메뉴 건너뛰기




Volumn 288, Issue 44, 2013, Pages 31689-31700

Balanced production of ribosome components is required for proper G/S transition in saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROLIFERATION; CELLS; CYTOLOGY; PROTEINS;

EID: 84887123065     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.500488     Document Type: Article
Times cited : (35)

References (68)
  • 2
    • 0035902108 scopus 로고    scopus 로고
    • Genome maintenance mechanisms for preventing cancer
    • DOI 10.1038/35077232
    • Hoeijmakers, J. H. (2001) Genome maintenance mechanisms for preventing cancer. Nature 411, 366-374 (Pubitemid 32467046)
    • (2001) Nature , vol.411 , Issue.6835 , pp. 366-374
    • Hoeijmakers, J.H.J.1
  • 3
    • 85015066476 scopus 로고    scopus 로고
    • DNA damage and repair
    • DOI 10.1038/nature01408
    • Friedberg, E. C. (2003) DNA damage and repair. Nature 421, 436-440 (Pubitemid 36157951)
    • (2003) Nature , vol.421 , Issue.6921 , pp. 436-440
    • Friedberg, E.C.1
  • 4
    • 79958748581 scopus 로고    scopus 로고
    • Chromosomes and cancer cells
    • Thompson, S. L., and Compton, D. A. (2011) Chromosomes and cancer cells. Chromosome Res. 19, 433-444
    • (2011) Chromosome Res. , vol.19 , pp. 433-444
    • Thompson, S.L.1    Compton, D.A.2
  • 5
    • 0033229970 scopus 로고    scopus 로고
    • The economics of ribosome biosynthesis in yeast
    • DOI 10.1016/S0968-0004(99)01460-7, PII S0968000499014607
    • Warner, J. R. (1999) The economics of ribosome biosynthesis in yeast. Trends Biochem. Sci. 24, 437-440 (Pubitemid 29528205)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.11 , pp. 437-440
    • Warner, J.R.1
  • 7
    • 34347336512 scopus 로고    scopus 로고
    • Potential interface between ribosomal protein production and pre-rRNA processing
    • DOI 10.1128/MCB.02062-06
    • Rudra, D., Mallick, J., Zhao, Y., and Warner, J. R. (2007) Potential interface between ribosomal protein production and pre-rRNA processing. Mol. Cell. Biol. 27, 4815-4824 (Pubitemid 47016134)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.13 , pp. 4815-4824
    • Rudra, D.1    Mallick, J.2    Zhao, Y.3    Warner, J.R.4
  • 8
    • 0033805924 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae transcription elongation mutants are defective in PUR5 induction in response to nucleotide depletion
    • Shaw, R. J., and Reines, D. (2000) Saccharomyces cerevisiae transcription elongation mutants are defective in PUR5 induction in response to nucleotide depletion. Mol. Cell. Biol. 20, 7427-7437
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7427-7437
    • Shaw, R.J.1    Reines, D.2
  • 9
    • 0035980130 scopus 로고    scopus 로고
    • Regulation of an IMP dehydrogenase gene and its overexpression in drug-sensitive transcription elongation mutants of yeast
    • Shaw, R. J., and Wilson., J. L., Smith, K. T., and Reines, D. (2001) Regulation of an IMP dehydrogenase gene and its overexpression in drug-sensitive transcription elongation mutants of yeast. J. Biol. Chem. 276, 32905-32916
    • (2001) J. Biol. Chem. , vol.276 , pp. 32905-32916
    • Shaw, R.J.1    Wilson, J.L.2    Smith, K.T.3    Reines, D.4
  • 10
    • 0033839222 scopus 로고    scopus 로고
