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Volumn 1843, Issue 12, 2014, Pages 2913-2925

DERA is the human deoxyribose phosphate aldolase and is involved in stress response

Author keywords

Apoptosis; Deoxynucleoside metabolism; Deoxyribose phosphate aldolase; Metabolic stress; Stress granule

Indexed keywords

ADENOSINE TRIPHOSPHATE; DEOXYINOSINE; DEOXYRIBOSE PHOSPHATE ALDOLASE; FRUCTOSE BISPHOSPHATE ALDOLASE; UNCLASSIFIED DRUG;

EID: 84907481823     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2014.09.007     Document Type: Article
Times cited : (25)

References (75)
  • 1
    • 0000863021 scopus 로고
    • Enzymatic synthesis and breakdown of desoxyribose phosphate
    • Racker E. Enzymatic synthesis and breakdown of desoxyribose phosphate. J. Biol. Chem. 1952, 196:347-365.
    • (1952) J. Biol. Chem. , vol.196 , pp. 347-365
    • Racker, E.1
  • 2
    • 0018688787 scopus 로고
    • Evidence for the existence of three promoters for the deo operon of Escherichia coli K12 in vitro
    • Valentin-Hansen P., Hammer-Jespersen K., Buxton R.S. Evidence for the existence of three promoters for the deo operon of Escherichia coli K12 in vitro. J. Mol. Biol. 1979, 133:1-17.
    • (1979) J. Mol. Biol. , vol.133 , pp. 1-17
    • Valentin-Hansen, P.1    Hammer-Jespersen, K.2    Buxton, R.S.3
  • 3
    • 0020325954 scopus 로고
    • The primary structure of Escherichia coli K12 2-deoxyribose 5-phosphate aldolase. Nucleotide sequence of the deoC gene and the amino acid sequence of the enzyme
    • Valentin-Hansen P., Boëtius F., Hammer-Jespersen K., Svendsen I. The primary structure of Escherichia coli K12 2-deoxyribose 5-phosphate aldolase. Nucleotide sequence of the deoC gene and the amino acid sequence of the enzyme. Eur. J. Biochem. 1982, 125:561-566.
    • (1982) Eur. J. Biochem. , vol.125 , pp. 561-566
    • Valentin-Hansen, P.1    Boëtius, F.2    Hammer-Jespersen, K.3    Svendsen, I.4
  • 4
    • 0025345398 scopus 로고
    • Deoxyribose-5-phosphate aldolase as a synthetic catalyst
    • Barbas C.F., Wang Y.F., Wong C.H. Deoxyribose-5-phosphate aldolase as a synthetic catalyst. J. Am. Chem. Soc. 1990, 112:2013-2014. 10.1021/ja00161a064.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 2013-2014
    • Barbas, C.F.1    Wang, Y.F.2    Wong, C.H.3
  • 5
    • 0029010689 scopus 로고
    • Crystallization and preliminary crystallographic data for class I deoxyribose-5-phosphate aldolase from Escherichia coli: an application of reverse screening
    • Stura E.A., Ghosh S., Garcia-Junceda E., Chen L., Wong C.H., Wilson I.A. Crystallization and preliminary crystallographic data for class I deoxyribose-5-phosphate aldolase from Escherichia coli: an application of reverse screening. Proteins 1995, 22:67-72. 10.1002/prot.340220110.
    • (1995) Proteins , vol.22 , pp. 67-72
    • Stura, E.A.1    Ghosh, S.2    Garcia-Junceda, E.3    Chen, L.4    Wong, C.H.5    Wilson, I.A.6
  • 6
    • 0035850820 scopus 로고    scopus 로고
    • Observation of covalent intermediates in an enzyme mechanism at atomic resolution
    • Heine A., DeSantis G., Luz J.G., Mitchell M., Wong C.H., Wilson I.A. Observation of covalent intermediates in an enzyme mechanism at atomic resolution. Science 2001, 294:369-374. 10.1126/science.1063601.
    • (2001) Science , vol.294 , pp. 369-374
    • Heine, A.1    DeSantis, G.2    Luz, J.G.3    Mitchell, M.4    Wong, C.H.5    Wilson, I.A.6
  • 7
    • 16644397302 scopus 로고    scopus 로고
    • Structure of aldolase from Thermus thermophilus HB8 showing the contribution of oligomeric state to thermostability
    • Lokanath N.K., Shiromizu I., Ohshima N., Nodake Y., Sugahara M., Yokoyama S., et al. Structure of aldolase from Thermus thermophilus HB8 showing the contribution of oligomeric state to thermostability. Acta Crystallogr. D Biol. Crystallogr. 2004, 60:1816-1823. 10.1107/S0907444904020190.
