메뉴 건너뛰기




Volumn 189, Issue 4, 2010, Pages 739-754

Quantitative proteomics combined with BAC TransgeneOmics reveals in vivo protein interactions

Author keywords

[No Author keywords available]

Indexed keywords

ANAPHASE PROMOTING COMPLEX; GREEN FLUORESCENT PROTEIN; ISOPROTEIN; PERICENTRIN;

EID: 77952344256     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200911091     Document Type: Article
Times cited : (362)

References (66)
  • 1
    • 34948901399 scopus 로고    scopus 로고
    • Aurora-A: The maker and breaker of spindle poles
    • doi:10.1242/jcs.013136
    • Barr, A.R., and F. Gergely. 2007. Aurora-A: the maker and breaker of spindle poles. J. Cell Sci. 120:2987-2996. doi:10.1242/jcs.013136
    • (2007) J. Cell Sci. , vol.120 , pp. 2987-2996
    • Barr, A.R.1    Gergely, F.2
  • 2
    • 25444485717 scopus 로고    scopus 로고
    • Aurora a activates D-TACC-Msps complexes exclusively at centrosomes to stabilize centrosomal microtubules
    • doi:10.1083/jcb.200504097
    • Barros, T.P., K. Kinoshita, A.A. Hyman, and J.W. Raff. 2005. Aurora A activates D-TACC-Msps complexes exclusively at centrosomes to stabilize centrosomal microtubules. J. Cell Biol. 170:1039-1046. doi:10.1083/jcb.200504097
    • (2005) J. Cell Biol. , vol.170 , pp. 1039-1046
    • Barros, T.P.1    Kinoshita, K.2    Hyman, A.A.3    Raff, J.W.4
  • 3
    • 0042420427 scopus 로고    scopus 로고
    • TAC-1 and ZYG-9 form a complex that promotes microtubule assembly in C. elegans embryos
    • doi:10.1016/S0960-9822(03)00582-7
    • Bellanger, J.M., and P. Gönczy. 2003. TAC-1 and ZYG-9 form a complex that promotes microtubule assembly in C. elegans embryos. Curr. Biol. 13: 1488-1498. doi:10.1016/S0960-9822(03)00582-7
    • (2003) Curr. Biol. , vol.13 , pp. 1488-1498
    • Bellanger, J.M.1    Gönczy, P.2
  • 4
    • 48249109896 scopus 로고    scopus 로고
    • Building a spindle of the correct length in human cells requires the interaction between TPX2 and Aurora A
    • doi:10.1083/jcb.200802005
    • Bird, A.W., and A.A. Hyman. 2008. Building a spindle of the correct length in human cells requires the interaction between TPX2 and Aurora A. J. Cell Biol. 182:289-300. doi:10.1083/jcb.200802005
    • (2008) J. Cell Biol. , vol.182 , pp. 289-300
    • Bird, A.W.1    Hyman, A.A.2
  • 5
    • 0037337310 scopus 로고    scopus 로고
    • A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling
    • doi:10.1038/nbt790
    • Blagoev, B., I. Kratchmarova, S.E. Ong, M. Nielsen, L.J. Foster, and M. Mann. 2003. A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. Nat. Biotechnol. 21:315-318. doi:10.1038/nbt790
    • (2003) Nat. Biotechnol. , vol.21 , pp. 315-318
    • Blagoev, B.1    Kratchmarova, I.2    Ong, S.E.3    Nielsen, M.4    Foster, L.J.5    Mann, M.6
  • 6
    • 26944490411 scopus 로고    scopus 로고
    • A combined approach for the localization and tandem affinity purification of protein complexes from metazoans
    • doi:10.1126/stke.2662005p11
    • Cheeseman, I.M., and A. Desai. 2005. A combined approach for the localization and tandem affinity purification of protein complexes from metazoans. Sci. STKE. 2005:p11. doi:10.1126/stke.2662005p11
