메뉴 건너뛰기




Volumn 197, Issue 1, 2012, Pages 45-57

Nuclear translation visualized by ribosome-bound nascent chain puromycylation

Author keywords

[No Author keywords available]

Indexed keywords

MONOCLONAL ANTIBODY; PUROMYCIN;

EID: 84860274834     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201112145     Document Type: Article
Times cited : (218)

References (50)
  • 1
    • 84870738307 scopus 로고
    • Amino acid incorporation by isolated thymus nuclei I. The role of desoxyribonucleic acid in protein synthesis
    • Allfrey, V.G. 1954. Amino acid incorporation by isolated thymus nuclei. I. The role of desoxyribonucleic acid in protein synthesis. Proc. Natl. Acad. Sci. USA. 40:881-885. http://dx.doi.org/10.1073/pnas.40.10.881
    • (1954) Proc. Natl. Acad. Sci. USA. , vol.40 , pp. 881-885
    • Allfrey, V.G.1
  • 2
    • 36949084573 scopus 로고
    • Protein synthesis in isolated cell nuclei
    • Allfrey, V.G., A.E. Mirsky, and S. Osawa. 1955. Protein synthesis in isolated cell nuclei. Nature. 176:1042-1049. http://dx.doi.org/10.1038/1761042a0
    • (1955) Nature , vol.176 , pp. 1042-1049
    • Allfrey, V.G.1    Mirsky, A.E.2    Osawa, S.3
  • 3
    • 79961016996 scopus 로고    scopus 로고
    • Major source of antigenic peptides for the MHC class I pathway is produced during the pioneer round of mRNA translation
    • Apcher, S., C. Daskalogianni, F. Lejeune, B. Manoury, G. Imhoos, L. Heslop, and R. Fåhraeus. 2011. Major source of antigenic peptides for the MHC class I pathway is produced during the pioneer round of mRNA translation. Proc. Natl. Acad. Sci. USA. 108:11572-11577. http://dx.doi.org/10.1073/pnas.1104104108
    • (2011) Proc. Natl. Acad. Sci. USA. , vol.108 , pp. 11572-11577
    • Apcher, S.1    Daskalogianni, C.2    Lejeune, F.3    Manoury, B.4    Imhoos, G.5    Heslop, L.6    Fåhraeus, R.7
  • 4
    • 34250898483 scopus 로고    scopus 로고
    • Viral alteration of cellular translational machinery increases defective ribosomal products
    • Berglund, P., D. Finzi, J.R. Bennink, and J.W. Yewdell. 2007. Viral alteration of cellular translational machinery increases defective ribosomal products. J. Virol. 81:7220-7229. http://dx.doi.org/10.1128/JVI.00137-07
    • (2007) J. Virol. , vol.81 , pp. 7220-7229
    • Berglund, P.1    Finzi, D.2    Bennink, J.R.3    Yewdell, J.W.4
  • 6
    • 0002018482 scopus 로고
    • The nucleolus in cell metabolism
    • Birnstiel, M. 1967. The nucleolus in cell metabolism. Annu. Rev. Plant Physiol. 18:25-58. http://dx.doi.org/10.1146/annurev.pp.18.060167.000325
    • (1967) Annu. Rev. Plant Physiol. , vol.18 , pp. 25-58
    • Birnstiel, M.1
  • 7
    • 0007995733 scopus 로고
    • Intranuclear site of histone synthesis
    • Birnstiel, M.L., and W.G. Flamm. 1964. Intranuclear site of histone synthesis. Science. 145:1435-1437. http://dx.doi.org/10.1126/science.145.3639.1435
    • (1964) Science , vol.145 , pp. 1435-1437
    • Birnstiel, M.L.1    Flamm, W.G.2
  • 8
    • 0036321944 scopus 로고    scopus 로고
    • Hijacking the translation apparatus by RNA viruses
    • Bushell, M., and P. Sarnow. 2002. Hijacking the translation apparatus by RNA viruses. J. Cell Biol. 158:395-399. http://dx.doi.org/10.1083/jcb.200205044
    • (2002) J. Cell Biol. , vol.158 , pp. 395-399
    • Bushell, M.1    Sarnow, P.2
  • 9
    • 2342640073 scopus 로고    scopus 로고
    • Does protein synthesis occur in the nucleus? Curr
    • Dahlberg, J.E., and E. Lund. 2004. Does protein synthesis occur in the nucleus? Curr. Opin. Cell Biol. 16:335-338. http://dx.doi.org/10.1016/j.ceb.2004.03.006
    • (2004) Opin. Cell Biol. , vol.16 , pp. 335-338
    • Dahlberg, J.E.1    Lund, E.2
  • 11
    • 78650675638 scopus 로고    scopus 로고
    • RNA polymerase II inhibitors dissociate antigenic peptide generation from normal viral protein synthesis: a role for nuclear translation in defective ribosomal product synthesis?