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 1816-1823
    • Lokanath, N.K.1    Shiromizu, I.2    Ohshima, N.3    Nodake, Y.4    Sugahara, M.5    Yokoyama, S.6
  • 8
    • 0037855777 scopus 로고    scopus 로고
    • The first crystal structure of archaeal aldolase. Unique tetrameric structure of 2-deoxy-d-ribose-5-phosphate aldolase from the hyperthermophilic archaea Aeropyrum pernix
    • Sakuraba H., Tsuge H., Shimoya I., Kawakami R., Goda S., Kawarabayasi Y., et al. The first crystal structure of archaeal aldolase. Unique tetrameric structure of 2-deoxy-d-ribose-5-phosphate aldolase from the hyperthermophilic archaea Aeropyrum pernix. J. Biol. Chem. 2003, 278:10799-10806. 10.1074/jbc.M212449200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10799-10806
    • Sakuraba, H.1    Tsuge, H.2    Shimoya, I.3    Kawakami, R.4    Goda, S.5    Kawarabayasi, Y.6
  • 9
    • 34548374935 scopus 로고
    • Polycarboxylic acid activation of rat liver deoxyribose phosphate aldolase
    • Jiang N.S., Groth D.P. Polycarboxylic acid activation of rat liver deoxyribose phosphate aldolase. J. Biol. Chem. 1962, 237:3339-3341.
    • (1962) J. Biol. Chem. , vol.237 , pp. 3339-3341
    • Jiang, N.S.1    Groth, D.P.2
  • 10
    • 12644302758 scopus 로고
    • Deoxyribose Phosphate Aldolase From Rat Liver
    • Roscoe H.G., Nelson W.L. Deoxyribose Phosphate Aldolase From Rat Liver. J. Biol. Chem. 1964, 239:8-11.
    • (1964) J. Biol. Chem. , vol.239 , pp. 8-11
    • Roscoe, H.G.1    Nelson, W.L.2
  • 11
    • 0014197536 scopus 로고
    • Deoxyribose 5-phosphate aldolase. II. Purification and properties of the rat liver enzyme
    • Groth D.P. Deoxyribose 5-phosphate aldolase. II. Purification and properties of the rat liver enzyme. J. Biol. Chem. 1967, 242:155-159.
    • (1967) J. Biol. Chem. , vol.242 , pp. 155-159
    • Groth, D.P.1
  • 13
    • 0014951963 scopus 로고
    • Purification and properties of deoxyriboaldolase from human erythrocytes
    • Jedziniak J.A., Lionetti F.J. Purification and properties of deoxyriboaldolase from human erythrocytes. Biochim. Biophys. Acta 1970, 212:478-487.
    • (1970) Biochim. Biophys. Acta , vol.212 , pp. 478-487
    • Jedziniak, J.A.1    Lionetti, F.J.2
  • 14
    • 0018744540 scopus 로고
    • Deoxyribose 5-phosphate aldolase: an enzyme that peaks in the G2 phase of rat hepatoma cells
    • Lincoln D.W., Hoffee P. Deoxyribose 5-phosphate aldolase: an enzyme that peaks in the G2 phase of rat hepatoma cells. Arch. Biochem. Biophys. 1979, 193:392-397.
    • (1979) Arch. Biochem. Biophys. , vol.193 , pp. 392-397
    • Lincoln, D.W.1    Hoffee, P.2
  • 16
    • 33846647534 scopus 로고    scopus 로고
    • Purine and pyrimidine nucleosides preserve human astrocytoma cell adenylate energy charge under ischemic conditions
    • Balestri F., Giannecchini M., Sgarrella F., Carta M.C., Tozzi M.G., Camici M. Purine and pyrimidine nucleosides preserve human astrocytoma cell adenylate energy charge under ischemic conditions. Neurochem. Int. 2007, 50:517-523. 10.1016/j.neuint.2006.10.005.
    • (2007) Neurochem. Int. , vol.50 , pp. 517-523
    • Balestri, F.1    Giannecchini, M.2    Sgarrella, F.3    Carta, M.C.4    Tozzi, M.G.5    Camici, M.6
  • 17
    • 0014323016 scopus 로고
    • Characteristics of the deo operon: role in thymine utilization and sensitivity to deoxyribonucleosides
    • Lomax M.S., Greenberg G.R. Characteristics of the deo operon: role in thymine utilization and sensitivity to deoxyribonucleosides. J. Bacteriol. 1968, 96:501-514.
    • (1968) J. Bacteriol. , vol.96 , pp. 501-514
    • Lomax, M.S.1    Greenberg, G.R.2
  • 18
    • 77049164570 scopus 로고
    • The enzymatic synthesis of nucleosides. I. Thymidine phosphorylase in mammalian tissue
    • Friedken M., Roberts D. The enzymatic synthesis of nucleosides. I. Thymidine phosphorylase in mammalian tissue. J. Biol. Chem. 1954, 207:245-256.