    • (2005) Sci. STKE , vol.2005
    • Cheeseman, I.M.1    Desai, A.2
  • 7
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • doi:10.1038/nbt.1511
    • Cox, J., and M. Mann. 2008. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26:1367-1372. doi:10.1038/nbt.1511
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 8
    • 0034939685 scopus 로고    scopus 로고
    • Msps protein is localized to acentrosomal poles to ensure bipolarity of Drosophila meiotic spindles
    • doi:10.1038/35083025
    • Cullen, C.F., and H. Ohkura. 2001. Msps protein is localized to acentrosomal poles to ensure bipolarity of Drosophila meiotic spindles. Nat. Cell Biol. 3:637-642. doi:10.1038/35083025
    • (2001) Nat. Cell Biol. , vol.3 , pp. 637-642
    • Cullen, C.F.1    Ohkura, H.2
  • 9
    • 0038168170 scopus 로고    scopus 로고
    • Mitotic and stress-induced phosphorylation of HsPI3K-C2alpha targets the protein for degradation
    • doi:10.1074/jbc.M301657200
    • Didichenko, S.A., C.M. Fragoso, and M. Thelen. 2003. Mitotic and stress-induced phosphorylation of HsPI3K-C2alpha targets the protein for degradation. J. Biol. Chem. 278:26055-26064. doi:10.1074/jbc.M301657200
    • (2003) J. Biol. Chem. , vol.278 , pp. 26055-26064
    • Didichenko, S.A.1    Fragoso, C.M.2    Thelen, M.3
  • 10
    • 0028218025 scopus 로고
    • Pericentrin, a highly conserved centrosome protein involved in microtubule organization
    • doi:10.1016/0092-8674(94)90504-5
    • Doxsey, S.J., P. Stein, L. Evans, P.D. Calarco, and M. Kirschner. 1994. Pericentrin, a highly conserved centrosome protein involved in microtubule organization. Cell. 76:639-650. doi:10.1016/0092-8674(94)90504-5
    • (1994) Cell. , vol.76 , pp. 639-650
    • Doxsey, S.J.1    Stein, P.2    Evans, L.3    Calarco, P.D.4    Kirschner, M.5
  • 11
    • 0042622508 scopus 로고    scopus 로고
    • The centrosomal proteins pericentrin and kendrin are encoded by alternatively spliced products of one gene
    • doi:10.1016/S0888-7543(03)00119-8
    • Flory, M.R., and T.N. Davis. 2003. The centrosomal proteins pericentrin and kendrin are encoded by alternatively spliced products of one gene. Genomics. 82:401-405. doi:10.1016/S0888-7543(03)00119-8
    • (2003) Genomics. , vol.82 , pp. 401-405
    • Flory, M.R.1    Davis, T.N.2
  • 12
    • 38749152785 scopus 로고    scopus 로고
    • CDK5RAP2 is a pericentriolar protein that functions in centrosomal attachment of the gamma-tubulin ring complex
    • doi:10.1091/mbc.E07-04-0371
    • Fong, K.W., Y.K. Choi, J.B. Rattner, and R.Z. Qi. 2008. CDK5RAP2 is a pericentriolar protein that functions in centrosomal attachment of the gamma-tubulin ring complex. Mol. Biol. Cell. 19:115-125. doi:10.1091/mbc.E07-04- 0371
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 115-125
    • Fong, K.W.1    Choi, Y.K.2    Rattner, J.B.3    Qi, R.Z.4
  • 13
    • 0035103107 scopus 로고    scopus 로고
    • The class II phosphoinositide 3-kinase C2alpha is activated by clathrin and regulates clathrin-mediated membrane trafficking