    • Dolan, B.P., J.J. Knowlton, A. David, J.R. Bennink, and J.W. Yewdell. 2010. RNA polymerase II inhibitors dissociate antigenic peptide generation from normal viral protein synthesis: a role for nuclear translation in defective ribosomal product synthesis? J. Immunol. 185:6728-6733. http://dx.doi.org/10.4049/jimmunol.1002543
    • (2010) J. Immunol. , vol.185 , pp. 6728-6733
    • Dolan, B.P.1    Knowlton, J.J.2    David, A.3    Bennink, J.R.4    Yewdell, J.W.5
  • 12
    • 0034707668 scopus 로고    scopus 로고
    • Nuclear eukaryotic initiation factor 4E (eIF4E) colocalizes with splicing factors in speckles
    • Dostie, J., F. Lejbkowicz, and N. Sonenberg. 2000. Nuclear eukaryotic initiation factor 4E (eIF4E) colocalizes with splicing factors in speckles. J. Cell Biol. 148:239-247. http://dx.doi.org/10.1083/jcb.148.2.239
    • (2000) J. Cell Biol. , vol.148 , pp. 239-247
    • Dostie, J.1    Lejbkowicz, F.2    Sonenberg, N.3
  • 13
    • 0030928059 scopus 로고    scopus 로고
    • Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells
    • Eggers, D.K., W.J. Welch, and W.J. Hansen. 1997. Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells. Mol. Biol. Cell. 8:1559-1573.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 1559-1573
    • Eggers, D.K.1    Welch, W.J.2    Hansen, W.J.3
  • 14
    • 1642570265 scopus 로고    scopus 로고
    • A nuclear translation-like factor eIF4AIII is recruited to the mRNA during splicing and functions in nonsense-mediated decay
    • Ferraiuolo, M.A., C.S. Lee, L.W. Ler, J.L. Hsu, M. Costa-Mattioli, M.J. Luo, R. Reed, and N. Sonenberg. 2004. A nuclear translation-like factor eIF4AIII is recruited to the mRNA during splicing and functions in nonsense-mediated decay. Proc. Natl. Acad. Sci. USA. 101:4118-4123. http://dx.doi.org/10.1073/pnas.0400933101
    • (2004) Proc. Natl. Acad. Sci. USA. , vol.101 , pp. 4118-4123
    • Ferraiuolo, M.A.1    Lee, C.S.2    Ler, L.W.3    Hsu, J.L.4    Costa-Mattioli, M.5    Luo, M.J.6    Reed, R.7    Sonenberg, N.8
  • 15
    • 0017577805 scopus 로고
    • Inhibition of translation in eukaryotic systems by harringtonine
    • Fresno, M., A. Jiménez, and D. Vázquez. 1977. Inhibition of translation in eukaryotic systems by harringtonine. Eur. J. Biochem. 72:323-330. http://dx.doi.org/10.1111/j.1432-1033.1977.tb11256.x
    • (1977) Eur. J. Biochem. , vol.72 , pp. 323-330
    • Fresno, M.1    Jiménez, A.2    Vázquez, D.3
  • 16
    • 0037781517 scopus 로고    scopus 로고
    • The puzzling lateral flexible stalk of the ribosome
    • Gonzalo, P., and J.P. Reboud. 2003. The puzzling lateral flexible stalk of the ribosome. Biol. Cell. 95:179-193. http://dx.doi.org/10.1016/S0248-4900(03) 00034-0
    • (2003) Biol. Cell. , vol.95 , pp. 179-193
    • Gonzalo, P.1    Reboud, J.P.2
  • 18
    • 4043164045 scopus 로고    scopus 로고
    • Nuclear localization of aminoacyl-tRNA synthetases using single-cell capillary electrophoresis laser-induced fluorescence analysis