    • (1954) J. Biol. Chem. , vol.207 , pp. 245-256
    • Friedken, M.1    Roberts, D.2
  • 19
    • 77049163441 scopus 로고
    • The enzymatic synthesis of nucleosides. II. Thymidine and related pyrimidine nucleosides
    • Friedken M., Roberts D. The enzymatic synthesis of nucleosides. II. Thymidine and related pyrimidine nucleosides. J. Biol. Chem. 1954, 207:257-266.
    • (1954) J. Biol. Chem. , vol.207 , pp. 257-266
    • Friedken, M.1    Roberts, D.2
  • 20
    • 36148960475 scopus 로고    scopus 로고
    • Molecular identification of mammalian phosphopentomutase and glucose-1,6-bisphosphate synthase, two members of the alpha-D-phosphohexomutase family
    • Maliekal P., Sokolova T., Vertommen D., Veiga-da-Cunha M., Van Schaftingen E. Molecular identification of mammalian phosphopentomutase and glucose-1,6-bisphosphate synthase, two members of the alpha-D-phosphohexomutase family. J. Biol. Chem. 2007, 282:31844-31851. 10.1074/jbc.M706818200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 31844-31851
    • Maliekal, P.1    Sokolova, T.2    Vertommen, D.3    Veiga-da-Cunha, M.4    Van Schaftingen, E.5
  • 21
    • 0034452004 scopus 로고    scopus 로고
    • Purine nucleoside phosphorylases: properties, functions, and clinical aspects
    • Bzowska A., Kulikowska E., Shugar D. Purine nucleoside phosphorylases: properties, functions, and clinical aspects. Pharmacol. Ther. 2000, 88:349-425.
    • (2000) Pharmacol. Ther. , vol.88 , pp. 349-425
    • Bzowska, A.1    Kulikowska, E.2    Shugar, D.3
  • 22
    • 0014429424 scopus 로고
    • Purine nucleoside phosphorylase from human erythrocytes. I. Purification and properties
    • Kim B.K., Cha S., Parks R.E. Purine nucleoside phosphorylase from human erythrocytes. I. Purification and properties. J. Biol. Chem. 1968, 243:1763-1770.
    • (1968) J. Biol. Chem. , vol.243 , pp. 1763-1770
    • Kim, B.K.1    Cha, S.2    Parks, R.E.3
  • 25
    • 77952628837 scopus 로고    scopus 로고
    • Regulation of translation by stress granules and processing bodies
    • Kedersha N., Anderson P. Regulation of translation by stress granules and processing bodies. Prog. Mol. Biol. Transl. Sci. 2009, 90:155-185. 10.1016/S1877-1173(09)90004-7.
    • (2009) Prog. Mol. Biol. Transl. Sci. , vol.90 , pp. 155-185
    • Kedersha, N.1    Anderson, P.2
  • 26
    • 75849153303 scopus 로고    scopus 로고
    • The Universal Protein Resource (UniProt) in 2010
    • UniProt Consortium The Universal Protein Resource (UniProt) in 2010. Nucleic Acids Res. 2010, 38:D142-D148.
    • (2010) Nucleic Acids Res. , vol.38 , pp. D142-D148
  • 27
    • 80054078476 scopus 로고    scopus 로고
    • Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
    • Sievers F., Wilm A., Dineen D., Gibson T.J., Karplus K., Li W., et al. Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega. Mol. Syst. Biol. 2011, 7:539. 10.1038/msb.2011.75.
    • (2011) Mol. Syst. Biol. , vol.7 , pp. 539
    • Sievers, F.1    Wilm, A.2    Dineen, D.3    Gibson, T.J.4    Karplus, K.5    Li, W.6
  • 28
    • 0037129827 scopus 로고    scopus 로고
    • Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes
    • (RESEARCH0034)
    • Vandesompele J., De Preter K., Pattyn F., Poppe B., Van Roy N., De Paepe A., et al. Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biol. 2002, 3. (RESEARCH0034).
    • (2002) Genome Biol. , vol.3
    • Vandesompele, J.1    De Preter, K.2    Pattyn, F.3    Poppe, B.4    Van Roy, N.5    De Paepe, A.6
  • 29
    • 57049148002 scopus 로고    scopus 로고
    • Molecular characterization of human Argonaute-containing ribonucleoprotein complexes and their bound target mRNAs
    • Landthaler M., Gaidatzis D., Rothballer A., Chen P.Y., Soll S.J., Dinic L., et al. Molecular characterization of human Argonaute-containing ribonucleoprotein complexes and their bound target mRNAs. RNA 2008, 14:2580-2596. 10.1261/rna.1351608.
