메뉴 건너뛰기




Volumn 35, Issue 2, 2009, Pages 164-180

Two-Site Phosphorylation of EPRS Coordinates Multimodal Regulation of Noncanonical Translational Control Activity

Author keywords

RNA; SIGNALING

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE; GAMMA INTERFERON; GLUTAMYL PROLYL TRNA SYNTHETASE; MESSENGER RNA; RIBOSOME PROTEIN; SERINE; UNCLASSIFIED DRUG;

EID: 67651095905     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2009.05.028     Document Type: Article
Times cited : (103)

References (62)
  • 3
    • 0017716612 scopus 로고
    • The early influence of 17-β-oestradiol on 17 aminoacyl-tRNA synthetases of mouse uterus and liver. Phosphorylation as a regulation mechanism
    • Berg B.H. The early influence of 17-β-oestradiol on 17 aminoacyl-tRNA synthetases of mouse uterus and liver. Phosphorylation as a regulation mechanism. Biochim. Biophys. Acta 479 (1977) 152-171
    • (1977) Biochim. Biophys. Acta , vol.479 , pp. 152-171
    • Berg, B.H.1
  • 4
    • 0034141480 scopus 로고    scopus 로고
    • A recurrent RNA-binding domain is appended to eukaryotic aminoacyl-tRNA synthetases
    • Cahuzac B., Berthonneau E., Birlirakis N., Guittet E., and Mirande M. A recurrent RNA-binding domain is appended to eukaryotic aminoacyl-tRNA synthetases. EMBO J. 19 (2000) 445-452
    • (2000) EMBO J. , vol.19 , pp. 445-452
    • Cahuzac, B.1    Berthonneau, E.2    Birlirakis, N.3    Guittet, E.4    Mirande, M.5
  • 5
    • 0026341207 scopus 로고
    • Assay of protein kinases using peptides with basic residues for phosphocellulose binding
    • Casnellie J.E. Assay of protein kinases using peptides with basic residues for phosphocellulose binding. Methods Enzymol. 200 (1991) 115-120
    • (1991) Methods Enzymol. , vol.200 , pp. 115-120
    • Casnellie, J.E.1
  • 6
    • 0025365655 scopus 로고
    • Does protein phosphorylation play a role in translational control by eukaryotic aminoacyl-tRNA synthetases?
    • Clemens M.J. Does protein phosphorylation play a role in translational control by eukaryotic aminoacyl-tRNA synthetases?. Trends Biochem. Sci. 15 (1990) 172-175
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 172-175
    • Clemens, M.J.1
  • 7
    • 0034383949 scopus 로고    scopus 로고
    • The regulation of protein function by multisite phosphorylation-a 25 year update
    • Cohen P. The regulation of protein function by multisite phosphorylation-a 25 year update. Trends Biochem. Sci. 25 (2000) 596-601
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 596-601
    • Cohen, P.1
  • 9
    • 0020344274 scopus 로고
    • Regulation of the aminoacyl-tRNA synthetase complex of rat liver by phosphorylation/dephosphorylation in vitro and in vivo
    • Damuni Z., Caudwell F.B., and Cohen P. Regulation of the aminoacyl-tRNA synthetase complex of rat liver by phosphorylation/dephosphorylation in vitro and in vivo. Eur. J. Biochem. 129 (1982) 57-65
    • (1982) Eur. J. Biochem. , vol.129 , pp. 57-65
    • Damuni, Z.1    Caudwell, F.B.2    Cohen, P.3
  • 10
    • 0037154965 scopus 로고    scopus 로고
    • Gene-specific regulation by general translation factors
    • Dever T.E. Gene-specific regulation by general translation factors. Cell 108 (2002) 545-556
    • (2002) Cell , vol.108 , pp. 545-556
    • Dever, T.E.1
  • 11
    • 0030445778 scopus 로고    scopus 로고
    • Tripping the switch fantastic: how a protein kinase cascade can convert graded inputs into switch-like outputs
