메뉴 건너뛰기




Volumn 86, Issue 2, 2005, Pages 159-171

Coordinate stabilization of growth-regulatory transcripts in T cell malignancies

Author keywords

Cutaneous T cell lymphoma; Gene expression; Malignancy; Microarray; mRNA decay; mRNA stability; T cell; T cell leukemia; T lymphocyte

Indexed keywords

ARTICLE; CANCER GROWTH; CELL GROWTH; CONTROLLED STUDY; GENE CONTROL; GENE EXPRESSION; GENE OVEREXPRESSION; GENETIC CODE; GENETIC TRANSCRIPTION; HUMAN; HUMAN CELL; PHENOTYPE; PRIORITY JOURNAL; T CELL LEUKEMIA; T CELL LYMPHOMA; T LYMPHOCYTE; UPREGULATION;

EID: 21544481148     PISSN: 08887543     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ygeno.2005.04.013     Document Type: Article
Times cited : (23)

References (58)
  • 1
    • 4644288309 scopus 로고    scopus 로고
    • Microarray-based analyses of mRNA decay in the regulation of mammalian gene expression
    • A. Raghavan, and P.R. Bohjanen Microarray-based analyses of mRNA decay in the regulation of mammalian gene expression Brief Funct. Genom. Proteom. 3 2004 112 124
    • (2004) Brief Funct. Genom. Proteom. , vol.3 , pp. 112-124
    • Raghavan, A.1    Bohjanen, P.R.2
  • 3
    • 0025300577 scopus 로고
    • A 3′ truncation of MYC caused by chromosomal translocation in a human T-cell leukemia increases mRNA stability
    • D.F. Aghib A 3′ truncation of MYC caused by chromosomal translocation in a human T-cell leukemia increases mRNA stability Oncogene 5 1990 707 711
    • (1990) Oncogene , vol.5 , pp. 707-711
    • Aghib, D.F.1
  • 4
    • 0344148793 scopus 로고
    • Removal of a 67-base-pair sequence in the noncoding region of protooncogene fos converts it to a transforming gene
    • F. Meijlink, T. Curran, A.D. Miller, and I.M. Verma Removal of a 67-base-pair sequence in the noncoding region of protooncogene fos converts it to a transforming gene Proc. Natl. Acad. Sci. U. S. A. 82 1985 4987 4991
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 4987-4991
    • Meijlink, F.1    Curran, T.2    Miller, A.D.3    Verma, I.M.4
  • 5
    • 0024364648 scopus 로고
    • Removal of an mRNA destabilizing element correlates with the increased oncogenicity of proto-oncogene fos
    • V. Raymond, J.A. Atwater, and I.M. Verma Removal of an mRNA destabilizing element correlates with the increased oncogenicity of proto-oncogene fos Oncogene Res. 5 1989 1 12
    • (1989) Oncogene Res. , vol.5 , pp. 1-12
    • Raymond, V.1    Atwater, J.A.2    Verma, I.M.3
  • 6
    • 2642530367 scopus 로고    scopus 로고
    • Impact of microarray technology in clinical oncology
    • E.A. Raetz, and P.J. Moos Impact of microarray technology in clinical oncology Cancer Invest. 22 2004 312 320
    • (2004) Cancer Invest. , vol.22 , pp. 312-320
    • Raetz, E.A.1    Moos, P.J.2
  • 7
    • 0036324634 scopus 로고    scopus 로고
    • Quantitative assessment of filter-based cDNA microarrays: Gene expression profiles of human T-lymphoma cell lines
    • J.M. Dodson, P.T. Charles, D.A. Stenger, and J.J. Pancrazio Quantitative assessment of filter-based cDNA microarrays: gene expression profiles of human T-lymphoma cell lines Bioinformatics 18 2002 953 960
    • (2002) Bioinformatics , vol.18 , pp. 953-960
    • Dodson, J.M.1    Charles, P.T.2    Stenger, D.A.3    Pancrazio, J.J.4
  • 8
    • 0038798678 scopus 로고    scopus 로고
    • Macroarray analysis of the effects of JP-8 jet fuel on gene expression in Jurkat cells
    • L.A. Espinoza, and M.E. Smulson Macroarray analysis of the effects of JP-8 jet fuel on gene expression in Jurkat cells Toxicology 189 2003 181 190
    • (2003) Toxicology , vol.189 , pp. 181-190
    • Espinoza, L.A.1    Smulson, M.E.2
  • 9
    • 0034041299 scopus 로고    scopus 로고
    • Genomic views of the immune system
    • L.M. Staudt, and P.O. Brown Genomic views of the immune system Annu. Rev. Immunol. 18 2000 829 859