    • (2008) RNA , vol.14 , pp. 2580-2596
    • Landthaler, M.1    Gaidatzis, D.2    Rothballer, A.3    Chen, P.Y.4    Soll, S.J.5    Dinic, L.6
  • 30
    • 77956215470 scopus 로고    scopus 로고
    • Rapid, simple and high yield production of recombinant proteins in mammalian cells using a versatile episomal system
    • Magistrelli G., Malinge P., Lissilaa R., Fagète S., Guilhot F., Moine V., et al. Rapid, simple and high yield production of recombinant proteins in mammalian cells using a versatile episomal system. Protein Expr. Purif. 2010, 72:209-216. 10.1016/j.pep.2010.04.007.
    • (2010) Protein Expr. Purif. , vol.72 , pp. 209-216
    • Magistrelli, G.1    Malinge, P.2    Lissilaa, R.3    Fagète, S.4    Guilhot, F.5    Moine, V.6
  • 31
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho S.N., Hunt H.D., Horton R.M., Pullen J.K., Pease L.R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 1989, 77:51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 32
    • 65749119848 scopus 로고    scopus 로고
    • Stress granules
    • Anderson P., Kedersha N. Stress granules. Curr. Biol. 2009, 19:R397-R398. 10.1016/j.cub.2009.03.013.
    • (2009) Curr. Biol. , vol.19 , pp. R397-R398
    • Anderson, P.1    Kedersha, N.2
  • 33
    • 0014250428 scopus 로고
    • 2-Deoxyribose gene-enzyme complex in salmonella typhimurium I. Isolation and enzymatic characterization of 2-deoxyribose-negative mutants
    • Hoffee P. 2-Deoxyribose gene-enzyme complex in salmonella typhimurium I. Isolation and enzymatic characterization of 2-deoxyribose-negative mutants. J. Bacteriol. 1968, 95:449.
    • (1968) J. Bacteriol. , vol.95 , pp. 449
    • Hoffee, P.1
  • 34
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller A., Nesvizhskii A.I., Kolker E., Aebersold R. Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal. Chem. 2002, 74:5383-5392.
    • (2002) Anal. Chem. , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 35
    • 57349170258 scopus 로고    scopus 로고
    • Regulatory role of human AP-endonuclease (APE1/Ref-1) in YB-1-mediated activation of the multidrug resistance gene MDR1
    • Chattopadhyay R., Das S., Maiti A.K., Boldogh I., Xie J., Hazra T.K., et al. Regulatory role of human AP-endonuclease (APE1/Ref-1) in YB-1-mediated activation of the multidrug resistance gene MDR1. Mol. Cell Biol. 2008, 28:7066-7080. 10.1128/MCB.00244-08.
    • (2008) Mol. Cell Biol. , vol.28 , pp. 7066-7080
    • Chattopadhyay, R.1    Das, S.2    Maiti, A.K.3    Boldogh, I.4    Xie, J.5    Hazra, T.K.6
  • 36
    • 0035877851 scopus 로고    scopus 로고
    • Stimulation of human endonuclease III by Y box-binding protein 1 (DNA-binding protein B). Interaction between a base excision repair enzyme and a transcription factor
    • Marenstein D.R., Ocampo M.T., Chan M.K., Altamirano A., Basu A.K., Boorstein R.J., et al. Stimulation of human endonuclease III by Y box-binding protein 1 (DNA-binding protein B). Interaction between a base excision repair enzyme and a transcription factor. J. Biol. Chem. 2001, 276:21242-21249. 10.1074/jbc.M101594200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21242-21249
    • Marenstein, D.R.1    Ocampo, M.T.2    Chan, M.K.3    Altamirano, A.4    Basu, A.K.5    Boorstein, R.J.6
  • 37
    • 35348971904 scopus 로고    scopus 로고
    • Stimulation of NEIL2-mediated oxidized base excision repair via YB-1 interaction during oxidative stress
    • Das S., Chattopadhyay R., Bhakat K.K., Boldogh I., Kohno K., Prasad R., et al. Stimulation of NEIL2-mediated oxidized base excision repair via YB-1 interaction during oxidative stress. J. Biol. Chem. 2007, 282:28474-28484. 10.1074/jbc.M704672200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 28474-28484
    • Das, S.1    Chattopadhyay, R.2    Bhakat, K.K.3    Boldogh, I.4    Kohno, K.5    Prasad, R.6
  • 38
    • 0035328667 scopus 로고    scopus 로고
    • Oncogenic TLS/ERG and EWS/Fli-1 fusion proteins inhibit RNA splicing mediated by YB-1 protein
    • Chansky H.A., Hu M., Hickstein D.D., Yang L. Oncogenic TLS/ERG and EWS/Fli-1 fusion proteins inhibit RNA splicing mediated by YB-1 protein. Cancer Res. 2001, 61:3586-3590.