    • In vitro effects of mycophenolic acid on cell cycle and activation of human lymphocytes
    • DOI 10.1016/S0009-8981(00)00297-7, PII S0009898100002977
    • Heinschink, A., Raab, M., Daxecker, H., Griesmacher, A., and Müller, M. M. (2000) In vitro effects of mycophenolic acid on cell cycle and activation of human lymphocytes. Clin. Chim. Acta 300, 23-28 (Pubitemid 30665771)
    • (2000) Clinica Chimica Acta , vol.300 , Issue.1-2 , pp. 23-28
    • Heinschink, A.1    Raab, M.2    Daxecker, H.3    Griesmacher, A.4    Muller, M.M.5
  • 11
    • 0032523010 scopus 로고    scopus 로고
    • Effects of guanine nucleotide depletion on cell cycle progression in human T lymphocytes
    • Laliberté, J., Yee, A., Xiong, Y., and Mitchell, B. S. (1998) Effects of guanine nucleotide depletion on cell cycle progression in human T lymphocytes. Blood 91, 2896-2904 (Pubitemid 28227540)
    • (1998) Blood , vol.91 , Issue.8 , pp. 2896-2904
    • Laliberte, J.1    Yee, A.2    Xiong, Y.3    Mitchell, B.S.4
  • 12
    • 33646439982 scopus 로고    scopus 로고
    • Identification of type 1 inosine monophosphate dehydrogenase as an antiangiogenic drug target
    • Chong, C. R., and Qian., D. Z., Pan, F., Wei, Y., Pili, R., and Sullivan., D. J. Jr., and Liu, J. O. (2006) Identification of type 1 inosine monophosphate dehydrogenase as an antiangiogenic drug target. J. Med. Chem. 49, 2677-2680
    • (2006) J. Med. Chem. , vol.49 , pp. 2677-2680
    • Chong, C.R.1    Qian, D.Z.2    Pan, F.3    Wei, Y.4    Pili, R.5    Sullivan Jr., D.J.6    Liu, J.O.7
  • 13
    • 0035824515 scopus 로고    scopus 로고
    • Proteome analysis and morphological studies reveal multiple effects of the immunosuppressive drug mycophenolic acid specifically resulting from guanylic nucleotide depletion
    • Escobar-Henriques, M., Balguerie, A., Monribot, C., Boucherie, H., and Daignan-Fornier, B. (2001) Proteome analysis and morphological studies reveal multiple effects of the immunosuppressive drug mycophenolic acid specifically resulting from guanylic nucleotide depletion. J. Biol. Chem. 276, 46237-46242
    • (2001) J. Biol. Chem. , vol.276 , pp. 46237-46242
    • Escobar-Henriques, M.1    Balguerie, A.2    Monribot, C.3    Boucherie, H.4    Daignan-Fornier, B.5
  • 14
    • 0042208190 scopus 로고    scopus 로고
    • Functional distinctions between IMP dehydrogenase genes in providing mycophenolate resistance and guanine prototrophy to yeast
    • DOI 10.1074/jbc.M303736200
    • Hyle, J. W., and Shaw., R. J., and Reines, D. (2003) Functional distinctions between IMP dehydrogenase genes in providing mycophenolate resistance and guanine prototrophy to yeast. J. Biol. Chem. 278, 28470-28478 (Pubitemid 36935749)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.31 , pp. 28470-28478
    • Hyle, J.W.1    Shaw, R.J.2    Reines, D.3
  • 16
    • 45549098246 scopus 로고    scopus 로고
    • Mycophenolic acid activation of p53 requires ribosomal proteins L5 and L11
    • Sun, X. X., and Dai., M. S., and Lu, H. (2008) Mycophenolic acid activation of p53 requires ribosomal proteins L5 and L11. J. Biol. Chem. 283, 12387-12392
    • (2008) J. Biol. Chem. , vol.283 , pp. 12387-12392
    • Sun, X.X.1    Dai, M.S.2    Lu, H.3
  • 17
    • 77955479087 scopus 로고    scopus 로고