    • (2000) Annu. Rev. Immunol. , vol.18 , pp. 829-859
    • Staudt, L.M.1    Brown, P.O.2
  • 10
    • 0037223402 scopus 로고    scopus 로고
    • P38 mitogen-activated protein kinase-dependent and -independent signaling of mRNA stability of AU-rich element-containing transcripts
    • M.A. Frevel p38 mitogen-activated protein kinase-dependent and -independent signaling of mRNA stability of AU-rich element-containing transcripts Mol. Cell. Biol. 23 2003 425 436
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 425-436
    • Frevel, M.A.1
  • 11
    • 0035233239 scopus 로고    scopus 로고
    • Genomic-scale measurement of mRNA turnover and the mechanisms of action of the anti-cancer drug flavopiridol
    • L.T. Lam Genomic-scale measurement of mRNA turnover and the mechanisms of action of the anti-cancer drug flavopiridol Genome Biol. 2 2001 (RESEARCH0041)
    • (2001) Genome Biol. , vol.2
    • Lam, L.T.1
  • 12
    • 0037115826 scopus 로고    scopus 로고
    • Genome-wide analysis of mRNA decay in resting and activated primary human T lymphocytes
    • A. Raghavan Genome-wide analysis of mRNA decay in resting and activated primary human T lymphocytes Nucleic Acids Res. 30 2002 5529 5538
    • (2002) Nucleic Acids Res. , vol.30 , pp. 5529-5538
    • Raghavan, A.1
  • 13
    • 0038362750 scopus 로고    scopus 로고
    • Heterogeneity in control of mRNA stability by AU-rich elements
    • J.M. Tebo Heterogeneity in control of mRNA stability by AU-rich elements J. Biol. Chem. 278 2003 12085 12093
    • (2003) J. Biol. Chem. , vol.278 , pp. 12085-12093
    • Tebo, J.M.1
  • 14
    • 0041523923 scopus 로고    scopus 로고
    • Decay rates of human mRNAs: Correlation with functional characteristics and sequence attributes
    • E. Yang Decay rates of human mRNAs: correlation with functional characteristics and sequence attributes Genome Res. 13 2003 1863 1872
    • (2003) Genome Res. , vol.13 , pp. 1863-1872
    • Yang, E.1
  • 15
    • 0037252788 scopus 로고    scopus 로고
    • ARED 2.0: An update of AU-rich element mRNA database
    • T. Bakheet, B.R. Williams, and K.S. Khabar ARED 2.0: an update of AU-rich element mRNA database Nucleic Acids Res. 31 2003 421 423
    • (2003) Nucleic Acids Res. , vol.31 , pp. 421-423
    • Bakheet, T.1    Williams, B.R.2    Khabar, K.S.3
  • 16
    • 7944225681 scopus 로고    scopus 로고
    • Patterns of coordinate down-regulation of ARE-containing transcripts following immune cell activation
    • A. Raghavan Patterns of coordinate down-regulation of ARE-containing transcripts following immune cell activation Genomics 84 2004 1002 1013
    • (2004) Genomics , vol.84 , pp. 1002-1013
    • Raghavan, A.1
  • 17
    • 0024327899 scopus 로고
    • Clonal expansion versus functional clonal inactivation: A costimulatory signalling pathway determines the outcome of T cell antigen receptor occupancy
    • D.L. Mueller, M.K. Jenkins, and R.H. Schwartz Clonal expansion versus functional clonal inactivation: a costimulatory signalling pathway determines the outcome of T cell antigen receptor occupancy Annu. Rev. Immunol. 7 1989 445 480
    • (1989) Annu. Rev. Immunol. , vol.7 , pp. 445-480
    • Mueller, D.L.1    Jenkins, M.K.2    Schwartz, R.H.3
  • 18
    • 0024506159 scopus 로고
    • Regulation of lymphokine messenger RNA stability by a surface-mediated T cell activation pathway
    • T. Lindsten, C.H. June, J.A. Ledbetter, G. Stella, and C.B. Thompson Regulation of lymphokine messenger RNA stability by a surface-mediated T cell activation pathway Science 244 1989 339 343
    • (1989) Science , vol.244 , pp. 339-343
    • Lindsten, T.1    June, C.H.2    Ledbetter, J.A.3    Stella, G.4    Thompson, C.B.5
  • 19
    • 0037335034 scopus 로고    scopus 로고
