메뉴 건너뛰기




Volumn 157, Issue 6, 2011, Pages 1573-1588

Oxidative stress-related responses of Bifidobacterium longum subsp. longum BBMN68 at the proteomic level after exposure to oxygen

Author keywords

[No Author keywords available]

Indexed keywords

ALKYL HYDROPEROXIDE REDUCTASE C22; BBMN68; CELL PROTEIN; CERULOPLASMIN; DNA BINDING FERRITIN LIKE PROTEIN; ENOLASE; IRON; NUCLEOTIDE PYROPHOSPHATASE; NUCLEOTIDE TRIPHOSPHATE; OXYGEN; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE; PROBIOTIC AGENT; PYRIDINE NUCLEOTIDE DISULFIDE REDUCTASE; RIBONUCLEOTIDE REDUCTASE; UNCLASSIFIED DRUG;

EID: 79958146340     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.044297-0     Document Type: Article
Times cited : (70)

References (67)
  • 1
    • 0034981052 scopus 로고    scopus 로고
    • Ribosomeassociated protein that inhibits translation at the aminoacyl-tRNA binding stage
    • Agafonov, D. E., Kolb, V. A. & Spirin, A. S. (2001). Ribosomeassociated protein that inhibits translation at the aminoacyl-tRNA binding stage. EMBO Rep 2, 399-402.
    • (2001) EMBO Rep , vol.2 , pp. 399-402
    • Agafonov, D.E.1    Kolb, V.A.2    Spirin, A.S.3
  • 2
    • 34147109920 scopus 로고    scopus 로고
    • Linear array of conserved sequence motifs to discriminate protein subfamilies: Study on pyridine nucleotide-disulfide reductases
    • Avila, C. L., Rapisarda, V. A., Farías, R. N., De Las Rivas, J. & Chehín, R. (2007). Linear array of conserved sequence motifs to discriminate protein subfamilies: study on pyridine nucleotide-disulfide reductases. BMC Bioinformatics 8, 96.
    • (2007) BMC Bioinformatics , vol.8 , pp. 96
    • Avila, C.L.1    Rapisarda, V.A.2    Farías, R.N.3    de Las Rivas, J.4    Chehín, R.5
  • 3
    • 0842264185 scopus 로고    scopus 로고
    • The strict anaerobe Bacteroides fragilis grows in and benefits from nanomolar concentrations of oxygen
    • Baughn, A. D. & Malamy, M. H. (2004). The strict anaerobe Bacteroides fragilis grows in and benefits from nanomolar concentrations of oxygen. Nature 427, 441-444.
    • (2004) Nature , vol.427 , pp. 441-444
    • Baughn, A.D.1    Malamy, M.H.2
  • 5
    • 54449085909 scopus 로고    scopus 로고
    • Probiotics: Overview of microbiological and immunological characteristics
    • Blandino, G., Fazio, D. & Di Marco, R. (2008). Probiotics: overview of microbiological and immunological characteristics. Expert Rev Anti Infect Ther 6, 497-508.
    • (2008) Expert Rev Anti Infect Ther , vol.6 , pp. 497-508
    • Blandino, G.1    Fazio, D.2    di Marco, R.3
  • 6
    • 0034648827 scopus 로고    scopus 로고
    • Peroxynitrite reductase activity of bacterial peroxiredoxins
    • Bryk, R., Griffin, P. & Nathan, C. (2000). Peroxynitrite reductase activity of bacterial peroxiredoxins. Nature 407, 211-215.
    • (2000) Nature , vol.407 , pp. 211-215
    • Bryk, R.1    Griffin, P.2    Nathan, C.3
  • 8
    • 35548995356 scopus 로고    scopus 로고
    • The RNA degradosome of Escherichia coli: An mRNA-degrading machine assembled on RNase E
    • Carpousis, A. J. (2007). The RNA degradosome of Escherichia coli: an mRNA-degrading machine assembled on RNase E. Annu Rev Microbiol 61, 71-87.
    • (2007) Annu Rev Microbiol , vol.61 , pp. 71-87
    • Carpousis, A.J.1
  • 10
    • 27144476584 scopus 로고    scopus 로고
    • Reassessment of protein stability, DNA binding, and protection of Mycobacterium smegmatis Dps
    • Ceci, P., Ilari, A., Falvo, E., Giangiacomo, L. & Chiancone, E. (2005). Reassessment of protein stability, DNA binding, and protection of Mycobacterium smegmatis Dps. J Biol Chem 280, 34776-34785.