    • Perturbation of 60S ribosomal biogenesis results in ribosomal protein L5- and L11-dependent p53 activation
    • Sun, X. X., and Wang., Y. G., Xirodimas, D. P., and Dai, M. S. (2010) Perturbation of 60S ribosomal biogenesis results in ribosomal protein L5- and L11-dependent p53 activation. J. Biol. Chem. 285, 25812-25821
    • (2010) J. Biol. Chem. , vol.285 , pp. 25812-25821
    • Sun, X.X.1    Wang, Y.G.2    Xirodimas, D.P.3    Dai, M.S.4
  • 18
    • 34247204753 scopus 로고    scopus 로고
    • 5-fluorouracil activation of p53 involves an MDM2-ribosomal protein interaction
    • DOI 10.1074/jbc.M610621200
    • Sun, X. X., and Dai., M. S., and Lu, H. (2007) 5-Fluorouracil activation of p53 involves an MDM2-ribosomal protein interaction. J. Biol. Chem. 282, 8052-8059 (Pubitemid 47093604)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.11 , pp. 8052-8059
    • Sun, X.-X.1    Dai, M.-S.2    Lu, H.3
  • 19
    • 33747654496 scopus 로고    scopus 로고
    • Regulation of the MDM2-p53 pathway by ribosomal protein L11 involves a post-ubiquitination mechanism
    • DOI 10.1074/jbc.M602596200
    • Dai, M. S., Shi, D., Jin, Y., Sun, X. X., Zhang, Y., and Grossman., S. R., and Lu, H. (2006) Regulation of the MDM2-p53 pathway by ribosomal protein L11 involves a post-ubiquitination mechanism. J. Biol. Chem. 281, 24304-24313 (Pubitemid 44274203)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.34 , pp. 24304-24313
    • Dai, M.-S.1    Shi, D.2    Jin, Y.3    Sun, X.-X.4    Zhang, Y.5    Grossman, S.R.6    Lu, H.7
  • 20
    • 46149087535 scopus 로고    scopus 로고
    • Aberrant expression of nucleostemin activates p53 and induces cell cycle arrest via inhibition of MDM2
    • DOI 10.1128/MCB.01662-07
    • Dai, M. S., and Sun., X. X., and Lu, H. (2008) Aberrant expression of nucleostemin activates p53 and induces cell cycle arrest via inhibition of MDM2. Mol. Cell. Biol. 28, 4365-4376 (Pubitemid 351904958)
    • (2008) Molecular and Cellular Biology , vol.28 , Issue.13 , pp. 4365-4376
    • Dai, M.-S.1    Sun, X.-X.2    Lu, H.3
  • 21
    • 7244238177 scopus 로고    scopus 로고
    • Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5
    • DOI 10.1074/jbc.M403722200
    • Dai, M. S., and Lu, H. (2004) Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5. J. Biol. Chem. 279, 44475-44482 (Pubitemid 39430853)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.43 , pp. 44475-44482
    • Dai, M.-S.1    Lu, H.2
  • 22
    • 84858980187 scopus 로고    scopus 로고
    • Ubiquitin - And MDM2 E3 ligase-independent proteasomal turnover of nucleostemin in response to GTP depletion
    • Lo, D., and Dai., M. S., Sun, X. X., Zeng, S. X., and Lu, H. (2012) Ubiquitin - and MDM2 E3 ligase-independent proteasomal turnover of nucleostemin in response to GTP depletion. J. Biol. Chem. 287, 10013-10020
    • (2012) J. Biol. Chem. , vol.287 , pp. 10013-10020
    • Lo, D.1    Dai, M.S.2    Sun, X.X.3    Zeng, S.X.4    Lu, H.5
  • 23
    • 0038724615 scopus 로고    scopus 로고
    • Regulation of HDM2 activity by the ribosomal protein L11
    • DOI 10.1016/S1535-6108(03)00134-X
    • Lohrum, M. A., and Ludwig., R. L., Kubbutat, M. H., Hanlon, M., and Vousden, K. H. (2003) Regulation of HDM2 activity by the ribosomal protein L11. Cancer Cell 3, 577-587 (Pubitemid 36808652)
