메뉴 건너뛰기




Volumn 114, Issue , 2015, Pages 39-47

Heterogeneity of the translational machinery: Variations on a common theme

Author keywords

Gene expression regulation; Protein synthesis; Ribosome heterogeneity; Stress response; Translation regulation

Indexed keywords

INITIATION FACTOR; RIBOSOME PROTEIN; RIBOSOME RNA; TRANSFER RNA;

EID: 84930377142     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2014.12.011     Document Type: Review
Times cited : (65)

References (129)
  • 1
    • 44449166478 scopus 로고    scopus 로고
    • RNA-binding proteins and post-transcriptional gene regulation
    • T. Glisovic, J.L. Bachorik, J. Yong, and G. Dreyfuss RNA-binding proteins and post-transcriptional gene regulation FEBS Lett. 582 2008 1977 1986
    • (2008) FEBS Lett , vol.582 , pp. 1977-1986
    • Glisovic, T.1    Bachorik, J.L.2    Yong, J.3    Dreyfuss, G.4
  • 6
    • 84863889691 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation: new insights and challenges
    • A.G. Hinnebusch, and J.R. Lorsch The mechanism of eukaryotic translation initiation: new insights and challenges Cold Spring Harb. Perspect. Biol. 4 2012
    • (2012) Cold Spring Harb. Perspect. Biol. , vol.4
    • Hinnebusch, A.G.1    Lorsch, J.R.2
  • 7
    • 0037112055 scopus 로고    scopus 로고
    • The roles of individual eukaryotic translation initiation factors in ribosomal scanning and initiation codon selection
    • T.V. Pestova, and V.G. Kolupaeva The roles of individual eukaryotic translation initiation factors in ribosomal scanning and initiation codon selection Genes Dev. 16 2002 2906 2922
    • (2002) Genes Dev , vol.16 , pp. 2906-2922
    • Pestova, T.V.1    Kolupaeva, V.G.2
  • 8
    • 84881666192 scopus 로고    scopus 로고
    • The initiation of mammalian protein synthesis and mRNA scanning mechanism
    • I.B. Lomakin, and T.A. Steitz The initiation of mammalian protein synthesis and mRNA scanning mechanism Nature 500 2013 307 311
    • (2013) Nature , vol.500 , pp. 307-311
    • Lomakin, I.B.1    Steitz, T.A.2
  • 9
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • R.J. Jackson, C.U. Hellen, and T.V. Pestova The mechanism of eukaryotic translation initiation and principles of its regulation Nat. Rev. Mol. Cell Biol. 11 2010 113 127
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 10
    • 33646896955 scopus 로고    scopus 로고
    • Internal initiation: IRES elements of picornaviruses and hepatitis c virus
    • S.K. Jang Internal initiation: IRES elements of picornaviruses and hepatitis c virus Virus Res. 119 2006 2 15
    • (2006) Virus Res , vol.119 , pp. 2-15
    • Jang, S.K.1
  • 11
    • 66049161006 scopus 로고    scopus 로고
    • Recent mechanistic insights into eukaryotic ribosomes
    • M.V. Rodnina, and W. Wintermeyer Recent mechanistic insights into eukaryotic ribosomes Curr. Opin. Cell Biol. 21 2009 435 443
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 435-443
    • Rodnina, M.V.1    Wintermeyer, W.2
  • 12
    • 84863904349 scopus 로고    scopus 로고
    • The elongation, termination, and recycling phases of translation in eukaryotes
    • T.E. Dever, and R. Green The elongation, termination, and recycling phases of translation in eukaryotes Cold Spring Harb. Perspect. Biol. 4 2012 a013706
    • (2012) Cold Spring Harb. Perspect. Biol. , vol.4
    • Dever, T.E.1    Green, R.2
  • 13
    • 77449133028 scopus 로고    scopus 로고
    • Elongation in translation as a dynamic interaction among the ribosome, tRNA, and elongation factors EF-G and EF-Tu
    • X. Agirrezabala, and J. Frank Elongation in translation as a dynamic interaction among the ribosome, tRNA, and elongation factors EF-G and EF-Tu Q. Rev. Biophys. 42 2009 159 200
    • (2009) Q. Rev. Biophys. , vol.42 , pp. 159-200
    • Agirrezabala, X.1    Frank, J.2
  • 14
    • 0035812714 scopus 로고    scopus 로고
    • A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3
    • A.V. Zavialov, R.H. Buckingham, and M. Ehrenberg A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3 Cell 107 2001 115 124
    • (2001) Cell , vol.107 , pp. 115-124
    • Zavialov, A.V.1    Buckingham, R.H.2    Ehrenberg, M.3
  • 15
    • 79960471842 scopus 로고    scopus 로고
    • Structural aspects of translation termination on the ribosome
    • A.A. Korostelev Structural aspects of translation termination on the ribosome RNA 17 2011 1409 1421
    • (2011) RNA , vol.17 , pp. 1409-1421
    • Korostelev, A.A.1
  • 16
    • 84872802687 scopus 로고    scopus 로고
    • Tying up loose ends: ribosome recycling in eukaryotes and archaea
    • E. Nurenberg, and R. Tampe Tying up loose ends: ribosome recycling in eukaryotes and archaea Trends Biochem. Sci. 38 2013 64 74
    • (2013) Trends Biochem. Sci. , vol.38 , pp. 64-74
    • Nurenberg, E.1    Tampe, R.2
  • 17
    • 0037373552 scopus 로고    scopus 로고
    • Bacterial translational control at atomic resolution
    • P. Romby, and M. Springer Bacterial translational control at atomic resolution Trends Genet. TIG 19 2003 155 161
    • (2003) Trends Genet. TIG , vol.19 , pp. 155-161
    • Romby, P.1    Springer, M.2
  • 18
    • 5044229348 scopus 로고    scopus 로고
    • Molecular mechanisms of translational control
    • F. Gebauer, and M.W. Hentze Molecular mechanisms of translational control Nat. Rev. Mol. Cell Biol. 5 2004 827 835
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 827-835
    • Gebauer, F.1    Hentze, M.W.2
  • 19
    • 0014894231 scopus 로고
    • Functional heterogeneity of the 30S ribosomal subunit of E. coli
    • J. Van Duin, and C.G. Kurland Functional heterogeneity of the 30S ribosomal subunit of E. coli Mol. Gen. Genet. 109 1970 169 176
    • (1970) Mol. Gen. Genet. , vol.109 , pp. 169-176
    • Van Duin, J.1    Kurland, C.G.2
  • 21
    • 0015450476 scopus 로고
    • Heterogeneity of ribosomal populations in Escherichia coli cells grown in different media
    • E. Deusser Heterogeneity of ribosomal populations in Escherichia coli cells grown in different media Mol. Gen. Genet. 119 1972 249 258
    • (1972) Mol. Gen. Genet. , vol.119 , pp. 249-258
    • Deusser, E.1
  • 23
    • 35148812923 scopus 로고    scopus 로고
    • The ribosome filter redux
    • V.P. Mauro, and G.M. Edelman The ribosome filter redux Cell Cycle 6 2007 2246 2251
    • (2007) Cell Cycle , vol.6 , pp. 2246-2251
    • Mauro, V.P.1    Edelman, G.M.2
  • 24
    • 35548973466 scopus 로고    scopus 로고
    • Functional specificity among ribosomal proteins regulates gene expression
    • S. Komili, N.G. Farny, F.P. Roth, and P.A. Silver Functional specificity among ribosomal proteins regulates gene expression Cell 131 2007 557 571
    • (2007) Cell , vol.131 , pp. 557-571
    • Komili, S.1    Farny, N.G.2    Roth, F.P.3    Silver, P.A.4
  • 25
    • 0019795908 scopus 로고
    • Regulation of synthesis of cell-specific ribosomal proteins during differentiation of Dictyostelium discoideum
    • S. Ramagopal, and H.L. Ennis Regulation of synthesis of cell-specific ribosomal proteins during differentiation of Dictyostelium discoideum Proc. Natl. Acad. Sci. U. S. A. 78 1981 3083 3087
    • (1981) Proc. Natl. Acad. Sci. U. S. A. , vol.78 , pp. 3083-3087
    • Ramagopal, S.1    Ennis, H.L.2
  • 26
    • 0015493886 scopus 로고
    • Ribosomal proteins: variation of the protein composition in Escherichia coli ribosomes as function of growth rate
    • E. Deusser, and H.G. Wittmann Ribosomal proteins: variation of the protein composition in Escherichia coli ribosomes as function of growth rate Nature 238 1972 269 270
    • (1972) Nature , vol.238 , pp. 269-270
    • Deusser, E.1    Wittmann, H.G.2
  • 27
  • 28
    • 0015694849 scopus 로고
    • Ribosome heterogenecity. The nonuniform distribution of specific ribosomal proteins among different functional classes of ribosomes
    • T.A. Bickle, G.A. Howard, and R.R. Traut Ribosome heterogenecity. The nonuniform distribution of specific ribosomal proteins among different functional classes of ribosomes J. Biol. Chem. 248 1973 4862 4864
    • (1973) J. Biol. Chem. , vol.248 , pp. 4862-4864
    • Bickle, T.A.1    Howard, G.A.2    Traut, R.R.3
  • 29
    • 58649086299 scopus 로고    scopus 로고
    • An unexpected type of ribosomes induced by kasugamycin: a look into ancestral times of protein synthesis?
