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Volumn 4, Issue 4, 2013, Pages 387-396

Metabolite sensing in eukaryotic mRNA biology

Author keywords

[No Author keywords available]

Indexed keywords

ACONITATE HYDRATASE; ADENOSINE DEAMINASE; DOUBLE STRANDED RNA; FUNGAL PROTEIN; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; MESSENGER RNA; PHYTIC ACID; RNA BINDING PROTEIN; THIA PROTEIN; UNCLASSIFIED DRUG;

EID: 84879149824     PISSN: 17577004     EISSN: 17577012     Source Type: Journal    
DOI: 10.1002/wrna.1167     Document Type: Article
Times cited : (10)

References (80)
  • 2
    • 0028225462 scopus 로고
    • SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis
    • Wang X, Sato R, Brown MS, Hua X, Goldstein JL. SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis. Cell 1994, 77:53-62.
    • (1994) Cell , vol.77 , pp. 53-62
    • Wang, X.1    Sato, R.2    Brown, M.S.3    Hua, X.4    Goldstein, J.L.5
  • 3
    • 0036183630 scopus 로고    scopus 로고
    • The mechanisms of action of PPARs
    • Berger J, Moller DE. The mechanisms of action of PPARs. Annu Rev Med 2002, 53:409-435.
    • (2002) Annu Rev Med , vol.53 , pp. 409-435
    • Berger, J.1    Moller, D.E.2
  • 4
    • 80054976920 scopus 로고    scopus 로고
    • Molecular basis underlying LuxR family transcription factors and function diversity and implications for novel antibiotic drug targets
    • Zeng L-R, Xie J-P. Molecular basis underlying LuxR family transcription factors and function diversity and implications for novel antibiotic drug targets. J Cell Biochem 2011, 112:3079-3084.
    • (2011) J Cell Biochem , vol.112 , pp. 3079-3084
    • Zeng, L.-R.1    Xie, J.-P.2
  • 6
    • 38349148383 scopus 로고    scopus 로고
    • Inositol polyphosphates: a new frontier for regulating gene expression
    • Alcázar-Román AR, Wente SR. Inositol polyphosphates: a new frontier for regulating gene expression. Chromosoma 2007, 117:1-13.
    • (2007) Chromosoma , vol.117 , pp. 1-13
    • Alcázar-Román, A.R.1    Wente, S.R.2
  • 8
    • 27144527479 scopus 로고    scopus 로고
    • Regulation of bacterial gene expression by riboswitches
    • Winkler WC, Breaker RR. Regulation of bacterial gene expression by riboswitches. Annu Rev Microbiol 2005, 59:487-517.
    • (2005) Annu Rev Microbiol , vol.59 , pp. 487-517
    • Winkler, W.C.1    Breaker, R.R.2
  • 9
    • 67650713931 scopus 로고    scopus 로고
    • The structural and functional diversity of metabolite-binding riboswitches
    • Roth A, Breaker RR. The structural and functional diversity of metabolite-binding riboswitches. Annu Rev Biochem 2009, 78:305-334.
    • (2009) Annu Rev Biochem , vol.78 , pp. 305-334
    • Roth, A.1    Breaker, R.R.2
  • 11
    • 0346366823 scopus 로고    scopus 로고
    • Thiamine-regulated gene expression of Aspergillus oryzae thiA requires splicing of the intron containing a riboswitch-like domain in the 5′-UTR
    • Kubodera T, Watanabe M, Yoshiuchi K, Yamashita N, Nishimura A, Nakai S, Gomi K, Hanamoto H. Thiamine-regulated gene expression of Aspergillus oryzae thiA requires splicing of the intron containing a riboswitch-like domain in the 5′-UTR. FEBS Lett 2003, 555:516-520.
    • (2003) FEBS Lett , vol.555 , pp. 516-520
    • Kubodera, T.1    Watanabe, M.2    Yoshiuchi, K.3    Yamashita, N.4    Nishimura, A.5    Nakai, S.6    Gomi, K.7    Hanamoto, H.8
  • 12
    • 34249278470 scopus 로고    scopus 로고
    • Control of alternative RNA splicing and gene expression by eukaryotic riboswitches
    • Cheah MT, Wachter A, Sudarsan N, Breaker RR. Control of alternative RNA splicing and gene expression by eukaryotic riboswitches. Nature 2007, 447:497-500.
