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Volumn 9, Issue 5, 2014, Pages

Proteomic analysis of Trypanosoma cruzi response to ionizing radiation stress

Author keywords

[No Author keywords available]

Indexed keywords

ISOPROTEIN; POLYPEPTIDE; PROTEOME; PROTOZOAL PROTEIN;

EID: 84901368845     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0097526     Document Type: Article
Times cited : (15)

References (48)
  • 3
    • 84876524000 scopus 로고    scopus 로고
    • Vaccination using recombinants influenza and adenoviruses encoding amastigote surface protein-2 are highly effective on protection against Trypanosoma cruzi infection
    • Barbosa RPA, Galvao B, Dos Santos LI, Sales PA, Marques PE, et al. (2013) Vaccination using recombinants influenza and adenoviruses encoding amastigote surface protein-2 are highly effective on protection against Trypanosoma cruzi infection. Plos One 8: e61795.
    • (2013) Plos One , vol.8
    • Barbosa, R.P.A.1    Galvao, B.2    Dos Santos, L.I.3    Sales, P.A.4    Marques, P.E.5
  • 4
    • 84883372900 scopus 로고    scopus 로고
    • Benznidazole and posaconazole in experimental Chagas disease: Positive interaction in concomitant and sequential treatments
    • Diniz LF, Urbina JA, De Andrade IM, Mazzeti AL, Martins TAF, et al. (2013) Benznidazole and posaconazole in experimental Chagas disease: positive interaction in concomitant and sequential treatments. PLoS neglected tropical diseases 7: e2367.
    • (2013) PLoS Neglected Tropical Diseases , vol.7
    • Diniz, L.F.1    Urbina, J.A.2    De Andrade, I.M.3    Mazzeti, A.L.4    Martins, T.A.F.5
  • 5
    • 77954207000 scopus 로고    scopus 로고
    • Chagas disease: Pushing through the pipeline
    • Clayton J (2010) Chagas disease: pushing through the pipeline. Nature 465: S12-S15.
    • (2010) Nature , vol.465
    • Clayton, J.1
  • 10
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • Stadtman ER (1993) Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu Rev Biochem 62: 797-821.
    • (1993) Annu Rev Biochem , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 11
    • 0022310512 scopus 로고
    • Chemical changes induced in DNA by ionizing radiation
    • Hutchinson F (1985) Chemical changes induced in DNA by ionizing radiation. Proc Nucleic Acid Res Mol Biol 32: 115-154.
    • (1985) Proc Nucleic Acid Res Mol Biol , vol.32 , pp. 115-154
    • Hutchinson, F.1
  • 12
    • 0027954494 scopus 로고
    • Free radicals in biology: Oxidative stress and the effects of ionizing radiation
    • Riley PA (1994) Free radicals in biology: oxidative stress and the effects of ionizing radiation. Int J Radiat Biol 65: 27-33.
    • (1994) Int J Radiat Biol , vol.65 , pp. 27-33
    • Riley, P.A.1
  • 13
    • 84876558612 scopus 로고    scopus 로고
    • Extremophiles Microbiology and Biotechnology
    • Gwin KR, Battista JR, editors. Caister Academic Press
    • Anitori RP (2012) Extremophiles Microbiology and Biotechnology. In: Gwin KR, Battista JR, editors.Ionizing-radiation resistant microorganisms. Caister Academic Press.pp. 25-52.
    • (2012) Ionizing-radiation Resistant Microorganisms , pp. 25-52
    • Anitori, R.P.1
  • 14
    • 33845545984 scopus 로고    scopus 로고
    • Engineering of Deinococcus radiodurans R1 for bioprecipitation of uranium from dilute nuclear waste
    • DOI 10.1128/AEM.01362-06
    • Appukuttan D, Rao AS, Apte SK (2006) Engineering of Deinococcus radiodurans R1 for bioprecipitation of uranium from dilute nuclear waste. Applied and Environmental Microbiology 72: 7873-7878. (Pubitemid 44927696)
    • (2006) Applied and Environmental Microbiology , vol.72 , Issue.12 , pp. 7873-7878
    • Appukuttan, D.1    Rao, A.S.2    Apte, S.K.3
  • 15
    • 34247375191 scopus 로고    scopus 로고
    • Protein oxidation implicated as the primary determinant of bacterial radioresistance
