메뉴 건너뛰기




Volumn 403, Issue 2, 2010, Pages 220-224

Human proteins that specifically bind to 8-oxoguanine-containing RNA and their responses to oxidative stress

Author keywords

Binding protein; HNRNPC; HNRNPD; Oxidative stress

Indexed keywords

8 HYDROXYGUANINE; CELL EXTRACT; HYDROGEN PEROXIDE; ISOPROTEIN; NUCLEAR PROTEIN; RIBONUCLEOPROTEIN; RNA; SMALL INTERFERING RNA;

EID: 78649911059     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.11.011     Document Type: Article
Times cited : (39)

References (23)
  • 1
    • 84967683966 scopus 로고    scopus 로고
    • Yin and yan of mitochondrial ROS
    • Imperial College Press, London, K.K. Singh (Ed.)
    • Starskov A., Wallace K.B. Yin and yan of mitochondrial ROS. Oxidative Stress, Disease and Cancer 2006, 1-60. Imperial College Press, London. K.K. Singh (Ed.).
    • (2006) Oxidative Stress, Disease and Cancer , pp. 1-60
    • Starskov, A.1    Wallace, K.B.2
  • 2
    • 0028342951 scopus 로고
    • Repair of oxidative damage to DNA: enzyme and biology
    • Demple B., Harrison L. Repair of oxidative damage to DNA: enzyme and biology. Annu. Rev. Biochem. 1994, 63:915-948.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 915-948
    • Demple, B.1    Harrison, L.2
  • 3
    • 84967436535 scopus 로고    scopus 로고
    • Oxidative damage to nucleotide: consequences and preventive mechanisms
    • Imperial College Press, London, K.K. Singh (Ed.)
    • Nakatsu Y., Sekiguchi M. Oxidative damage to nucleotide: consequences and preventive mechanisms. Oxidative Stress, Disease and Cancer 2006, 221-252. Imperial College Press, London. K.K. Singh (Ed.).
    • (2006) Oxidative Stress, Disease and Cancer , pp. 221-252
    • Nakatsu, Y.1    Sekiguchi, M.2
  • 4
    • 0022809670 scopus 로고
    • Formation of 8-hydroxyguanine moiety in cellular DNA by agents producing oxygen radicals and evidence for its repair
    • Kasai H., Crain P.F., Kuchino Y., et al. Formation of 8-hydroxyguanine moiety in cellular DNA by agents producing oxygen radicals and evidence for its repair. Carcinogenesis 1986, 7:1849-1851.
    • (1986) Carcinogenesis , vol.7 , pp. 1849-1851
    • Kasai, H.1    Crain, P.F.2    Kuchino, Y.3
  • 5
    • 0025902273 scopus 로고
    • Endogenous mutagens and the causes of aging and cancer
    • Ames B.N., Gold L.S. Endogenous mutagens and the causes of aging and cancer. Mutat. Res. 1991, 250:3-16.
    • (1991) Mutat. Res. , vol.250 , pp. 3-16
    • Ames, B.N.1    Gold, L.S.2
  • 6
    • 0030879766 scopus 로고    scopus 로고
    • Counteraction by MutT protein of translational errors caused by oxidative damage
    • Taddei F., Hayakawa H., Bouton M., et al. Counteraction by MutT protein of translational errors caused by oxidative damage. Science 1997, 278:128-130.
    • (1997) Science , vol.278 , pp. 128-130
    • Taddei, F.1    Hayakawa, H.2    Bouton, M.3
  • 7
    • 20444440728 scopus 로고    scopus 로고
    • Structure of the cross-β spine of amyloid-like fibrils
    • Nelson R., Sawaya M.R., Balbirnie M., et al. Structure of the cross-β spine of amyloid-like fibrils. Nature 2005, 435:773-778.
    • (2005) Nature , vol.435 , pp. 773-778
    • Nelson, R.1    Sawaya, M.R.2    Balbirnie, M.3
  • 8
    • 77649240855 scopus 로고    scopus 로고
    • Identifying of the amylome proteins capable of forming amyloid-like fibrils
