
    • 77950998789 scopus 로고    scopus 로고
    • Evidence that transcript cleavage is essential for RNA polymerase II transcription and cell viability
    • S. Sigurdsson, A.B. Dirac-Svejstrup, and J.Q. Svejstrup Evidence that transcript cleavage is essential for RNA polymerase II transcription and cell viability Mol. Cell 38 2010 202 210
    • (2010) Mol. Cell , vol.38 , pp. 202-210
    • Sigurdsson, S.1    Dirac-Svejstrup, A.B.2    Svejstrup, J.Q.3
  • 44
    • 20444428382 scopus 로고    scopus 로고
    • Multiple mechanisms confining RNA polymerase II ubiquitylation to polymerases undergoing transcriptional arrest
    • B.P. Somesh, J. Reid, W.F. Liu, T.M. Søgaard, H. Erdjument-Bromage, P. Tempst, and J.Q. Svejstrup Multiple mechanisms confining RNA polymerase II ubiquitylation to polymerases undergoing transcriptional arrest Cell 121 2005 913 923
    • (2005) Cell , vol.121 , pp. 913-923
    • Somesh, B.P.1    Reid, J.2    Liu, W.F.3    Søgaard, T.M.4    Erdjument-Bromage, H.5    Tempst, P.6    Svejstrup, J.Q.7
  • 45
    • 33947720525 scopus 로고    scopus 로고
    • Communication between distant sites in RNA polymerase II through ubiquitylation factors and the polymerase CTD
    • B.P. Somesh, S. Sigurdsson, H. Saeki, H. Erdjument-Bromage, P. Tempst, and J.Q. Svejstrup Communication between distant sites in RNA polymerase II through ubiquitylation factors and the polymerase CTD Cell 129 2007 57 68
    • (2007) Cell , vol.129 , pp. 57-68
    • Somesh, B.P.1    Sigurdsson, S.2    Saeki, H.3    Erdjument-Bromage, H.4    Tempst, P.5    Svejstrup, J.Q.6
  • 46
    • 0034913423 scopus 로고    scopus 로고
    • Importin-beta-like nuclear transport receptors
    • REVIEWS3008
    • A.C. Ström, and K. Weis Importin-beta-like nuclear transport receptors Genome Biol. 2 2001 REVIEWS3008
    • (2001) Genome Biol. , vol.2
    • Ström, A.C.1    Weis, K.2
  • 48
    • 77954759085 scopus 로고    scopus 로고
    • The interface between transcription and mechanisms maintaining genome integrity
    • J.Q. Svejstrup The interface between transcription and mechanisms maintaining genome integrity Trends Biochem. Sci. 35 2010 333 338
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 333-338
    • Svejstrup, J.Q.1
  • 49
    • 0032560478 scopus 로고    scopus 로고
    • A member of the Ran-binding protein family, yrb2p, is involved in nuclear protein export
    • T. Taura, H. Krebber, and P.A. Silver A member of the Ran-binding protein family, yrb2p, is involved in nuclear protein export Proc. Natl. Acad. Sci. USA 95 1998 7427 7432
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7427-7432
    • Taura, T.1    Krebber, H.2    Silver, P.A.3
  • 53
    • 23144449208 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-like proteins as multifunctional signals
    • R.L. Welchman, C. Gordon, and R.J. Mayer Ubiquitin and ubiquitin-like proteins as multifunctional signals Nat. Rev. Mol. Cell Biol. 6 2005 599 609
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 599-609
    • Welchman, R.L.1    Gordon, C.2    Mayer, R.J.3
  • 55
    • 84872414012 scopus 로고    scopus 로고
    • Ubiquitylation and degradation of elongating RNA polymerase II: The last resort
    • M.D. Wilson, M. Harreman, and J.Q. Svejstrup Ubiquitylation and degradation of elongating RNA polymerase II: the last resort Biochim. Biophys. Acta 1829 2013 151 157
    • (2013) Biochim. Biophys. Acta , vol.1829 , pp. 151-157
    • Wilson, M.D.1    Harreman, M.2    Svejstrup, J.Q.3
  • 57
    • 58049200543 scopus 로고    scopus 로고
    • Mammalian Elongin A complex mediates DNA-damage-induced ubiquitylation and degradation of Rpb1
    • T. Yasukawa, T. Kamura, S. Kitajima, R.C. Conaway, J.W. Conaway, and T. Aso Mammalian Elongin A complex mediates DNA-damage-induced ubiquitylation and degradation of Rpb1 EMBO J. 27 2008 3256 3266
    • (2008) EMBO J. , vol.27 , pp. 3256-3266
    • Yasukawa, T.1    Kamura, T.2    Kitajima, S.3    Conaway, R.C.4    Conaway, J.W.5    Aso, T.6
  • 58
    • 0029047324 scopus 로고