    • (2003) Cancer Cell , vol.3 , Issue.6 , pp. 577-587
    • Lohrum, M.A.E.1    Ludwig, R.L.2    Kubbutat, M.H.G.3    Hanlon, M.4    Vousden, K.H.5
  • 24
    • 0242721592 scopus 로고    scopus 로고
    • Ribosomal Protein L11 Negatively Regulates Oncoprotein MDM2 and Mediates a p53-Dependent Ribosomal-Stress Checkpoint Pathway
    • DOI 10.1128/MCB.23.23.8902-8912.2003
    • Zhang, Y., and Wolf., G. W., Bhat, K., Jin, A., Allio, T., and Burkhart., W. A., and Xiong, Y. (2003) Ribosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway. Mol. Cell. Biol. 23, 8902-8912 (Pubitemid 37433388)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.23 , pp. 8902-8912
    • Zhang, Y.1    Wolf, G.W.2    Bhat, K.3    Jin, A.4    Allio, T.5    Burkhart, W.A.6    Xiong, Y.7
  • 25
    • 3242715867 scopus 로고    scopus 로고
    • Essential role of ribosomal protein L11 in mediating growth inhibition-induced p53 activation
    • DOI 10.1038/sj.emboj.7600247
    • Bhat, K. P., Itahana, K., Jin, A., and Zhang, Y. (2004) Essential role of ribosomal protein L11 in mediating growth inhibition-induced p53 activation. EMBO J. 23, 2402-2412 (Pubitemid 38954847)
    • (2004) EMBO Journal , vol.23 , Issue.12 , pp. 2402-2412
    • Bhat, K.P.1    Itahana, K.2    Jin, A.3    Zhang, Y.4
  • 26
    • 4344685939 scopus 로고    scopus 로고
    • Ribosomal protein L23 activates p53 by inhibiting MDM2 function in response to ribosomal perturbation but not to translation inhibition
    • DOI 10.1128/MCB.24.17.7654-7668.2004
    • Dai, M. S., and Zeng., S. X., Jin, Y., Sun, X. X., David, L., and Lu, H. (2004) Ribosomal protein L23 activates p53 by inhibiting MDM2 function in response to ribosomal perturbation but not to translation inhibition. Mol. Cell. Biol. 24, 7654-7668 (Pubitemid 39121491)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.17 , pp. 7654-7668
    • Dai, M.-S.1    Zeng, S.X.2    Jin, Y.3    Sun, X.-X.4    David, L.5    Lu, H.6
  • 27
    • 4344660471 scopus 로고    scopus 로고
    • Inhibition of HDM2 and activation of p53 by ribosomal protein L23
    • DOI 10.1128/MCB.24.17.7669-7680.2004
    • Jin, A., Itahana, K., O'Keefe, K., and Zhang, Y. (2004) Inhibition of HDM2 and activation of p53 by ribosomal protein L23. Mol. Cell. Biol. 24, 7669-7680 (Pubitemid 39121492)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.17 , pp. 7669-7680
    • Jin, A.1    Itahana, K.2    O'Keefe, K.3    Zhang, Y.4
  • 28
    • 34547620115 scopus 로고    scopus 로고
    • Ribosomal protein S7 as a novel modulator of p53-MDM2 interaction: Binding to MDM2, stabilization of p53 protein, and activation of p53 function
    • DOI 10.1038/sj.onc.1210327, PII 1210327
    • Chen, D., Zhang, Z., Li, M., Wang, W., Li, Y., Rayburn, E. R., and Hill., D. L., Wang, H., and Zhang, R. (2007) Ribosomal protein S7 as a novel modulator of p53-MDM2 interaction: binding to MDM2, stabilization of p53 protein, and activation of p53 function. Oncogene 26, 5029-5037 (Pubitemid 47206956)
    • (2007) Oncogene , vol.26 , Issue.35 , pp. 5029-5037
    • Chen, D.1    Zhang, Z.2    Li, M.3    Wang, W.4    Li, Y.5    Rayburn, E.R.6    Hill, D.L.7    Wang, H.8    Zhang, R.9
  • 30
    • 79959570611 scopus 로고    scopus 로고
    • Interplay between ribosomal protein S27a and MDM2 protein in p53 activation in response to ribosomal stress
