메뉴 건너뛰기




Volumn 100, Issue , 2014, Pages 25-36

Modulation of the yeast protein interactome in response to DNA damage

Author keywords

DNA damage; MMS; P bodies; Protein interaction network; Protein fragment complementation assay; Yeast

Indexed keywords

DNA; EXOCYST; EXOCYST 84; FUNGAL PROTEIN; LAS17 PROTEIN; MESSENGER RNA; NOP7 PROTEIN; UNCLASSIFIED DRUG; DIHYDROFOLATE REDUCTASE; FUNGAL RNA; MESYLIC ACID METHYL ESTER; METHOTREXATE; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84897034514     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2013.11.007     Document Type: Article
Times cited : (15)

References (66)
  • 1
    • 70849112486 scopus 로고    scopus 로고
    • Cell signaling in space and time: where proteins come together and when they're apart
    • Scott J.D., Pawson T. Cell signaling in space and time: where proteins come together and when they're apart. Science 2009, 326:1220-1224.
    • (2009) Science , vol.326 , pp. 1220-1224
    • Scott, J.D.1    Pawson, T.2
  • 3
    • 84856094560 scopus 로고    scopus 로고
    • Differential network biology
    • Ideker T., Krogan N.J. Differential network biology. Mol Syst Biol 2012, 8:565.
    • (2012) Mol Syst Biol , vol.8 , pp. 565
    • Ideker, T.1    Krogan, N.J.2
  • 4
    • 0041766297 scopus 로고    scopus 로고
    • Screening for nitric oxide-dependent protein-protein interactions
    • Matsumoto A., Comatas K.E., Liu L., Stamler J.S. Screening for nitric oxide-dependent protein-protein interactions. Science 2003, 301:657-661.
    • (2003) Science , vol.301 , pp. 657-661
    • Matsumoto, A.1    Comatas, K.E.2    Liu, L.3    Stamler, J.S.4
  • 6
    • 79960245388 scopus 로고    scopus 로고
    • Selected reaction monitoring mass spectrometry reveals the dynamics of signaling through the GRB2 adaptor
    • Bisson N., James D.A., Ivosev G., Tate S.A., Bonner R., Taylor L., et al. Selected reaction monitoring mass spectrometry reveals the dynamics of signaling through the GRB2 adaptor. Nat Biotechnol 2011, 29:653-658.
    • (2011) Nat Biotechnol , vol.29 , pp. 653-658
    • Bisson, N.1    James, D.A.2    Ivosev, G.3    Tate, S.A.4    Bonner, R.5    Taylor, L.6
  • 8
    • 77956048943 scopus 로고    scopus 로고
    • A toolkit of protein-fragment complementation assays for studying and dissecting large-scale and dynamic protein-protein interactions in living cells
    • Michnick S.W., Ear P.H., Landry C., Malleshaiah M.K., Messier V. A toolkit of protein-fragment complementation assays for studying and dissecting large-scale and dynamic protein-protein interactions in living cells. Methods Enzymol 2010, 470:335-368.
    • (2010) Methods Enzymol , vol.470 , pp. 335-368
    • Michnick, S.W.1    Ear, P.H.2    Landry, C.3    Malleshaiah, M.K.4    Messier, V.5
  • 9
    • 84877819731 scopus 로고    scopus 로고
    • Transcriptional divergence plays a role in the rewiring of protein interaction networks after gene duplication
    • Gagnon-Arsenault I., Marois Blanchet F.C., Rochette S., Diss G., Dube A.K., Landry C.R. Transcriptional divergence plays a role in the rewiring of protein interaction networks after gene duplication. J Proteome 2013, 81:112-125.
    • (2013) J Proteome , vol.81 , pp. 112-125
    • Gagnon-Arsenault, I.1    Marois Blanchet, F.C.2    Rochette, S.3    Diss, G.4    Dube, A.K.5    Landry, C.R.6
  • 10
    • 84879798118 scopus 로고    scopus 로고
    • A systematic approach for the genetic dissection of protein complexes in living cells
    • Diss G., Dube A.K., Boutin J., Gagnon-Arsenault I., Landry C.R. A systematic approach for the genetic dissection of protein complexes in living cells. Cell reports. 2013, 3:2155-2167.