    • Daly MJ, Gaidamakova EK, Matrosova VY, Vasilenko A, Zhai M, et al. (2007) Protein oxidation implicated as the primary determinant of bacterial radioresistance. PLoS Biol 5: e92
    • (2007) PLoS Biol , vol.5
    • Daly, M.J.1    Gaidamakova, E.K.2    Matrosova, V.Y.3    Vasilenko, A.4    Zhai, M.5
  • 16
    • 84856074134 scopus 로고    scopus 로고
    • Gamma radiation-induced proteome of Deinococcus radiodurans primarily targets DNA repair and oxidative stress alleviation
    • Basu B, Apte SK (2012) Gamma radiation-induced proteome of Deinococcus radiodurans primarily targets DNA repair and oxidative stress alleviation. Molecular & cellular proteomics 11: 1.
    • (2012) Molecular & Cellular Proteomics , vol.11 , pp. 1
    • Basu, B.1    Apte, S.K.2
  • 18
    • 0028214539 scopus 로고
    • A common pyrimidine-rich motif governs trans-splicing and polyadenylation of tubulin polycistronic pre-mRNA in trypanosomes
    • Matthews KR, Tschudi C, Ullu E (1994) A common pyrimidine-rich motif governs trans-splicing and polyadenylation of tubulin polycistronic pre-mRNA in trypanosomes. Genes Dev 8: 491-501. (Pubitemid 24071188)
    • (1994) Genes and Development , vol.8 , Issue.4 , pp. 491-501
    • Matthews, K.R.1    Tschadi, C.2    Ullu, E.3
  • 19
    • 0034616415 scopus 로고    scopus 로고
    • AU-rich elements in the 3'-untranslated region of a new mucin-type gene family of Trypanosoma cruzi confers mRNA instability and modulates translation efficiency
    • DOI 10.1074/jbc.275.14.10218
    • Di Noia JM, D'Orso I, Sánchez DO, Frasch ACC (2000) AU-rich elements in the 3-untranslated region of a new mucin-type gene family of Trypanosoma cruzi confers mRNA instability and modulates translation efficiency. J Biol Chem 275: 10218-10227. (Pubitemid 30202078)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.14 , pp. 10218-10227
    • Di, N.J.M.1    D'Orso, I.2    Sanchez, D.O.3    Frasch, A.C.C.4
  • 20
    • 0035844181 scopus 로고    scopus 로고
    • Functionally different AU- and G-rich cis-elements confer developmentally regulated mRNA stability in Trypanosoma cruzi by interaction with specific RNA-binding proteins
    • D'Orso I, Frasch AC (2001) Functionally different AU- and G-rich cis-elements confer developmentally regulated mRNA stability in Trypanosoma cruzi by interaction with specific RNA-binding proteins. J Biol Chem 276: 15783-15793.
    • (2001) J Biol Chem , vol.276 , pp. 15783-15793
    • D'Orso, I.1    Frasch, A.C.2
  • 23
    • 84864953147 scopus 로고    scopus 로고
    • Evolutionary conservation and diversification of the translation initiation apparatus in Trypanosomatids
    • Zinoviev A, Shapira M (2012) Evolutionary conservation and diversification of the translation initiation apparatus in Trypanosomatids. Comparative and Functional Genomics 2012: 1-10.
    • (2012) Comparative and Functional Genomics , vol.2012 , pp. 1-10
    • Zinoviev, A.1    Shapira, M.2
  • 25
    • 21244495253 scopus 로고    scopus 로고
    • The development of the DIGE system: 2D fluorescence difference gel analysis technology
    • DOI 10.1007/s00216-005-3126-3
    • Marouga R, David S, Hawkins E (2005) The development of the DIGE system: 2D fluorescence difference gel analysis technology. Anal Bioanal Chem 382: 669-678. (Pubitemid 40890994)
    • (2005) Analytical and Bioanalytical Chemistry , vol.382 , Issue.3 , pp. 669-678
    • Marouga, R.1    David, S.2    Hawkins, E.3
  • 29
    • 28444475607 scopus 로고    scopus 로고
    • Correlation between mRNA and protein abundance in Desulfovibrio vulgaris: A multiple regression to identify sources of variations
    • DOI 10.1016/j.bbrc.2005.11.055, PII S0006291X05025842
    • Nie L, Wu G, Zhang W (2006) Correlation between mRNA and protein abundance in Desulfovibrio vulgaris: a multiple regression to identify sources of variations. Biochemical and biophysical research communications 339: 603-610. (Pubitemid 41739710)