    • Sun, X. X., DeVine, T., Challagundla, K. B., and Dai, M. S. (2011) Interplay between ribosomal protein S27a and MDM2 protein in p53 activation in response to ribosomal stress. J. Biol. Chem. 286, 22730-22741
    • (2011) J. Biol. Chem. , vol.286 , pp. 22730-22741
    • Sun, X.X.1    DeVine, T.2    Challagundla, K.B.3    Dai, M.S.4
  • 34
    • 0025779517 scopus 로고
    • MPS1 and MPS2: Novel yeast genes defining distinct steps of spindle pole body duplication
    • Winey, M., Goetsch, L., Baum, P., and Byers, B. (1991) MPS1 and MPS2: novel yeast genes defining distinct steps of spindle pole body duplication. J. Cell Biol. 114, 745-754 (Pubitemid 21909840)
    • (1991) Journal of Cell Biology , vol.114 , Issue.4 , pp. 745-754
    • Winey, M.1    Goetsch, L.2    Baum, P.3    Byers, B.4
  • 35
    • 0033509092 scopus 로고    scopus 로고
    • Protein trans-acting factors involved in ribosome biogenesis in Saccharomyces cerevisiae
    • Kressler, D., Linder, P., and de La Cruz, J. (1999) Protein trans-acting factors involved in ribosome biogenesis in Saccharomyces cerevisiae. Mol. Cell. Biol. 19, 7897-7912 (Pubitemid 30413985)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.12 , pp. 7897-7912
    • Kressler, D.1    Linder, P.2    De La Cruz, J.3
  • 37
    • 0029143936 scopus 로고
    • The duplicated saccharomyces cerevisiae gene SSM1 encodes a eucaryotic homolog of the eubacterial and archaebacterial L1 ribosomal proteins
    • Petitjean, A., Bonneaud, N., and Lacroute, F. (1995) The duplicated Saccharomyces cerevisiae gene SSM1 encodes a eucaryotic homolog of the eubacterial and archaebacterial L1 ribosomal proteins. Mol. Cell. Biol. 15, 5071-5081
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5071-5081
    • Petitjean, A.1    Bonneaud, N.2    Lacroute, F.3
  • 41
    • 0032247498 scopus 로고    scopus 로고
    • In vivo mutational analysis of ribosomal RNA in saccharomyces cerevisiae
    • Venema, J., and Planta., R. J., and Raué, H. A. (1998) In vivo mutational analysis of ribosomal RNA in Saccharomyces cerevisiae. Methods Mol. Biol. 77, 257-270
    • (1998) Methods Mol. Biol. , vol.77 , pp. 257-270
    • Venema, J.1    Planta, R.J.2    Raué, H.A.3
  • 42
    • 33846926262 scopus 로고    scopus 로고
    • Characterization of Saccharomyces cerevisiae Npa2p (Urb2p) reveals a low-molecular-mass complex containing Dbp6p, Npa1p (Urb1p), Nop8p, and Rsa3p involved in early steps of 60S ribosomal subunit biogenesis
    • DOI 10.1128/MCB.01523-06
    • Rosado, I.V., Dez, C., Lebaron, S., Caizergues-Ferrer, M., Henry, Y., and de la Cruz, J. (2007) Characterization of Saccharomyces cerevisiae Npa2p (Urb2p) revealsalow-molecular-mass complex containing Dbp6p, Npa1p (Urb1p), Nop8p, and Rsa3p involved in early steps of 60S ribosomal subunit biogenesis. Mol. Cell. Biol. 27, 1207-1221 (Pubitemid 46239805)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.4 , pp. 1207-1221
    • Rosado, I.V.1    Dez, C.2    Lebaron, S.3    Caizergues-Ferrer, M.4    Henry, Y.5    De La Cruz, J.6
  • 43
    • 49549154829 scopus 로고
    • Sequential gene function in the initiation of saccharomyces cerevisiae DNA synthesis
    • Hereford, L. M., and Hartwell, L. H. (1974) Sequential gene function in the initiation of Saccharomyces cerevisiae DNA synthesis. J. Mol. Biol. 84, 445-461