    • (2007) Nature , vol.447 , pp. 497-500
    • Cheah, M.T.1    Wachter, A.2    Sudarsan, N.3    Breaker, R.R.4
  • 13
    • 38049169167 scopus 로고    scopus 로고
    • Thiamine biosynthesis in algae is regulated by riboswitches
    • Croft MT, Moulin M, Webb ME, Smith AG. Thiamine biosynthesis in algae is regulated by riboswitches. Proc Natl Acad Sci 2007, 104:20770-20775.
    • (2007) Proc Natl Acad Sci , vol.104 , pp. 20770-20775
    • Croft, M.T.1    Moulin, M.2    Webb, M.E.3    Smith, A.G.4
  • 14
    • 53149095767 scopus 로고    scopus 로고
    • Switching the light on plant riboswitches
    • Bocobza SE, Aharoni A. Switching the light on plant riboswitches. Trends Plant Sci 2008, 13:526-533.
    • (2008) Trends Plant Sci , vol.13 , pp. 526-533
    • Bocobza, S.E.1    Aharoni, A.2
  • 15
    • 0038136962 scopus 로고    scopus 로고
    • Metabolite-binding RNA domains are present in the genes of eukaryotes
    • Sudarsan N, Barrick JE, Breaker RR. Metabolite-binding RNA domains are present in the genes of eukaryotes. RNA 2003, 9:644-647.
    • (2003) RNA , vol.9 , pp. 644-647
    • Sudarsan, N.1    Barrick, J.E.2    Breaker, R.R.3
  • 16
    • 46049091176 scopus 로고    scopus 로고
    • Structural basis of thiamine pyrophosphate analogues binding to the eukaryotic riboswitch
    • Thore S, Frick C, Ban N. Structural basis of thiamine pyrophosphate analogues binding to the eukaryotic riboswitch. J Am Chem Soc 2008, 130:8116-8117.
    • (2008) J Am Chem Soc , vol.130 , pp. 8116-8117
    • Thore, S.1    Frick, C.2    Ban, N.3
  • 17
    • 33744469562 scopus 로고    scopus 로고
    • Structure of the eukaryotic thiamine pyrophosphate riboswitch with its regulatory ligand
    • Thore S, Leibundgut M, Ban N. Structure of the eukaryotic thiamine pyrophosphate riboswitch with its regulatory ligand. Science 2006, 312:1208-1211.
    • (2006) Science , vol.312 , pp. 1208-1211
    • Thore, S.1    Leibundgut, M.2    Ban, N.3
  • 18
    • 0042834096 scopus 로고    scopus 로고
    • Regulation of the vitamin B12 metabolism and transport in bacteria by a conserved RNA structural element
    • Vitreschak AG, Rodionov DA, Mironov AA, Gelfand MS. Regulation of the vitamin B12 metabolism and transport in bacteria by a conserved RNA structural element. RNA 2003, 9:1084-1097.
    • (2003) RNA , vol.9 , pp. 1084-1097
    • Vitreschak, A.G.1    Rodionov, D.A.2    Mironov, A.A.3    Gelfand, M.S.4
  • 22
    • 41649108068 scopus 로고    scopus 로고
    • Confirmation of a second natural preQ1 aptamer class in Streptococcaceae bacteria
    • Meyer MM, Roth A, Chervin SM, Garcia GA, Breaker RR. Confirmation of a second natural preQ1 aptamer class in Streptococcaceae bacteria. RNA 2008, 14:685-695.
    • (2008) RNA , vol.14 , pp. 685-695
    • Meyer, M.M.1    Roth, A.2    Chervin, S.M.3    Garcia, G.A.4    Breaker, R.R.5
  • 23
    • 23144463910 scopus 로고    scopus 로고
    • RibEx: a web server for locating riboswitches and other conserved bacterial regulatory elements
    • Abreu-Goodger C, Merino E. RibEx: a web server for locating riboswitches and other conserved bacterial regulatory elements. Nucleic Acids Res 2005, 33:W690-W692.