    • doi:10.1016/S1097-2765(01)00191-5
    • Gaidarov, I., M.E. Smith, J. Domin, and J.H. Keen. 2001. The class II phosphoinositide 3-kinase C2alpha is activated by clathrin and regulates clathrin-mediated membrane trafficking. Mol. Cell. 7:443-449. doi:10.1016/S1097-2765(01)00191-5
    • (2001) Mol. Cell. , vol.7 , pp. 443-449
    • Gaidarov, I.1    Smith, M.E.2    Domin, J.3    Keen, J.H.4
  • 16
    • 0037314330 scopus 로고    scopus 로고
    • The ch-TOG/XMAP215 protein is essential for spindle pole organization in human somatic cells
    • DOI 10.1101/gad.245603
    • Gergely, F., V.M. Draviam, and J.W. Raff. 2003. The ch-TOG/XMAP215 protein is essential for spindle pole organization in human somatic cells. Genes Dev. 17:336-341. doi:10.1101/gad.245603 (Pubitemid 36182191)
    • (2003) Genes and Development , vol.17 , Issue.3 , pp. 336-341
    • Gergely, F.1    Draviam, V.M.2    Raff, J.W.3
  • 17
    • 0037017398 scopus 로고    scopus 로고
    • Drosophila Aurora a kinase is required to localize D-TACC to centrosomes and to regulate astral microtubules
    • doi:10.1083/jcb.200108135
    • Giet, R., D. McLean, S. Descamps, M.J. Lee, J.W. Raff, C. Prigent, and D.M. Glover. 2002. Drosophila Aurora A kinase is required to localize D-TACC to centrosomes and to regulate astral microtubules. J. Cell Biol. 156:437-451. doi:10.1083/jcb.200108135
    • (2002) J. Cell Biol. , vol.156 , pp. 437-451
    • Giet, R.1    McLean, D.2    Descamps, S.3    Lee, M.J.4    Raff, J.W.5    Prigent, C.6    Glover, D.M.7
  • 18
    • 0034574615 scopus 로고    scopus 로고
    • The PACT domain, a conserved centrosomal targeting motif in the coiled-coil proteins AKAP450 and pericentrin
    • Gillingham, A.K., and S. Munro. 2000. The PACT domain, a conserved centrosomal targeting motif in the coiled-coil proteins AKAP450 and pericentrin. EMBO Rep. 1:524-529.
    • (2000) EMBO Rep. , vol.1 , pp. 524-529
    • Gillingham, A.K.1    Munro, S.2
  • 19
  • 20
    • 58549085778 scopus 로고    scopus 로고
    • An integrated work-flow for charting the human interaction proteome: Insights into the PP2A system
    • doi:10.1038/msb.2008.75
    • Glatter, T., A. Wepf, R. Aebersold, and M. Gstaiger. 2009. An integrated work-flow for charting the human interaction proteome: insights into the PP2A system. Mol. Syst. Biol. 5:237. doi:10.1038/msb.2008.75
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 237
    • Glatter, T.1    Wepf, A.2    Aebersold, R.3    Gstaiger, M.4
  • 21
    • 38349078475 scopus 로고    scopus 로고
    • Cep68 and Cep215 (Cdk5rap2) are required for centrosome cohesion
    • doi:10.1242/jcs.020248
    • Graser, S., Y.D. Stierhof, and E.A. Nigg. 2007. Cep68 and Cep215 (Cdk5rap2) are required for centrosome cohesion. J. Cell Sci. 120:4321-4331. doi:10.1242/jcs.020248
    • (2007) J. Cell Sci. , vol.120 , pp. 4321-4331
    • Graser, S.1    Stierhof, Y.D.2    Nigg, E.A.3
  • 23
    • 31944437434 scopus 로고    scopus 로고
    • Nudel contributes to microtubule anchoring at the mother centriole and is involved in both dynein-dependent and -independent centrosomal protein assembly