    • (1974) J. Mol. Biol. , vol.84 , pp. 445-461
    • Hereford, L.M.1    Hartwell, L.H.2
  • 45
    • 0023244075 scopus 로고
    • Transcriptional and translational regulation of ribosomal protein formation during mouse myoblast differentiation
    • Agrawal, M. G., and Bowman, L. H. (1987) Transcriptional and translational regulation of ribosomal protein formation during mouse myoblast differentiation. J. Biol. Chem. 262, 4868-4875 (Pubitemid 17102864)
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.10 , pp. 4868-4875
    • Agrawal, M.G.1    Bowman, L.H.2
  • 46
    • 0023757899 scopus 로고
    • The accumulation of three yeast ribosomal proteins under conditions of excess mRNA is determined primarily by fast protein decay
    • Maicas, E., and Pluthero., F. G., and Friesen, J. D. (1988) The accumulation of three yeast ribosomal proteins under conditions of excess mRNA is determined primarily by fast protein decay. Mol. Cell. Biol. 8, 169-175
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 169-175
    • Maicas, E.1    Pluthero, F.G.2    Friesen, J.D.3
  • 47
    • 0015232932 scopus 로고
    • Persistent cytoplasmic synthesis of ribosomal proteins during the selective inhibition of ribosomal RNA synthesis
    • Craig, N, and Perry, R. P. (1971) Persistent cytoplasmic synthesis of ribosomal proteins during the selective inhibition of ribosomal RNA synthesis. Nat. New Biol. 229, 75-80
    • (1971) Nat. New Biol. , vol.229 , pp. 75-80
    • Craig, N.1    Perry, R.P.2
  • 48
    • 0015238667 scopus 로고
    • Lifetime of the messenger RNAs which code for ribosomal proteins in L-cells
    • Craig, N, and Kelley., D. E., and Perry, R. P. (1971) Lifetime of the messenger RNAs which code for ribosomal proteins in L-cells. Biochim. Biophys. Acta 246, 493-498
    • (1971) Biochim. Biophys. Acta , vol.246 , pp. 493-498
    • Craig, N.1    Kelley, D.E.2    Perry, R.P.3
  • 49
    • 0017760147 scopus 로고
    • In the absence of ribosomal RNA synthesis, the ribosomal proteins of HeLa cells are synthesized normally and degraded rapidly
    • DOI 10.1016/0022-2836(77)90157-7
    • Warner, J. R. (1977) In the absence of ribosomal RNA synthesis, the ribosomal proteins of HeLa cells are synthesized normally and degraded rapidly. J. Mol. Biol. 115, 315-333 (Pubitemid 8198756)
    • (1977) Journal of Molecular Biology , vol.115 , Issue.3 , pp. 315-333
    • Warner, J.R.1
  • 50
    • 0027444947 scopus 로고
    • S cerevisiae 26S protease mutants arrest cell division in G2/metaphase
    • DOI 10.1038/366358a0
    • 2/metaphase. Nature 366, 358-362 (Pubitemid 23349365)
    • (1993) Nature , vol.366 , Issue.6453 , pp. 358-362
    • Ghislain, M.1    Udvardy, A.2    Mann, C.3
  • 51
    • 0027211846 scopus 로고
    • Yeast ribosomal protein L1 is required for the stability of newly synthesized 5S rRNA and the assembly of 60S ribosomal subunits
    • Deshmukh, M., and Tsay., Y. F., Paulovich, A. G., and Woolford, J. L., Jr. (1993) Yeast ribosomal protein L1 is required for the stability of newly synthesized 5S rRNA and the assembly of 60S ribosomal subunits. Mol. Cell. Biol. 13, 2835-2845 (Pubitemid 23133955)
    • (1993) Molecular and Cellular Biology , vol.13 , Issue.5 , pp. 2835-2845