    • Ferrell Jr. J.E. Tripping the switch fantastic: how a protein kinase cascade can convert graded inputs into switch-like outputs. Trends Biochem. Sci. 21 (1996) 460-466
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 460-466
    • Ferrell Jr., J.E.1
  • 12
    • 5044229348 scopus 로고    scopus 로고
    • Molecular mechanisms of translational control
    • Gebauer F., and Hentze M.W. 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
  • 13
    • 33646266474 scopus 로고    scopus 로고
    • Conformational changes in protein loops and helices induced by post-translational phosphorylation
    • Groban E.S., Narayanan A., and Jacobson M.P. Conformational changes in protein loops and helices induced by post-translational phosphorylation. PLoS Comput. Biol. 2 (2006) e32
    • (2006) PLoS Comput. Biol. , vol.2
    • Groban, E.S.1    Narayanan, A.2    Jacobson, M.P.3
  • 15
    • 0036901003 scopus 로고    scopus 로고
    • Multisite phosphorylation provides sophisticated regulation of transcription factors
    • Holmberg C.I., Tran S.E., Eriksson J.E., and Sistonen L. Multisite phosphorylation provides sophisticated regulation of transcription factors. Trends Biochem. Sci. 27 (2002) 619-627
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 619-627
    • Holmberg, C.I.1    Tran, S.E.2    Eriksson, J.E.3    Sistonen, L.4
  • 16
    • 43449132366 scopus 로고    scopus 로고
    • Multisite phosphorylation regulates Bim stability and apoptotic activity
    • Hübner A., Barrett T., Flavell R.A., and Davis R.J. Multisite phosphorylation regulates Bim stability and apoptotic activity. Mol. Cell 30 (2008) 415-425
    • (2008) Mol. Cell , vol.30 , pp. 415-425
    • Hübner, A.1    Barrett, T.2    Flavell, R.A.3    Davis, R.J.4
  • 17
    • 0033782994 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis
    • Ibba M., and Söll D. Aminoacyl-tRNA synthesis. Annu. Rev. Biochem. 69 (2000) 617-650
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 617-650
    • Ibba, M.1    Söll, D.2
  • 18
    • 0034719153 scopus 로고    scopus 로고
    • Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: Identification of RNA-binding residues and functional implications for tandem repeats
    • Jeong E.J., Hwang G.S., Kim K.H., Kim M.J., Kim S., and Kim K.S. Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: Identification of RNA-binding residues and functional implications for tandem repeats. Biochemistry 39 (2000) 15775-15782
    • (2000) Biochemistry , vol.39 , pp. 15775-15782
    • Jeong, E.J.1    Hwang, G.S.2    Kim, K.H.3    Kim, M.J.4    Kim, S.5    Kim, K.S.6
  • 19
    • 40849118528 scopus 로고    scopus 로고
    • WHEP domains direct noncanonical function of glutamyl-prolyl tRNA synthetase in translational control of gene expression
    • Jia J., Arif A., Ray P.S., and Fox P.L. WHEP domains direct noncanonical function of glutamyl-prolyl tRNA synthetase in translational control of gene expression. Mol. Cell 29 (2008) 679-690
    • (2008) Mol. Cell , vol.29 , pp. 679-690
    • Jia, J.1    Arif, A.2    Ray, P.S.3    Fox, P.L.4
  • 20
    • 33846004827 scopus 로고    scopus 로고
    • L13a blocks 48S assembly: Role of a general initiation factor in mRNA-specific translational control
    • Kapasi P., Chaudhuri S., Vyas K., Baus D., Komar A.A., Fox P.L., Merrick W.C., and Mazumder B. L13a blocks 48S assembly: Role of a general initiation factor in mRNA-specific translational control. Mol. Cell 25 (2007) 113-126
    • (2007) Mol. Cell , vol.25 , pp. 113-126
