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Volumn 115, Issue 2, 2003, Pages 187-198

Regulated release of L13a from the 60S ribosomal subunit as a mechanism of transcript-specific translational control

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; RIBOSOME PROTEIN;

EID: 0142227209     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(03)00773-6     Document Type: Article
Times cited : (275)

References (62)
  • 1
    • 0033601196 scopus 로고    scopus 로고
    • The action of N-terminal acetyltransferases on yeast ribosomal proteins
    • Arnold R.J., Polevoda B., Reilly J.P., Sherman F. The action of N-terminal acetyltransferases on yeast ribosomal proteins. J. Biol. Chem. 274:1999;37035-37040.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37035-37040
    • Arnold, R.J.1    Polevoda, B.2    Reilly, J.P.3    Sherman, F.4
  • 3
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A. The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science. 289:2000;905-920.
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 4
    • 0037169360 scopus 로고    scopus 로고
    • Human interferon-γ mRNA autoregulates its translation through a pseudoknot that activates the interferon-inducible protein kinase PKR
    • Ben-Asouli Y., Banai Y., Pel-Or Y., Shir A., Kaempfer R. Human interferon-γ mRNA autoregulates its translation through a pseudoknot that activates the interferon-inducible protein kinase PKR. Cell. 108:2002;221-232.
    • (2002) Cell , vol.108 , pp. 221-232
    • Ben-Asouli, Y.1    Banai, Y.2    Pel-Or, Y.3    Shir, A.4    Kaempfer, R.5
  • 5
    • 0036709869 scopus 로고    scopus 로고
    • Structure to function relationships in ceruloplasmin: A 'moonlighting' protein
    • Bielli P., Calabrese L. Structure to function relationships in ceruloplasmin. a 'moonlighting' protein Cell. Mol. Life Sci. 59:2002;1413-1427.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1413-1427
    • Bielli, P.1    Calabrese, L.2
  • 6
    • 0025015684 scopus 로고
    • The yeast 5S rRNA binding ribosomal protein YL3 is phosphorylated in vivo
    • Campos F., Corona-Reyes M., Zinker S. The yeast 5S rRNA binding ribosomal protein YL3 is phosphorylated in vivo. Biochim. Biophys. Acta. 1087:1990;142-146.
    • (1990) Biochim. Biophys. Acta , vol.1087 , pp. 142-146
    • Campos, F.1    Corona-Reyes, M.2    Zinker, S.3
  • 7
    • 0027964689 scopus 로고
    • A leucine zipper-like motif and a basic region-leucine zipper-like element in rat ribosomal protein L13a. Identification of the tum-transplantation antigen P198
    • Chan Y.L., Olvera J., Gluck A., Wool I.G. A leucine zipper-like motif and a basic region-leucine zipper-like element in rat ribosomal protein L13a. Identification of the tum-transplantation antigen P198. J. Biol. Chem. 269:1994;5589-5594.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5589-5594
    • Chan, Y.L.1    Olvera, J.2    Gluck, A.3    Wool, I.G.4
  • 9
    • 0036707527 scopus 로고    scopus 로고
    • 3′ end processing of Drosophila melanogaster histone pre-mRNAs: Requirement for phosphorylated Drosophila stem-loop binding protein and coevolution of the histone pre-mRNA processing system
    • Dominski Z., Yang X.C., Raska C.S., Santiago C., Borchers C.H., Duronio R.J., Marzluff W.F. 3′ end processing of Drosophila melanogaster histone pre-mRNAs. requirement for phosphorylated Drosophila stem-loop binding protein and coevolution of the histone pre-mRNA processing system Mol. Cell. Biol. 22:2002;6648-6660.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6648-6660
    • Dominski, Z.1    Yang, X.C.2    Raska, C.S.3    Santiago, C.4    Borchers, C.H.5    Duronio, R.J.6    Marzluff, W.F.7
  • 10
    • 0030062182 scopus 로고    scopus 로고
    • Role of endogenous ceruloplasmin in LDL oxidation by human U937 monocytic cells
    • Ehrenwald E., Fox P.L. Role of endogenous ceruloplasmin in LDL oxidation by human U937 monocytic cells. J. Clin. Invest. 97:1996;884-890.