    • (2013) Cell reports. , vol.3 , pp. 2155-2167
    • Diss, G.1    Dube, A.K.2    Boutin, J.3    Gagnon-Arsenault, I.4    Landry, C.R.5
  • 11
    • 84874473100 scopus 로고    scopus 로고
    • QPCA: a scalable assay to measure the perturbation of protein-protein interactions in living cells
    • Freschi L., Torres-Quiroz F., Dube A.K., Landry C.R. qPCA: a scalable assay to measure the perturbation of protein-protein interactions in living cells. Mol Biosyst 2013, 9:36-43.
    • (2013) Mol Biosyst , vol.9 , pp. 36-43
    • Freschi, L.1    Torres-Quiroz, F.2    Dube, A.K.3    Landry, C.R.4
  • 13
    • 70350504453 scopus 로고    scopus 로고
    • The DNA-damage response in human biology and disease
    • Jackson S.P., Bartek J. The DNA-damage response in human biology and disease. Nature 2009, 461:1071-1078.
    • (2009) Nature , vol.461 , pp. 1071-1078
    • Jackson, S.P.1    Bartek, J.2
  • 14
    • 84856019858 scopus 로고    scopus 로고
    • The DNA damage response and cancer therapy
    • Lord C.J., Ashworth A. The DNA damage response and cancer therapy. Nature 2012, 481:287-294.
    • (2012) Nature , vol.481 , pp. 287-294
    • Lord, C.J.1    Ashworth, A.2
  • 15
    • 81255197643 scopus 로고    scopus 로고
    • Yeast: an experimental organism for 21st Century biology
    • Botstein D., Fink G.R. Yeast: an experimental organism for 21st Century biology. Genetics 2011, 189:695-704.
    • (2011) Genetics , vol.189 , pp. 695-704
    • Botstein, D.1    Fink, G.R.2
  • 16
    • 44449131125 scopus 로고    scopus 로고
    • Orthology and functional conservation in eukaryotes
    • Dolinski K., Botstein D. Orthology and functional conservation in eukaryotes. Annu Rev Genet 2007, 41:465-507.
    • (2007) Annu Rev Genet , vol.41 , pp. 465-507
    • Dolinski, K.1    Botstein, D.2
  • 17
    • 0036626032 scopus 로고    scopus 로고
    • Nobel lecture. Yeast and cancer
    • Hartwell L.H. Nobel lecture. Yeast and cancer. Biosci Rep 2002, 22:373-394.
    • (2002) Biosci Rep , vol.22 , pp. 373-394
    • Hartwell, L.H.1
  • 18
    • 84866156212 scopus 로고    scopus 로고
    • Components of a Fanconi-like pathway control Pso2-independent DNA interstrand crosslink repair in yeast
    • Ward T.A., Dudasova Z., Sarkar S., Bhide M.R., Vlasakova D., Chovanec M., et al. Components of a Fanconi-like pathway control Pso2-independent DNA interstrand crosslink repair in yeast. PLoS Genet 2012, 8:e1002884.
    • (2012) PLoS Genet , vol.8
    • Ward, T.A.1    Dudasova, Z.2    Sarkar, S.3    Bhide, M.R.4    Vlasakova, D.5    Chovanec, M.6
  • 19
    • 80053451692 scopus 로고    scopus 로고
    • Genome-wide analysis of heteroduplex DNA in mismatch repair-deficient yeast cells reveals novel properties of meiotic recombination pathways
    • Martini E., Borde V., Legendre M., Audic S., Regnault B., Soubigou G., et al. Genome-wide analysis of heteroduplex DNA in mismatch repair-deficient yeast cells reveals novel properties of meiotic recombination pathways. PLoS Genet 2011, 7:e1002305.