    • Goldschmidt L., Teng P.K., Riek R., Eisenberg D. Identifying of the amylome proteins capable of forming amyloid-like fibrils. Proc. Natl. Acad. Sci. USA 2010, 107:3487-3492.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 3487-3492
    • Goldschmidt, L.1    Teng, P.K.2    Riek, R.3    Eisenberg, D.4
  • 9
    • 0035928817 scopus 로고    scopus 로고
    • Specific binding of 8-oxoguanine-containing RNA to polynucleotide phosphorylase protein
    • Hayakawa H., Kuwano M., Sekiguch M. Specific binding of 8-oxoguanine-containing RNA to polynucleotide phosphorylase protein. Biochemistry 2001, 40:9977-9982.
    • (2001) Biochemistry , vol.40 , pp. 9977-9982
    • Hayakawa, H.1    Kuwano, M.2    Sekiguch, M.3
  • 10
    • 0037168641 scopus 로고    scopus 로고
    • Identification and cloning of human polynucleotide phosphorylase, hPNPase old-35 in the context of terminal differentiation and cellular senescence
    • Leszczyniecka M., Kang D., Sarkar D., et al. Identification and cloning of human polynucleotide phosphorylase, hPNPase old-35 in the context of terminal differentiation and cellular senescence. Proc. Natl. Acad. Sci. USA 2002, 99:16636-16641.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16636-16641
    • Leszczyniecka, M.1    Kang, D.2    Sarkar, D.3
  • 11
    • 0036977391 scopus 로고    scopus 로고
    • Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into six-membered PNPase-like ring
    • Rajimakers R., Egberts W.V., van Venrooji W.J., Pruijn G.J.M. Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into six-membered PNPase-like ring. J. Mol. Biol. 2002, 323:653-663.
    • (2002) J. Mol. Biol. , vol.323 , pp. 653-663
    • Rajimakers, R.1    Egberts, W.V.2    van Venrooji, W.J.3    Pruijn, G.J.M.4
  • 12
    • 0037869109 scopus 로고    scopus 로고
    • Human polynucleotide phosphorylase HPNPase, is localized in mitochondria
    • Piwowarski J., Grzechnik P., Dziembowski A., et al. Human polynucleotide phosphorylase HPNPase, is localized in mitochondria. J. Mol. Biol. 2003, 329:853-857.
    • (2003) J. Mol. Biol. , vol.329 , pp. 853-857
    • Piwowarski, J.1    Grzechnik, P.2    Dziembowski, A.3
  • 13
    • 33744752455 scopus 로고    scopus 로고
    • Human polynucleotide phosphorylase protein in response to oxidative stress
    • Hayakawa H., Sekiguchi M. Human polynucleotide phosphorylase protein in response to oxidative stress. Biochemistry 2006, 45:6749-6755.
    • (2006) Biochemistry , vol.45 , pp. 6749-6755
    • Hayakawa, H.1    Sekiguchi, M.2
  • 14
    • 44649097525 scopus 로고    scopus 로고
    • Human polynucleotide phosphorylase reduces oxidative RNA damage and protects HeLa cell against oxidative stress
    • Wu J., Li Z. Human polynucleotide phosphorylase reduces oxidative RNA damage and protects HeLa cell against oxidative stress. Biochem. Biophys. Res. Commun. 2008, 372:288-292.
    • (2008) Biochem. Biophys. Res. Commun. , vol.372 , pp. 288-292
    • Wu, J.1    Li, Z.2
  • 15
    • 67651229135 scopus 로고    scopus 로고
    • Large-scale proteomics analysis of tryrosine-phosphorylation induced by T-cell receptor or B-cell receptor activation reveals new signaling pathways
    • Matsumoto M., Oyamada K., Takahashi H., et al. Large-scale proteomics analysis of tryrosine-phosphorylation induced by T-cell receptor or B-cell receptor activation reveals new signaling pathways. Proteomics 2009, 9:3549-3563.