    • (1996) J. Clin. Invest. , vol.97 , pp. 884-890
    • Ehrenwald, E.1    Fox, P.L.2
  • 11
    • 0024593537 scopus 로고
    • The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis
    • Finley D., Bartel B., Varshavsky A. The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis. Nature. 338:1989;394-401.
    • (1989) Nature , vol.338 , pp. 394-401
    • Finley, D.1    Bartel, B.2    Varshavsky, A.3
  • 12
    • 0026013498 scopus 로고
    • Induction of ceruloplasmin gene expression in rat lung during inflammation and hyperoxia
    • Fleming R.E., Whitman I.P., Gitlin J.D. Induction of ceruloplasmin gene expression in rat lung during inflammation and hyperoxia. Am. J. Physiol. 260:1991;L68-L74.
    • (1991) Am. J. Physiol. , vol.260
    • Fleming, R.E.1    Whitman, I.P.2    Gitlin, J.D.3
  • 13
    • 0037716752 scopus 로고    scopus 로고
    • Drosophila sex-lethal inhibits the stable association of the 40S ribosomal subunit with msl-2 mRNA
    • Gebauer F., Grskovic M., Hentze M.W. Drosophila sex-lethal inhibits the stable association of the 40S ribosomal subunit with msl-2 mRNA. Mol. Cell. 11:2003;1397-1404.
    • (2003) Mol. Cell , vol.11 , pp. 1397-1404
    • Gebauer, F.1    Grskovic, M.2    Hentze, M.W.3
  • 14
    • 0031816970 scopus 로고    scopus 로고
    • Aceruloplasminemia
    • Gitlin J.D. Aceruloplasminemia. Pediatr. Res. 44:1998;271-276.
    • (1998) Pediatr. Res. , vol.44 , pp. 271-276
    • Gitlin, J.D.1
  • 16
    • 0013355591 scopus 로고    scopus 로고
    • Putting the brake on inflammation
    • Kirkpatrick P. Putting the brake on inflammation. Nat. Rev. Drug Discov. 1:2002;99.
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 99
    • Kirkpatrick, P.1
  • 19
    • 0037302253 scopus 로고    scopus 로고
    • Phosphorylation of rubella virus capsid regulates its RNA binding activity and virus replication
    • Law L.M., Everitt J.C., Beatch M.D., Holmes C.F., Hobman T.C. Phosphorylation of rubella virus capsid regulates its RNA binding activity and virus replication. J. Virol. 77:2003;1764-1771.
    • (2003) J. Virol. , vol.77 , pp. 1764-1771
    • Law, L.M.1    Everitt, J.C.2    Beatch, M.D.3    Holmes, C.F.4    Hobman, T.C.5
  • 21
    • 0021763631 scopus 로고
    • Methylated proteins and amino acids in the ribosomes of Saccharomyces cerevisiae
    • Lhoest J., Lobet Y., Costers E., Colson C. Methylated proteins and amino acids in the ribosomes of Saccharomyces cerevisiae. Eur. J. Biochem. 141:1984;585-590.
    • (1984) Eur. J. Biochem. , vol.141 , pp. 585-590
    • Lhoest, J.1    Lobet, Y.2    Costers, E.3    Colson, C.4
  • 23
  • 24
    • 0014433054 scopus 로고
    • Ribosome-catalysed peptidyl transfer: The polyphenylalanine system
    • Maden B.E., Traut R.R., Monro R.E. Ribosome-catalysed peptidyl transfer. the polyphenylalanine system J. Mol. Biol. 35:1968;333-345.
    • (1968) J. Mol. Biol. , vol.35 , pp. 333-345
    • Maden, B.E.1    Traut, R.R.2    Monro, R.E.3
  • 25
    • 0031039529 scopus 로고    scopus 로고
    • The gene for histone RNA hairpin binding protein is located on human chromosome 4 and encodes a novel type of RNA binding protein
    • Martin F., Schaller A., Eglite S., Schumperli D., Muller B. The gene for histone RNA hairpin binding protein is located on human chromosome 4 and encodes a novel type of RNA binding protein. EMBO J. 16:1997;769-778.