    • (2011) PLoS Genet , vol.7
    • Martini, E.1    Borde, V.2    Legendre, M.3    Audic, S.4    Regnault, B.5    Soubigou, G.6
  • 20
    • 84865715286 scopus 로고    scopus 로고
    • Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress
    • Tkach J.M., Yimit A., Lee A.Y., Riffle M., Costanzo M., Jaschob D., et al. Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 2012, 14:966-976.
    • (2012) Nat Cell Biol , vol.14 , pp. 966-976
    • Tkach, J.M.1    Yimit, A.2    Lee, A.Y.3    Riffle, M.4    Costanzo, M.5    Jaschob, D.6
  • 21
    • 0033573938 scopus 로고    scopus 로고
    • Global response of Saccharomyces cerevisiae to an alkylating agent
    • Jelinsky S.A., Samson L.D. Global response of Saccharomyces cerevisiae to an alkylating agent. Proc Natl Acad Sci U S A 1999, 96:1486-1491.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 1486-1491
    • Jelinsky, S.A.1    Samson, L.D.2
  • 22
    • 34547499407 scopus 로고    scopus 로고
    • Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases
    • Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases. Proc Natl Acad Sci U S A 2007, 104:10364-10369.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 10364-10369
    • Smolka, M.B.1    Albuquerque, C.P.2    Chen, S.H.3    Zhou, H.4
  • 23
    • 84860325854 scopus 로고    scopus 로고
    • Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response
    • Beli P., Lukashchuk N., Wagner S.A., Weinert B.T., Olsen J.V., Baskcomb L., et al. Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response. Mol Cell 2012, 46:212-225.
    • (2012) Mol Cell , vol.46 , pp. 212-225
    • Beli, P.1    Lukashchuk, N.2    Wagner, S.A.3    Weinert, B.T.4    Olsen, J.V.5    Baskcomb, L.6
  • 25
    • 84872821321 scopus 로고    scopus 로고
    • Dissection of DNA damage responses using multiconditional genetic interaction maps
    • Guenole A., Srivas R., Vreeken K., Wang Z.Z., Wang S., Krogan N.J., et al. Dissection of DNA damage responses using multiconditional genetic interaction maps. Mol Cell 2013, 49:346-358.
    • (2013) Mol Cell , vol.49 , pp. 346-358
    • Guenole, A.1    Srivas, R.2    Vreeken, K.3    Wang, Z.Z.4    Wang, S.5    Krogan, N.J.6
  • 27
    • 79551539500 scopus 로고    scopus 로고
    • Integrative features of the yeast phosphoproteome and protein-protein interaction map
    • Yachie N., Saito R., Sugiyama N., Tomita M., Ishihama Y. Integrative features of the yeast phosphoproteome and protein-protein interaction map. PLoS Comput Biol 2011, 7:e1001064.
    • (2011) PLoS Comput Biol , vol.7
    • Yachie, N.1    Saito, R.2    Sugiyama, N.3    Tomita, M.4    Ishihama, Y.5
  • 30
    • 70450203033 scopus 로고    scopus 로고
    • Mixtools: an R package for analyzing finite mixture models
    • Benaglia T., Chauveau D., Hunter D.R., Young D. Mixtools: an R package for analyzing finite mixture models. J Stat Softw 2009, 32:1-29.
    • (2009) J Stat Softw , vol.32 , pp. 1-29
    • Benaglia, T.1    Chauveau, D.2    Hunter, D.R.3    Young, D.4
  • 33
    • 79953845487 scopus 로고    scopus 로고
    • Systematic exploration of essential yeast gene function with temperature-sensitive mutants
    • Li Z., Vizeacoumar F.J., Bahr S., Li J., Warringer J., Vizeacoumar F.S., et al. Systematic exploration of essential yeast gene function with temperature-sensitive mutants. Nat Biotechnol 2011, 29:361-367.