    • A.C. Kaberdina, W. Szaflarski, K.H. Nierhaus, and I. Moll An unexpected type of ribosomes induced by kasugamycin: a look into ancestral times of protein synthesis? Mol. Cell 33 2009 227 236
    • (2009) Mol. Cell , vol.33 , pp. 227-236
    • Kaberdina, A.C.1    Szaflarski, W.2    Nierhaus, K.H.3    Moll, I.4
  • 30
    • 0032563095 scopus 로고    scopus 로고
    • Ribosomal protein S1 is required for translation of most, if not all, natural mRNAs in Escherichia coli in vivo
    • M.A. Sorensen, J. Fricke, and S. Pedersen Ribosomal protein S1 is required for translation of most, if not all, natural mRNAs in Escherichia coli in vivo J. Mol. Biol. 280 1998 561 569
    • (1998) J. Mol. Biol. , vol.280 , pp. 561-569
    • Sorensen, M.A.1    Fricke, J.2    Pedersen, S.3
  • 31
    • 0032476065 scopus 로고    scopus 로고
    • Discrimination of 5′-terminal start codons by translation initiation factor 3 is mediated by ribosomal protein S1
    • I. Moll, A. Resch, and U. Blasi Discrimination of 5′-terminal start codons by translation initiation factor 3 is mediated by ribosomal protein S1 FEBS Lett. 436 1998 213 217
    • (1998) FEBS Lett , vol.436 , pp. 213-217
    • Moll, I.1    Resch, A.2    Blasi, U.3
  • 32
    • 80053181098 scopus 로고    scopus 로고
    • S1 ribosomal protein and the interplay between translation and mRNA decay
    • F. Delvillani, G. Papiani, G. Deho, and F. Briani S1 ribosomal protein and the interplay between translation and mRNA decay Nucleic Acids Res. 39 2011 7702 7715
    • (2011) Nucleic Acids Res , vol.39 , pp. 7702-7715
    • Delvillani, F.1    Papiani, G.2    Deho, G.3    Briani, F.4
  • 34
    • 0036139519 scopus 로고    scopus 로고
    • Differential expression of genes coding for ribosomal proteins in different human tissues
    • S. Bortoluzzi, F. d'Alessi, C. Romualdi, and G.A. Danieli Differential expression of genes coding for ribosomal proteins in different human tissues Bioinformatics 17 2001 1152 1157
    • (2001) Bioinformatics , vol.17 , pp. 1152-1157
    • Bortoluzzi, S.1    D'Alessi, F.2    Romualdi, C.3    Danieli, G.A.4
  • 35
    • 79955537355 scopus 로고    scopus 로고
    • Ribosome-mediated specificity in Hox mRNA translation and vertebrate tissue patterning
    • N. Kondrashov, A. Pusic, C.R. Stumpf, K. Shimizu, and A.C. Hsieh Ribosome-mediated specificity in Hox mRNA translation and vertebrate tissue patterning Cell 145 2011 383 397
    • (2011) Cell , vol.145 , pp. 383-397
    • Kondrashov, N.1    Pusic, A.2    Stumpf, C.R.3    Shimizu, K.4    Hsieh, A.C.5
  • 36
    • 84902654766 scopus 로고    scopus 로고
    • Ribosome-omics of the human ribosome
    • V. Gupta, and J.R. Warner Ribosome-omics of the human ribosome RNA 20 2014 1004 1013
    • (2014) RNA , vol.20 , pp. 1004-1013
    • Gupta, V.1    Warner, J.R.2
  • 37
    • 84890554843 scopus 로고    scopus 로고
    • Parkin induces upregulation of 40S ribosomal protein SA and posttranslational modification of cytokeratins 8 and 18 in human cervical cancer cells
    • D.G. Song, Y.S. Kim, B.C. Jung, K.J. Rhee, and C.H. Pan Parkin induces upregulation of 40S ribosomal protein SA and posttranslational modification of cytokeratins 8 and 18 in human cervical cancer cells Appl. Biochem. Biotechnol. 171 2013 1630 1638
    • (2013) Appl. Biochem. Biotechnol. , vol.171 , pp. 1630-1638
    • Song, D.G.1    Kim, Y.S.2    Jung, B.C.3    Rhee, K.J.4    Pan, C.H.5
  • 38
  • 39
    • 58949104207 scopus 로고    scopus 로고
    • 67-kDa laminin receptor in human bile duct carcinoma
    • D. Li, J. Chen, Z. Gao, X. Li, and X. Yan 67-kDa laminin receptor in human bile duct carcinoma Eur. Surg. Res. 42 2009 168 173
    • (2009) Eur. Surg. Res. , vol.42 , pp. 168-173
    • Li, D.1    Chen, J.2    Gao, Z.3    Li, X.4    Yan, X.5
  • 40
    • 84897061004 scopus 로고    scopus 로고
    • V-erbA generates ribosomes devoid of RPL11 and regulates translational activity in avian erythroid progenitors
    • A.T. Nguyen-Lefebvre, G. Leprun, V. Morin, J. Vinuelas, and Y. Coute V-erbA generates ribosomes devoid of RPL11 and regulates translational activity in avian erythroid progenitors Oncogene 33 2014 1581 1589
    • (2014) Oncogene , vol.33 , pp. 1581-1589
    • Nguyen-Lefebvre, A.T.1    Leprun, G.2    Morin, V.3    Vinuelas, J.4    Coute, Y.5
  • 41
    • 84872000078 scopus 로고    scopus 로고
    • A ribosome-specialized translation initiation pathway is required for cap-dependent translation of vesicular stomatitis virus mRNAs
    • A.S. Lee, R. Burdeinick-Kerr, and S.P. Whelan A ribosome-specialized translation initiation pathway is required for cap-dependent translation of vesicular stomatitis virus mRNAs Proc. Natl. Acad. Sci. U. S. A. 110 2013 324 329
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 324-329
    • Lee, A.S.1    Burdeinick-Kerr, R.2    Whelan, S.P.3
  • 42
    • 63649157049 scopus 로고    scopus 로고
    • How common are extraribosomal functions of ribosomal proteins?