    • Kapasi, P.1    Chaudhuri, S.2    Vyas, K.3    Baus, D.4    Komar, A.A.5    Fox, P.L.6    Merrick, W.C.7    Mazumder, B.8
  • 21
    • 0035937134 scopus 로고    scopus 로고
    • Glutamine-dependent antiapoptotic interaction of human glutaminyl-tRNA synthetase with apoptosis signal-regulating kinase 1
    • Ko Y.G., Kim E.Y., Kim T., Park H., Park H.S., Choi E.J., and Kim S. Glutamine-dependent antiapoptotic interaction of human glutaminyl-tRNA synthetase with apoptosis signal-regulating kinase 1. J. Biol. Chem. 276 (2001) 6030-6036
    • (2001) J. Biol. Chem. , vol.276 , pp. 6030-6036
    • Ko, Y.G.1    Kim, E.Y.2    Kim, T.3    Park, H.4    Park, H.S.5    Choi, E.J.6    Kim, S.7
  • 22
    • 0036744432 scopus 로고    scopus 로고
    • Novel regulatory interactions and activities of mammalian tRNA synthetases
    • Ko Y.G., Park H., and Kim S. Novel regulatory interactions and activities of mammalian tRNA synthetases. Proteomics 2 (2002) 1304-1310
    • (2002) Proteomics , vol.2 , pp. 1304-1310
    • Ko, Y.G.1    Park, H.2    Kim, S.3
  • 23
    • 39549104965 scopus 로고    scopus 로고
    • An important role for the multienzyme aminoacyl-tRNA synthetase complex in mammalian translation and cell growth
    • Kyriacou S.V., and Deutscher M.P. An important role for the multienzyme aminoacyl-tRNA synthetase complex in mammalian translation and cell growth. Mol. Cell 29 (2008) 419-427
    • (2008) Mol. Cell , vol.29 , pp. 419-427
    • Kyriacou, S.V.1    Deutscher, M.P.2
  • 24
    • 26444461483 scopus 로고    scopus 로고
    • Nonconventional involvement of LysRS in the molecular mechanism of USF2 transcriptional activity in FcεRI-activated mast cells
    • Lee Y.N., and Razin E. Nonconventional involvement of LysRS in the molecular mechanism of USF2 transcriptional activity in FcεRI-activated mast cells. Mol. Cell. Biol. 25 (2005) 8904-8912
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8904-8912
    • Lee, Y.N.1    Razin, E.2
  • 25
    • 4444369924 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetase complexes: beyond translation
    • Lee S.W., Cho B.H., Park S.G., and Kim S. Aminoacyl-tRNA synthetase complexes: beyond translation. J. Cell Sci. 117 (2004) 3725-3734
    • (2004) J. Cell Sci. , vol.117 , pp. 3725-3734
    • Lee, S.W.1    Cho, B.H.2    Park, S.G.3    Kim, S.4
  • 26
    • 1342287127 scopus 로고    scopus 로고
    • The function of lysyl-tRNA synthetase and Ap4A as signaling regulators of MITF activity in FcεRI-activated mast cells
    • Lee Y.N., Nechushtan H., Figov N., and Razin E. The function of lysyl-tRNA synthetase and Ap4A as signaling regulators of MITF activity in FcεRI-activated mast cells. Immunity 20 (2004) 145-151
    • (2004) Immunity , vol.20 , pp. 145-151
    • Lee, Y.N.1    Nechushtan, H.2    Figov, N.3    Razin, E.4
  • 28
    • 0032568588 scopus 로고    scopus 로고
    • Phosphorylation-induced structural change in phospholamban and its mutants, detected by intrinsic fluorescence
    • Li M., Cornea R.L., Autry J.M., Jones L.R., and Thomas D.D. Phosphorylation-induced structural change in phospholamban and its mutants, detected by intrinsic fluorescence. Biochemistry 37 (1998) 7869-7877
    • (1998) Biochemistry , vol.37 , pp. 7869-7877
    • Li, M.1    Cornea, R.L.2    Autry, J.M.3    Jones, L.R.4    Thomas, D.D.5
  • 30
    • 0020560563 scopus 로고
    • Myositis autoantibody inhibits histidyl-tRNA synthetase: a model for autoimmunity