    • (2011) Nat Biotechnol , vol.29 , pp. 361-367
    • Li, Z.1    Vizeacoumar, F.J.2    Bahr, S.3    Li, J.4    Warringer, J.5    Vizeacoumar, F.S.6
  • 35
    • 0032826786 scopus 로고    scopus 로고
    • NORF5/HUG1 is a component of the MEC1-mediated checkpoint response to DNA damage and replication arrest in Saccharomyces cerevisiae
    • Basrai M.A., Velculescu V.E., Kinzler K.W., Hieter P. NORF5/HUG1 is a component of the MEC1-mediated checkpoint response to DNA damage and replication arrest in Saccharomyces cerevisiae. Mol. Cell Biol 1999, 19:7041-7049.
    • (1999) Mol. Cell Biol , vol.19 , pp. 7041-7049
    • Basrai, M.A.1    Velculescu, V.E.2    Kinzler, K.W.3    Hieter, P.4
  • 36
    • 0037168646 scopus 로고    scopus 로고
    • A genome-wide screen for methyl methanesulfonate-sensitive mutants reveals genes required for S phase progression in the presence of DNA damage
    • Chang M., Bellaoui M., Boone C., Brown G.W. A genome-wide screen for methyl methanesulfonate-sensitive mutants reveals genes required for S phase progression in the presence of DNA damage. Proc Natl Acad Sci U S A 2002, 99:16934-16939.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 16934-16939
    • Chang, M.1    Bellaoui, M.2    Boone, C.3    Brown, G.W.4
  • 37
    • 37249067732 scopus 로고    scopus 로고
    • The origin of protein interactions and allostery in colocalization
    • Kuriyan J., Eisenberg D. The origin of protein interactions and allostery in colocalization. Nature 2007, 450:983-990.
    • (2007) Nature , vol.450 , pp. 983-990
    • Kuriyan, J.1    Eisenberg, D.2
  • 38
    • 2442417331 scopus 로고    scopus 로고
    • Interaction of human DNA polymerase eta with monoubiquitinated PCNA: a possible mechanism for the polymerase switch in response to DNA damage
    • Kannouche P.L., Wing J., Lehmann A.R. Interaction of human DNA polymerase eta with monoubiquitinated PCNA: a possible mechanism for the polymerase switch in response to DNA damage. Mol Cell 2004, 14:491-500.
    • (2004) Mol Cell , vol.14 , pp. 491-500
    • Kannouche, P.L.1    Wing, J.2    Lehmann, A.R.3
  • 39
    • 78650590282 scopus 로고    scopus 로고
    • Graded enhancement of p53 binding to CREB-binding protein (CBP) by multisite phosphorylation
    • Lee C.W., Ferreon J.C., Ferreon A.C., Arai M., Wright P.E. Graded enhancement of p53 binding to CREB-binding protein (CBP) by multisite phosphorylation. Proc Natl Acad Sci U S A 2010, 107:19290-19295.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 19290-19295
    • Lee, C.W.1    Ferreon, J.C.2    Ferreon, A.C.3    Arai, M.4    Wright, P.E.5
  • 40
    • 33847417585 scopus 로고    scopus 로고
    • P bodies and the control of mRNA translation and degradation
    • Parker R., Sheth U. P bodies and the control of mRNA translation and degradation. Mol Cell 2007, 25:635-646.
    • (2007) Mol Cell , vol.25 , pp. 635-646
    • Parker, R.1    Sheth, U.2
  • 42
    • 58049161508 scopus 로고    scopus 로고
    • Roles of eukaryotic Lsm proteins in the regulation of mRNA function
    • Tharun S. Roles of eukaryotic Lsm proteins in the regulation of mRNA function. Int Rev Cell Mol Biol 2009, 272:149-189.
    • (2009) Int Rev Cell Mol Biol , vol.272 , pp. 149-189
    • Tharun, S.1
  • 44
    • 0034599976 scopus 로고    scopus 로고
    • A Sm-like protein complex that participates in mRNA degradation
    • Bouveret E., Rigaut G., Shevchenko A., Wilm M., Seraphin B. A Sm-like protein complex that participates in mRNA degradation. EMBO J 2000, 19:1661-1671.