    • DOI 10.1091/mbc.E05-04-0360
    • Guo, J., Z. Yang, W. Song, Q. Chen, F. Wang, Q. Zhang, and X. Zhu. 2006. Nudel contributes to microtubule anchoring at the mother centriole and is involved in both dynein-dependent and -independent centrosomal protein assembly. Mol. Biol. Cell. 17:680-689. doi:10.1091/mbc.E05-04-0360 (Pubitemid 43191103)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.2 , pp. 680-689
    • Guo, J.1    Yang, Z.2    Song, W.3    Chen, Q.4    Wang, F.5    Zhang, Q.6    Zhu, X.7
  • 24
    • 67650128400 scopus 로고    scopus 로고
    • Plk1-dependent recruitment of gamma-tubulin complexes to mitotic centrosomes involves multiple PCM components
    • doi:10.1371/journal.pone.0005976
    • Haren, L., T. Stearns, and J. Lüders. 2009. Plk1-dependent recruitment of gamma-tubulin complexes to mitotic centrosomes involves multiple PCM components. PLoS One. 4:e5976. doi:10.1371/journal.pone.0005976
    • (2009) PLoS One , vol.4
    • Haren, L.1    Stearns, T.2    Lüders, J.3
  • 26
    • 62049085851 scopus 로고    scopus 로고
    • Adaptor Aly and co-adaptor Thoc5 function in the Tap-p15-mediated nuclear export of HSP70 mRNA
    • doi:10.1038/emboj.2009.5
    • Katahira, J., H. Inoue, E. Hurt, and Y. Yoneda. 2009. Adaptor Aly and co-adaptor Thoc5 function in the Tap-p15-mediated nuclear export of HSP70 mRNA. EMBO J. 28:556-567. doi:10.1038/emboj.2009.5
    • (2009) EMBO J. , vol.28 , pp. 556-567
    • Katahira, J.1    Inoue, H.2    Hurt, E.3    Yoneda, Y.4
  • 27
    • 25444493845 scopus 로고    scopus 로고
    • Aurora a phosphorylation of TACC3/maskin is required for centrosome-dependent microtubule assembly in mitosis
    • DOI 10.1083/jcb.200503023
    • Kinoshita, K., T.L. Noetzel, L. Pelletier, K. Mechtler, D.N. Drechsel, A. Schwager, M. Lee, J.W. Raff, and A.A. Hyman. 2005. Aurora A phosphorylation of TACC3/maskin is required for centrosome-dependent microtubule assembly in mitosis. J. Cell Biol. 170:1047-1055. doi:10.1083/jcb.200503023 (Pubitemid 41362637)
    • (2005) Journal of Cell Biology , vol.170 , Issue.7 , pp. 1047-1055
    • Kinoshita, K.1    Noetzel, T.L.2    Pelletier, L.3    Mechtler, K.4    Drechsel, D.N.5    Schwager, A.6    Lee, M.7    Raff, J.W.8    Hyman, A.A.9
  • 28
    • 14044262340 scopus 로고    scopus 로고
    • RNA interference rescue by bacterial artificial chromosome transgenesis in mammalian tissue culture cells
    • doi:10.1073/pnas.0409861102
    • Kittler, R., L. Pelletier, C. Ma, I. Poser, S. Fischer, A.A. Hyman, and F. Buchholz. 2005. RNA interference rescue by bacterial artificial chromosome transgenesis in mammalian tissue culture cells. Proc. Natl. Acad. Sci. USA. 102:2396-2401. doi:10.1073/pnas.0409861102
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 2396-2401
    • Kittler, R.1    Pelletier, L.2    Ma, C.3    Poser, I.4    Fischer, S.5    Hyman, A.A.6    Buchholz, F.7
  • 29
    • 35848955168 scopus 로고    scopus 로고
    • Mass spectrometry-based functional proteomics: From molecular machines to protein networks
    • DOI 10.1038/nmeth1093, PII NMETH1093