    • Mathews M.B., and Bernstein R.M. Myositis autoantibody inhibits histidyl-tRNA synthetase: a model for autoimmunity. Nature 304 (1983) 177-179
    • (1983) Nature , vol.304 , pp. 177-179
    • Mathews, M.B.1    Bernstein, R.M.2
  • 31
    • 0142227209 scopus 로고    scopus 로고
    • Regulated release of L13a from the 60S ribosomal subunit as a mechanism of transcript-specific translational control
    • Mazumder B., Sampath P., Seshadri V., Maitra R.K., DiCorleto P., and Fox P.L. Regulated release of L13a from the 60S ribosomal subunit as a mechanism of transcript-specific translational control. Cell 115 (2003) 187-198
    • (2003) Cell , vol.115 , pp. 187-198
    • Mazumder, B.1    Sampath, P.2    Seshadri, V.3    Maitra, R.K.4    DiCorleto, P.5    Fox, P.L.6
  • 32
    • 0031971228 scopus 로고    scopus 로고
    • Multisite phosphorylation and the integration of stress signals at p53
    • Meek D.W. Multisite phosphorylation and the integration of stress signals at p53. Cell. Signal. 10 (1998) 159-166
    • (1998) Cell. Signal. , vol.10 , pp. 159-166
    • Meek, D.W.1
  • 33
    • 0022033589 scopus 로고
    • A complex from cultured Chinese hamster ovary cells containing nine aminoacyl-tRNA synthetases. Thermolabile leucyl-tRNA synthetase from the tsH1 mutant cell line is an integral component of this complex
    • Mirande M., Le Corre D., and Waller J.P. A complex from cultured Chinese hamster ovary cells containing nine aminoacyl-tRNA synthetases. Thermolabile leucyl-tRNA synthetase from the tsH1 mutant cell line is an integral component of this complex. Eur. J. Biochem. 147 (1985) 281-289
    • (1985) Eur. J. Biochem. , vol.147 , pp. 281-289
    • Mirande, M.1    Le Corre, D.2    Waller, J.P.3
  • 34
    • 55049140658 scopus 로고    scopus 로고
    • DAPK-ZIPK-L13a axis constitutes a negative-feedback module regulating inflammatory gene expression
    • Mukhopadhyay R., Ray P.S., Arif A., Brady A.K., Kinter M., and Fox P.L. DAPK-ZIPK-L13a axis constitutes a negative-feedback module regulating inflammatory gene expression. Mol. Cell 32 (2008) 371-382
    • (2008) Mol. Cell , vol.32 , pp. 371-382
    • Mukhopadhyay, R.1    Ray, P.S.2    Arif, A.3    Brady, A.K.4    Kinter, M.5    Fox, P.L.6
  • 36
    • 0042622251 scopus 로고    scopus 로고
    • Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs
    • Obenauer J.C., Cantley L.C., and Yaffe M.B. Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs. Nucleic Acids Res. 31 (2003) 3635-3641
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3635-3641
    • Obenauer, J.C.1    Cantley, L.C.2    Yaffe, M.B.3
  • 37
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., and Mann M. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127 (2006) 635-648
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 38
    • 25144489447 scopus 로고    scopus 로고
    • Functional expansion of aminoacyl-tRNA synthetases and their interacting factors: new perspectives on housekeepers
    • Park S.G., Ewalt K.L., and Kim S. Functional expansion of aminoacyl-tRNA synthetases and their interacting factors: new perspectives on housekeepers. Trends Biochem. Sci. 30 (2005) 569-574
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 569-574
    • Park, S.G.1    Ewalt, K.L.2    Kim, S.3
  • 41
    • 0022178606 scopus 로고
    • Alteration of aminoacyl-tRNA synthetase activities by phosphorylation with casein kinase I
    • Pendergast A.M., and Traugh J.A. Alteration of aminoacyl-tRNA synthetase activities by phosphorylation with casein kinase I. J. Biol. Chem. 260 (1985) 11769-11774