    • How the ubiquitin-proteasome system controls transcription
    • M. Muratani, and W.P. Tansey How the ubiquitin-proteasome system controls transcription Nat. Rev. Mol. Cell Biol. 4 2003 192 201
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 192-201
    • Muratani, M.1    Tansey, W.P.2
  • 21
    • 0027992730 scopus 로고
    • Repair of spontaneously deamidated HPr phosphocarrier protein catalyzed by the l-isoaspartate-(d-aspartate) O-methyltransferase
    • T.V. Brennan, J.W. Anderson, Z. Jia, E.B. Waygood, and S. Clarke Repair of spontaneously deamidated HPr phosphocarrier protein catalyzed by the l-isoaspartate-(d-aspartate) O-methyltransferase J. Biol. Chem. 269 1994 24586 24595
    • (1994) J. Biol. Chem. , vol.269 , pp. 24586-24595
    • Brennan, T.V.1    Anderson, J.W.2    Jia, Z.3    Waygood, E.B.4    Clarke, S.5
  • 22
    • 0029620843 scopus 로고
    • Human ClpP protease: CDNA sequence, tissue-specific expression and chromosomal assignment of the gene
    • P. Bross, B.S. Andresen, I. Knudsen, T.A. Kruse, and N. Gregersen Human ClpP protease: cDNA sequence, tissue-specific expression and chromosomal assignment of the gene FEBS Lett. 377 1995 249 252
    • (1995) FEBS Lett. , vol.377 , pp. 249-252
    • Bross, P.1    Andresen, B.S.2    Knudsen, I.3    Kruse, T.A.4    Gregersen, N.5
  • 23
    • 5144220294 scopus 로고    scopus 로고
    • Influence of casein kinase II in tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis in human rhabdomyosarcoma cells
    • K. Izeradjene, L. Douglas, A. Delaney, and J.A. Houghton Influence of casein kinase II in tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis in human rhabdomyosarcoma cells Clin. Cancer Res. 10 2004 6650 6660
    • (2004) Clin. Cancer Res. , vol.10 , pp. 6650-6660
    • Izeradjene, K.1    Douglas, L.2    Delaney, A.3    Houghton, J.A.4
  • 24
    • 0035825193 scopus 로고    scopus 로고
    • Differential localization of Rho GTPases in live cells: Regulation by hypervariable regions and RhoGDI binding
    • D. Michaelson Differential localization of Rho GTPases in live cells: regulation by hypervariable regions and RhoGDI binding J. Cell Biol. 152 2001 111 126
    • (2001) J. Cell Biol. , vol.152 , pp. 111-126
    • Michaelson, D.1
  • 25
    • 0034235101 scopus 로고    scopus 로고
    • Isolation and preliminary characterization of the human and mouse homologues of the bacterial cell cycle gene era
    • R.A. Britton Isolation and preliminary characterization of the human and mouse homologues of the bacterial cell cycle gene era Genomics 67 2000 78 82
    • (2000) Genomics , vol.67 , pp. 78-82
    • Britton, R.A.1
  • 26
    • 0034663532 scopus 로고    scopus 로고
    • In vitro expansion of mammalian telomere repeats by DNA polymerase alpha-primase
    • K. Nozawa, M. Suzuki, M. Takemura, and S. Yoshida In vitro expansion of mammalian telomere repeats by DNA polymerase alpha-primase Nucleic Acids Res. 28 2000 3117 3124
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3117-3124
    • Nozawa, K.1    Suzuki, M.2    Takemura, M.3    Yoshida, S.4
  • 27
    • 0034682833 scopus 로고    scopus 로고
    • Expression of human topoisomerase I with a partial deletion of the linker region yields monomeric and dimeric enzymes that respond differently to camptothecin
    • G.C. Ireton, L. Stewart, L.H. Parker, and J.J. Champoux Expression of human topoisomerase I with a partial deletion of the linker region yields monomeric and dimeric enzymes that respond differently to camptothecin J. Biol. Chem. 275 2000 25820 25830
    • (2000) J. Biol. Chem. , vol.275 , pp. 25820-25830
    • Ireton, G.C.1    Stewart, L.2    Parker, L.H.3    Champoux, J.J.4
  • 28
    • 1842578717 scopus 로고    scopus 로고
    • Dynamic interaction between BAF and emerin revealed by FRAP, FLIP, and FRET analyses in living HeLa cells