    • Köcher, T., and G. Superti-Furga. 2007. Mass spectrometry-based functional proteomics: from molecular machines to protein networks. Nat. Methods. 4:807-815. doi:10.1038/nmeth1093 (Pubitemid 350055577)
    • (2007) Nature Methods , vol.4 , Issue.10 , pp. 807-815
    • Kocher, T.1    Superti-Furga, G.2
  • 32
    • 0034947117 scopus 로고    scopus 로고
    • Msps/XMAP215 interacts with the centrosomal protein D-TACC to regulate microtubule behaviour
    • doi:10.1038/35083033
    • Lee, M.J., F. Gergely, K. Jeffers, S.Y. Peak-Chew, and J.W. Raff. 2001. Msps/XMAP215 interacts with the centrosomal protein D-TACC to regulate microtubule behaviour. Nat. Cell Biol. 3:643-649. doi:10.1038/35083033
    • (2001) Nat. Cell Biol. , vol.3 , pp. 643-649
    • Lee, M.J.1    Gergely, F.2    Jeffers, K.3    Peak-Chew, S.Y.4    Raff, J.W.5
  • 33
    • 34347218996 scopus 로고    scopus 로고
    • Localization of human TACC3 to mitotic spindles is mediated by phosphorylation on Ser558 by Aurora A: A novel pharmacodynamic method for measuring Aurora a activity
    • doi:10.1158/0008-5472.CAN-07-0122
    • LeRoy, P.J., J.J. Hunter, K.M. Hoar, K.E. Burke, V. Shinde, J. Ruan, D. Bowman, K. Galvin, and J.A. Ecsedy. 2007. Localization of human TACC3 to mitotic spindles is mediated by phosphorylation on Ser558 by Aurora A: a novel pharmacodynamic method for measuring Aurora A activity. Cancer Res. 67:5362-5370. doi:10.1158/0008-5472.CAN-07-0122
    • (2007) Cancer Res. , vol.67 , pp. 5362-5370
    • LeRoy, P.J.1    Hunter, J.J.2    Hoar, K.M.3    Burke, K.E.4    Shinde, V.5    Ruan, J.6    Bowman, D.7    Galvin, K.8    Ecsedy, J.A.9
  • 34
    • 0035086902 scopus 로고    scopus 로고
    • Kendrin/pericentrin-B, a centrosome protein with homology to pericentrin that complexes with PCM-1
    • Li, Q., D. Hansen, A. Killilea, H.C. Joshi, R.E. Palazzo, and R. Balczon. 2001. Kendrin/pericentrin-B, a centrosome protein with homology to pericentrin that complexes with PCM-1. J. Cell Sci. 114:797-809. (Pubitemid 32237152)
    • (2001) Journal of Cell Science , vol.114 , Issue.4 , pp. 797-809
    • Li, Q.1    Hansen, D.2    Killilea, A.3    Joshi, H.C.4    Palazzo, R.E.5    Balczon, R.6
  • 36
    • 33845329203 scopus 로고    scopus 로고
    • Functional and quantitative proteomics using SILAC
    • doi:10.1038/nrm2067
    • Mann, M. 2006. Functional and quantitative proteomics using SILAC. Nat. Rev. Mol. Cell Biol. 7:952-958. doi:10.1038/nrm2067
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 952-958
    • Mann, M.1
  • 37
    • 22344438756 scopus 로고    scopus 로고
    • Recruitment of the human TREX complex to mRNA during splicing
    • doi:10.1101/gad.1302205
    • Masuda, S., R. Das, H. Cheng, E. Hurt, N. Dorman, and R. Reed. 2005. Recruitment of the human TREX complex to mRNA during splicing. Genes Dev. 19:1512-1517. doi:10.1101/gad.1302205
    • (2005) Genes Dev. , vol.19 , pp. 1512-1517
    • Masuda, S.1    Das, R.2    Cheng, H.3    Hurt, E.4    Dorman, N.5    Reed, R.6
  • 38
    • 33748279259 scopus 로고    scopus 로고
    • Emi1 stably binds and inhibits the anaphase-promoting complex/cyclosome as a pseudosubstrate inhibitor