    • (2009) Proteomics , vol.9 , pp. 3549-3563
    • Matsumoto, M.1    Oyamada, K.2    Takahashi, H.3
  • 16
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptide per protein
    • Ishihama Y., Oda Y., Tabata T., Sato T., et al. Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptide per protein. Mol. Cell. Proteomics 2005, 4:1265-1272.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3    Sato, T.4
  • 17
    • 0029111578 scopus 로고
    • The UUAG-specific binding protein, heterogeneous nuclear ribonucleoprotein D0. Common modular structure and binding properties of the 2×BRD-Gly family
    • Kajita Y., Nakayama J., Aizawa M., Ishikawa F. The UUAG-specific binding protein, heterogeneous nuclear ribonucleoprotein D0. Common modular structure and binding properties of the 2×BRD-Gly family. J. Biol. Chem. 1995, 270:22167-22175.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22167-22175
    • Kajita, Y.1    Nakayama, J.2    Aizawa, M.3    Ishikawa, F.4
  • 18
    • 0035951294 scopus 로고    scopus 로고
    • An antiparallel four-helix bundle orients the high-affinity RNA binding sites in hnRNP C: a mechanism for RNA chaperonin activity
    • Shahied L., Braswell E.H., LeStourgeon W.M., Krezel A.M. An antiparallel four-helix bundle orients the high-affinity RNA binding sites in hnRNP C: a mechanism for RNA chaperonin activity. J. Mol. Biol. 2001, 305:817-828.
    • (2001) J. Mol. Biol. , vol.305 , pp. 817-828
    • Shahied, L.1    Braswell, E.H.2    LeStourgeon, W.M.3    Krezel, A.M.4
  • 19
    • 0037119975 scopus 로고    scopus 로고
    • Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein
    • Will C.L., Urlaub H., Achsel T., et al. Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein. EMBO J. 2002, 21:4978-4988.
    • (2002) EMBO J. , vol.21 , pp. 4978-4988
    • Will, C.L.1    Urlaub, H.2    Achsel, T.3
  • 20
    • 0034192841 scopus 로고    scopus 로고
    • Identification of two novel proteins that interact with germ-cell-specific RNA-binding proteins DAZ and DAZL1
    • Tsui S., Dai T., Roettger S., et al. Identification of two novel proteins that interact with germ-cell-specific RNA-binding proteins DAZ and DAZL1. Genomics 2000, 65:266-273.
    • (2000) Genomics , vol.65 , pp. 266-273
    • Tsui, S.1    Dai, T.2    Roettger, S.3
  • 21
    • 0029871812 scopus 로고    scopus 로고
    • Mechanisms and control of mRNA turnover in Saccharomyces cerevisiae
    • Caponigro G., Parker R. Mechanisms and control of mRNA turnover in Saccharomyces cerevisiae. Microbiol. Rev. 1996, 60:233-249.
    • (1996) Microbiol. Rev. , vol.60 , pp. 233-249
    • Caponigro, G.1    Parker, R.2
  • 22
    • 0141819096 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities
    • Lejeune F., Li X., Maquat L.E. Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities. Mol. Cell 2003, 12:675-687.
    • (2003) Mol. Cell , vol.12 , pp. 675-687
    • Lejeune, F.1    Li, X.2    Maquat, L.E.3
  • 23
    • 34547623918 scopus 로고    scopus 로고
    • Quality control of eukaryotic mRNA: safeguarding cells from abnormal mRNA function
    • Isken O., Maquat L.E. Quality control of eukaryotic mRNA: safeguarding cells from abnormal mRNA function. Gene Dev. 2007, 21:1833-1856.
    • (2007) Gene Dev. , vol.21 , pp. 1833-1856
    • Isken, O.1    Maquat, L.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.