    • (2000) EMBO J , vol.19 , pp. 1661-1671
    • Bouveret, E.1    Rigaut, G.2    Shevchenko, A.3    Wilm, M.4    Seraphin, B.5
  • 45
    • 0033564627 scopus 로고    scopus 로고
    • Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin
    • Salgado-Garrido J., Bragado-Nilsson E., Kandels-Lewis S., Seraphin B. Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin. EMBO J 1999, 18:3451-3462.
    • (1999) EMBO J , vol.18 , pp. 3451-3462
    • Salgado-Garrido, J.1    Bragado-Nilsson, E.2    Kandels-Lewis, S.3    Seraphin, B.4
  • 46
    • 0035824883 scopus 로고    scopus 로고
    • Purification and characterization of the 1.0 MDa CCR4-NOT complex identifies two novel components of the complex
    • Chen J., Rappsilber J., Chiang Y.C., Russell P., Mann M., Denis C.L. Purification and characterization of the 1.0 MDa CCR4-NOT complex identifies two novel components of the complex. J Mol Biol 2001, 314:683-694.
    • (2001) J Mol Biol , vol.314 , pp. 683-694
    • Chen, J.1    Rappsilber, J.2    Chiang, Y.C.3    Russell, P.4    Mann, M.5    Denis, C.L.6
  • 47
    • 1642411849 scopus 로고    scopus 로고
    • Mdt1, a novel Rad53 FHA1 domain-interacting protein, modulates DNA damage tolerance and G(2)/M cell cycle progression in Saccharomyces cerevisiae
    • Pike B.L., Yongkiettrakul S., Tsai M.D., Heierhorst J. Mdt1, a novel Rad53 FHA1 domain-interacting protein, modulates DNA damage tolerance and G(2)/M cell cycle progression in Saccharomyces cerevisiae. Mol Cell Biol 2004, 24:2779-2788.
    • (2004) Mol Cell Biol , vol.24 , pp. 2779-2788
    • Pike, B.L.1    Yongkiettrakul, S.2    Tsai, M.D.3    Heierhorst, J.4
  • 48
    • 0030614360 scopus 로고    scopus 로고
    • Requirement of the DEAD-Box protein ded1p for messenger RNA translation
    • Chuang R.Y., Weaver P.L., Liu Z., Chang T.H. Requirement of the DEAD-Box protein ded1p for messenger RNA translation. Science 1997, 275:1468-1471.
    • (1997) Science , vol.275 , pp. 1468-1471
    • Chuang, R.Y.1    Weaver, P.L.2    Liu, Z.3    Chang, T.H.4
  • 49
    • 43049138051 scopus 로고    scopus 로고
    • Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease
    • Kraft C., Deplazes A., Sohrmann M., Peter M. Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease. Nat Cell Biol 2008, 10:602-610.
    • (2008) Nat Cell Biol , vol.10 , pp. 602-610
    • Kraft, C.1    Deplazes, A.2    Sohrmann, M.3    Peter, M.4
  • 50
    • 0842285405 scopus 로고    scopus 로고
    • Recruitment of Cdc28 by Whi3 restricts nuclear accumulation of the G1 cyclin-Cdk complex to late G1
    • Wang H., Gari E., Verges E., Gallego C., Aldea M. Recruitment of Cdc28 by Whi3 restricts nuclear accumulation of the G1 cyclin-Cdk complex to late G1. EMBO J 2004, 23:180-190.
    • (2004) EMBO J , vol.23 , pp. 180-190
    • Wang, H.1    Gari, E.2    Verges, E.3    Gallego, C.4    Aldea, M.5
  • 51
    • 0035499508 scopus 로고    scopus 로고
    • Whi3 binds the mRNA of the G1 cyclin CLN3 to modulate cell fate in budding yeast
    • Gari E., Volpe T., Wang H., Gallego C., Futcher B., Aldea M. Whi3 binds the mRNA of the G1 cyclin CLN3 to modulate cell fate in budding yeast. Genes Dev 2001, 15:2803-2808.