    • T. Shimi Dynamic interaction between BAF and emerin revealed by FRAP, FLIP, and FRET analyses in living HeLa cells J. Struct. Biol. 147 2004 31 41
    • (2004) J. Struct. Biol. , vol.147 , pp. 31-41
    • Shimi, T.1
  • 29
    • 0034730502 scopus 로고    scopus 로고
    • Characterization of the histone H1-binding protein, NASP, as a cell cycle-regulated somatic protein
    • R.T. Richardson Characterization of the histone H1-binding protein, NASP, as a cell cycle-regulated somatic protein J. Biol. Chem. 275 2000 30378 30386
    • (2000) J. Biol. Chem. , vol.275 , pp. 30378-30386
    • Richardson, R.T.1
  • 30
    • 0038387444 scopus 로고    scopus 로고
    • Re-evaluating the role of heat-shock protein-peptide interactions in tumour immunity
    • C.V. Nicchitta Re-evaluating the role of heat-shock protein-peptide interactions in tumour immunity Nat. Rev. Immunol. 3 2003 427 432
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 427-432
    • Nicchitta, C.V.1
  • 31
    • 0242667828 scopus 로고    scopus 로고
    • Analysing differential gene expression in cancer
    • P. Liang, and A.B. Pardee Analysing differential gene expression in cancer Nat. Rev. Cancer 3 2003 869 876
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 869-876
    • Liang, P.1    Pardee, A.B.2
  • 32
    • 0042991383 scopus 로고    scopus 로고
    • H2AX haploinsufficiency modifies genomic stability and tumor susceptibility
    • A. Celeste H2AX haploinsufficiency modifies genomic stability and tumor susceptibility Cell 114 2003 371 383
    • (2003) Cell , vol.114 , pp. 371-383
    • Celeste, A.1
  • 33
    • 0038771139 scopus 로고    scopus 로고
    • Structure and specificity of the vertebrate anti-mutator uracil-DNA glycosylase SMUG1
    • J.E. Wibley, T.R. Waters, K. Haushalter, G.L. Verdine, and L.H. Pearl Structure and specificity of the vertebrate anti-mutator uracil-DNA glycosylase SMUG1 Mol. Cell 11 2003 1647 1659
    • (2003) Mol. Cell , vol.11 , pp. 1647-1659
    • Wibley, J.E.1    Waters, T.R.2    Haushalter, K.3    Verdine, G.L.4    Pearl, L.H.5
  • 34
  • 36
    • 0032516626 scopus 로고    scopus 로고
    • Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin
    • E. Carballo, W.S. Lai, and P.J. Blackshear Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin Science 281 1998 1001 1005
    • (1998) Science , vol.281 , pp. 1001-1005
    • Carballo, E.1    Lai, W.S.2    Blackshear, P.J.3
  • 37
    • 18044371822 scopus 로고    scopus 로고
    • AU binding proteins recruit the exosome to degrade ARE-containing mRNAs
    • C.Y. Chen AU binding proteins recruit the exosome to degrade ARE-containing mRNAs Cell 107 2001 451 464
    • (2001) Cell , vol.107 , pp. 451-464
    • Chen, C.Y.1
  • 38
    • 0025819310 scopus 로고
    • An inducible cytoplasmic factor (AU-B) binds selectively to AUUUA multimers in the 3′ untranslated region of lymphokine mRNA
    • P.R. Bohjanen, B. Petryniak, C.H. June, C.B. Thompson, and T. Lindsten An inducible cytoplasmic factor (AU-B) binds selectively to AUUUA multimers in the 3′ untranslated region of lymphokine mRNA Mol. Cell. Biol. 11 1991 3288 3295
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3288-3295
    • Bohjanen, P.R.1    Petryniak, B.2    June, C.H.3    Thompson, C.B.4    Lindsten, T.5
  • 40
    • 0032526427 scopus 로고    scopus 로고
    • Overexpression of HuR, a nuclear-cytoplasmic shuttling protein, increases the in vivo stability of ARE-containing mRNAs
    • X.C. Fan, and J.A. Steitz Overexpression of HuR, a nuclear-cytoplasmic shuttling protein, increases the in vivo stability of ARE-containing mRNAs EMBO J. 17 1998 3448 3460
    • (1998) EMBO J. , vol.17 , pp. 3448-3460
    • Fan, X.C.1    Steitz, J.A.2
  • 41
    • 0033555659 scopus 로고    scopus 로고