    • (2006) Biochemical and Biophysical Research Communications , vol.339 , Issue.2 , pp. 603-610
    • Nie, L.1    Wu, G.2    Zhang, W.3
  • 30
    • 84859611662 scopus 로고    scopus 로고
    • Comparative analysis of different label-free mass spectrometry based protein abundance estimates and their correlation with RNA-Seq gene expression data
    • Ning K, Fermin D, Nesvizhskii AI (2012) Comparative analysis of different label-free mass spectrometry based protein abundance estimates and their correlation with RNA-Seq gene expression data. Journal of proteome research 11: 2261-2271.
    • (2012) Journal of Proteome Research , vol.11 , pp. 2261-2271
    • Ning, K.1    Fermin, D.2    Nesvizhskii, A.I.3
  • 31
    • 84871874013 scopus 로고    scopus 로고
    • Comparative proteomics of two life cycle stages of stable isotope-labeled Trypanosoma brucei reveals novel components of the parasite's host adaptation machinery
    • Butter F, Bucerius F, Michel M, Cicova Z, Mann M, et al. (2013) Comparative proteomics of two life cycle stages of stable isotope-labeled Trypanosoma brucei reveals novel components of the parasite's host adaptation machinery. Molecular & Cellular Proteomics 12: 172-179.
    • (2013) Molecular & Cellular Proteomics , vol.12 , pp. 172-179
    • Butter, F.1    Bucerius, F.2    Michel, M.3    Cicova, Z.4    Mann, M.5
  • 32
    • 84865448443 scopus 로고    scopus 로고
    • Comparative proteomics reveals a significant bias toward alternative protein isoforms with conserved structure and function
    • Ezkurdia I, del Pozo A, Frankish A, Rodriguez JM, Harrow J, et al. (2012) Comparative proteomics reveals a significant bias toward alternative protein isoforms with conserved structure and function. Molecular biology and evolution 29: 2265-2283.
    • (2012) Molecular Biology and Evolution , vol.29 , pp. 2265-2283
    • Ezkurdia, I.1    Del Pozo, A.2    Frankish, A.3    Rodriguez, J.M.4    Harrow, J.5
  • 33
    • 79955619183 scopus 로고    scopus 로고
    • Trans-splicing in trypanosomes: Machinery and its impact on the parasite transcriptome
    • Michaeli S (2011) Trans-splicing in trypanosomes: machinery and its impact on the parasite transcriptome. Future microbiology 6: 459-474.
    • (2011) Future Microbiology , vol.6 , pp. 459-474
    • Michaeli, S.1
  • 35
    • 58349118483 scopus 로고    scopus 로고
    • Quantitative protein expression profiling reveals extensive post-transcriptional regulation and post-translational modifications in schizont-stage malaria parasites
    • Foth BJ, Zhang N, Mok S, Preiser PR, Bozdech Z (2008) Quantitative protein expression profiling reveals extensive post-transcriptional regulation and post-translational modifications in schizont-stage malaria parasites. Genome biology 9: 177.
    • (2008) Genome Biology , vol.9 , pp. 177
    • Foth, B.J.1    Zhang, N.2    Mok, S.3    Preiser, P.R.4    Bozdech, Z.5
  • 36
    • 0141521671 scopus 로고    scopus 로고
    • The interplay between folding-facilitating mechanisms in Trypanosoma cruzi endoplasmic reticulum
    • DOI 10.1091/mbc.E03-04-0228
    • Conte L, Labriola C, Cazzulo JJ, Docampo R, Parodi AJ (2003) The interplay between folding-facilitating mechanisms in Trypanosoma cruzi endoplasmic reticulum. Molecular Biology of The Cell 14: 3529-3540. (Pubitemid 37151606)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.9 , pp. 3529-3540
    • Conte, I.1    Labriola, C.2    Cazzulo, J.J.3    Docampo, R.4    Parodi, A.J.5
  • 37
    • 0027416155 scopus 로고
    • Evolution of glutamate dehydrogenase genes: Evidence for two paralogous protein families and unusual branching patterns of the archaebacteria in the universal tree of life