    • (2001) Genes Dev , vol.15 , pp. 2803-2808
    • Gari, E.1    Volpe, T.2    Wang, H.3    Gallego, C.4    Futcher, B.5    Aldea, M.6
  • 52
    • 0032570562 scopus 로고    scopus 로고
    • Ultraviolet radiation-induced ubiquitination and proteasomal degradation of the large subunit of RNA polymerase II. Implications for transcription-coupled DNA repair
    • Ratner J.N., Balasubramanian B., Corden J., Warren S.L., Bregman D.B. Ultraviolet radiation-induced ubiquitination and proteasomal degradation of the large subunit of RNA polymerase II. Implications for transcription-coupled DNA repair. J Biol Chem 1998, 273:5184-5189.
    • (1998) J Biol Chem , vol.273 , pp. 5184-5189
    • Ratner, J.N.1    Balasubramanian, B.2    Corden, J.3    Warren, S.L.4    Bregman, D.B.5
  • 53
    • 0035807072 scopus 로고    scopus 로고
    • Ultraviolet radiation alters the phosphorylation of RNA polymerase II large subunit and accelerates its proteasome-dependent degradation
    • Luo Z., Zheng J., Lu Y., Bregman D.B. Ultraviolet radiation alters the phosphorylation of RNA polymerase II large subunit and accelerates its proteasome-dependent degradation. Mutat Res 2001, 486:259-274.
    • (2001) Mutat Res , vol.486 , pp. 259-274
    • Luo, Z.1    Zheng, J.2    Lu, Y.3    Bregman, D.B.4
  • 54
    • 0037148786 scopus 로고    scopus 로고
    • A Rad26-Def1 complex coordinates repair and RNA pol II proteolysis in response to DNA damage
    • Woudstra E.C., Gilbert C., Fellows J., Jansen L., Brouwer J., Erdjument-Bromage H., et al. A Rad26-Def1 complex coordinates repair and RNA pol II proteolysis in response to DNA damage. Nature 2002, 415:929-933.
    • (2002) Nature , vol.415 , pp. 929-933
    • Woudstra, E.C.1    Gilbert, C.2    Fellows, J.3    Jansen, L.4    Brouwer, J.5    Erdjument-Bromage, H.6
  • 55
    • 80054736893 scopus 로고    scopus 로고
    • An ataxia-telangiectasia-mutated (ATM) kinase mediated response to DNA damage down-regulates the mRNA-binding potential of THOC5
    • Ramachandran S., Tran D.D., Klebba-Faerber S., Kardinal C., Whetton A.D., Tamura T. An ataxia-telangiectasia-mutated (ATM) kinase mediated response to DNA damage down-regulates the mRNA-binding potential of THOC5. RNA 2011, 17:1957-1966.
    • (2011) RNA , vol.17 , pp. 1957-1966
    • Ramachandran, S.1    Tran, D.D.2    Klebba-Faerber, S.3    Kardinal, C.4    Whetton, A.D.5    Tamura, T.6
  • 56
    • 81755172940 scopus 로고    scopus 로고
    • Keeping proteasomes under control-a role for phosphorylation in the nucleus
    • Sha Z., Peth A., Goldberg A.L. Keeping proteasomes under control-a role for phosphorylation in the nucleus. Proc Natl Acad Sci U S A 2011, 108:18573-18574.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 18573-18574
    • Sha, Z.1    Peth, A.2    Goldberg, A.L.3
  • 57
    • 84867176120 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system of Saccharomyces cerevisiae
    • Finley D., Ulrich H.D., Sommer T., Kaiser P. The ubiquitin-proteasome system of Saccharomyces cerevisiae. Genetics 2012, 192:319-360.
    • (2012) Genetics , vol.192 , pp. 319-360
    • Finley, D.1    Ulrich, H.D.2    Sommer, T.3    Kaiser, P.4
  • 58
    • 19944388882 scopus 로고    scopus 로고
    • Proteasome involvement in the repair of DNA double-strand breaks
    • Krogan N.J., Lam M.H., Fillingham J., Keogh M.C., Gebbia M., Li J., et al. Proteasome involvement in the repair of DNA double-strand breaks. Mol Cell 2004, 16:1027-1034.