    • doi:10.1101/gad.1454006
    • Miller, J.J., M.K. Summers, D.V. Hansen, M.V. Nachury, N.L. Lehman, A. Loktev, and P.K. Jackson. 2006. Emi1 stably binds and inhibits the anaphase-promoting complex/cyclosome as a pseudosubstrate inhibitor. Genes Dev. 20:2410-2420. doi:10.1101/gad.1454006
    • (2006) Genes Dev. , vol.20 , pp. 2410-2420
    • Miller, J.J.1    Summers, M.K.2    Hansen, D.V.3    Nachury, M.V.4    Lehman, N.L.5    Loktev, A.6    Jackson, P.K.7
  • 39
    • 1642523688 scopus 로고    scopus 로고
    • HGTSE-1 expression stimulates cytoplasmic localization of p53
    • doi:10.1074/jbc.M311123200
    • Monte, M., R. Benetti, L. Collavin, L. Marchionni, G. Del Sal, and C. Schneider. 2004. hGTSE-1 expression stimulates cytoplasmic localization of p53. J. Biol. Chem. 279:11744-11752. doi:10.1074/jbc.M311123200
    • (2004) J. Biol. Chem. , vol.279 , pp. 11744-11752
    • Monte, M.1    Benetti, R.2    Collavin, L.3    Marchionni, L.4    Del Sal, G.5    Schneider, C.6
  • 40
    • 0035337803 scopus 로고    scopus 로고
    • Techniques: Recombinogenic engineering-new options for cloning and manipulating DNA
    • doi:10.1016/S0968-0004(00)01757-6
    • Muyrers, J.P., Y. Zhang, and A.F. Stewart. 2001. Techniques: recombinogenic engineering-new options for cloning and manipulating DNA. Trends Biochem. Sci. 26:325-331. doi:10.1016/S0968-0004(00)01757-6
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 325-331
    • Muyrers, J.P.1    Zhang, Y.2    Stewart, A.F.3
  • 43
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • doi:10.1074/mcp.M200025-MCP200
    • Ong, S.E., B. Blagoev, I. Kratchmarova, D.B. Kristensen, H. Steen, A. Pandey, and M. Mann. 2002. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics. 1:376-386. doi:10.1074/mcp.M200025-MCP200
    • (2002) Mol. Cell. Proteomics. , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 44
    • 0037277179 scopus 로고    scopus 로고
    • Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: The yeast proteome
    • doi:10.1021/pr025556v
    • Peng, J., J.E. Elias, C.C. Thoreen, L.J. Licklider, and S.P. Gygi. 2003. Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: the yeast proteome. J. Proteome Res. 2:43-50. doi:10.1021/pr025556v
    • (2003) J. Proteome Res. , vol.2 , pp. 43-50
    • Peng, J.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5
  • 45
    • 48449090926 scopus 로고    scopus 로고
    • The TACC proteins: TACC-ling microtubule dynamics and centrosome function
    • doi:10.1016/j.tcb.2008.06.005
    • Peset, I., and I. Vernos. 2008. The TACC proteins: TACC-ling microtubule dynamics and centrosome function. Trends Cell Biol. 18:379-388. doi:10.1016/j.tcb.2008.06.005
    • (2008) Trends Cell Biol. , vol.18 , pp. 379-388
    • Peset, I.1    Vernos, I.2
  • 46
    • 0034654399 scopus 로고    scopus 로고
    • The KEN box: An APC recognition signal distinct from the D box targeted by Cdh1
    • Pfleger, C.M., and M.W. Kirschner. 2000. The KEN box: an APC recognition signal distinct from the D box targeted by Cdh1. Genes Dev. 14:655-665.