    • J.R. Warner, and K.B. McIntosh How common are extraribosomal functions of ribosomal proteins? Mol. Cell 34 2009 3 11
    • (2009) Mol. Cell , vol.34 , pp. 3-11
    • Warner, J.R.1    McIntosh, K.B.2
  • 43
    • 1942452749 scopus 로고    scopus 로고
    • Proof and evolutionary analysis of ancient genome duplication in the yeast Saccharomyces cerevisiae
    • M. Kellis, B.W. Birren, and E.S. Lander Proof and evolutionary analysis of ancient genome duplication in the yeast Saccharomyces cerevisiae Nature 428 2004 617 624
    • (2004) Nature , vol.428 , pp. 617-624
    • Kellis, M.1    Birren, B.W.2    Lander, E.S.3
  • 44
    • 80054680031 scopus 로고    scopus 로고
    • Introns within ribosomal protein genes regulate the production and function of yeast ribosomes
    • J. Parenteau, M. Durand, G. Morin, J. Gagnon, and J.F. Lucier Introns within ribosomal protein genes regulate the production and function of yeast ribosomes Cell 147 2011 320 331
    • (2011) Cell , vol.147 , pp. 320-331
    • Parenteau, J.1    Durand, M.2    Morin, G.3    Gagnon, J.4    Lucier, J.F.5
  • 45
    • 33845703824 scopus 로고    scopus 로고
    • A fail-safe system for the ribosome under zinc-limiting conditions in Bacillus subtilis
    • Y. Natori, H. Nanamiya, G. Akanuma, S. Kosono, and T. Kudo A fail-safe system for the ribosome under zinc-limiting conditions in Bacillus subtilis Mol. Microbiol. 63 2007 294 307
    • (2007) Mol. Microbiol. , vol.63 , pp. 294-307
    • Natori, Y.1    Nanamiya, H.2    Akanuma, G.3    Kosono, S.4    Kudo, T.5
  • 46
    • 84879963839 scopus 로고    scopus 로고
    • Specialized yeast ribosomes: a customized tool for selective mRNA translation
    • J.W. Bauer, C. Brandl, O. Haubenreisser, B. Wimmer, and M. Weber Specialized yeast ribosomes: a customized tool for selective mRNA translation PLoS One 8 2013 e67609
    • (2013) PLoS One , vol.8
    • Bauer, J.W.1    Brandl, C.2    Haubenreisser, O.3    Wimmer, B.4    Weber, M.5
  • 47
    • 84861555764 scopus 로고    scopus 로고
    • P1 and P2 protein heterodimer binding to the P0 protein of Saccharomyces cerevisiae is relatively non-specific and a source of ribosomal heterogeneity
    • D. Cardenas, J. Revuelta-Cervantes, A. Jimenez-Diaz, H. Camargo, and M. Remacha P1 and P2 protein heterodimer binding to the P0 protein of Saccharomyces cerevisiae is relatively non-specific and a source of ribosomal heterogeneity Nucleic Acids Res. 40 2012 4520 4529
    • (2012) Nucleic Acids Res , vol.40 , pp. 4520-4529
    • Cardenas, D.1    Revuelta-Cervantes, J.2    Jimenez-Diaz, A.3    Camargo, H.4    Remacha, M.5
  • 48
    • 0034777661 scopus 로고    scopus 로고
    • The organization of cytoplasmic ribosomal protein genes in the Arabidopsis genome
    • A. Barakat, K. Szick-Miranda, I.F. Chang, R. Guyot, and G. Blanc The organization of cytoplasmic ribosomal protein genes in the Arabidopsis genome Plant Physiol. 127 2001 398 415
    • (2001) Plant Physiol , vol.127 , pp. 398-415
    • Barakat, A.1    Szick-Miranda, K.2    Chang, I.F.3    Guyot, R.4    Blanc, G.5
  • 49
    • 82555184787 scopus 로고    scopus 로고
    • Transcriptional regulation of ribosome components are determined by stress according to cellular compartments in Arabidopsis thaliana
    • R. Sormani, C. Masclaux-Daubresse, F. Daniel-Vedele, and F. Chardon Transcriptional regulation of ribosome components are determined by stress according to cellular compartments in Arabidopsis thaliana PLoS One 6 2011 e28070
    • (2011) PLoS One , vol.6
    • Sormani, R.1    Masclaux-Daubresse, C.2    Daniel-Vedele, F.3    Chardon, F.4
  • 50
    • 77955702868 scopus 로고    scopus 로고
    • Plant L10 ribosomal proteins have different roles during development and translation under ultraviolet-B stress
    • M.L. Falcone Ferreyra, A. Pezza, J. Biarc, A.L. Burlingame, and P. Casati Plant L10 ribosomal proteins have different roles during development and translation under ultraviolet-B stress Plant Physiol. 153 2010 1878 1894
    • (2010) Plant Physiol , vol.153 , pp. 1878-1894
    • Falcone Ferreyra, M.L.1    Pezza, A.2    Biarc, J.3    Burlingame, A.L.4    Casati, P.5
  • 51
    • 0035173004 scopus 로고    scopus 로고
    • An Arabidopsis minute-like phenotype caused by a semi-dominant mutation in a RIBOSOMAL PROTEIN S5 gene
    • D. Weijers, M. Franke-van Dijk, R.J. Vencken, A. Quint, and P. Hooykaas An Arabidopsis minute-like phenotype caused by a semi-dominant mutation in a RIBOSOMAL PROTEIN S5 gene Development 128 2001 4289 4299
    • (2001) Development , vol.128 , pp. 4289-4299
    • Weijers, D.1    Franke-Van Dijk, M.2    Vencken, R.J.3    Quint, A.4    Hooykaas, P.5
  • 52
    • 17844367135 scopus 로고    scopus 로고
    • High heterogeneity within the ribosomal proteins of the Arabidopsis thaliana 80S ribosome
    • P. Giavalisco, D. Wilson, T. Kreitler, H. Lehrach, and J. Klose High heterogeneity within the ribosomal proteins of the Arabidopsis thaliana 80S ribosome Plant Mol. Biol. 57 2005 577 591
    • (2005) Plant Mol. Biol. , vol.57 , pp. 577-591
    • Giavalisco, P.1    Wilson, D.2    Kreitler, T.3    Lehrach, H.4    Klose, J.5
  • 53
    • 84903650274 scopus 로고    scopus 로고
    • Ribosomal protein RPL27a promotes female gametophyte development in a dose-dependent manner
    • A. Zsogon, D. Szakonyi, X. Shi, and M.E. Byrne Ribosomal protein RPL27a promotes female gametophyte development in a dose-dependent manner Plant Physiol. 165 2014 1133 1143
    • (2014) Plant Physiol , vol.165 , pp. 1133-1143
    • Zsogon, A.1    Szakonyi, D.2    Shi, X.3    Byrne, M.E.4
  • 54
    • 77951942401 scopus 로고    scopus 로고
    • The human RPS4 paralogue on Yq11.223 encodes a structurally conserved ribosomal protein and is preferentially expressed during spermatogenesis
    • A.M. Lopes, R.N. Miguel, C.A. Sargent, P.J. Ellis, and A. Amorim The human RPS4 paralogue on Yq11.223 encodes a structurally conserved ribosomal protein and is preferentially expressed during spermatogenesis BMC Mol. Biol. 11 2010 33 10.1186/1471-2199-11-33
    • (2010) BMC Mol. Biol. , vol.11 , pp. 33
    • Lopes, A.M.1    Miguel, R.N.2    Sargent, C.A.3    Ellis, P.J.4    Amorim, A.5
  • 55
    • 84894434971 scopus 로고    scopus 로고
    • RPL39L is an example of a recently evolved ribosomal protein paralog that shows highly specific tissue expression patterns and is upregulated in ESCs and HCC tumors