    • (2005) Nucleic Acids Res , vol.33
    • Abreu-Goodger, C.1    Merino, E.2
  • 25
    • 80053523254 scopus 로고    scopus 로고
    • The evolution of RNAs with multiple functions
    • Dinger ME, Gascoigne DK, Mattick JS. The evolution of RNAs with multiple functions. Biochimie 2011, 93:2013-2018.
    • (2011) Biochimie , vol.93 , pp. 2013-2018
    • Dinger, M.E.1    Gascoigne, D.K.2    Mattick, J.S.3
  • 26
    • 71449114713 scopus 로고    scopus 로고
    • Exceptional structured noncoding RNAs revealed by bacterial metagenome analysis
    • Weinberg Z, Perreault J, Meyer MM, Breaker RR. Exceptional structured noncoding RNAs revealed by bacterial metagenome analysis. Nature 2009, 462:656-659.
    • (2009) Nature , vol.462 , pp. 656-659
    • Weinberg, Z.1    Perreault, J.2    Meyer, M.M.3    Breaker, R.R.4
  • 27
    • 79958251726 scopus 로고    scopus 로고
    • Identification of CRISPR and riboswitch related RNAs among novel noncoding RNAs of the euryarchaeon Pyrococcus abyssi
    • Phok K, Moisan A, Rinaldi D, Brucato N, Carpousis AJ, Gaspin C, Clouet-d'Orval B. Identification of CRISPR and riboswitch related RNAs among novel noncoding RNAs of the euryarchaeon Pyrococcus abyssi. BMC Genomics 2011, 12:312.
    • (2011) BMC Genomics , vol.12 , pp. 312
    • Phok, K.1    Moisan, A.2    Rinaldi, D.3    Brucato, N.4    Carpousis, A.J.5    Gaspin, C.6    Clouet-d'Orval, B.7
  • 28
    • 81855205059 scopus 로고    scopus 로고
    • ADAR proteins: double-stranded RNA and Z-DNA binding domains
    • Barraud P, Allain FH-T. ADAR proteins: double-stranded RNA and Z-DNA binding domains. Curr Top Microbiol Immunol 2012, 353:35-60.
    • (2012) Curr Top Microbiol Immunol , vol.353 , pp. 35-60
    • Barraud, P.1    Allain, F.-T.2
  • 29
    • 77951922861 scopus 로고    scopus 로고
    • Molecular diversity through RNA editing: a balancing act
    • Farajollahi S, Maas S. Molecular diversity through RNA editing: a balancing act. Trends Genet 2010, 26:221-230.
    • (2010) Trends Genet , vol.26 , pp. 221-230
    • Farajollahi, S.1    Maas, S.2
  • 31
    • 33344477023 scopus 로고    scopus 로고
    • ADAR2-dependent RNA editing of AMPA receptor subunit GluR2 determines vulnerability of neurons in forebrain ischemia
    • Peng PL, Zhong X, Tu W, Soundarapandian MM, Molner P, Zhu D, Lau L, Liu S, Liu F, Lu Y. ADAR2-dependent RNA editing of AMPA receptor subunit GluR2 determines vulnerability of neurons in forebrain ischemia. Neuron 2006, 49:719-733.
    • (2006) Neuron , vol.49 , pp. 719-733
    • Peng, P.L.1    Zhong, X.2    Tu, W.3    Soundarapandian, M.M.4    Molner, P.5    Zhu, D.6    Lau, L.7    Liu, S.8    Liu, F.9    Lu, Y.10
  • 32
    • 0345133268 scopus 로고    scopus 로고
    • Modulation of RNA editing by functional nucleolar sequestration of ADAR2
    • Sansam CL, Wells KS, Emeson RB. Modulation of RNA editing by functional nucleolar sequestration of ADAR2. Proc Natl Acad Sci U S A 2003, 100:14018-14023.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 14018-14023
    • Sansam, C.L.1    Wells, K.S.2    Emeson, R.B.3
  • 33
    • 73049104019 scopus 로고    scopus 로고
    • Identification of a selective nuclear import signal in adenosine deaminases acting on RNA
    • Nucleic Acids Res
    • Maas S, Gommans WM. Identification of a selective nuclear import signal in adenosine deaminases acting on RNA. Nucleic Acids Res 2009, 37:5822-5829.