    • (2004) Mol Cell , vol.16 , pp. 1027-1034
    • Krogan, N.J.1    Lam, M.H.2    Fillingham, J.3    Keogh, M.C.4    Gebbia, M.5    Li, J.6
  • 59
    • 0010586475 scopus 로고    scopus 로고
    • The 19S regulatory complex of the proteasome functions independently of proteolysis in nucleotide excision repair
    • Russell S.J., Reed S.H., Huang W., Friedberg E.C., Johnston S.A. The 19S regulatory complex of the proteasome functions independently of proteolysis in nucleotide excision repair. Mol Cell 1999, 3:687-695.
    • (1999) Mol Cell , vol.3 , pp. 687-695
    • Russell, S.J.1    Reed, S.H.2    Huang, W.3    Friedberg, E.C.4    Johnston, S.A.5
  • 60
    • 77649196564 scopus 로고    scopus 로고
    • Proteasome nuclear activity affects chromosome stability by controlling the turnover of Mms22, a protein important for DNA repair
    • Ben-Aroya S., Agmon N., Yuen K., Kwok T., McManus K., Kupiec M., et al. Proteasome nuclear activity affects chromosome stability by controlling the turnover of Mms22, a protein important for DNA repair. PLoS Genet 2010, 6:e1000852.
    • (2010) PLoS Genet , vol.6
    • Ben-Aroya, S.1    Agmon, N.2    Yuen, K.3    Kwok, T.4    McManus, K.5    Kupiec, M.6
  • 61
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege C., Pfander B., Moldovan G.L., Pyrowolakis G., Jentsch S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 2002, 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
  • 62
    • 33749506057 scopus 로고    scopus 로고
    • Mms2-Ubc13 covalently bound to ubiquitin reveals the structural basis of linkage-specific polyubiquitin chain formation
    • Eddins M.J., Carlile C.M., Gomez K.M., Pickart C.M., Wolberger C. Mms2-Ubc13 covalently bound to ubiquitin reveals the structural basis of linkage-specific polyubiquitin chain formation. Nat Struct Mol Biol 2006, 13:915-920.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 915-920
    • Eddins, M.J.1    Carlile, C.M.2    Gomez, K.M.3    Pickart, C.M.4    Wolberger, C.5
  • 63
    • 0034600851 scopus 로고    scopus 로고
    • Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair
    • Ulrich H.D., Jentsch S. Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair. EMBO J 2000, 19:3388-3397.
    • (2000) EMBO J , vol.19 , pp. 3388-3397
    • Ulrich, H.D.1    Jentsch, S.2
  • 64
    • 0032835492 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome protein Las17p interacts with the Arp2/3 complex
    • Madania A., Dumoulin P., Grava S., Kitamoto H., Scharer-Brodbeck C., Soulard A., et al. The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome protein Las17p interacts with the Arp2/3 complex. Mol Biol Cell 1999, 10:3521-3538.
    • (1999) Mol Biol Cell , vol.10 , pp. 3521-3538
    • Madania, A.1    Dumoulin, P.2    Grava, S.3    Kitamoto, H.4    Scharer-Brodbeck, C.5    Soulard, A.6
  • 65
    • 56849087971 scopus 로고    scopus 로고
    • The dynamics of mammalian P body transport, assembly, and disassembly in vivo
    • Aizer A., Brody Y., Ler L.W., Sonenberg N., Singer R.H., Shav-Tal Y. The dynamics of mammalian P body transport, assembly, and disassembly in vivo. Mol Biol Cell 2008, 19:4154-4166.
    • (2008) Mol Biol Cell , vol.19 , pp. 4154-4166
    • Aizer, A.1    Brody, Y.2    Ler, L.W.3    Sonenberg, N.4    Singer, R.H.5    Shav-Tal, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.