    • (2001) Cancer Res. , vol.61 , pp. 3586-3590
    • Chansky, H.A.1    Hu, M.2    Hickstein, D.D.3    Yang, L.4
  • 39
    • 0035976989 scopus 로고    scopus 로고
    • The major messenger ribonucleoprotein particle protein p50 (YB-1) promotes nucleic acid strand annealing
    • Skabkin M.A., Evdokimova V., Thomas A.A., Ovchinnikov L.P. The major messenger ribonucleoprotein particle protein p50 (YB-1) promotes nucleic acid strand annealing. J. Biol. Chem. 2001, 276:44841-44847. 10.1074/jbc.M107581200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44841-44847
    • Skabkin, M.A.1    Evdokimova, V.2    Thomas, A.A.3    Ovchinnikov, L.P.4
  • 40
    • 38449123517 scopus 로고    scopus 로고
    • Mammalian stress granules and processing bodies
    • Kedersha N., Anderson P. Mammalian stress granules and processing bodies. Methods Enzymol. 2007, 431:61-81. 10.1016/S0076-6879(07)31005-7.
    • (2007) Methods Enzymol. , vol.431 , pp. 61-81
    • Kedersha, N.1    Anderson, P.2
  • 42
    • 0030825963 scopus 로고    scopus 로고
    • Nuclear translocation of the Y-box binding protein by ultraviolet irradiation
    • Koike K., Uchiumi T., Ohga T., Toh S., Wada M., Kohno K., et al. Nuclear translocation of the Y-box binding protein by ultraviolet irradiation. FEBS Lett. 1997, 417:390-394.
    • (1997) FEBS Lett. , vol.417 , pp. 390-394
    • Koike, K.1    Uchiumi, T.2    Ohga, T.3    Toh, S.4    Wada, M.5    Kohno, K.6
  • 43
    • 0037705425 scopus 로고    scopus 로고
    • Splicing factor SRp30c interaction with Y-box protein-1 confers nuclear YB-1 shuttling and alternative splice site selection
    • Raffetseder U., Frye B., Rauen T., Jürchott K., Royer H.-D., Jansen P.L., et al. Splicing factor SRp30c interaction with Y-box protein-1 confers nuclear YB-1 shuttling and alternative splice site selection. J. Biol. Chem. 2003, 278:18241-18248. 10.1074/jbc.M212518200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18241-18248
    • Raffetseder, U.1    Frye, B.2    Rauen, T.3    Jürchott, K.4    Royer, H.-D.5    Jansen, P.L.6
  • 45
    • 0033611157 scopus 로고    scopus 로고
    • RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules
    • Kedersha N.L., Gupta M., Li W., Miller I., Anderson P. RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules. J. Cell Biol. 1999, 147:1431-1442.
    • (1999) J. Cell Biol. , vol.147 , pp. 1431-1442
    • Kedersha, N.L.1    Gupta, M.2    Li, W.3    Miller, I.4    Anderson, P.5
  • 46
    • 0034638837 scopus 로고    scopus 로고
    • Dynamic shuttling of TIA-1 accompanies the recruitment of mRNA to mammalian stress granules
    • Kedersha N., Cho M.R., Li W., Yacono P.W., Chen S., Gilks N., et al. Dynamic shuttling of TIA-1 accompanies the recruitment of mRNA to mammalian stress granules. J. Cell Biol. 2000, 151:1257-1268.
    • (2000) J. Cell Biol. , vol.151 , pp. 1257-1268
    • Kedersha, N.1    Cho, M.R.2    Li, W.3    Yacono, P.W.4    Chen, S.5    Gilks, N.6
  • 47
    • 2442566370 scopus 로고    scopus 로고
    • Cytoplasmic foci are sites of mRNA decay in human cells
    • Cougot N., Babajko S., Séraphin B. Cytoplasmic foci are sites of mRNA decay in human cells. J. Cell Biol. 2004, 165:31-40. 10.1083/jcb.200309008.
    • (2004) J. Cell Biol. , vol.165 , pp. 31-40
    • Cougot, N.1    Babajko, S.2    Séraphin, B.3
  • 48
    • 70350367745 scopus 로고    scopus 로고
    • Unravelling the ultrastructure of stress granules and associated P-bodies in human cells
    • Souquere S., Mollet S., Kress M., Dautry F., Pierron G., Weil D. Unravelling the ultrastructure of stress granules and associated P-bodies in human cells. J. Cell Sci. 2009, 122:3619-3626. 10.1242/jcs.054437.
    • (2009) J. Cell Sci. , vol.122 , pp. 3619-3626
    • Souquere, S.1    Mollet, S.2    Kress, M.3    Dautry, F.4    Pierron, G.5    Weil, D.6
  • 49
    • 72149095755 scopus 로고    scopus 로고
    • Eukaryotic stress granules: the ins and outs of translation
    • Buchan J.R., Parker R. Eukaryotic stress granules: the ins and outs of translation. Mol. Cell 2009, 36:932-941. 10.1016/j.molcel.2009.11.020.