    • (1985) J. Biol. Chem. , vol.260 , pp. 11769-11774
    • Pendergast, A.M.1    Traugh, J.A.2
  • 42
    • 0023644749 scopus 로고
    • Regulation of phosphorylation of aminoacyl-tRNA synthetases in the high molecular weight core complex in reticulocytes
    • Pendergast A.M., Venema R.C., and Traugh J.A. Regulation of phosphorylation of aminoacyl-tRNA synthetases in the high molecular weight core complex in reticulocytes. J. Biol. Chem. 262 (1987) 5939-5942
    • (1987) J. Biol. Chem. , vol.262 , pp. 5939-5942
    • Pendergast, A.M.1    Venema, R.C.2    Traugh, J.A.3
  • 44
    • 34247118887 scopus 로고    scopus 로고
    • Signalling to translation: how signal transduction pathways control the protein synthetic machinery
    • Proud C.G. Signalling to translation: how signal transduction pathways control the protein synthetic machinery. Biochem. J. 403 (2007) 217-234
    • (2007) Biochem. J. , vol.403 , pp. 217-234
    • Proud, C.G.1
  • 46
    • 34547235967 scopus 로고    scopus 로고
    • A post-transcriptional pathway represses monocyte VEGF-A expression and angiogenic activity
    • Ray P.S., and Fox P.L. A post-transcriptional pathway represses monocyte VEGF-A expression and angiogenic activity. EMBO J. 26 (2007) 3360-3372
    • (2007) EMBO J. , vol.26 , pp. 3360-3372
    • Ray, P.S.1    Fox, P.L.2
  • 47
    • 34247131410 scopus 로고    scopus 로고
    • Macromolecular complexes as depots for releasable regulatory proteins
    • Ray P.S., Arif A., and Fox P.L. Macromolecular complexes as depots for releasable regulatory proteins. Trends Biochem. Sci. 32 (2007) 158-164
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 158-164
    • Ray, P.S.1    Arif, A.2    Fox, P.L.3
  • 48
    • 60149091561 scopus 로고    scopus 로고
    • A stress-responsive RNA switch regulates VEGFA expression
    • Ray P.S., Jia J., Yao P., Majumder M., Hatzoglou M., and Fox P.L. A stress-responsive RNA switch regulates VEGFA expression. Nature 457 (2009) 915-919
    • (2009) Nature , vol.457 , pp. 915-919
    • Ray, P.S.1    Jia, J.2    Yao, P.3    Majumder, M.4    Hatzoglou, M.5    Fox, P.L.6
  • 49
    • 0035478911 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetases: potential markers of genetic code development
    • Ribas de Pouplana L., and Schimmel P. Aminoacyl-tRNA synthetases: potential markers of genetic code development. Trends Biochem. Sci. 26 (2001) 591-596
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 591-596
    • Ribas de Pouplana, L.1    Schimmel, P.2
  • 51
    • 0034671360 scopus 로고    scopus 로고
    • Macromolecular assemblage of aminoacyl-tRNA synthetases: Quantitative analysis of protein-protein interactions and mechanism of complex assembly
    • Robinson J.C., Kerjan P., and Mirande M. Macromolecular assemblage of aminoacyl-tRNA synthetases: Quantitative analysis of protein-protein interactions and mechanism of complex assembly. J. Mol. Biol. 304 (2000) 983-994
    • (2000) J. Mol. Biol. , vol.304 , pp. 983-994
    • Robinson, J.C.1    Kerjan, P.2    Mirande, M.3
  • 52
    • 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., and 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
  • 54
    • 33846671062 scopus 로고    scopus 로고
    • Tuning bulk electrostatics to regulate protein function
    • Serber Z., and Ferrell Jr. J.E. Tuning bulk electrostatics to regulate protein function. Cell 128 (2007) 441-444