    • (2000) Genes Dev. , vol.14 , pp. 655-665
    • Pfleger, C.M.1    Kirschner, M.W.2
  • 48
    • 3042566967 scopus 로고    scopus 로고
    • Growth-regulated expression and G0-specific turnover of the mRNA that encodes URH49, a mammalian DExH/D box protein that is highly related to the mRNA export protein UAP56
    • doi:10.1093/nar/gkh347
    • Pryor, A., L. Tung, Z. Yang, F. Kapadia, T.H. Chang, and L.F. Johnson. 2004. Growth-regulated expression and G0-specific turnover of the mRNA that encodes URH49, a mammalian DExH/D box protein that is highly related to the mRNA export protein UAP56. Nucleic Acids Res. 32:1857-1865. doi:10.1093/nar/gkh347
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1857-1865
    • Pryor, A.1    Tung, L.2    Yang, Z.3    Kapadia, F.4    Chang, T.H.5    Johnson, L.F.6
  • 50
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • doi:10.1038/nprot.2007.261
    • Rappsilber, J., M. Mann, and Y. Ishihama. 2007. Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat. Protoc. 2:1896-1906. doi:10.1038/nprot.2007.261
    • (2007) Nat. Protoc. , vol.2 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 52
    • 19344374094 scopus 로고    scopus 로고
    • TREX, SR proteins and export of mRNA
    • doi:10.1016/j.ceb.2005.04.011
    • Reed, R., and H. Cheng. 2005. TREX, SR proteins and export of mRNA. Curr. Opin. Cell Biol. 17:269-273. doi:10.1016/j.ceb.2005.04.011
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 269-273
    • Reed, R.1    Cheng, H.2
  • 53
    • 0037154964 scopus 로고    scopus 로고
    • A conserved mRNA export machinery coupled to pre-mRNA splicing
    • doi:10.1016/S0092-8674(02)00627-X
    • Reed, R., and E. Hurt. 2002. A conserved mRNA export machinery coupled to pre-mRNA splicing. Cell. 108:523-531. doi:10.1016/S0092-8674(02)00627-X
    • (2002) Cell. , vol.108 , pp. 523-531
    • Reed, R.1    Hurt, E.2
  • 54
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • doi:10.1038/13732
    • Rigaut, G., A. Shevchenko, B. Rutz, M. Wilm, M. Mann, and B. Séraphin. 1999. A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol. 17:1030-1032. doi:10.1038/13732
    • (1999) Nat. Biotechnol. , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Séraphin, B.6
  • 55
    • 17844394685 scopus 로고    scopus 로고
    • Clathrin is required for the function of the mitotic spindle
    • doi:10.1038/nature03502
    • Royle, S.J., N.A. Bright, and L. Lagnado. 2005. Clathrin is required for the function of the mitotic spindle. Nature. 434:1152-1157. doi:10.1038/ nature03502
    • (2005) Nature , vol.434 , pp. 1152-1157
    • Royle, S.J.1    Bright, N.A.2    Lagnado, L.3
  • 57
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • doi:10.1016/j.cell.2009.04.042
    • Sowa, M.E., E.J. Bennett, S.P. Gygi, and J.W. Harper. 2009. Defining the human deubiquitinating enzyme interaction landscape. Cell. 138:389-403. doi:10.1016/j.cell.2009.04.042
    • (2009) Cell. , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 58
    • 0042921206 scopus 로고    scopus 로고
    • Caenorhabditis elegans TAC-1 and ZYG-9 form a complex that is essential for long astral and spindle microtubules
    • doi:10.1016/S0960-9822(03)00597-9
    • Srayko, M., S. Quintin, A. Schwager, and A.A. Hyman. 2003. Caenorhabditis elegans TAC-1 and ZYG-9 form a complex that is essential for long astral and spindle microtubules. Curr. Biol. 13:1506-1511. doi:10.1016/S0960-9822(03)00597- 9
    • (2003) Curr. Biol. , vol.13 , pp. 1506-1511