    • (2009) , vol.37 , pp. 5822-5829
    • Maas, S.1    Gommans, W.M.2
  • 34
    • 0033529064 scopus 로고    scopus 로고
    • Regulation of alternative splicing by RNA editing
    • Rueter SM, Dawson TR, Emeson RB. Regulation of alternative splicing by RNA editing. Nature 1999, 399:75-80.
    • (1999) Nature , vol.399 , pp. 75-80
    • Rueter, S.M.1    Dawson, T.R.2    Emeson, R.B.3
  • 35
    • 0033943052 scopus 로고    scopus 로고
    • dADAR, a Drosophila double-stranded RNA-specific adenosine deaminase is highly developmentally regulated and is itself a target for RNA editing
    • Palladino MJ, Keegan LP, O'Connell MA, Reenan RA. dADAR, a Drosophila double-stranded RNA-specific adenosine deaminase is highly developmentally regulated and is itself a target for RNA editing. RNA 2000, 6:1004-1018.
    • (2000) RNA , vol.6 , pp. 1004-1018
    • Palladino, M.J.1    Keegan, L.P.2    O'Connell, M.A.3    Reenan, R.A.4
  • 36
    • 34447542355 scopus 로고    scopus 로고
    • RNA binding-independent dimerization of adenosine deaminases acting on RNA and dominant negative effects of nonfunctional subunits on dimer functions
    • Valente L, Nishikura K. RNA binding-independent dimerization of adenosine deaminases acting on RNA and dominant negative effects of nonfunctional subunits on dimer functions. J Biol Chem 2007, 282:16054-16061.
    • (2007) J Biol Chem , vol.282 , pp. 16054-16061
    • Valente, L.1    Nishikura, K.2
  • 37
    • 17844384227 scopus 로고    scopus 로고
    • Regulation of serotonin 2C receptor pre-mRNA editing by serotonin A2
    • Schmauss C. Regulation of serotonin 2C receptor pre-mRNA editing by serotonin A2. Int Rev Neurobiol 2005, 63:83-100.
    • (2005) Int Rev Neurobiol , vol.63 , pp. 83-100
    • Schmauss, C.1
  • 39
    • 84867164960 scopus 로고    scopus 로고
    • IP6 (Inositol Hexaphosphate) as a signaling molecule
    • Kalam Shamsuddin A, Bose S. IP6 (Inositol Hexaphosphate) as a signaling molecule. Curr Signal Transd Therapy 2012, 7:289-304.
    • (2012) Curr Signal Transd Therapy , vol.7 , pp. 289-304
    • Kalam Shamsuddin, A.1    Bose, S.2
  • 40
    • 77955273674 scopus 로고    scopus 로고
    • The REM phase of gene regulation
    • Hentze MW, Preiss T. The REM phase of gene regulation. Trends Biochem Sci 2010, 35:423-426.
    • (2010) Trends Biochem Sci , vol.35 , pp. 423-426
    • Hentze, M.W.1    Preiss, T.2
  • 41
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress
    • Hentze MW, Kühn LC. Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proc Natl Acad Sci U S A 1996, 93:8175-8182.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kühn, L.C.2
  • 42
    • 0033826764 scopus 로고    scopus 로고
    • Iron regulatory proteins and the molecular control of mammalian iron metabolism
    • Eisenstein RS. Iron regulatory proteins and the molecular control of mammalian iron metabolism. Annu Rev Nutr 2000, 20:627-662.
    • (2000) Annu Rev Nutr , vol.20 , pp. 627-662
    • Eisenstein, R.S.1
  • 44
    • 0034731457 scopus 로고    scopus 로고
    • Combinatorial mRNA regulation: iron regulatory proteins and iso-iron-responsive elements (Iso-IREs)
    • Theil EC, Eisenstein RS. Combinatorial mRNA regulation: iron regulatory proteins and iso-iron-responsive elements (Iso-IREs). J Biol Chem 2000, 275:40659-40662.