    • (2007) Cell , vol.128 , pp. 441-444
    • Serber, Z.1    Ferrell Jr., J.E.2
  • 55
    • 0036892971 scopus 로고    scopus 로고
    • Intron positions delineate the evolutionary path of a pervasively appended peptide in five human aminoacyl-tRNA synthetases
    • Shiba K. Intron positions delineate the evolutionary path of a pervasively appended peptide in five human aminoacyl-tRNA synthetases. J. Mol. Evol. 55 (2002) 727-733
    • (2002) J. Mol. Evol. , vol.55 , pp. 727-733
    • Shiba, K.1
  • 56
    • 0343177223 scopus 로고    scopus 로고
    • A structural basis for substrate specificities of protein Ser/Thr kinases: Primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1
    • Songyang Z., Lu K.P., Kwon Y.T., Tsai L.H., Filhol O., Cochet C., Brickey D.A., Soderling T.R., Bartleson C., Graves D.J., et al. A structural basis for substrate specificities of protein Ser/Thr kinases: Primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1. Mol. Cell. Biol. 16 (1996) 6486-6493
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6486-6493
    • Songyang, Z.1    Lu, K.P.2    Kwon, Y.T.3    Tsai, L.H.4    Filhol, O.5    Cochet, C.6    Brickey, D.A.7    Soderling, T.R.8    Bartleson, C.9    Graves, D.J.10
  • 58
    • 30944463204 scopus 로고    scopus 로고
    • Inhibition of tumor angiogenesis by a natural fragment of a tRNA synthetase
    • Tzima E., and Schimmel P. Inhibition of tumor angiogenesis by a natural fragment of a tRNA synthetase. Trends Biochem. Sci. 31 (2006) 7-10
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 7-10
    • Tzima, E.1    Schimmel, P.2
  • 59
    • 0025754306 scopus 로고
    • Protein kinase C phosphorylates glutamyl-tRNA synthetase in rabbit reticulocytes stimulated by tumor promoting phorbol esters
    • Venema R.C., and Traugh J.A. Protein kinase C phosphorylates glutamyl-tRNA synthetase in rabbit reticulocytes stimulated by tumor promoting phorbol esters. J. Biol. Chem. 266 (1991) 5298-5302
    • (1991) J. Biol. Chem. , vol.266 , pp. 5298-5302
    • Venema, R.C.1    Traugh, J.A.2
  • 60
    • 58249110558 scopus 로고    scopus 로고
    • Genome-wide polysome profiling reveals an inflammation-responsive post-transcriptional operon in IFN-γ-activated monocytes
    • Vyas K., Chaudhuri S., Leaman D.W., Komar A.A., Musiyenko A., Barik S., and Mazumder B. Genome-wide polysome profiling reveals an inflammation-responsive post-transcriptional operon in IFN-γ-activated monocytes. Mol. Cell. Biol. 29 (2009) 458-470
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 458-470
    • Vyas, K.1    Chaudhuri, S.2    Leaman, D.W.3    Komar, A.A.4    Musiyenko, A.5    Barik, S.6    Mazumder, B.7
  • 61
    • 33644668804 scopus 로고    scopus 로고
    • A three-dimensional working model of the multienzyme complex of aminoacyl-tRNA synthetases based on electron microscopic placements of tRNA and proteins
    • Wolfe C.L., Warrington J.A., Treadwell L., and Norcum M.T. A three-dimensional working model of the multienzyme complex of aminoacyl-tRNA synthetases based on electron microscopic placements of tRNA and proteins. J. Biol. Chem. 280 (2005) 38870-38878
    • (2005) J. Biol. Chem. , vol.280 , pp. 38870-38878
    • Wolfe, C.L.1    Warrington, J.A.2    Treadwell, L.3    Norcum, M.T.4
  • 62
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright P.E., and Dyson H.J. Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm. J. Mol. Biol. 293 (1999) 321-331
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.