    • Gunasekera, N., S.W. Lee, S. Kim, K. Musier-Forsyth, and E. Arriaga. 2004. Nuclear localization of aminoacyl-tRNA synthetases using single-cell capillary electrophoresis laser-induced fluorescence analysis. Anal. Chem. 76:4741-4746. http://dx.doi.org/10.1021/ac049567e
    • (2004) Anal. Chem. , vol.76 , pp. 4741-4746
    • Gunasekera, N.1    Lee, S.W.2    Kim, S.3    Musier-Forsyth, K.4    Arriaga, E.5
  • 19
    • 0038013670 scopus 로고    scopus 로고
    • Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit
    • Hansen, J.L., P.B. Moore, and T.A. Steitz. 2003. Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit. J. Mol. Biol. 330:1061-1075. http://dx.doi.org/10.1016/S0022-2836(03) 00668-5
    • (2003) J. Mol. Biol. , vol.330 , pp. 1061-1075
    • Hansen, J.L.1    Moore, P.B.2    Steitz, T.A.3
  • 20
    • 0035839002 scopus 로고    scopus 로고
    • Coupled transcription and translation within nuclei of mammalian cells
    • Iborra, F.J., D.A. Jackson, and P.R. Cook. 2001. Coupled transcription and translation within nuclei of mammalian cells. Science. 293:1139-1142. http://dx.doi.org/10.1126/science.1061216
    • (2001) Science , vol.293 , pp. 1139-1142
    • Iborra, F.J.1    Jackson, D.A.2    Cook, P.R.3
  • 22
    • 0015540372 scopus 로고
    • Inhibition of reticulocyte peptidechain initiation by pactamycin: accumulation of inactive ribosomal initiation complexes
    • Kappen, L.S., H. Suzuki, and I.H. Goldberg. 1973. Inhibition of reticulocyte peptidechain initiation by pactamycin: accumulation of inactive ribosomal initiation complexes. Proc. Natl. Acad. Sci. USA. 70:22-26. http://dx.doi.org/10.1073/pnas.70.1.22
    • (1973) Proc. Natl. Acad. Sci. USA. , vol.70 , pp. 22-26
    • Kappen, L.S.1    Suzuki, H.2    Goldberg, I.H.3
  • 23
    • 34848865040 scopus 로고    scopus 로고
    • Colocalization of transcription and translation within cytoplasmic poxvirus factories coordinates viral expression and subjugates host functions
    • Katsafanas, G.C., and B. Moss. 2007. Colocalization of transcription and translation within cytoplasmic poxvirus factories coordinates viral expression and subjugates host functions. Cell Host Microbe. 2:221-228. http://dx.doi.org/10.1016/j.chom.2007.08.005
    • (2007) Cell Host Microbe , vol.2 , pp. 221-228
    • Katsafanas, G.C.1    Moss, B.2
  • 24
    • 0036154218 scopus 로고    scopus 로고
    • Evidence that ternary complex (eIF2-GTP-tRNA(i)(Met))-deficient preinitiation complexes are core constituents of mammalian stress granules
    • Kedersha, N., S. Chen, N. Gilks, W. Li, I.J. Miller, J. Stahl, and P. Anderson. 2002. Evidence that ternary complex (eIF2-GTP-tRNA(i)(Met))-deficient preinitiation complexes are core constituents of mammalian stress granules. Mol. Biol. Cell. 13:195-210. http://dx.doi.org/10.1091/mbc.01-05-0221
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 195-210
    • Kedersha, N.1    Chen, S.2    Gilks, N.3    Li, W.4    Miller, I.J.5    Stahl, J.6    Anderson, P.7
  • 25
    • 69949191661 scopus 로고    scopus 로고
    • Aberrant mRNA transcripts and the nonsense-mediated decay proteins UPF2 and UPF3 are enriched in the Arabidopsis nucleolus