    • (1997) EMBO J. , vol.16 , pp. 769-778
    • Martin, F.1    Schaller, A.2    Eglite, S.3    Schumperli, D.4    Muller, B.5
  • 26
    • 0025363528 scopus 로고
    • Modification of the accessibility of ribosomal proteins after elongation factor 2 binding to rat liver ribosomes and during translocation
    • Marzouki A., Lavergne J.P., Reboud J.P., Reboud A.M. Modification of the accessibility of ribosomal proteins after elongation factor 2 binding to rat liver ribosomes and during translocation. Biochim. Biophys. Acta. 1048:1990;238-244.
    • (1990) Biochim. Biophys. Acta , vol.1048 , pp. 238-244
    • Marzouki, A.1    Lavergne, J.P.2    Reboud, J.P.3    Reboud, A.M.4
  • 27
    • 0025189709 scopus 로고
    • Ribosome and protein synthesis modifications after infection of human epidermoid carcinoma cells with herpes simplex virus type 1
    • Masse T., Garcin D., Jacquemont B., Madjar J.J. Ribosome and protein synthesis modifications after infection of human epidermoid carcinoma cells with herpes simplex virus type 1. Mol. Gen. Genet. 220:1990;377-388.
    • (1990) Mol. Gen. Genet. , vol.220 , pp. 377-388
    • Masse, T.1    Garcin, D.2    Jacquemont, B.3    Madjar, J.J.4
  • 29
    • 0032827602 scopus 로고    scopus 로고
    • Delayed translational silencing of ceruloplasmin transcript in gamma interferon-activated U937 monocytic cells: Role of the 3′ untranslated region
    • Mazumder B., Fox P.L. Delayed translational silencing of ceruloplasmin transcript in gamma interferon-activated U937 monocytic cells. Role of the 3′ untranslated region Mol. Cell. Biol. 19:1999;6898-6905.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6898-6905
    • Mazumder, B.1    Fox, P.L.2
  • 30
    • 0031571216 scopus 로고    scopus 로고
    • Induction of ceruloplasmin synthesis by IFN-γ in human monocytic cells
    • Mazumder B., Mukhopadhyay C.K., Prok A., Cathcart M.K., Fox P.L. Induction of ceruloplasmin synthesis by IFN-γ in human monocytic cells. J. Immunol. 159:1997;1938-1944.
    • (1997) J. Immunol. , vol.159 , pp. 1938-1944
    • Mazumder, B.1    Mukhopadhyay, C.K.2    Prok, A.3    Cathcart, M.K.4    Fox, P.L.5
  • 31
    • 0034811090 scopus 로고    scopus 로고
    • Translational silencing of ceruloplasmin requires the essential elements of mRNA circularization: Poly(A) tail, poly(A)-binding protein, and eukaryotic translation initiation factor 4G
    • Mazumder B., Seshadri V., Imataka H., Sonenberg N., Fox P.L. Translational silencing of ceruloplasmin requires the essential elements of mRNA circularization. Poly(A) tail, poly(A)-binding protein, and eukaryotic translation initiation factor 4G Mol. Cell. Biol. 21:2001;6440-6449.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6440-6449
    • Mazumder, B.1    Seshadri, V.2    Imataka, H.3    Sonenberg, N.4    Fox, P.L.5
  • 32
    • 0037308625 scopus 로고    scopus 로고
    • Translational control by the 3′-UTR: The ends specify the means
    • Mazumder B., Seshadri V., Fox P.L. Translational control by the 3′-UTR. the ends specify the means Trends Biochem. Sci. 28:2003;91-98.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 91-98
    • Mazumder, B.1    Seshadri, V.2    Fox, P.L.3
  • 34
    • 0043268903 scopus 로고    scopus 로고
    • The structural basis of large ribosomal subunit function
    • Moore P.B., Steitz T.A. The structural basis of large ribosomal subunit function. Annu. Rev. Biochem. 72:2003;813-850.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 813-850
    • Moore, P.B.1    Steitz, T.A.2
  • 35
    • 0032160381 scopus 로고    scopus 로고
    • IRP-1 binding to ferritin mRNA prevents the recruitment of the small ribosomal subunit by the cap-binding complex eIF4F
    • Muckenthaler M., Gray N.K., Hentze M.W. IRP-1 binding to ferritin mRNA prevents the recruitment of the small ribosomal subunit by the cap-binding complex eIF4F. Mol. Cell. 2:1998;383-388.