    • (2009) Mol. Cell , vol.36 , pp. 932-941
    • Buchan, J.R.1    Parker, R.2
  • 50
    • 74449089659 scopus 로고    scopus 로고
    • RhoA/ROCK1 signaling regulates stress granule formation and apoptosis
    • Tsai N.-P., Wei L.-N. RhoA/ROCK1 signaling regulates stress granule formation and apoptosis. Cell. Signal. 2010, 22:668-675. 10.1016/j.cellsig.2009.12.001.
    • (2010) Cell. Signal. , vol.22 , pp. 668-675
    • Tsai, N.-P.1    Wei, L.-N.2
  • 51
    • 0016432857 scopus 로고
    • Genetic analysis of thymidine-resistant and low-thymine-requiring mutants of Escherichia coli K-12 induced by bacteriophage Mu-1
    • Buxton R.S. Genetic analysis of thymidine-resistant and low-thymine-requiring mutants of Escherichia coli K-12 induced by bacteriophage Mu-1. J. Bacteriol. 1975, 121:475-484.
    • (1975) J. Bacteriol. , vol.121 , pp. 475-484
    • Buxton, R.S.1
  • 52
    • 0026537005 scopus 로고
    • Deoxyribose 5-phosphate aldolase of Bacillus cereus: purification and properties
    • Sgarrella F., Del Corso A., Tozzi M.G., Camici M. Deoxyribose 5-phosphate aldolase of Bacillus cereus: purification and properties. Biochim. Biophys. Acta 1992, 1118:130-133.
    • (1992) Biochim. Biophys. Acta , vol.1118 , pp. 130-133
    • Sgarrella, F.1    Del Corso, A.2    Tozzi, M.G.3    Camici, M.4
  • 53
    • 70449221806 scopus 로고
    • Deoxyribose5-phosphate metabolism by normal liver and malignant hepatoma
    • Boxer G.E., Shonk C.E. Deoxyribose5-phosphate metabolism by normal liver and malignant hepatoma. J. Biol. Chem. 1958, 233:535-540.
    • (1958) J. Biol. Chem. , vol.233 , pp. 535-540
    • Boxer, G.E.1    Shonk, C.E.2
  • 54
    • 0014005461 scopus 로고
    • The role of deoxyribose 5-phosphate aldolase in the synthesis of deoxyribonucleotide in mammalian cells
    • Groth D.P., Jiang N. The role of deoxyribose 5-phosphate aldolase in the synthesis of deoxyribonucleotide in mammalian cells. Biochem. Biophys. Res. Commun. 1966, 22:62-68.
    • (1966) Biochem. Biophys. Res. Commun. , vol.22 , pp. 62-68
    • Groth, D.P.1    Jiang, N.2
  • 55
    • 84861150401 scopus 로고    scopus 로고
    • Rhythmic nucleotide synthesis in the liver: temporal segregation of metabolites
    • Fustin J.-M., Doi M., Yamada H., Komatsu R., Shimba S., Okamura H. Rhythmic nucleotide synthesis in the liver: temporal segregation of metabolites. Cell Rep. 2012, 1:341-349. 10.1016/j.celrep.2012.03.001.
    • (2012) Cell Rep. , vol.1 , pp. 341-349
    • Fustin, J.-M.1    Doi, M.2    Yamada, H.3    Komatsu, R.4    Shimba, S.5    Okamura, H.6
  • 56
    • 84860839465 scopus 로고    scopus 로고
    • Update on the phenotypic spectrum of Lesch-Nyhan disease and its attenuated variants
    • Torres R.J., Puig J.G., Jinnah H.A. Update on the phenotypic spectrum of Lesch-Nyhan disease and its attenuated variants. Curr. Rheumatol. Rep. 2012, 14:189-194. 10.1007/s11926-011-0231-5.
    • (2012) Curr. Rheumatol. Rep. , vol.14 , pp. 189-194
    • Torres, R.J.1    Puig, J.G.2    Jinnah, H.A.3
  • 57
    • 0029136533 scopus 로고
    • The role of nucleotides in human nutrition
    • Carver J.D., Allan Walker W. The role of nucleotides in human nutrition. J. Nutr. Biochem. 1995, 6:58-72. 10.1016/0955-2863(94)00019-I.
    • (1995) J. Nutr. Biochem. , vol.6 , pp. 58-72
    • Carver, J.D.1    Allan Walker, W.2
  • 58
    • 54849420699 scopus 로고    scopus 로고
    • Rcl is a novel ETV1/ER81 target gene upregulated in breast tumors
    • Shin S., Bosc D.G., Ingle J.N., Spelsberg T.C., Janknecht R. Rcl is a novel ETV1/ER81 target gene upregulated in breast tumors. J. Cell. Biochem. 2008, 105:866-874. 10.1002/jcb.21884.