    • A conditional allele of the novel repeat-containing yeast nucleoporin RAT7/NUP159 causes both rapid cessation of mRNA export and reversible clustering of nuclear pore complexes
    • L.C. Gorsch, T.C. Dockendorff, and C.N. Cole A conditional allele of the novel repeat-containing yeast nucleoporin RAT7/NUP159 causes both rapid cessation of mRNA export and reversible clustering of nuclear pore complexes J. Cell Biol. 129 1995 939 955
    • (1995) J. Cell Biol. , vol.129 , pp. 939-955
    • Gorsch, L.C.1    Dockendorff, T.C.2    Cole, C.N.3
  • 59
    • 58649104923 scopus 로고    scopus 로고
    • An iron-sulfur cluster domain in Elp3 important for the structural integrity of elongator
    • C. Greenwood, L.A. Selth, A.B. Dirac-Svejstrup, and J.Q. Svejstrup An iron-sulfur cluster domain in Elp3 important for the structural integrity of elongator J. Biol. Chem. 284 2009 141 149
    • (2009) J. Biol. Chem. , vol.284 , pp. 141-149
    • Greenwood, C.1    Selth, L.A.2    Dirac-Svejstrup, A.B.3    Svejstrup, J.Q.4
  • 61
    • 0037019599 scopus 로고    scopus 로고
    • Incision of a 1,3-intrastrand d(GpTpG)-cisplatin adduct by nucleotide excision repair proteins from yeast
    • S.E. Kong, and J.Q. Svejstrup Incision of a 1,3-intrastrand d(GpTpG)-cisplatin adduct by nucleotide excision repair proteins from yeast DNA Repair (Amst.) 1 2002 731 741
    • (2002) DNA Repair (Amst.) , vol.1 , pp. 731-741
    • Kong, S.E.1    Svejstrup, J.Q.2
  • 64
    • 0033168194 scopus 로고    scopus 로고
    • The NES-Crm1p export pathway is not a major mRNA export route in Saccharomyces cerevisiae
    • M. Neville, and M. Rosbash The NES-Crm1p export pathway is not a major mRNA export route in Saccharomyces cerevisiae EMBO J. 18 1999 3746 3756
    • (1999) EMBO J. , vol.18 , pp. 3746-3756
    • Neville, M.1    Rosbash, M.2
  • 65
    • 71349084952 scopus 로고    scopus 로고
    • Mechanistic analysis of PCNA poly-ubiquitylation by the ubiquitin protein ligases Rad18 and Rad5
    • J.L. Parker, and H.D. Ulrich Mechanistic analysis of PCNA poly-ubiquitylation by the ubiquitin protein ligases Rad18 and Rad5 EMBO J. 28 2009 3657 3666
    • (2009) EMBO J. , vol.28 , pp. 3657-3666
    • Parker, J.L.1    Ulrich, H.D.2
  • 66
    • 0025978949 scopus 로고
    • Getting started with yeast
    • C. Guthrie, G.R. Fink, Academic Press, Inc. San Diego
    • F. Sherman Getting started with yeast C. Guthrie, G.R. Fink, Guide to Yeast Genetics and Molecular Biology 1991 Academic Press, Inc. San Diego 3 20
    • (1991) Guide to Yeast Genetics and Molecular Biology , pp. 3-20
    • Sherman, F.1
  • 67
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • R.S. Sikorski, and P. Hieter A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae Genetics 122 1989 19 27
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 68
    • 0034963119 scopus 로고    scopus 로고
    • A modular polycistronic expression system for overexpressing protein complexes in Escherichia coli
    • S. Tan A modular polycistronic expression system for overexpressing protein complexes in Escherichia coli Protein Expr. Purif. 21 2001 224 234
    • (2001) Protein Expr. Purif. , vol.21 , pp. 224-234
    • Tan, S.1
  • 69
    • 0034721669 scopus 로고    scopus 로고
    • Cleavage of cohesin by the CD clan protease separin triggers anaphase in yeast
    • F. Uhlmann, D. Wernic, M.A. Poupart, E.V. Koonin, and K. Nasmyth Cleavage of cohesin by the CD clan protease separin triggers anaphase in yeast Cell 103 2000 375 386
    • (2000) Cell , vol.103 , pp. 375-386
    • Uhlmann, F.1    Wernic, D.2    Poupart, M.A.3    Koonin, E.V.4    Nasmyth, K.5
  • 70
    • 0033791447 scopus 로고    scopus 로고
    • Proteasomal proteomics: Identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes
    • R. Verma, S. Chen, R. Feldman, D. Schieltz, J. Yates, J. Dohmen, and R.J. Deshaies Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes Mol. Biol. Cell 11 2000 3425 3439
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3425-3439
    • Verma, R.1    Chen, S.2    Feldman, R.3    Schieltz, D.4    Yates, J.5    Dohmen, J.6    Deshaies, R.J.7


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