    • (1998) Mol. Cell , vol.2 , pp. 383-388
    • Muckenthaler, M.1    Gray, N.K.2    Hentze, M.W.3
  • 36
    • 0030851818 scopus 로고    scopus 로고
    • Identification of the prooxidant site of human ceruloplasmin: A model for oxidative damage by copper bound to protein surfaces
    • Mukhopadhyay C.K., Mazumder B., Lindley P.F., Fox P.L. Identification of the prooxidant site of human ceruloplasmin. a model for oxidative damage by copper bound to protein surfaces Proc. Natl. Acad. Sci. USA. 94:1997;11546-11551.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11546-11551
    • Mukhopadhyay, C.K.1    Mazumder, B.2    Lindley, P.F.3    Fox, P.L.4
  • 37
    • 0037180812 scopus 로고    scopus 로고
    • Points of control in inflammation
    • Nathan C. Points of control in inflammation. Nature. 420:2002;846-852.
    • (2002) Nature , vol.420 , pp. 846-852
    • Nathan, C.1
  • 38
    • 0026639881 scopus 로고
    • Unusual resistance of peptidyl transferase to protein extraction procedures
    • Noller H.F., Hoffarth V., Zimniak L. Unusual resistance of peptidyl transferase to protein extraction procedures. Science. 256:1992;1416-1419.
    • (1992) Science , vol.256 , pp. 1416-1419
    • Noller, H.F.1    Hoffarth, V.2    Zimniak, L.3
  • 39
    • 0014027719 scopus 로고
    • The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum
    • Osaki S., Johnson D.A., Frieden E. The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum. J. Biol. Chem. 241:1966;2746-2751.
    • (1966) J. Biol. Chem. , vol.241 , pp. 2746-2751
    • Osaki, S.1    Johnson, D.A.2    Frieden, E.3
  • 40
    • 0035951373 scopus 로고    scopus 로고
    • Lipoxygenase mRNA silencing in erythroid differentiation: The 3′UTR regulatory complex controls 60S ribosomal subunit joining
    • Ostareck D.H., Ostareck-Lederer A., Shatsky I.N., Hentze M.W. Lipoxygenase mRNA silencing in erythroid differentiation. the 3′UTR regulatory complex controls 60S ribosomal subunit joining Cell. 104:2001;281-290.
    • (2001) Cell , vol.104 , pp. 281-290
    • Ostareck, D.H.1    Ostareck-Lederer, A.2    Shatsky, I.N.3    Hentze, M.W.4
  • 42
    • 0034603039 scopus 로고    scopus 로고
    • Role of tyrosine phosphorylation in the regulation of the interaction of heterogenous nuclear ribonucleoprotein K protein with its protein and RNA partners
    • Ostrowski J., Schullery D.S., Denisenko O.N., Higaki Y., Watts J., Aebersold R., Stempka L., Gschwendt M., Bomsztyk K. Role of tyrosine phosphorylation in the regulation of the interaction of heterogenous nuclear ribonucleoprotein K protein with its protein and RNA partners. J. Biol. Chem. 275:2000;3619-3628.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3619-3628
    • Ostrowski, J.1    Schullery, D.S.2    Denisenko, O.N.3    Higaki, Y.4    Watts, J.5    Aebersold, R.6    Stempka, L.7    Gschwendt, M.8    Bomsztyk, K.9
  • 44
    • 0028981381 scopus 로고
    • Ribosomal acidic phosphoproteins P1 and P2 are not required for cell viability but regulate the pattern of protein expression in Saccharomyces cerevisiae
    • Remacha M., Jimenez-Diaz A., Bermejo B., Rodriguez-Gabriel M.A., Guarinos E., Ballesta J.P. Ribosomal acidic phosphoproteins P1 and P2 are not required for cell viability but regulate the pattern of protein expression in Saccharomyces cerevisiae. Mol. Cell. Biol. 15:1995;4754-4762.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4754-4762
    • Remacha, M.1    Jimenez-Diaz, A.2    Bermejo, B.3    Rodriguez-Gabriel, M.A.4    Guarinos, E.5    Ballesta, J.P.6
  • 46
    • 0025870212 scopus 로고
    • Interactions of serum copper, selenium, and low density lipoprotein cholesterol in atherogenesis
    • Salonen J.T., Salonen R., Seppänen K., Kantola M., Suntioinen S., Korpela H. Interactions of serum copper, selenium, and low density lipoprotein cholesterol in atherogenesis. BMJ. 302:1991;756-760.