    • Kim, S.H., O.A. Koroleva, D. Lewandowska, A.F. Pendle, G.P. Clark, C.G. Simpson, P.J. Shaw, and J.W. Brown. 2009. Aberrant mRNA transcripts and the nonsense-mediated decay proteins UPF2 and UPF3 are enriched in the Arabidopsis nucleolus. Plant Cell. 21:2045-2057. http://dx.doi.org/10.1105/tpc.109.067736
    • (2009) Plant Cell , vol.21 , pp. 2045-2057
    • Kim, S.H.1    Koroleva, O.A.2    Lewandowska, D.3    Pendle, A.F.4    Clark, G.P.5    Simpson, C.G.6    Shaw, P.J.7    Brown, J.W.8
  • 26
    • 35548973466 scopus 로고    scopus 로고
    • Functional specificity among ribosomal proteins regulates gene expression
    • Komili, S., N.G. Farny, F.P. Roth, and P.A. Silver. 2007. Functional specificity among ribosomal proteins regulates gene expression. Cell. 131:557-571. http://dx.doi.org/10.1016/j.cell.2007.08.037
    • (2007) Cell , vol.131 , pp. 557-571
    • Komili, S.1    Farny, N.G.2    Roth, F.P.3    Silver, P.A.4
  • 27
    • 0026705268 scopus 로고
    • A fraction of the mRNA 5' cap-binding protein, eukaryotic initiation factor 4E, localizes to the nucleus
    • Lejbkowicz, F., C. Goyer, A. Darveau, S. Neron, R. Lemieux, and N. Sonenberg. 1992. A fraction of the mRNA 5' cap-binding protein, eukaryotic initiation factor 4E, localizes to the nucleus. Proc. Natl. Acad. Sci. USA. 89:9612-9616. http://dx.doi.org/10.1073/pnas.89.20.9612
    • (1992) Proc. Natl. Acad. Sci. USA. , vol.89 , pp. 9612-9616
    • Lejbkowicz, F.1    Goyer, C.2    Darveau, A.3    Neron, S.4    Lemieux, R.5    Sonenberg, N.6
  • 28
    • 1442358797 scopus 로고    scopus 로고
    • Dendritic cell aggresome-like induced structures are dedicated areas for ubiquitination and storage of newly synthesized defective proteins
    • Lelouard, H., V. Ferrand, D. Marguet, J. Bania, V. Camosseto, A. David, E. Gatti, and P. Pierre. 2004. Dendritic cell aggresome-like induced structures are dedicated areas for ubiquitination and storage of newly synthesized defective proteins. J. Cell Biol. 164:667-675. http://dx.doi.org/10.1083/jcb.200312073
    • (2004) J. Cell Biol. , vol.164 , pp. 667-675
    • Lelouard, H.1    Ferrand, V.2    Marguet, D.3    Bania, J.4    Camosseto, V.5    David, A.6    Gatti, E.7    Pierre, P.8
  • 30
    • 1842283293 scopus 로고
    • Localization of the puromycin binding site on the large ribosomal subunit of Escherichia coli by immunoelectron microscopy
    • Lührmann, R., R. Bald, M. Stöffler-Meilicke, and G. Stöffler. 1981. Localization of the puromycin binding site on the large ribosomal subunit of Escherichia coli by immunoelectron microscopy. Proc. Natl. Acad. Sci. USA. 78: 7276-7280. http://dx.doi.org/10.1073/pnas.78.12.7276
    • (1981) Proc. Natl. Acad. Sci. USA. , vol.78 , pp. 7276-7280
    • Lührmann, R.1    Bald, R.2    Stöffler-Meilicke, M.3    Stöffler, G.4
  • 31
    • 0032509304 scopus 로고    scopus 로고
    • Proofreading and aminoacylation of tRNAs before export from the nucleus
    • Lund, E., and J.E. Dahlberg. 1998. Proofreading and aminoacylation of tRNAs before export from the nucleus. Science. 282:2082-2085. http://dx.doi.org/10.1126/science.282.5396.2082