    • ELAV proteins stabilize deadenylated intermediates in a novel in vitro mRNA deadenylation/degradation system
    • L.P. Ford, J. Watson, J.D. Keene, and J. Wilusz ELAV proteins stabilize deadenylated intermediates in a novel in vitro mRNA deadenylation/degradation system Genes Dev. 13 1999 188 201
    • (1999) Genes Dev. , vol.13 , pp. 188-201
    • Ford, L.P.1    Watson, J.2    Keene, J.D.3    Wilusz, J.4
  • 42
    • 0035930565 scopus 로고    scopus 로고
    • HuA and tristetraprolin are induced following T cell activation and display distinct but overlapping RNA binding specificities
    • A. Raghavan HuA and tristetraprolin are induced following T cell activation and display distinct but overlapping RNA binding specificities J. Biol. Chem. 276 2001 47958 47965
    • (2001) J. Biol. Chem. , vol.276 , pp. 47958-47965
    • Raghavan, A.1
  • 43
    • 0036924040 scopus 로고    scopus 로고
    • Nuclear export of NF90 is required for interleukin-2 mRNA stabilization
    • J. Shim, H. Lim, R.Y. J, and M. Karin Nuclear export of NF90 is required for interleukin-2 mRNA stabilization Mol. Cell 10 2002 1331 1344
    • (2002) Mol. Cell , vol.10 , pp. 1331-1344
    • Shim, J.1    Lim, H.2    Yates III, J.R.3    Karin, M.4
  • 44
    • 0034806974 scopus 로고    scopus 로고
    • Versatile role for hnRNP D isoforms in the differential regulation of cytoplasmic mRNA turnover
    • N. Xu, C.Y. Chen, and A.B. Shyu Versatile role for hnRNP D isoforms in the differential regulation of cytoplasmic mRNA turnover Mol. Cell. Biol. 21 2001 6960 6971
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6960-6971
    • Xu, N.1    Chen, C.Y.2    Shyu, A.B.3
  • 45
    • 0036289532 scopus 로고    scopus 로고
    • Eukaryotic mRNPs may represent posttranscriptional operons
    • J.D. Keene, and S.A. Tenenbaum Eukaryotic mRNPs may represent posttranscriptional operons Mol. Cell 9 2002 1161 1167
    • (2002) Mol. Cell , vol.9 , pp. 1161-1167
    • Keene, J.D.1    Tenenbaum, S.A.2
  • 46
    • 0027480969 scopus 로고
    • Serum concentration and localization in tumor cells of proteasomes in patients with hematologic malignancy and their pathophysiologic significance
    • M. Wada Serum concentration and localization in tumor cells of proteasomes in patients with hematologic malignancy and their pathophysiologic significance J. Lab. Clin. Med. 121 1993 215 223
    • (1993) J. Lab. Clin. Med. , vol.121 , pp. 215-223
    • Wada, M.1
  • 47
    • 0035889941 scopus 로고    scopus 로고
    • Plasma proteasome level is a potential marker in patients with solid tumors and hemopoietic malignancies
    • T. Lavabre-Bertrand Plasma proteasome level is a potential marker in patients with solid tumors and hemopoietic malignancies Cancer 92 2001 2493 2500
    • (2001) Cancer , vol.92 , pp. 2493-2500
    • Lavabre-Bertrand, T.1
  • 48
    • 0034640110 scopus 로고    scopus 로고
    • A proteasome howdunit: The case of the missing signal
    • R. Verma, and R.J. Deshaies A proteasome howdunit: the case of the missing signal Cell 101 2000 341 344
    • (2000) Cell , vol.101 , pp. 341-344
    • Verma, R.1    Deshaies, R.J.2
  • 49
    • 0028276554 scopus 로고
    • Degradation of the tumor suppressor protein p53 by the ubiquitin-mediated proteolytic system requires a novel species of ubiquitin-carrier protein, E2
    • A. Ciechanover, D. Shkedy, M. Oren, and B. Bercovich Degradation of the tumor suppressor protein p53 by the ubiquitin-mediated proteolytic system requires a novel species of ubiquitin-carrier protein, E2 J. Biol. Chem. 269 1994 9582 9589
    • (1994) J. Biol. Chem. , vol.269 , pp. 9582-9589
    • Ciechanover, A.1    Shkedy, D.2    Oren, M.3    Bercovich, B.4
  • 50
    • 0028342731 scopus 로고
    • Complete reconstitution of conjugation and subsequent degradation of the tumor suppressor protein p53 by purified components of the ubiquitin proteolytic system