    • (2000) J Biol Chem , vol.275 , pp. 40659-40662
    • Theil, E.C.1    Eisenstein, R.S.2
  • 45
    • 0027452550 scopus 로고
    • Regulating the fate of mRNA: the control of cellular iron metabolism
    • Klausner RD, Rouault TA, Harford JB. Regulating the fate of mRNA: the control of cellular iron metabolism. Cell 1993, 72:19-28.
    • (1993) Cell , vol.72 , pp. 19-28
    • Klausner, R.D.1    Rouault, T.A.2    Harford, J.B.3
  • 46
    • 0642349271 scopus 로고    scopus 로고
    • Post-transcriptional regulation of human iron metabolism by iron regulatory proteins
    • Rouault TA. Post-transcriptional regulation of human iron metabolism by iron regulatory proteins. Blood Cells Mol Dis 2002, 29:309-314.
    • (2002) Blood Cells Mol Dis , vol.29 , pp. 309-314
    • Rouault, T.A.1
  • 47
    • 0037096190 scopus 로고    scopus 로고
    • The iron regulatory proteins: targets and modulators of free radical reactions and oxidative damage
    • Cairo G, Recalcati S, Pietrangelo A, Minotti G. The iron regulatory proteins: targets and modulators of free radical reactions and oxidative damage. Free Radic Biol Med 2002, 32:1237-1243.
    • (2002) Free Radic Biol Med , vol.32 , pp. 1237-1243
    • Cairo, G.1    Recalcati, S.2    Pietrangelo, A.3    Minotti, G.4
  • 48
    • 0027479724 scopus 로고
    • A double life: cytosolic aconitase as a regulatory RNA binding protein
    • Klausner RD, Rouault TA. A double life: cytosolic aconitase as a regulatory RNA binding protein. Mol Biol Cell 1993, 4:1-5.
    • (1993) Mol Biol Cell , vol.4 , pp. 1-5
    • Klausner, R.D.1    Rouault, T.A.2
  • 49
    • 0024439456 scopus 로고
    • The iron-responsive element binding protein: a method for the affinity purification of a regulatory RNA-binding protein
    • Rouault TA, Hentze MW, Haile DJ, Harford JB, Klausner RD. The iron-responsive element binding protein: a method for the affinity purification of a regulatory RNA-binding protein. Proc Natl Acad Sci U S A 1989, 86:5768-5772.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 5768-5772
    • Rouault, T.A.1    Hentze, M.W.2    Haile, D.J.3    Harford, J.B.4    Klausner, R.D.5
  • 50
    • 0025099393 scopus 로고
    • A high yield affinity purification method for specific RNA-binding proteins: isolation of the iron regulatory factor from human placenta
    • Neupert B, Thompson NA, Meyer C, Kühn LC. A high yield affinity purification method for specific RNA-binding proteins: isolation of the iron regulatory factor from human placenta. Nucleic Acids Res 1990, 18:51-55.
    • (1990) Nucleic Acids Res , vol.18 , pp. 51-55
    • Neupert, B.1    Thompson, N.A.2    Meyer, C.3    Kühn, L.C.4
  • 52
    • 0026508809 scopus 로고
    • Expression of active iron regulatory factor from a full-length human cDNA by in vitro transcription/translation
    • Hirling H, Emery-Goodman A, Thompson N, Neupert B, Seiser C, Kühn LC. Expression of active iron regulatory factor from a full-length human cDNA by in vitro transcription/translation. Nucleic Acids Res 1992, 20:33-39.
    • (1992) Nucleic Acids Res , vol.20 , pp. 33-39
    • Hirling, H.1    Emery-Goodman, A.2    Thompson, N.3    Neupert, B.4    Seiser, C.5    Kühn, L.C.6
  • 53
    • 0025865421 scopus 로고
    • Homology between IRE-BP, a regulatory RNA-binding protein, aconitase, and isopropylmalate isomerase
    • Hentze MW, Argos P. Homology between IRE-BP, a regulatory RNA-binding protein, aconitase, and isopropylmalate isomerase. Nucleic Acids Res 1991, 19:1739-1740.