    • (1998) Science , vol.282 , pp. 2082-2085
    • Lund, E.1    Dahlberg, J.E.2
  • 32
    • 0037126063 scopus 로고    scopus 로고
    • The ribosome filter hypothesis
    • Mauro, V.P., and G.M. Edelman. 2002. The ribosome filter hypothesis. Proc. Natl. Acad. Sci. USA. 99:12031-12036. http://dx.doi.org/10.1073/pnas.192442499
    • (2002) Proc. Natl. Acad. Sci. USA. , vol.99 , pp. 12031-12036
    • Mauro, V.P.1    Edelman, G.M.2
  • 33
    • 0035008608 scopus 로고    scopus 로고
    • Interaction of eukaryotic translation initiation factor 4G with the nuclear cap-binding complex provides a link between nuclear and cytoplasmic functions of the m(7) guanosine cap
    • McKendrick, L., E. Thompson, J. Ferreira, S.J. Morley, and J.D. Lewis. 2001. Interaction of eukaryotic translation initiation factor 4G with the nuclear cap-binding complex provides a link between nuclear and cytoplasmic functions of the m(7) guanosine cap. Mol. Cell. Biol. 21:3632-3641. http://dx.doi.org/10.1128/MCB.21.11.3632-3641.2001
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3632-3641
    • McKendrick, L.1    Thompson, E.2    Ferreira, J.3    Morley, S.J.4    Lewis, J.D.5
  • 34
    • 0034644704 scopus 로고    scopus 로고
    • Active aminoacyl-tRNA synthetases are present in nuclei as a high molecular weight multienzyme complex
    • Nathanson, L., and M.P. Deutscher. 2000. Active aminoacyl-tRNA synthetases are present in nuclei as a high molecular weight multienzyme complex. J. Biol. Chem. 275:31559-31562. http://dx.doi.org/10.1074/jbc.C000385200
    • (2000) J. Biol. Chem. , vol.275 , pp. 31559-31562
    • Nathanson, L.1    Deutscher, M.P.2
  • 35
    • 0037278925 scopus 로고    scopus 로고
    • Nuclear protein synthesis: a reevaluation
    • Nathanson, L., T. Xia, and M.P. Deutscher. 2003. Nuclear protein synthesis: a reevaluation. RNA. 9:9-13. http://dx.doi.org/10.1261/rna.2990203
    • (2003) RNA , vol.9 , pp. 9-13
    • Nathanson, L.1    Xia, T.2    Deutscher, M.P.3
  • 36
    • 0034688997 scopus 로고    scopus 로고
    • The nucleolus and the four ribonucleoproteins of translation
    • Pederson, T., and J.C. Politz. 2000. The nucleolus and the four ribonucleoproteins of translation. J. Cell Biol. 148:1091-1095. http://dx.doi.org/10.1083/jcb.148.6.1091
    • (2000) J. Cell Biol. , vol.148 , pp. 1091-1095
    • Pederson, T.1    Politz, J.C.2
  • 37
    • 0015195582 scopus 로고
    • Inhibitors of ribosome functions
    • Pestka, S. 1971. Inhibitors of ribosome functions. Annu. Rev. Microbiol. 25:487-562. http://dx.doi.org/10.1146/annurev.mi.25.100171.002415
    • (1971) Annu. Rev. Microbiol. , vol.25 , pp. 487-562
    • Pestka, S.1
  • 38
    • 0015502063 scopus 로고
    • Studies on transfer ribonucleic acid-ribosome complexes XXI. Effect of antibiotics on peptidylpuromycin synthesis by mammalian polyribosomes
    • Pestka, S., H. Rosenfeld, R. Harris, and H. Hintikka. 1972. Studies on transfer ribonucleic acid-ribosome complexes. XXI. Effect of antibiotics on peptidylpuromycin synthesis by mammalian polyribosomes. J. Biol. Chem. 247: 6895-6900.