    • (2008) J. Cell. Biochem. , vol.105 , pp. 866-874
    • Shin, S.1    Bosc, D.G.2    Ingle, J.N.3    Spelsberg, T.C.4    Janknecht, R.5
  • 59
    • 34247230158 scopus 로고    scopus 로고
    • The c-Myc target gene Rcl (C6orf108) encodes a novel enzyme, deoxynucleoside 5'-monophosphate N-glycosidase
    • Ghiorghi Y.K., Zeller K.I., Dang C.V., Kaminski P.A. The c-Myc target gene Rcl (C6orf108) encodes a novel enzyme, deoxynucleoside 5'-monophosphate N-glycosidase. J. Biol. Chem. 2007, 282:8150-8156. 10.1074/jbc.M610648200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 8150-8156
    • Ghiorghi, Y.K.1    Zeller, K.I.2    Dang, C.V.3    Kaminski, P.A.4
  • 60
    • 84875438466 scopus 로고    scopus 로고
    • Mechanisms regulating airway nucleotides
    • Picher M. Mechanisms regulating airway nucleotides. Subcell. Biochem. 2011, 55:17-49. 10.1007/978-94-007-1217-1_2.
    • (2011) Subcell. Biochem. , vol.55 , pp. 17-49
    • Picher, M.1
  • 61
    • 0037413355 scopus 로고    scopus 로고
    • Structure-based mutagenesis approaches toward expanding the substrate specificity of D-2-deoxyribose-5-phosphate aldolase
    • DeSantis G., Liu J., Clark D.P., Heine A., Wilson I.A., Wong C.-H. Structure-based mutagenesis approaches toward expanding the substrate specificity of D-2-deoxyribose-5-phosphate aldolase. Bioorg. Med. Chem. 2003, 11:43-52.
    • (2003) Bioorg. Med. Chem. , vol.11 , pp. 43-52
    • DeSantis, G.1    Liu, J.2    Clark, D.P.3    Heine, A.4    Wilson, I.A.5    Wong, C.-H.6
  • 62
    • 84859815885 scopus 로고    scopus 로고
    • Combination of chemical genetics and phosphoproteomics for kinase signaling analysis enables confident identification of cellular downstream targets
    • (O111.012351)
    • Oppermann F.S., Grundner-Culemann K., Kumar C., Gruss O.J., Jallepalli P.V., Daub H. Combination of chemical genetics and phosphoproteomics for kinase signaling analysis enables confident identification of cellular downstream targets. Mol. Cell. Proteomics 2012, 11. (O111.012351). 10.1074/mcp.O111.012351.
    • (2012) Mol. Cell. Proteomics , vol.11
    • Oppermann, F.S.1    Grundner-Culemann, K.2    Kumar, C.3    Gruss, O.J.4    Jallepalli, P.V.5    Daub, H.6
  • 63
    • 84858439862 scopus 로고    scopus 로고
    • Insights into the regulation of protein abundance from proteomic and transcriptomic analyses
    • Vogel C., Marcotte E.M. Insights into the regulation of protein abundance from proteomic and transcriptomic analyses. Nat. Rev. Genet. 2012, 13:227-232. 10.1038/nrg3185.
    • (2012) Nat. Rev. Genet. , vol.13 , pp. 227-232
    • Vogel, C.1    Marcotte, E.M.2
  • 64
    • 0031427093 scopus 로고    scopus 로고
    • Apoptosis and proliferation under conditions of deoxynucleotide pool imbalance in liver of folate/methyl deficient rats
    • James S.J., Miller B.J., Basnakian A.G., Pogribny I.P., Pogribna M., Muskhelishvili L. Apoptosis and proliferation under conditions of deoxynucleotide pool imbalance in liver of folate/methyl deficient rats. Carcinogenesis 1997, 18:287-293.
    • (1997) Carcinogenesis , vol.18 , pp. 287-293
    • James, S.J.1    Miller, B.J.2    Basnakian, A.G.3    Pogribny, I.P.4    Pogribna, M.5    Muskhelishvili, L.6
  • 65
    • 84859866797 scopus 로고    scopus 로고
    • Stress granules contribute to α-globin homeostasis in differentiating erythroid cells
    • Ghisolfi L., Dutt S., McConkey M.E., Ebert B.L., Anderson P. Stress granules contribute to α-globin homeostasis in differentiating erythroid cells. Biochem. Biophys. Res. Commun. 2012, 420:768-774. 10.1016/j.bbrc.2012.03.070.
    • (2012) Biochem. Biophys. Res. Commun. , vol.420 , pp. 768-774
    • Ghisolfi, L.1    Dutt, S.2    McConkey, M.E.3    Ebert, B.L.4    Anderson, P.5
  • 66
    • 33746516731 scopus 로고    scopus 로고
    • HnRNP A1 relocalization to the stress granules reflects a role in the stress response
    • Guil S., Long J.C., Cáceres J.F. hnRNP A1 relocalization to the stress granules reflects a role in the stress response. Mol. Cell Biol. 2006, 26:5744-5758. 10.1128/MCB.00224-06.