    • Srayko, M.1    Quintin, S.2    Schwager, A.3    Hyman, A.A.4
  • 60
    • 0036169031 scopus 로고    scopus 로고
    • Genesis: Cluster analysis of microarray data
    • doi:10.1093/bioinformatics/18.1.207
    • Sturn, A., J. Quackenbush, and Z. Trajanoski. 2002. Genesis: cluster analysis of microarray data. Bioinformatics. 18:207-208. doi:10.1093/ bioinformatics/18.1.207
    • (2002) Bioinformatics , vol.18 , pp. 207-208
    • Sturn, A.1    Quackenbush, J.2    Trajanoski, Z.3
  • 61
    • 36749100886 scopus 로고    scopus 로고
    • Toward a high-resolution view of nuclear dynamics
    • doi:10.1126/science.1142033
    • Trinkle-Mulcahy, L., and A.I. Lamond. 2007. Toward a high-resolution view of nuclear dynamics. Science. 318:1402-1407. doi:10.1126/science.1142033
    • (2007) Science , vol.318 , pp. 1402-1407
    • Trinkle-Mulcahy, L.1    Lamond, A.I.2
  • 62
    • 0035942271 scopus 로고    scopus 로고
    • Significance analysis of micro-arrays applied to the ionizing radiation response
    • doi:10.1073/pnas.091062498
    • Tusher, V.G., R. Tibshirani, and G. Chu. 2001. Significance analysis of micro-arrays applied to the ionizing radiation response. Proc. Natl. Acad. Sci. USA. 98:5116-5121. doi:10.1073/pnas.091062498
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5116-5121
    • Tusher, V.G.1    Tibshirani, R.2    Chu, G.3
  • 63
    • 0032167455 scopus 로고    scopus 로고
    • A novel p53-inducible gene coding for a microtubule-localized protein with G2-phase-specific expression
    • doi:10.1093/emboj/17.17.5015
    • Utrera, R., L. Collavin, D. Lazarević, D. Delia, and C. Schneider. 1998. A novel p53-inducible gene coding for a microtubule-localized protein with G2-phase-specific expression. EMBO J. 17:5015-5025. doi:10.1093/emboj/17. 17.5015
    • (1998) EMBO J. , vol.17 , pp. 5015-5025
    • Utrera, R.1    Collavin, L.2    Lazarević, D.3    Delia, D.4    Schneider, C.5
  • 64
    • 49549121813 scopus 로고    scopus 로고
    • High confidence determination of specific protein-protein interactions using quantitative mass spectrometry
    • doi:10.1016/j.copbio.2008.06.001
    • Vermeulen, M., N.C. Hubner, and M. Mann. 2008. High confidence determination of specific protein-protein interactions using quantitative mass spectrometry. Curr. Opin. Biotechnol. 19:331-337. doi:10.1016/j.copbio.2008.06. 001
    • (2008) Curr. Opin. Biotechnol. , vol.19 , pp. 331-337
    • Vermeulen, M.1    Hubner, N.C.2    Mann, M.3
  • 65
    • 0033179986 scopus 로고    scopus 로고
    • A human nuclear-localized chaperone that regulates dimerization, DNA binding, and transcriptional activity of bZIP proteins
    • doi:10.1016/S1097-2765(00)80369-X
    • Virbasius, C.M., S. Wagner, and M.R. Green. 1999. A human nuclear-localized chaperone that regulates dimerization, DNA binding, and transcriptional activity of bZIP proteins. Mol. Cell. 4:219-228. doi:10.1016/S1097-2765(00)80369-X
    • (1999) Mol. Cell. , vol.4 , pp. 219-228
    • Virbasius, C.M.1    Wagner, S.2    Green, M.R.3
  • 66
    • 0031664853 scopus 로고    scopus 로고
    • A new logic for DNA engineering using recombination in Escherichia coli
    • doi:10.1038/2417
    • Zhang, Y., F. Buchholz, J.P. Muyrers, and A.F. Stewart. 1998. A new logic for DNA engineering using recombination in Escherichia coli. Nat. Genet. 20:123-128. doi:10.1038/2417
    • (1998) Nat. Genet. , vol.20 , pp. 123-128
    • Zhang, Y.1    Buchholz, F.2    Muyrers, J.P.3    Stewart, A.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.