    • (1972) J. Biol. Chem. , vol.247 , pp. 6895-6900
    • Pestka, S.1    Rosenfeld, H.2    Harris, R.3    Hintikka, H.4
  • 39
    • 0016442420 scopus 로고
    • Degradation of abnormal proteins in Escherichia coli Formation of protein inclusions in cells exposed to amino acid analogs
    • Prouty, W.F., M.J. Karnovsky, and A.L. Goldberg. 1975. Degradation of abnormal proteins in Escherichia coli. Formation of protein inclusions in cells exposed to amino acid analogs. J. Biol. Chem. 250:1112-1122.
    • (1975) J. Biol. Chem. , vol.250 , pp. 1112-1122
    • Prouty, W.F.1    Karnovsky, M.J.2    Goldberg, A.L.3
  • 40
    • 33749548838 scopus 로고    scopus 로고
    • Visualization of mRNA translation in living cells
    • Rodriguez, A.J., S.M. Shenoy, R.H. Singer, and J. Condeelis. 2006. Visualization of mRNA translation in living cells. J. Cell Biol. 175:67-76. http://dx.doi.org/10.1083/jcb.200512137
    • (2006) J. Cell Biol. , vol.175 , pp. 67-76
    • Rodriguez, A.J.1    Shenoy, S.M.2    Singer, R.H.3    Condeelis, J.4
  • 41
    • 63949084607 scopus 로고    scopus 로고
    • SUnSET, a nonradioactive method to monitor protein synthesis
    • Schmidt, E.K., G. Clavarino, M. Ceppi, and P. Pierre. 2009. SUnSET, a nonradioactive method to monitor protein synthesis. Nat. Methods. 6:275-277. http://dx.doi.org/10.1038/nmeth.1314
    • (2009) Nat. Methods. , vol.6 , pp. 275-277
    • Schmidt, E.K.1    Clavarino, G.2    Ceppi, M.3    Pierre, P.4
  • 43
    • 70349780560 scopus 로고    scopus 로고
    • The eIF3 interactome reveals the translasome, a supercomplex linking protein synthesis and degradation machineries
    • Sha, Z., L.M. Brill, R. Cabrera, O. Kleifeld, J.S. Scheliga, M.H. Glickman, E.C. Chang, and D.A. Wolf. 2009. The eIF3 interactome reveals the translasome, a supercomplex linking protein synthesis and degradation machineries. Mol. Cell. 36:141-152. http://dx.doi.org/10.1016/j.molcel.2009.09.026
    • (2009) Mol. Cell. , vol.36 , pp. 141-152
    • Sha, Z.1    Brill, L.M.2    Cabrera, R.3    Kleifeld, O.4    Scheliga, J.S.5    Glickman, M.H.6    Chang, E.C.7    Wolf, D.A.8
  • 44
    • 3342935872 scopus 로고    scopus 로고
    • A general approach to detect protein expression in vivo using fluorescent puromycin conjugates
    • Starck, S.R., H.M. Green, J. Alberola-Ila, and R.W. Roberts. 2004. A general approach to detect protein expression in vivo using fluorescent puromycin conjugates. Chem. Biol. 11:999-1008. http://dx.doi.org/10.1016/j.chembiol.2004.05.011
    • (2004) Chem. Biol. , vol.11 , pp. 999-1008
    • Starck, S.R.1    Green, H.M.2    Alberola-Ila, J.3    Roberts, R.W.4
  • 45
    • 42949117285 scopus 로고    scopus 로고
    • Analysis of mRNA partitioning between the cytosol and endoplasmic reticulum compartments of mammalian cells