    • (2006) Mol. Cell Biol. , vol.26 , pp. 5744-5758
    • Guil, S.1    Long, J.C.2    Cáceres, J.F.3
  • 67
    • 34548550361 scopus 로고    scopus 로고
    • The exon-junction-complex-component metastatic lymph node 51 functions in stress-granule assembly
    • Baguet A., Degot S., Cougot N., Bertrand E., Chenard M.-P., Wendling C., et al. The exon-junction-complex-component metastatic lymph node 51 functions in stress-granule assembly. J. Cell Sci. 2007, 120:2774-2784. 10.1242/jcs.009225.
    • (2007) J. Cell Sci. , vol.120 , pp. 2774-2784
    • Baguet, A.1    Degot, S.2    Cougot, N.3    Bertrand, E.4    Chenard, M.-P.5    Wendling, C.6
  • 68
    • 84055178425 scopus 로고    scopus 로고
    • Critical roles of RNA helicase DDX3 and its interactions with eIF4E/PABP1 in stress granule assembly and stress response
    • Shih J.-W., Wang W.-T., Tsai T.-Y., Kuo C.-Y., Li H.-K., Lee Y.-H.Wu. Critical roles of RNA helicase DDX3 and its interactions with eIF4E/PABP1 in stress granule assembly and stress response. Biochem. J. 2012, 441:119-129. 10.1042/BJ20110739.
    • (2012) Biochem. J. , vol.441 , pp. 119-129
    • Shih, J.-W.1    Wang, W.-T.2    Tsai, T.-Y.3    Kuo, C.-Y.4    Li, H.-K.5    Lee, Y.-H.6
  • 69
    • 34247360454 scopus 로고    scopus 로고
    • Probing the mRNA processing body using protein macroarrays and "autoantigenomics"
    • Yang W.-H., Bloch D.B. Probing the mRNA processing body using protein macroarrays and "autoantigenomics". RNA 2007, 13:704-712. 10.1261/rna.411907.
    • (2007) RNA , vol.13 , pp. 704-712
    • Yang, W.-H.1    Bloch, D.B.2
  • 70
    • 80051713296 scopus 로고    scopus 로고
    • Angiogenin-induced tRNA fragments inhibit translation initiation
    • Ivanov P., Emara M.M., Villen J., Gygi S.P., Anderson P. Angiogenin-induced tRNA fragments inhibit translation initiation. Mol. Cell 2011, 43:613-623. 10.1016/j.molcel.2011.06.022.
    • (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
  • 71
    • 0025780867 scopus 로고
    • DNA binding properties of YB-1 and dbpA: binding to double-stranded, single-stranded, and abasic site containing DNAs
    • Hasegawa S.L., Doetsch P.W., Hamilton K.K., Martin A.M., Okenquist S.A., Lenz J., et al. DNA binding properties of YB-1 and dbpA: binding to double-stranded, single-stranded, and abasic site containing DNAs. Nucleic Acids Res. 1991, 19:4915-4920.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4915-4920
    • Hasegawa, S.L.1    Doetsch, P.W.2    Hamilton, K.K.3    Martin, A.M.4    Okenquist, S.A.5    Lenz, J.6
  • 72
    • 0037972159 scopus 로고    scopus 로고
    • Induction of oxidative DNA damage by arsenite and its trivalent and pentavalent methylated metabolites in cultured human cells and isolated DNA
    • Schwerdtle T., Walter I., Mackiw I., Hartwig A. Induction of oxidative DNA damage by arsenite and its trivalent and pentavalent methylated metabolites in cultured human cells and isolated DNA. Carcinogenesis 2003, 24:967-974.
    • (2003) Carcinogenesis , vol.24 , pp. 967-974
    • Schwerdtle, T.1    Walter, I.2    Mackiw, I.3    Hartwig, A.4
  • 73
  • 74
    • 79955957616 scopus 로고    scopus 로고
    • Poly(ADP-ribose) regulates stress responses and microRNA activity in the cytoplasm
    • Leung A.K.L., Vyas S., Rood J.E., Bhutkar A., Sharp P.A., Chang P. Poly(ADP-ribose) regulates stress responses and microRNA activity in the cytoplasm. Mol. Cell 2011, 42:489-499. 10.1016/j.molcel.2011.04.015.
    • (2011) Mol. Cell , vol.42 , pp. 489-499
    • Leung, A.K.L.1    Vyas, S.2    Rood, J.E.3    Bhutkar, A.4    Sharp, P.A.5    Chang, P.6
  • 75
    • 53349165578 scopus 로고    scopus 로고
    • A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly
    • Ohn T., Kedersha N., Hickman T., Tisdale S., Anderson P. A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly. Nat. Cell Biol. 2008, 10:1224-1231. 10.1038/ncb1783.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1224-1231
    • Ohn, T.1    Kedersha, N.2    Hickman, T.3    Tisdale, S.4    Anderson, P.5


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