    • Q.W. Wong, J. Li, S.R. Ng, S.G. Lim, and H. Yang RPL39L is an example of a recently evolved ribosomal protein paralog that shows highly specific tissue expression patterns and is upregulated in ESCs and HCC tumors RNA Biol. 11 2014 33 41
    • (2014) RNA Biol , vol.11 , pp. 33-41
    • Wong, Q.W.1    Li, J.2    Ng, S.R.3    Lim, S.G.4    Yang, H.5
  • 56
    • 77949830499 scopus 로고    scopus 로고
    • Proteomic analysis of rodent ribosomes revealed heterogeneity including ribosomal proteins L10-like, L22-like 1, and L39-like
    • Y. Sugihara, H. Honda, T. Iida, T. Morinaga, and S. Hino Proteomic analysis of rodent ribosomes revealed heterogeneity including ribosomal proteins L10-like, L22-like 1, and L39-like J. Proteome Res. 9 2010 1351 1366
    • (2010) J. Proteome Res. , vol.9 , pp. 1351-1366
    • Sugihara, Y.1    Honda, H.2    Iida, T.3    Morinaga, T.4    Hino, S.5
  • 57
    • 84876700564 scopus 로고    scopus 로고
    • Identification and expression of an autosomal paralogue of ribosomal protein S4, X-linked, in mice: potential involvement of testis-specific ribosomal proteins in translation and spermatogenesis
    • Y. Sugihara, E. Sadohara, K. Yonezawa, M. Kugo, and K. Oshima Identification and expression of an autosomal paralogue of ribosomal protein S4, X-linked, in mice: potential involvement of testis-specific ribosomal proteins in translation and spermatogenesis Gene 521 2013 91 99
    • (2013) Gene , vol.521 , pp. 91-99
    • Sugihara, Y.1    Sadohara, E.2    Yonezawa, K.3    Kugo, M.4    Oshima, K.5
  • 58
    • 39749166860 scopus 로고    scopus 로고
    • Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation
    • B. Macek, F. Gnad, B. Soufi, C. Kumar, and J.V. Olsen Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation Mol. Cell. Proteomics 7 2008 299 307
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 299-307
    • Macek, B.1    Gnad, F.2    Soufi, B.3    Kumar, C.4    Olsen, J.V.5
  • 60
    • 44949193693 scopus 로고    scopus 로고
    • Acetylation of L12 increases interactions in the Escherichia coli ribosomal stalk complex
    • Y. Gordiyenko, S. Deroo, M. Zhou, H. Videler, and C.V. Robinson Acetylation of L12 increases interactions in the Escherichia coli ribosomal stalk complex J. Mol. Biol. 380 2008 404 414
    • (2008) J. Mol. Biol. , vol.380 , pp. 404-414
    • Gordiyenko, Y.1    Deroo, S.2    Zhou, M.3    Videler, H.4    Robinson, C.V.5
  • 61
    • 0037197887 scopus 로고    scopus 로고
    • Direct mass spectrometric analysis of intact proteins of the yeast large ribosomal subunit using capillary LC/FTICR
    • S.W. Lee, S.J. Berger, S. Martinovic, L. Pasa-Tolic, and G.A. Anderson Direct mass spectrometric analysis of intact proteins of the yeast large ribosomal subunit using capillary LC/FTICR Proc. Natl. Acad. Sci. U. S. A. 99 2002 5942 5947
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 5942-5947
    • Lee, S.W.1    Berger, S.J.2    Martinovic, S.3    Pasa-Tolic, L.4    Anderson, G.A.5
  • 63
    • 74449084888 scopus 로고    scopus 로고
    • Rmt1 catalyzes zinc-finger independent arginine methylation of ribosomal protein Rps2 in Saccharomyces cerevisiae
    • R.S. Lipson, K.J. Webb, and S.G. Clarke Rmt1 catalyzes zinc-finger independent arginine methylation of ribosomal protein Rps2 in Saccharomyces cerevisiae Biochem. Biophys. Res. Commun. 391 2010 1658 1662
    • (2010) Biochem. Biophys. Res. Commun. , vol.391 , pp. 1658-1662
    • Lipson, R.S.1    Webb, K.J.2    Clarke, S.G.3
  • 65
    • 0026144977 scopus 로고
    • Covalent modifications of ribosomal proteins in growing and aggregation-competent Dictyostelium discoideum: phosphorylation and methylation
    • S. Ramagopal Covalent modifications of ribosomal proteins in growing and aggregation-competent Dictyostelium discoideum: phosphorylation and methylation Biochem. Cell Biol. 69 1991 263 268
    • (1991) Biochem. Cell Biol. , vol.69 , pp. 263-268
    • Ramagopal, S.1
  • 66
    • 39749142082 scopus 로고    scopus 로고
    • Analysis of the Arabidopsis cytosolic ribosome proteome provides detailed insights into its components and their post-translational modification
    • A.J. Carroll, J.L. Heazlewood, J. Ito, and A.H. Millar Analysis of the Arabidopsis cytosolic ribosome proteome provides detailed insights into its components and their post-translational modification Mol. Cell. Proteomics 7 2008 347 369
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 347-369
    • Carroll, A.J.1    Heazlewood, J.L.2    Ito, J.3    Millar, A.H.4
  • 67
    • 16544392851 scopus 로고    scopus 로고
    • Crosslinking of ribosomal proteins to RNA in maize ribosomes by UV-B and its effects on translation
    • P. Casati, and V. Walbot Crosslinking of ribosomal proteins to RNA in maize ribosomes by UV-B and its effects on translation Plant Physiol. 136 2004 3319 3332
    • (2004) Plant Physiol , vol.136 , pp. 3319-3332
    • Casati, P.1    Walbot, V.2
  • 68
    • 0034635444 scopus 로고    scopus 로고
    • Activation of p70 ribosomal protein S6 kinase is an essential step in the DNA damage-dependent signaling pathway responsible for the ultraviolet B-mediated increase in interstitial collagenase (MMP-1) and stromelysin-1 (MMP-3) protein levels in human dermal fibroblasts
    • P. Brenneisen, J. Wenk, M. Wlaschek, T. Krieg, and K. Scharffetter-Kochanek Activation of p70 ribosomal protein S6 kinase is an essential step in the DNA damage-dependent signaling pathway responsible for the ultraviolet B-mediated increase in interstitial collagenase (MMP-1) and stromelysin-1 (MMP-3) protein levels in human dermal fibroblasts J. Biol. Chem. 275 2000 4336 4344
    • (2000) J. Biol. Chem. , vol.275 , pp. 4336-4344
    • Brenneisen, P.1    Wenk, J.2    Wlaschek, M.3    Krieg, T.4    Scharffetter-Kochanek, K.5
  • 69
    • 84879476747 scopus 로고    scopus 로고
    • Silencing of the nuclear RPS10 gene encoding mitochondrial ribosomal protein alters translation in Arabidopsis mitochondria
    • M. Kwasniak, P. Majewski, R. Skibior, A. Adamowicz, and M. Czarna Silencing of the nuclear RPS10 gene encoding mitochondrial ribosomal protein alters translation in Arabidopsis mitochondria Plant Cell 25 2013 1855 1867
    • (2013) Plant Cell , vol.25 , pp. 1855-1867