    • Benachenhou-Lafha N, Forterre P, Labedan B (1993) Evolution of glutamate dehydrogenase genes: evidence for two paralogous protein families and unusual branching patterns of the archaebacteria in the universal tree of life. J Mol Evol 36: 335-346. (Pubitemid 23121901)
    • (1993) Journal of Molecular Evolution , vol.36 , Issue.4 , pp. 335-346
    • Benachenhou-Lahfa, N.1    Forterre, P.2    Labedan, B.3
  • 38
    • 0032031552 scopus 로고    scopus 로고
    • The NADP+-linked glutamate dehydrogenase from Trypanosoma cruzi: Sequence, genomic organization and expression
    • Barderi P, Campetella O, Frasch ACC, Santome JA, Hellman U, et al. (1998) The NADP+-linked glutamate dehydrogenase from Trypanosoma cruzi: sequence, genomic organization and expression. Biochem J 330: 951-958.
    • (1998) Biochem J , vol.330 , pp. 951-958
    • Barderi, P.1    Campetella, O.2    Frasch, A.C.C.3    Santome, J.A.4    Hellman, U.5
  • 39
    • 49349112856 scopus 로고    scopus 로고
    • Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism
    • Krauth-Siegel RL, Comini MA (2008) Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism. Biochimica et Biophysica Acta 1780: 1236-1248.
    • (2008) Biochimica et Biophysica Acta , vol.1780 , pp. 1236-1248
    • Krauth-Siegel, R.L.1    Comini, M.A.2
  • 40
    • 84879758470 scopus 로고    scopus 로고
    • Biology of extreme radiation resistance: The way of Deinococcus radiodurans
    • Krisko A, Radman M (2013) Biology of extreme radiation resistance: The way of Deinococcus radiodurans. Cold Spring Harb Perspect Biol 5: 1-11.
    • (2013) Cold Spring Harb Perspect Biol , vol.5 , pp. 1-11
    • Krisko, A.1    Radman, M.2
  • 42
    • 77956269639 scopus 로고    scopus 로고
    • Protein damage and death by radiation in Escherichia coli and Deinococcus radiodurans
    • Krisko A, Radman M (2010) Protein damage and death by radiation in Escherichia coli and Deinococcus radiodurans. Proc Natl Acad Sci USA 107: 14373-14377.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 14373-14377
    • Krisko, A.1    Radman, M.2
  • 44
    • 79952799384 scopus 로고    scopus 로고
    • A major role for nonenzymatic antioxidant processes in the radioresistance of Halobacterium salinarum
    • Robinson CK, Webb K, Kaur A, Jaruga P, Dizdaroglu M, et al.(2011) A major role for nonenzymatic antioxidant processes in the radioresistance of Halobacterium salinarum. Journal of bacteriology 193: 1653-1662.
    • (2011) Journal of Bacteriology , vol.193 , pp. 1653-1662
    • Robinson, C.K.1    Webb, K.2    Kaur, A.3    Jaruga, P.4    Dizdaroglu, M.5
  • 45
    • 84855352363 scopus 로고    scopus 로고
    • Death by protein damage in irradiated cells
    • Daly MJ (2012) Death by protein damage in irradiated cells. DNA repair 11: 12-21.
    • (2012) DNA Repair , vol.11 , pp. 12-21
    • Daly, M.J.1
  • 47
    • 13244258359 scopus 로고    scopus 로고
    • Proteomic analysis of Deinococcus radiodurans recovering from gamma-irradiation
    • DOI 10.1002/pmic.200300875
    • Zhang C, Wei J, Zheng Z, Ying N, Sheng D, et al. (2005) Proteomic analysis of Deinococcus radiodurans recovering from gamma-irradiation. Proteomics 5: 138-143. (Pubitemid 40189646)
    • (2005) Proteomics , vol.5 , Issue.1 , pp. 138-143
    • Zhang, C.1    Wei, J.2    Zheng, Z.3    Ying, N.4    Sheng, D.5    Hua, Y.6
  • 48
    • 84893743575 scopus 로고    scopus 로고
    • There are more small amino acids and fewer aromatic rings in proteins of ionizing radiation-resistant bacteria
    • Sghaier H, Thorvaldsen S, Saied NM (2013) There are more small amino acids and fewer aromatic rings in proteins of ionizing radiation-resistant bacteria. Annals of Microbiology 1-9.
    • (2013) Annals of Microbiology , pp. 1-9
    • Sghaier, H.1    Thorvaldsen, S.2    Saied, N.M.3


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