    • (1991) BMJ , vol.302 , pp. 756-760
    • Salonen, J.T.1    Salonen, R.2    Seppänen, K.3    Kantola, M.4    Suntioinen, S.5    Korpela, H.6
  • 47
    • 0037371348 scopus 로고    scopus 로고
    • Transcript-selective translational silencing by gamma interferon is directed by a novel structural element in the ceruloplasmin mRNA 3′ untranslated region
    • Sampath P., Mazumder B., Seshadri V., Fox P.L. Transcript-selective translational silencing by gamma interferon is directed by a novel structural element in the ceruloplasmin mRNA 3′ untranslated region. Mol. Cell. Biol. 23:2003;1509-1519.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1509-1519
    • Sampath, P.1    Mazumder, B.2    Seshadri, V.3    Fox, P.L.4
  • 49
    • 0037447159 scopus 로고    scopus 로고
    • Ribosomal protein S15 represses its own translation via adaptation of an rRNA-like fold within its mRNA
    • Serganov A., Polonskaia A., Ehresmann B., Ehresmann C., Patel D.J. Ribosomal protein S15 represses its own translation via adaptation of an rRNA-like fold within its mRNA. EMBO J. 22:2003;1898-1908.
    • (2003) EMBO J. , vol.22 , pp. 1898-1908
    • Serganov, A.1    Polonskaia, A.2    Ehresmann, B.3    Ehresmann, C.4    Patel, D.J.5
  • 51
    • 0036892046 scopus 로고    scopus 로고
    • Casein kinase II phosphorylates the fragile X mental retardation protein and modulates its biological properties
    • Siomi M.C., Higashijima K., Ishizuka A., Siomi H. Casein kinase II phosphorylates the fragile X mental retardation protein and modulates its biological properties. Mol. Cell. Biol. 22:2002;8438-8447.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8438-8447
    • Siomi, M.C.1    Higashijima, K.2    Ishizuka, A.3    Siomi, H.4
  • 52
    • 0035798380 scopus 로고    scopus 로고
    • Structure of the 80S ribosome from Saccharomyces cerevisiae-tRNA- ribosome and subunit-subunit interactions
    • Spahn C.M., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G., Frank J. Structure of the 80S ribosome from Saccharomyces cerevisiae-tRNA- ribosome and subunit-subunit interactions. Cell. 107:2001;373-386.
    • (2001) Cell , vol.107 , pp. 373-386
    • Spahn, C.M.1    Beckmann, R.2    Eswar, N.3    Penczek, P.A.4    Sali, A.5    Blobel, G.6    Frank, J.7
  • 53
    • 0034616943 scopus 로고    scopus 로고
    • Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain
    • Spence J., Gali R.R., Dittmar G., Sherman F., Karin M., Finley D. Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain. Cell. 102:2000;67-76.
    • (2000) Cell , vol.102 , pp. 67-76
    • Spence, J.1    Gali, R.R.2    Dittmar, G.3    Sherman, F.4    Karin, M.5    Finley, D.6
  • 54
    • 0001331728 scopus 로고
    • Synthetic peptide vaccine design: Synthesis and properties of a high-density multiple antigenic peptide system
    • Tam J.P. Synthetic peptide vaccine design. Synthesis and properties of a high-density multiple antigenic peptide system Proc. Natl. Acad. Sci. USA. 85:1988;5409-5413.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5409-5413
    • Tam, J.P.1
  • 55
    • 0033634724 scopus 로고    scopus 로고
    • Multiple functions of an evolutionarily conserved RNA binding domain
    • Vilardell J., Yu S.J., Warner J.R. Multiple functions of an evolutionarily conserved RNA binding domain. Mol. Cell. 5:2000;761-766.