    • Stephens, S.B., R.D. Dodd, R.S. Lerner, B.M. Pyhtila, and C.V. Nicchitta. 2008. Analysis of mRNA partitioning between the cytosol and endoplasmic reticulum compartments of mammalian cells. Methods Mol. Biol. 419:197-214. http://dx.doi.org/10.1007/978-1-59745-033-1_14
    • (2008) Methods Mol. Biol. , vol.419 , pp. 197-214
    • Stephens, S.B.1    Dodd, R.D.2    Lerner, R.S.3    Pyhtila, B.M.4    Nicchitta, C.V.5
  • 46
    • 0029347097 scopus 로고
    • Puromycin induces apoptosis of developing chick sympathetic neurons in a similar manner to NGF-deprivation
    • Sugita, M., T. Morita, and T. Yonesaki. 1995. Puromycin induces apoptosis of developing chick sympathetic neurons in a similar manner to NGF-deprivation. Zoolog. Sci. 12:419-425. http://dx.doi.org/10.2108/zsj.12.419
    • (1995) Zoolog. Sci. , vol.12 , pp. 419-425
    • Sugita, M.1    Morita, T.2    Yonesaki, T.3
  • 47
    • 77950839936 scopus 로고    scopus 로고
    • Spatially restricting gene expression by local translation at synapses
    • Wang, D.O., K.C. Martin, and R.S. Zukin. 2010. Spatially restricting gene expression by local translation at synapses. Trends Neurosci. 33:173-182. http://dx.doi.org/10.1016/j.tins.2010.01.005
    • (2010) Trends Neurosci , vol.33 , pp. 173-182
    • Wang, D.O.1    Martin, K.C.2    Zukin, R.S.3
  • 48
    • 0036809882 scopus 로고    scopus 로고
    • Nonsenseassociated altered splicing: a frame-dependent response distinct from nonsense-mediated decay
    • Wang, J., Y.-F. Chang, J.I. Hamilton, and M.F. Wilkinson. 2002. Nonsenseassociated altered splicing: a frame-dependent response distinct from nonsense-mediated decay. Mol. Cell. 10:951-957. http://dx.doi.org/10.1016/S1097-2765(02)00635-4
    • (2002) Mol. Cell. , vol.10 , pp. 951-957
    • Wang, J.1    Chang, Y.-F.2    Hamilton, J.I.3    Wilkinson, M.F.4
  • 49
    • 33745833084 scopus 로고    scopus 로고
    • The DRiP hypothesis decennial: support, controversy, refinement and extension
    • Yewdell, J.W., and C.V. Nicchitta. 2006. The DRiP hypothesis decennial: support, controversy, refinement and extension. Trends Immunol. 27:368-373. http://dx.doi.org/10.1016/j.it.2006.06.008
    • (2006) Trends Immunol , vol.27 , pp. 368-373
    • Yewdell, J.W.1    Nicchitta, C.V.2
  • 50
    • 0014528303 scopus 로고
    • Protein synthesis in isolated nuclei and nucleoli of HeLa cells
    • Zimmerman, E.F., J. Hackney, P. Nelson, and I.M. Arias. 1969. Protein synthesis in isolated nuclei and nucleoli of HeLa cells. Biochemistry. 8:2636-2644. http://dx.doi.org/10.1021/bi00834a058
    • (1969) Biochemistry , vol.8 , pp. 2636-2644
    • Zimmerman, E.F.1    Hackney, J.2    Nelson, P.3    Arias, I.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.