    • Kwasniak, M.1    Majewski, P.2    Skibior, R.3    Adamowicz, A.4    Czarna, M.5
  • 70
    • 56949100388 scopus 로고    scopus 로고
    • Characterization of heterogeneous LSU rRNA profiles in Streptomyces coelicolor under different growth stages and conditions
    • H.L. Kim, W.S. Song, K. Kim, and K. Lee Characterization of heterogeneous LSU rRNA profiles in Streptomyces coelicolor under different growth stages and conditions Curr. Microbiol. 57 2008 537 541
    • (2008) Curr. Microbiol. , vol.57 , pp. 537-541
    • Kim, H.L.1    Song, W.S.2    Kim, K.3    Lee, K.4
  • 71
    • 84886713947 scopus 로고    scopus 로고
    • Multiple rRNA operons are essential for efficient cell growth and sporulation as well as outgrowth in Bacillus subtilis
    • K. Yano, T. Wada, S. Suzuki, K. Tagami, and T. Matsumoto Multiple rRNA operons are essential for efficient cell growth and sporulation as well as outgrowth in Bacillus subtilis Microbiology 159 2013 2225 2236
    • (2013) Microbiology , vol.159 , pp. 2225-2236
    • Yano, K.1    Wada, T.2    Suzuki, S.3    Tagami, K.4    Matsumoto, T.5
  • 72
    • 37549063435 scopus 로고    scopus 로고
    • Intragenomic 16S rDNA divergence in Haloarcula marismortui is an adaptation to different temperatures
    • A. Lopez-Lopez, S. Benlloch, M. Bonfa, F. Rodriguez-Valera, and A. Mira Intragenomic 16S rDNA divergence in Haloarcula marismortui is an adaptation to different temperatures J. Mol. Evol. 65 2007 687 696
    • (2007) J. Mol. Evol. , vol.65 , pp. 687-696
    • Lopez-Lopez, A.1    Benlloch, S.2    Bonfa, M.3    Rodriguez-Valera, F.4    Mira, A.5
  • 74
    • 0035933790 scopus 로고    scopus 로고
    • Functional equivalence of structurally distinct ribosomes in the malaria parasite, Plasmodium berghei
    • R.M. van Spaendonk, J. Ramesar, A. van Wigcheren, W. Eling, and A.L. Beetsma Functional equivalence of structurally distinct ribosomes in the malaria parasite, Plasmodium berghei J. Biol. Chem. 276 2001 22638 22647
    • (2001) J. Biol. Chem. , vol.276 , pp. 22638-22647
    • Van Spaendonk, R.M.1    Ramesar, J.2    Van Wigcheren, A.3    Eling, W.4    Beetsma, A.L.5
  • 75
    • 84865542836 scopus 로고    scopus 로고
    • Functional variants of 5S rRNA in the ribosomes of common sea urchin Paracentrotus lividus
    • E. Dimarco, E. Cascone, D. Bellavia, and F. Caradonna Functional variants of 5S rRNA in the ribosomes of common sea urchin Paracentrotus lividus Gene 508 2012 21 25
    • (2012) Gene , vol.508 , pp. 21-25
    • Dimarco, E.1    Cascone, E.2    Bellavia, D.3    Caradonna, F.4
  • 76
    • 0036629250 scopus 로고    scopus 로고
    • rRNA modifications and ribosome function
    • W.A. Decatur, and M.J. Fournier rRNA modifications and ribosome function Trends Biochem. Sci. 27 2002 344 351
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 344-351
    • Decatur, W.A.1    Fournier, M.J.2
  • 77
    • 77955643151 scopus 로고    scopus 로고
    • Digital genome-wide ncRNA expression, including SnoRNAs, across 11 human tissues using polyA-neutral amplification
    • J.C. Castle, C.D. Armour, M. Lower, D. Haynor, and M. Biery Digital genome-wide ncRNA expression, including SnoRNAs, across 11 human tissues using polyA-neutral amplification PLoS One 5 2010 e11779
    • (2010) PLoS One , vol.5
    • Castle, J.C.1    Armour, C.D.2    Lower, M.3    Haynor, D.4    Biery, M.5
  • 78
    • 84922180958 scopus 로고    scopus 로고
    • Pseudouridine profiling reveals regulated mRNA pseudouridylation in yeast and human cells
    • T.M. Carlile, M.F. Rojas-Duran, B. Zinshteyn, H. Shin, and K.M. Bartoli Pseudouridine profiling reveals regulated mRNA pseudouridylation in yeast and human cells Nature 515 7525 2014 143 146 10.1038/nature13802
    • (2014) Nature , vol.515 , Issue.7525 , pp. 143-146
    • Carlile, T.M.1    Rojas-Duran, M.F.2    Zinshteyn, B.3    Shin, H.4    Bartoli, K.M.5
  • 79
    • 84907527348 scopus 로고    scopus 로고
    • Transcriptome-wide mapping reveals widespread dynamic-regulated pseudouridylation of ncRNA and mRNA
    • S. Schwartz, D.A. Bernstein, M.R. Mumbach, M. Jovanovic, and R.H. Herbst Transcriptome-wide mapping reveals widespread dynamic-regulated pseudouridylation of ncRNA and mRNA Cell 159 2014 148 162
    • (2014) Cell , vol.159 , pp. 148-162
    • Schwartz, S.1    Bernstein, D.A.2    Mumbach, M.R.3    Jovanovic, M.4    Herbst, R.H.5
  • 80
    • 33646543044 scopus 로고    scopus 로고
    • Impaired control of IRES-mediated translation in X-linked dyskeratosis congenita
    • A. Yoon, G. Peng, Y. Brandenburger, O. Zollo, and W. Xu Impaired control of IRES-mediated translation in X-linked dyskeratosis congenita Science 312 2006 902 906
    • (2006) Science , vol.312 , pp. 902-906
    • Yoon, A.1    Peng, G.2    Brandenburger, Y.3    Zollo, O.4    Xu, W.5
  • 81
    • 80053563668 scopus 로고    scopus 로고
    • Selective translation of leaderless mRNAs by specialized ribosomes generated by MazF in Escherichia coli
    • O. Vesper, S. Amitai, M. Belitsky, K. Byrgazov, and A.C. Kaberdina Selective translation of leaderless mRNAs by specialized ribosomes generated by MazF in Escherichia coli Cell 147 2011 147 157
    • (2011) Cell , vol.147 , pp. 147-157
    • Vesper, O.1    Amitai, S.2    Belitsky, M.3    Byrgazov, K.4    Kaberdina, A.C.5
  • 82
    • 0030008368 scopus 로고    scopus 로고
    • An Escherichia coli chromosomal "addiction module" regulated by guanosine [corrected] 3′,5′-bispyrophosphate: a model for programmed bacterial cell death
    • E. Aizenman, H. Engelberg-Kulka, and G. Glaser An Escherichia coli chromosomal "addiction module" regulated by guanosine [corrected] 3′,5′-bispyrophosphate: a model for programmed bacterial cell death Proc. Natl. Acad. Sci. U. S. A. 93 1996 6059 6063
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 6059-6063
    • Aizenman, E.1    Engelberg-Kulka, H.2    Glaser, G.3
  • 83
    • 84890158770 scopus 로고    scopus 로고
    • Deregulation of translation due to post-transcriptional modification of rRNA explains why erm genes are inducible
    • P. Gupta, S. Sothiselvam, N. Vazquez-Laslop, and A.S. Mankin Deregulation of translation due to post-transcriptional modification of rRNA explains why erm genes are inducible Nat. Commun. 4 2013 1984
    • (2013) Nat. Commun. , vol.4 , pp. 1984
    • Gupta, P.1    Sothiselvam, S.2    Vazquez-Laslop, N.3    Mankin, A.S.4