    • (2000) Mol. Cell , vol.5 , pp. 761-766
    • Vilardell, J.1    Yu, S.J.2    Warner, J.R.3
  • 56
    • 0029974453 scopus 로고    scopus 로고
    • Extraribosomal functions of ribosomal proteins
    • Wool I.G. Extraribosomal functions of ribosomal proteins. Trends Biochem. Sci. 21:1996;164-165.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 164-165
    • Wool, I.G.1
  • 57
    • 0001320597 scopus 로고    scopus 로고
    • Mammalian ribosomes: The structure and the evolution of the proteins
    • M.B. Mathews, & N. Sonenberg. Plainview, NY: Cold Spring Harbor Laboratory Press. 481-503.pp
    • Wool I.G., Chan Y.-L., Glück A. Mammalian ribosomes. the structure and the evolution of the proteins Mathews M.B., Sonenberg N. Translational Control. J.W.B. Hershey. 1996;Cold Spring Harbor Laboratory Press, Plainview, NY. 481-503.pp.
    • (1996) Translational Control. J.W.B. Hershey
    • Wool, I.G.1    Chan, Y.-L.2    Glück, A.3
  • 58
    • 0026267012 scopus 로고
    • Preparation of synthetic mRNAs and analyses of translational efficiency in microinjected Xenopus oocytes
    • Wormington M. Preparation of synthetic mRNAs and analyses of translational efficiency in microinjected Xenopus oocytes. Methods Cell Biol. 36:1991;167-183.
    • (1991) Methods Cell Biol. , vol.36 , pp. 167-183
    • Wormington, M.1
  • 59
    • 0033580455 scopus 로고    scopus 로고
    • Interaction of the p23/p198 protein with ErbB-3
    • Yoo J.Y., Hamburger A.W. Interaction of the p23/p198 protein with ErbB-3. Gene. 229:1999;215-221.
    • (1999) Gene , vol.229 , pp. 215-221
    • Yoo, J.Y.1    Hamburger, A.W.2
  • 60
    • 0037423293 scopus 로고    scopus 로고
    • The Fragile X syndrome protein FMRP associates with BC1 RNA and regulates the translation of specific mRNAs at synapses
    • Zalfa F., Giorgi M., Primerano B., Moro A., Di Penta A., Reis S., Oostra B., Bagni C. The Fragile X syndrome protein FMRP associates with BC1 RNA and regulates the translation of specific mRNAs at synapses. Cell. 112:2003;317-327.
    • (2003) Cell , vol.112 , pp. 317-327
    • Zalfa, F.1    Giorgi, M.2    Primerano, B.3    Moro, A.4    Di Penta, A.5    Reis, S.6    Oostra, B.7    Bagni, C.8
  • 61
    • 0028251157 scopus 로고
    • Diverse mechanisms for regulating ribosomal protein synthesis in Escherichia coli
    • Zengel J.M., Lindahl L. Diverse mechanisms for regulating ribosomal protein synthesis in Escherichia coli. Prog. Nucleic Acid Res. Mol. Biol. 47:1994;331-370.
    • (1994) Prog. Nucleic Acid Res. Mol. Biol. , vol.47 , pp. 331-370
    • Zengel, J.M.1    Lindahl, L.2
  • 62
    • 0037447138 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of QKI mediates developmental signals to regulate mRNA metabolism
    • Zhang Y., Lu Z., Ku L., Chen Y., Wang H., Feng Y. Tyrosine phosphorylation of QKI mediates developmental signals to regulate mRNA metabolism. EMBO J. 22:2003;1801-1810.
    • (2003) EMBO J. , vol.22 , pp. 1801-1810
    • Zhang, Y.1    Lu, Z.2    Ku, L.3    Chen, Y.4    Wang, H.5    Feng, Y.6


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