    • Deshmukh, M.1    Tsay, Y.-F.2    Paulovich, A.G.3    Woolford Jr., J.L.4
  • 53
    • 23844511660 scopus 로고    scopus 로고
    • Synergistic defect in 60S ribosomal subunit assembly caused by a mutation of Rrs1p, a ribosomal protein L11-binding protein, and 3prime;-extension of 5S rRNA in Saccharomyces cerevisiae
    • DOI 10.1093/nar/gki772
    • Nariai, M., Tanaka, T., Okada, T., Shirai, C, Horigome, C, and Mizuta, K. (2005) Synergistic defect in 60S ribosomal subunit assembly caused by a mutation of Rrs1p, a ribosomal protein L11-binding protein, and 3'-extension of 5S rRNA in Saccharomyces cerevisiae. Nucleic Acids Res. 33, 4553-4562 (Pubitemid 41222570)
    • (2005) Nucleic Acids Research , vol.33 , Issue.14 , pp. 4553-4562
    • Nariai, M.1    Tanaka, T.2    Okada, T.3    Shirai, C.4    Horigome, C.5    Mizuta, K.6
  • 54
    • 2342664094 scopus 로고    scopus 로고
    • Rrs1p, a ribosomal protein L11-binding protein, is required for nuclear export of the 60S pre-ribosomal subunit in Saccharomyces cerevisiae
    • DOI 10.1016/j.febslet.2004.03.087, PII S001457930400393X
    • Miyoshi, K., Shirai, C, Horigome, C, Takenami, K., Kawasaki, J., and Mizuta, K. (2004) Rrs1p, a ribosomal protein L11-binding protein, is required for nuclear export of the 60S pre-ribosomal subunit in Saccharomyces cerevisiae. FEBS Lett. 565, 106-110 (Pubitemid 38595328)
    • (2004) FEBS Letters , vol.565 , Issue.1-3 , pp. 106-110
    • Miyoshi, K.1    Shirai, C.2    Horigome, C.3    Takenami, K.4    Kawasaki, J.5    Mizuta, K.6
  • 55
    • 0003418645 scopus 로고
    • A restriction point for control of normal animal cell proliferation
    • Pardee, A. B. (1974) A restriction point for control of normal animal cell proliferation. Proc. Natl. Acad. Sci. U.S.A. 71, 1286-1290
    • (1974) Proc. Natl. Acad. Sci. U.S.A. , vol.71 , pp. 1286-1290
    • Pardee, A.B.1
  • 56
    • 0034003005 scopus 로고    scopus 로고
    • Stress signals utilize multiple pathways to stabilize p53
    • DOI 10.1128/MCB.20.9.3224-3233.2000
    • Ashcroft, M., Taya, Y., and Vousden, K. H. (2000) Stress signals utilize multiple pathways to stabilize p53. Mol. Cell. Biol. 20, 3224-3233 (Pubitemid 30215034)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.9 , pp. 3224-3233
    • Ashcroft, M.1    Taya, Y.2    Vousden, K.H.3
  • 57
    • 21244504900 scopus 로고    scopus 로고
    • Genetic inactivation of the transcription factor TIF-IA leads to nucleolar disruption, cell cycle arrest, and p53-mediated apoptosis
    • DOI 10.1016/j.molcel.2005.05.023, PII S1097276505013493
    • Yuan, X., Zhou, Y., Casanova, E., Chai, M., Kiss, E., Gröne, H. J., Schütz, G., and Grummt, I. (2005) Genetic inactivation of the transcription factor TIF-IA leads to nucleolar disruption, cell cycle arrest, and p53-mediated apoptosis. Mol. Cell 19, 77-87 (Pubitemid 40884659)
    • (2005) Molecular Cell , vol.19 , Issue.1 , pp. 77-87
    • Yuan, X.1    Zhou, Y.2    Casanova, E.3    Chai, M.4    Kiss, E.5    Grone, H.-J.6    Schutz, G.7    Grummt, I.8
  • 59
    • 33846617666 scopus 로고    scopus 로고
    • S6-haploinsufficiency activates the p53 tumor suppressor
    • Panić, L., Montagne, J., Cokarić, M., and Volarević, S. (2007) S6-haploinsufficiency activates the p53 tumor suppressor. Cell Cycle 6, 20-24 (Pubitemid 46173875)