  • 84
    • 77954185197 scopus 로고    scopus 로고
    • Interplay between the ribosomal tunnel, nascent chain, and macrolides influences drug inhibition
    • A.L. Starosta, V.V. Karpenko, A.V. Shishkina, A. Mikolajka, and N.V. Sumbatyan Interplay between the ribosomal tunnel, nascent chain, and macrolides influences drug inhibition Chem. Biol. 17 2010 504 514
    • (2010) Chem. Biol. , vol.17 , pp. 504-514
    • Starosta, A.L.1    Karpenko, V.V.2    Shishkina, A.V.3    Mikolajka, A.4    Sumbatyan, N.V.5
  • 85
    • 84896498492 scopus 로고    scopus 로고
    • Partial methylation at Am100 in 18S rRNA of baker's yeast reveals ribosome heterogeneity on the level of eukaryotic rRNA modification
    • M. Buchhaupt, S. Sharma, S. Kellner, S. Oswald, and M. Paetzold Partial methylation at Am100 in 18S rRNA of baker's yeast reveals ribosome heterogeneity on the level of eukaryotic rRNA modification PLoS One 9 2014 e89640
    • (2014) PLoS One , vol.9
    • Buchhaupt, M.1    Sharma, S.2    Kellner, S.3    Oswald, S.4    Paetzold, M.5
  • 86
    • 81355153985 scopus 로고    scopus 로고
    • rRNA pseudouridylation defects affect ribosomal ligand binding and translational fidelity from yeast to human cells
    • K. Jack, C. Bellodi, D.M. Landry, R.O. Niederer, and A. Meskauskas rRNA pseudouridylation defects affect ribosomal ligand binding and translational fidelity from yeast to human cells Mol. Cell 44 2011 660 666
    • (2011) Mol. Cell , vol.44 , pp. 660-666
    • Jack, K.1    Bellodi, C.2    Landry, D.M.3    Niederer, R.O.4    Meskauskas, A.5
  • 87
    • 1642580810 scopus 로고    scopus 로고
    • Preferential translation of cold-shock mRNAs during cold adaptation
    • A.M. Giuliodori, A. Brandi, C.O. Gualerzi, and C.L. Pon Preferential translation of cold-shock mRNAs during cold adaptation RNA 10 2004 265 276
    • (2004) RNA , vol.10 , pp. 265-276
    • Giuliodori, A.M.1    Brandi, A.2    Gualerzi, C.O.3    Pon, C.L.4
  • 88
    • 0020574745 scopus 로고
    • Initiation factor and ribosome levels are coordinately controlled in Escherichia coli growing at different rates
    • J.G. Howe, and J.W. Hershey Initiation factor and ribosome levels are coordinately controlled in Escherichia coli growing at different rates J. Biol. Chem. 258 1983 1954 1959
    • (1983) J. Biol. Chem. , vol.258 , pp. 1954-1959
    • Howe, J.G.1    Hershey, J.W.2
  • 89
    • 0034254538 scopus 로고    scopus 로고
    • Selective stimulation of translation of leaderless mRNA by initiation factor 2: evolutionary implications for translation
    • S. Grill, C.O. Gualerzi, P. Londei, and U. Blasi Selective stimulation of translation of leaderless mRNA by initiation factor 2: evolutionary implications for translation EMBO J. 19 2000 4101 4110
    • (2000) EMBO J , vol.19 , pp. 4101-4110
    • Grill, S.1    Gualerzi, C.O.2    Londei, P.3    Blasi, U.4
  • 90
    • 0032896616 scopus 로고    scopus 로고
    • Translation initiation factor 3 antagonizes authentic start codon selection on leaderless mRNAs
    • K. Tedin, I. Moll, S. Grill, A. Resch, and A. Graschopf Translation initiation factor 3 antagonizes authentic start codon selection on leaderless mRNAs Mol. Microbiol. 31 1999 67 77
    • (1999) Mol. Microbiol. , vol.31 , pp. 67-77
    • Tedin, K.1    Moll, I.2    Grill, S.3    Resch, A.4    Graschopf, A.5
  • 91
    • 0035957756 scopus 로고    scopus 로고
    • Modulation of ribosomal recruitment to 5′-terminal start codons by translation initiation factors IF2 and IF3
    • S. Grill, I. Moll, D. Hasenohrl, C.O. Gualerzi, and U. Blasi Modulation of ribosomal recruitment to 5′-terminal start codons by translation initiation factors IF2 and IF3 FEBS Lett. 495 2001 167 171
    • (2001) FEBS Lett , vol.495 , pp. 167-171
    • Grill, S.1    Moll, I.2    Hasenohrl, D.3    Gualerzi, C.O.4    Blasi, U.5
  • 92
    • 71849102917 scopus 로고    scopus 로고
    • Eukaryotic and archaeal translation initiation factor 2: a heterotrimeric tRNA carrier
    • E. Schmitt, M. Naveau, and Y. Mechulam Eukaryotic and archaeal translation initiation factor 2: a heterotrimeric tRNA carrier FEBS Lett. 584 2010 405 412
    • (2010) FEBS Lett , vol.584 , pp. 405-412
    • Schmitt, E.1    Naveau, M.2    Mechulam, Y.3
  • 93
    • 79958804665 scopus 로고    scopus 로고
    • eIF2A mediates translation of hepatitis C viral mRNA under stress conditions
    • J.H. Kim, S.M. Park, J.H. Park, S.J. Keum, and S.K. Jang eIF2A mediates translation of hepatitis C viral mRNA under stress conditions EMBO J. 30 2011 2454 2464
    • (2011) EMBO J , vol.30 , pp. 2454-2464
    • Kim, J.H.1    Park, S.M.2    Park, J.H.3    Keum, S.J.4    Jang, S.K.5
  • 94
    • 84862991256 scopus 로고    scopus 로고
    • Leucine-tRNA initiates at CUG start codons for protein synthesis and presentation by MHC class I
    • S.R. Starck, V. Jiang, M. Pavon-Eternod, S. Prasad, and B. McCarthy Leucine-tRNA initiates at CUG start codons for protein synthesis and presentation by MHC class I Science 336 2012 1719 1723
    • (2012) Science , vol.336 , pp. 1719-1723
    • Starck, S.R.1    Jiang, V.2    Pavon-Eternod, M.3    Prasad, S.4    McCarthy, B.5
  • 95
    • 84900300350 scopus 로고    scopus 로고
    • PTENalpha, a PTEN isoform translated through alternative initiation, regulates mitochondrial function and energy metabolism
    • H. Liang, S. He, J. Yang, X. Jia, and P. Wang PTENalpha, a PTEN isoform translated through alternative initiation, regulates mitochondrial function and energy metabolism Cell Metab. 19 2014 836 848
    • (2014) Cell Metab. , vol.19 , pp. 836-848
    • Liang, H.1    He, S.2    Yang, J.3    Jia, X.4    Wang, P.5
  • 96
    • 77956245342 scopus 로고    scopus 로고
    • GTP-independent tRNA delivery to the ribosomal P-site by a novel eukaryotic translation factor
    • S.E. Dmitriev, I.M. Terenin, D.E. Andreev, P.A. Ivanov, and J.E. Dunaevsky GTP-independent tRNA delivery to the ribosomal P-site by a novel eukaryotic translation factor J. Biol. Chem. 285 2010 26779 26787
    • (2010) J. Biol. Chem. , vol.285 , pp. 26779-26787
    • Dmitriev, S.E.1    Terenin, I.M.2    Andreev, D.E.3    Ivanov, P.A.4    Dunaevsky, J.E.5
  • 97
    • 34547178178 scopus 로고    scopus 로고
    • Reconstitution reveals the functional core of mammalian eIF3