    • D. Shkedy, H. Gonen, B. Bercovich, and A. Ciechanover Complete reconstitution of conjugation and subsequent degradation of the tumor suppressor protein p53 by purified components of the ubiquitin proteolytic system FEBS Lett. 348 1994 126 130
    • (1994) FEBS Lett. , vol.348 , pp. 126-130
    • Shkedy, D.1    Gonen, H.2    Bercovich, B.3    Ciechanover, A.4
  • 51
    • 4344563161 scopus 로고    scopus 로고
    • Topors functions as an E3 ubiquitin ligase with specific E2 enzymes and ubiquitinates p53
    • R. Rajendra Topors functions as an E3 ubiquitin ligase with specific E2 enzymes and ubiquitinates p53 J. Biol. Chem. 279 2004 36440 36444
    • (2004) J. Biol. Chem. , vol.279 , pp. 36440-36444
    • Rajendra, R.1
  • 53
    • 7444248437 scopus 로고    scopus 로고
    • Bortezomib rapidly suppresses ubiquitin thiolesterification to ubiquitin-conjugating enzymes and inhibits ubiquitination of histones and type I inositol 1,4,5-trisphosphate receptor
    • Q. Xu, M. Farah, J.M. Webster, and R.J. Wojcikiewicz Bortezomib rapidly suppresses ubiquitin thiolesterification to ubiquitin-conjugating enzymes and inhibits ubiquitination of histones and type I inositol 1,4,5-trisphosphate receptor Mol. Cancer Ther. 3 2004 1263 1269
    • (2004) Mol. Cancer Ther. , vol.3 , pp. 1263-1269
    • Xu, Q.1    Farah, M.2    Webster, J.M.3    Wojcikiewicz, R.J.4
  • 54
    • 1842861723 scopus 로고    scopus 로고
    • The hierarchical relationship between MAPK signaling and ROS generation in human leukemia cells undergoing apoptosis in response to the proteasome inhibitor Bortezomib
    • C. Yu, M. Rahmani, P. Dent, and S. Grant The hierarchical relationship between MAPK signaling and ROS generation in human leukemia cells undergoing apoptosis in response to the proteasome inhibitor Bortezomib Exp. Cell Res. 295 2004 555 566
    • (2004) Exp. Cell Res. , vol.295 , pp. 555-566
    • Yu, C.1    Rahmani, M.2    Dent, P.3    Grant, S.4
  • 55
    • 1842581892 scopus 로고    scopus 로고
    • Regulation of T lymphocyte metabolism
    • K.A. Frauwirth, and C.B. Thompson Regulation of T lymphocyte metabolism J. Immunol. 172 2004 4661 4665
    • (2004) J. Immunol. , vol.172 , pp. 4661-4665
    • Frauwirth, K.A.1    Thompson, C.B.2
  • 56
    • 0033055772 scopus 로고    scopus 로고
    • The cis acting sequences responsible for the differential decay of the unstable MFA2 and stable PGK1 transcripts in yeast include the context of the translational start codon
    • T. LaGrandeur, and R. Parker The cis acting sequences responsible for the differential decay of the unstable MFA2 and stable PGK1 transcripts in yeast include the context of the translational start codon RNA 5 1999 420 433
    • (1999) RNA , vol.5 , pp. 420-433
    • Lagrandeur, T.1    Parker, R.2
  • 57
    • 4644284749 scopus 로고    scopus 로고
    • Recruitment of the Puf3 protein to its mRNA target for regulation of mRNA decay in yeast
    • J.S. Jackson Jr., S.S. Houshmandi, F. Lopez Leban, and W.M. Olivas Recruitment of the Puf3 protein to its mRNA target for regulation of mRNA decay in yeast RNA 10 2004 1625 1636
    • (2004) RNA , vol.10 , pp. 1625-1636
    • Jackson Jr., J.S.1    Houshmandi, S.S.2    Lopez Leban, F.3    Olivas, W.M.4
  • 58
    • 0035930565 scopus 로고    scopus 로고
    • HuA and tristetraprolin are induced following T cell activation and display distinct but overlapping RNA binding specificities
    • A. Raghavan HuA and tristetraprolin are induced following T cell activation and display distinct but overlapping RNA binding specificities J. Biol. Chem. 276 2001 47958 47965
    • (2001) J. Biol. Chem. , vol.276 , pp. 47958-47965
    • Raghavan, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.