    • (2007) Cell Cycle , vol.6 , Issue.1 , pp. 20-24
    • Panic, L.1    Montagne, J.2    Cokaric, M.3    Volarevic, S.4
  • 60
    • 34548489876 scopus 로고    scopus 로고
    • Balanced production of ribosomal proteins
    • DOI 10.1016/j.gene.2007.07.007, PII S0378111907003770
    • Perry, R. P. (2007) Balanced production of ribosomal proteins. Gene 401, 1-3 (Pubitemid 47379521)
    • (2007) Gene , vol.401 , Issue.1-2 , pp. 1-3
    • Perry, R.P.1
  • 63
    • 0021951868 scopus 로고
    • Cytotoxicity and the inhibition of ribosomal RNA processing in human colon carcinoma cells
    • Cohen, M. B., and Glazer, R. I. (1985) Cytotoxicity and the inhibition of ribosomal RNA processing in human colon carcinoma cells. Mol. Pharmacol. 27, 308-313 (Pubitemid 15137900)
    • (1985) Molecular Pharmacology , vol.27 , Issue.2 , pp. 308-313
    • Cohen, M.B.1    Glazer, R.I.2
  • 64
    • 0015223093 scopus 로고
    • Inhibition of the processing of ribosomal precursor RNA by intercalating agents
    • Snyder, A. L., and Kann., H. E. Jr., and Kohn, K. W. (1971) Inhibition of the processing of ribosomal precursor RNA by intercalating agents. J. Mol. Biol. 58, 555-565
    • (1971) J. Mol. Biol. , vol.58 , pp. 555-565
    • Snyder, A.L.1    Kann Jr., H.E.2    Kohn, K.W.3
  • 65
    • 0015973660 scopus 로고
    • Inhibition of ribosomal RNA maturation in novikoff hepatoma cells by toyocamycin, tubercidin, and 6-thioguanosine
    • Weiss, J. W., and Pitot, H. C. (1974) Inhibition of ribosomal RNA maturation in Novikoff hepatoma cells by toyocamycin, tubercidin, and 6-thioguanosine. Cancer Res. 34, 581-587
    • (1974) Cancer Res. , vol.34 , pp. 581-587
    • Weiss, J.W.1    Pitot, H.C.2
  • 66
    • 0016786638 scopus 로고
    • The inhibition of ribosomal RNA synthesis and maturation in novikoff hepatoma cells by 5-fluorouridine
    • Wilkinson, D. S., and Tlsty., T. D., and Hanas, R. J. (1975) The inhibition of ribosomal RNA synthesis and maturation in Novikoff hepatoma cells by 5-fluorouridine. Cancer Res. 35, 3014-3020
    • (1975) Cancer Res. , vol.35 , pp. 3014-3020
    • Wilkinson, D.S.1    Tlsty, T.D.2    Hanas, R.J.3
  • 67
    • 77951235652 scopus 로고    scopus 로고
    • Ribosomal protein L11 associates with c-myc at 5S rRNA and tRNA genes and regulates their expression
    • Dai, M. S., and Sun., X. X., and Lu, H. (2010) Ribosomal protein L11 associates with c-Myc at 5S rRNA and tRNA genes and regulates their expression. J. Biol. Chem. 285, 12587-12594
    • (2010) J. Biol. Chem. , vol.285 , pp. 12587-12594
    • Dai, M.S.1    Sun, X.X.2    Lu, H.3
  • 68
    • 84861209820 scopus 로고    scopus 로고
    • Physical and functional interaction between ribosomal protein L11 and the tumor suppressor ARF
    • Dai, M. S., and Challagundla., K. B., Sun, X. X., Palam, L. R., and Zeng., S. X., Wek, R. C., and Lu, H. (2012) Physical and functional interaction between ribosomal protein L11 and the tumor suppressor ARF. J. Biol. Chem. 287, 17120-17129
    • (2012) J. Biol. Chem. , vol.287 , pp. 17120-17129
    • Dai, M.S.1    Challagundla, K.B.2    Sun, X.X.3    Palam, L.R.4    Zeng, S.X.5    Wek, R.C.6    Lu, H.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.