    • M. Masutani, N. Sonenberg, S. Yokoyama, and H. Imataka Reconstitution reveals the functional core of mammalian eIF3 EMBO J. 26 2007 3373 3383
    • (2007) EMBO J , vol.26 , pp. 3373-3383
    • Masutani, M.1    Sonenberg, N.2    Yokoyama, S.3    Imataka, H.4
  • 98
    • 0017074486 scopus 로고
    • Differences between newly formed and recycled free small ribosome subunits in liver cytoplasm
    • R.H. Hinton, and B.M. Mullock Differences between newly formed and recycled free small ribosome subunits in liver cytoplasm Biochem. J. 158 1976 97 103
    • (1976) Biochem. J. , vol.158 , pp. 97-103
    • Hinton, R.H.1    Mullock, B.M.2
  • 99
    • 0018794770 scopus 로고
    • Initiation of mammalian protein synthesis. The multiple functions of the initiation factor eIF-3
    • H. Trachsel, and T. Staehelin Initiation of mammalian protein synthesis. The multiple functions of the initiation factor eIF-3 Biochim. Biophys. Acta 565 1979 305 314
    • (1979) Biochim. Biophys. Acta , vol.565 , pp. 305-314
    • Trachsel, H.1    Staehelin, T.2
  • 100
    • 0017396056 scopus 로고
    • Studies on native ribosomal subunits from rat liver. Purification and characterization of a ribosome dissociation factor
    • H.A. Thompson, I. Sadnik, J. Scheinbuks, and K. Moldave Studies on native ribosomal subunits from rat liver. Purification and characterization of a ribosome dissociation factor Biochemistry 16 1977 2221 2230
    • (1977) Biochemistry , vol.16 , pp. 2221-2230
    • Thompson, H.A.1    Sadnik, I.2    Scheinbuks, J.3    Moldave, K.4
  • 101
    • 10644277580 scopus 로고    scopus 로고
    • Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and its role in ribosomal dissociation and anti-association
    • V.G. Kolupaeva, A. Unbehaun, I.B. Lomakin, C.U. Hellen, and T.V. Pestova Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and its role in ribosomal dissociation and anti-association RNA 11 2005 470 486
    • (2005) RNA , vol.11 , pp. 470-486
    • Kolupaeva, V.G.1    Unbehaun, A.2    Lomakin, I.B.3    Hellen, C.U.4    Pestova, T.V.5
  • 102
    • 67349152700 scopus 로고    scopus 로고
    • Role of eIF3a in regulating cell cycle progression
    • Z. Dong, Z. Liu, P. Cui, R. Pincheira, and Y. Yang Role of eIF3a in regulating cell cycle progression Exp. Cell Res. 315 2009 1889 1894
    • (2009) Exp. Cell Res. , vol.315 , pp. 1889-1894
    • Dong, Z.1    Liu, Z.2    Cui, P.3    Pincheira, R.4    Yang, Y.5
  • 103
    • 55449106579 scopus 로고    scopus 로고
    • Poly(A)-binding protein-interacting protein 1 binds to eukaryotic translation initiation factor 3 to stimulate translation
    • Y. Martineau, M.C. Derry, X. Wang, A. Yanagiya, and J.J. Berlanga Poly(A)-binding protein-interacting protein 1 binds to eukaryotic translation initiation factor 3 to stimulate translation Mol. Cell. Biol. 28 2008 6658 6667
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 6658-6667
    • Martineau, Y.1    Derry, M.C.2    Wang, X.3    Yanagiya, A.4    Berlanga, J.J.5
  • 104
    • 0034671570 scopus 로고    scopus 로고
    • A new pathway of translational regulation mediated by eukaryotic initiation factor 3
    • J. Guo, D.J. Hui, W.C. Merrick, and G.C. Sen A new pathway of translational regulation mediated by eukaryotic initiation factor 3 EMBO J. 19 2000 6891 6899
    • (2000) EMBO J , vol.19 , pp. 6891-6899
    • Guo, J.1    Hui, D.J.2    Merrick, W.C.3    Sen, G.C.4
  • 105
    • 34247165835 scopus 로고    scopus 로고
    • Individual overexpression of five subunits of human translation initiation factor eIF3 promotes malignant transformation of immortal fibroblast cells
    • L. Zhang, X. Pan, and J.W. Hershey Individual overexpression of five subunits of human translation initiation factor eIF3 promotes malignant transformation of immortal fibroblast cells J. Biol. Chem. 282 2007 5790 5800
    • (2007) J. Biol. Chem. , vol.282 , pp. 5790-5800
    • Zhang, L.1    Pan, X.2    Hershey, J.W.3
  • 106
    • 84858767569 scopus 로고    scopus 로고
    • The tumor suppressive role of eIF3f and its function in translation inhibition and rRNA degradation
    • F. Wen, R. Zhou, A. Shen, A. Choi, and D. Uribe The tumor suppressive role of eIF3f and its function in translation inhibition and rRNA degradation PLoS One 7 2012 e34194
    • (2012) PLoS One , vol.7
    • Wen, F.1    Zhou, R.2    Shen, A.3    Choi, A.4    Uribe, D.5
  • 107
  • 108
    • 61749091373 scopus 로고    scopus 로고
    • Phosphorylation of the eukaryotic initiation factor 3f by cyclin-dependent kinase 11 during apoptosis
    • J. Shi, J.W. Hershey, and M.A. Nelson Phosphorylation of the eukaryotic initiation factor 3f by cyclin-dependent kinase 11 during apoptosis FEBS Lett. 583 2009 971 977
    • (2009) FEBS Lett , vol.583 , pp. 971-977
    • Shi, J.1    Hershey, J.W.2    Nelson, M.A.3
  • 110
    • 84905644629 scopus 로고    scopus 로고
    • tRNA gene diversity in the three domains of life
    • K. Fujishima, and A. Kanai tRNA gene diversity in the three domains of life Front. Genet. 5 2014 142
    • (2014) Front. Genet. , vol.5 , pp. 142
    • Fujishima, K.1    Kanai, A.2
  • 111
    • 84893147804 scopus 로고    scopus 로고
    • Slicing tRNAs to boost functional ncRNA diversity
    • J. Gebetsberger, and N. Polacek Slicing tRNAs to boost functional ncRNA diversity RNA Biol. 10 2013 1798 1806
    • (2013) RNA Biol , vol.10 , pp. 1798-1806
    • Gebetsberger, J.1    Polacek, N.2
  • 112
    • 80051713296 scopus 로고    scopus 로고
    • Angiogenin-induced tRNA fragments inhibit translation initiation
    • P. Ivanov, M.M. Emara, J. Villen, S.P. Gygi, and P. Anderson Angiogenin-induced tRNA fragments inhibit translation initiation Mol. Cell 43 2011 613 623
    • (2011) Mol. Cell , vol.43 , pp. 613-623
    • Ivanov, P.1    Emara, M.M.2    Villen, J.3    Gygi, S.P.4    Anderson, P.5
  • 113
    • 84872784032 scopus 로고    scopus 로고
    • tRNA-derived fragments target the ribosome and function as regulatory non-coding RNA in Haloferax volcanii
    • J. Gebetsberger, M. Zywicki, A. Kunzi, and N. Polacek tRNA-derived fragments target the ribosome and function as regulatory non-coding RNA in Haloferax volcanii Archaea 2012 2012 260909
    • (2012) Archaea , vol.2012 , pp. 260909
    • Gebetsberger, J.1    Zywicki, M.2    Kunzi, A.3    Polacek, N.4
  • 114
    • 84903388410 scopus 로고    scopus 로고
    • How many initiator tRNA genes does Escherichia coli need?