    • (1991) Nucleic Acids Res , vol.19 , pp. 1739-1740
    • Hentze, M.W.1    Argos, P.2
  • 54
    • 0026062191 scopus 로고
    • Structural relationship between an iron-regulated RNA-binding protein (IRE-BP) and aconitase: functional implications
    • Rouault TA, Stout CD, Kaptain S, Harford JB, Klausner RD. Structural relationship between an iron-regulated RNA-binding protein (IRE-BP) and aconitase: functional implications. Cell 1991, 64:881-883.
    • (1991) Cell , vol.64 , pp. 881-883
    • Rouault, T.A.1    Stout, C.D.2    Kaptain, S.3    Harford, J.B.4    Klausner, R.D.5
  • 56
    • 0026756095 scopus 로고
    • Reciprocal control of RNA-binding and aconitase activity in the regulation of the iron-responsive element binding protein: role of the iron-sulfur cluster
    • Haile DJ, Rouault TA, Tang CK, Chin J, Harford JB, Klausner RD. Reciprocal control of RNA-binding and aconitase activity in the regulation of the iron-responsive element binding protein: role of the iron-sulfur cluster. Proc Natl Acad Sci U S A 1992, 89:7536-7540.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 7536-7540
    • Haile, D.J.1    Rouault, T.A.2    Tang, C.K.3    Chin, J.4    Harford, J.B.5    Klausner, R.D.6
  • 57
    • 0027081042 scopus 로고
    • Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein
    • Kennedy MC, Mende-Mueller L, Blondin GA, Beinert H. Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein. Proc Natl Acad Sci U S A 1992, 89:11730-11734.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 11730-11734
    • Kennedy, M.C.1    Mende-Mueller, L.2    Blondin, G.A.3    Beinert, H.4
  • 60
    • 0028321733 scopus 로고
    • Optimal sequence and structure of iron-responsive elements. Selection of RNA stem-loops with high affinity for iron regulatory factor
    • Henderson BR, Menotti E, Bonnard C, Kühn LC. Optimal sequence and structure of iron-responsive elements. Selection of RNA stem-loops with high affinity for iron regulatory factor. J Biol Chem 1994, 269:17481-17489.
    • (1994) J Biol Chem , vol.269 , pp. 17481-17489
    • Henderson, B.R.1    Menotti, E.2    Bonnard, C.3    Kühn, L.C.4
  • 63
    • 0035138456 scopus 로고    scopus 로고
    • Targeted deletion of the gene encoding iron regulatory protein-2 causes misregulation of iron metabolism and neurodegenerative disease in mice
    • LaVaute T, Smith S, Cooperman S, Iwai K, Land W, Meyron-Holtz E, Drake SK, Miller G, Abu-Asab M, Tsokos M, et al. Targeted deletion of the gene encoding iron regulatory protein-2 causes misregulation of iron metabolism and neurodegenerative disease in mice. Nat Genet 2001, 27:209-214.
    • (2001) Nat Genet , vol.27 , pp. 209-214
    • LaVaute, T.1    Smith, S.2    Cooperman, S.3    Iwai, K.4    Land, W.5    Meyron-Holtz, E.6    Drake, S.K.7    Miller, G.8    Abu-Asab, M.9    Tsokos, M.10
  • 64
    • 23044503950 scopus 로고    scopus 로고
    • Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2
    • Cooperman SS, Meyron-Holtz EG, Olivierre-Wilson H, Ghosh MC, McConnell JP, Rouault TA. Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2. Blood 2005, 106:1084-1091.
    • (2005) Blood , vol.106 , pp. 1084-1091
    • Cooperman, S.S.1    Meyron-Holtz, E.G.2    Olivierre-Wilson, H.3    Ghosh, M.C.4    McConnell, J.P.5    Rouault, T.A.6
  • 65
    • 33645307993 scopus 로고    scopus 로고
    • Complete loss of iron regulatory proteins 1 and 2 prevents viability of murine zygotes beyond the blastocyst stage of embryonic development
    • Smith SR, Ghosh MC, Ollivierre-Wilson H, Hang Tong W, Rouault TA. Complete loss of iron regulatory proteins 1 and 2 prevents viability of murine zygotes beyond the blastocyst stage of embryonic development. Blood Cells Mol Dis 2006, 36:283-287.