    • L. Samhita, V. Nanjundiah, and U. Varshney How many initiator tRNA genes does Escherichia coli need? J. Bacteriol. 196 2014 2607 2615
    • (2014) J. Bacteriol. , vol.196 , pp. 2607-2615
    • Samhita, L.1    Nanjundiah, V.2    Varshney, U.3
  • 116
    • 0030875652 scopus 로고    scopus 로고
    • Requirements for ribosomal protein S1 for translation initiation of mRNAs with and without a 5′ leader sequence
    • K. Tedin, A. Resch, and U. Blasi Requirements for ribosomal protein S1 for translation initiation of mRNAs with and without a 5′ leader sequence Mol. Microbiol. 25 1997 189 199
    • (1997) Mol. Microbiol. , vol.25 , pp. 189-199
    • Tedin, K.1    Resch, A.2    Blasi, U.3
  • 117
    • 84904806049 scopus 로고    scopus 로고
    • RNA function. Ribosome stalling induced by mutation of a CNS-specific tRNA causes neurodegeneration
    • R. Ishimura, G. Nagy, I. Dotu, H. Zhou, and X.L. Yang RNA function. Ribosome stalling induced by mutation of a CNS-specific tRNA causes neurodegeneration Science 345 2014 455 459
    • (2014) Science , vol.345 , pp. 455-459
    • Ishimura, R.1    Nagy, G.2    Dotu, I.3    Zhou, H.4    Yang, X.L.5
  • 118
    • 79956328889 scopus 로고    scopus 로고
    • Enteric virulence associated protein VapC inhibits translation by cleavage of initiator tRNA
    • K.S. Winther, and K. Gerdes Enteric virulence associated protein VapC inhibits translation by cleavage of initiator tRNA Proc. Natl. Acad. Sci. U. S. A. 108 2011 7403 7407
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 7403-7407
    • Winther, K.S.1    Gerdes, K.2
  • 119
    • 0016665597 scopus 로고
    • Variation of ribosomal proteins with bacterial growth rate
    • A.N. Milne, W.W. Mak, and J.T. Wong Variation of ribosomal proteins with bacterial growth rate J. Bacteriol. 122 1975 89 92
    • (1975) J. Bacteriol. , vol.122 , pp. 89-92
    • Milne, A.N.1    Mak, W.W.2    Wong, J.T.3
  • 120
    • 84877741489 scopus 로고    scopus 로고
    • Ribosomal protein S1 functions as a termination factor in RNA synthesis by Qbeta phage replicase
    • N.N. Vasilyev, Z.S. Kutlubaeva, V.I. Ugarov, H.V. Chetverina, and A.B. Chetverin Ribosomal protein S1 functions as a termination factor in RNA synthesis by Qbeta phage replicase Nat. Commun. 4 2013 1781
    • (2013) Nat. Commun. , vol.4 , pp. 1781
    • Vasilyev, N.N.1    Kutlubaeva, Z.S.2    Ugarov, V.I.3    Chetverina, H.V.4    Chetverin, A.B.5
  • 121
    • 78649917229 scopus 로고    scopus 로고
    • The translation initiation factor 3f (eIF3f) exhibits a deubiquitinase activity regulating Notch activation
    • J. Moretti, P. Chastagner, S. Gastaldello, S.F. Heuss, and A.M. Dirac The translation initiation factor 3f (eIF3f) exhibits a deubiquitinase activity regulating Notch activation PLoS Biol. 8 2010 e1000545
    • (2010) PLoS Biol. , vol.8
    • Moretti, J.1    Chastagner, P.2    Gastaldello, S.3    Heuss, S.F.4    Dirac, A.M.5
  • 122
    • 63249134179 scopus 로고    scopus 로고
    • MAFbx/Atrogin-1 controls the activity of the initiation factor eIF3-f in skeletal muscle atrophy by targeting multiple C-terminal lysines
    • A. Csibi, M.P. Leibovitch, K. Cornille, L.A. Tintignac, and S.A. Leibovitch MAFbx/Atrogin-1 controls the activity of the initiation factor eIF3-f in skeletal muscle atrophy by targeting multiple C-terminal lysines J. Biol. Chem. 284 2009 4413 4421
    • (2009) J. Biol. Chem. , vol.284 , pp. 4413-4421
    • Csibi, A.1    Leibovitch, M.P.2    Cornille, K.3    Tintignac, L.A.4    Leibovitch, S.A.5
  • 124
    • 84886266176 scopus 로고    scopus 로고
    • Methylation of translation elongation factor 1A by the METTL10-like See1 methyltransferase facilitates tombusvirus replication in yeast and plants
    • Z. Li, P.A. Gonzalez, Z. Sasvari, T.G. Kinzy, and P.D. Nagy Methylation of translation elongation factor 1A by the METTL10-like See1 methyltransferase facilitates tombusvirus replication in yeast and plants Virology 448 2014 43 54
    • (2014) Virology , vol.448 , pp. 43-54
    • Li, Z.1    Gonzalez, P.A.2    Sasvari, Z.3    Kinzy, T.G.4    Nagy, P.D.5
  • 125
    • 35348866182 scopus 로고    scopus 로고
    • Versatile annotation and publication quality visualization of protein complexes using POLYVIEW-3D
    • A. Porollo, and J. Meller Versatile annotation and publication quality visualization of protein complexes using POLYVIEW-3D BMC Bioinform. 8 2007 316
    • (2007) BMC Bioinform. , vol.8 , pp. 316
    • Porollo, A.1    Meller, J.2
  • 126
    • 49649099901 scopus 로고    scopus 로고
    • Structural basis for translation termination on the 70S ribosome
    • M. Laurberg, H. Asahara, A. Korostelev, J. Zhu, and S. Trakhanov Structural basis for translation termination on the 70S ribosome Nature 454 2008 852 857
    • (2008) Nature , vol.454 , pp. 852-857
    • Laurberg, M.1    Asahara, H.2    Korostelev, A.3    Zhu, J.4    Trakhanov, S.5
  • 127
    • 0034703718 scopus 로고    scopus 로고
    • X-Ray structures of the universal translation initiation factor IF2/eIF5B: conformational changes on GDP and GTP binding
    • A. Roll-Mecak, C. Cao, T.E. Dever, and S.K. Burley X-Ray structures of the universal translation initiation factor IF2/eIF5B: conformational changes on GDP and GTP binding Cell 103 2000 781 792
    • (2000) Cell , vol.103 , pp. 781-792
    • Roll-Mecak, A.1    Cao, C.2    Dever, T.E.3    Burley, S.K.4
  • 128
    • 84878826802 scopus 로고    scopus 로고
    • Architecture of human translation initiation factor 3
    • J. Querol-Audi, C. Sun, J.M. Vogan, M.D. Smith, and Y. Gu Architecture of human translation initiation factor 3 Structure 21 2013 920 928
    • (2013) Structure , vol.21 , pp. 920-928
    • Querol-Audi, J.1    Sun, C.2    Vogan, J.M.3    Smith, M.D.4    Gu, Y.5
  • 129
    • 0018077590 scopus 로고
    • Crystal structure of yeast phenylalanine transfer RNA. I. Crystallographic refinement
    • J.L. Sussman, S.R. Holbrook, R.W. Warrant, G.M. Church, and S.H. Kim Crystal structure of yeast phenylalanine transfer RNA. I. Crystallographic refinement J. Mol. Biol. 123 1978 607 630
    • (1978) J. Mol. Biol. , vol.123 , pp. 607-630
    • Sussman, J.L.1    Holbrook, S.R.2    Warrant, R.W.3    Church, G.M.4    Kim, S.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.