    • (2006) Blood Cells Mol Dis , vol.36 , pp. 283-287
    • Smith, S.R.1    Ghosh, M.C.2    Ollivierre-Wilson, H.3    Hang Tong, W.4    Rouault, T.A.5
  • 66
    • 0032973950 scopus 로고    scopus 로고
    • New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase
    • Sirover MA. New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase. Biochim Biophys Acta 1999, 1432:159-184.
    • (1999) Biochim Biophys Acta , vol.1432 , pp. 159-184
    • Sirover, M.A.1
  • 68
    • 0022406559 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is one of the three major RNA-binding proteins of rabbit reticulocytes
    • Ryazanov AG. Glyceraldehyde-3-phosphate dehydrogenase is one of the three major RNA-binding proteins of rabbit reticulocytes. FEBS Lett 1985, 192:131-134.
    • (1985) FEBS Lett , vol.192 , pp. 131-134
    • Ryazanov, A.G.1
  • 69
    • 0027518424 scopus 로고
    • Sequence-specific binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase
    • Singh R, Green MR. Sequence-specific binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase. Science 1993, 259:365-368.
    • (1993) Science , vol.259 , pp. 365-368
    • Singh, R.1    Green, M.R.2
  • 70
    • 0037316278 scopus 로고    scopus 로고
    • Interaction of glyceraldehyde-3-phosphate dehydrogenase with secondary and tertiary RNA structural elements of the hepatitis A virus 3′ translated and non-translated regions
    • Dollenmaier G. Interaction of glyceraldehyde-3-phosphate dehydrogenase with secondary and tertiary RNA structural elements of the hepatitis A virus 3′ translated and non-translated regions. J Gen Virol 2003, 84:403-414.
    • (2003) J Gen Virol , vol.84 , pp. 403-414
    • Dollenmaier, G.1
  • 71
    • 0028816615 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase selectively binds AU-rich RNA in the NAD(+)-binding region (Rossmann fold)
    • Nagy E, Rigby WF. Glyceraldehyde-3-phosphate dehydrogenase selectively binds AU-rich RNA in the NAD(+)-binding region (Rossmann fold). J Biol Chem 1995, 270:2755-2763.
    • (1995) J Biol Chem , vol.270 , pp. 2755-2763
    • Nagy, E.1    Rigby, W.F.2
  • 72
    • 0035911221 scopus 로고    scopus 로고
    • Colony-stimulating factor 1 promotes progression of mammary tumors to malignancy
    • Lin EY, Nguyen AV, Russell RG, Pollard JW. Colony-stimulating factor 1 promotes progression of mammary tumors to malignancy. J Exp Med 2001, 193:727-740.
    • (2001) J Exp Med , vol.193 , pp. 727-740
    • Lin, E.Y.1    Nguyen, A.V.2    Russell, R.G.3    Pollard, J.W.4
  • 74
    • 0034726714 scopus 로고    scopus 로고
    • Identification of the NAD(+)-binding fold of glyceraldehyde-3-phosphate dehydrogenase as a novel RNA-binding domain
    • Nagy E, Henics T, Eckert M, Miseta A, Lightowlers RN, Kellermayer M. Identification of the NAD(+)-binding fold of glyceraldehyde-3-phosphate dehydrogenase as a novel RNA-binding domain. Biochem Biophys Res Commun 2000, 275:253-260.
    • (2000) Biochem Biophys Res Commun , vol.275 , pp. 253-260
    • Nagy, E.1    Henics, T.2    Eckert, M.3    Miseta, A.4    Lightowlers, R.N.5    Kellermayer, M.6
  • 76
    • 33645220015 scopus 로고    scopus 로고
    • Metabolic enzymes that bind RNA: yet another level of cellular regulatory network?
    • Cieśla J. Metabolic enzymes that bind RNA: yet another level of cellular regulatory network? Acta Biochim Pol 2006, 53:11-32.
    • (2006) Acta Biochim Pol , vol.53 , pp. 11-32
    • Cieśla, J.1


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