    • (2005) J Biol Chem , vol.280 , pp. 34776-34785
    • Ceci, P.1    Ilari, A.2    Falvo, E.3    Giangiacomo, L.4    Chiancone, E.5
  • 11
    • 0033823598 scopus 로고    scopus 로고
    • Contribution of dps to acid stress tolerance and oxidative stress tolerance in Escherichia coli O157: H7
    • Choi, S. H., Baumler, D. J. & Kaspar, C. W. (2000). Contribution of dps to acid stress tolerance and oxidative stress tolerance in Escherichia coli O157: H7. Appl Environ Microbiol 66, 3911-3916.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 3911-3916
    • Choi, S.H.1    Baumler, D.J.2    Kaspar, C.W.3
  • 12
    • 14644397208 scopus 로고    scopus 로고
    • Cytochrome bd oxidase, oxidative stress, and dioxygen tolerance of the strictly anaerobic bacterium Moorella thermoacetica
    • Das, A., Silaghi-Dumitrescu, R., Ljungdahl, L. G. & Kurtz, D. M., Jr (2005). Cytochrome bd oxidase, oxidative stress, and dioxygen tolerance of the strictly anaerobic bacterium Moorella thermoacetica. J Bacteriol 187, 2020-2029.
    • (2005) J Bacteriol , vol.187 , pp. 2020-2029
    • Das, A.1    Silaghi-Dumitrescu, R.2    Ljungdahl, L.G.3    Kurtz Jr., D.M.4
  • 13
    • 34250900982 scopus 로고    scopus 로고
    • Base-excision repair of oxidative DNA damage
    • David, S. S., O'Shea, V. L. & Kundu, S. (2007). Base-excision repair of oxidative DNA damage. Nature 447, 941-950.
    • (2007) Nature , vol.447 , pp. 941-950
    • David, S.S.1    O'Shea, V.L.2    Kundu, S.3
  • 16
    • 0026045587 scopus 로고
    • Superoxide sensitivity of the Escherichia coli aconitase
    • Gardner, P. R. & Fridovich, I. (1991). Superoxide sensitivity of the Escherichia coli aconitase. J Biol Chem 266, 19328-19333.
    • (1991) J Biol Chem , vol.266 , pp. 19328-19333
    • Gardner, P.R.1    Fridovich, I.2
  • 17
    • 33750462020 scopus 로고    scopus 로고
    • The Streptomyces NrdR transcriptional regulator is a Zn ribbon/ATP cone protein that binds to the promoter regions of class Ia and class II ribonucleotide reductase operons
    • Grinberg, I., Shteinberg, T., Gorovitz, B., Aharonowitz, Y., Cohen, G. & Borovok, I. (2006). The Streptomyces NrdR transcriptional regulator is a Zn ribbon/ATP cone protein that binds to the promoter regions of class Ia and class II ribonucleotide reductase operons. J Bacteriol 188, 7635-7644.
    • (2006) J Bacteriol , vol.188 , pp. 7635-7644
    • Grinberg, I.1    Shteinberg, T.2    Gorovitz, B.3    Aharonowitz, Y.4    Cohen, G.5    Borovok, I.6
  • 18
    • 14744297017 scopus 로고    scopus 로고
    • Differential DNA binding and protection by dimeric and dodecameric forms of the ferritin homolog Dps from Deinococcus radiodurans
    • Grove, A. & Wilkinson, S. P. (2005). Differential DNA binding and protection by dimeric and dodecameric forms of the ferritin homolog Dps from Deinococcus radiodurans. J Mol Biol 347, 495-508.
    • (2005) J Mol Biol , vol.347 , pp. 495-508
    • Grove, A.1    Wilkinson, S.P.2
  • 19
    • 0038813712 scopus 로고    scopus 로고
    • Bimodal protection of DNA by Mycobacterium smegmatis DNA-binding protein from stationary phase cells
    • Gupta, S. & Chatterji, D. (2003). Bimodal protection of DNA by Mycobacterium smegmatis DNA-binding protein from stationary phase cells. J Biol Chem 278, 5235-5241.
    • (2003) J Biol Chem , vol.278 , pp. 5235-5241
    • Gupta, S.1    Chatterji, D.2
  • 20
    • 75849150278 scopus 로고    scopus 로고
    • Dps-like proteins: Structural and functional insights into a versatile protein family
    • Haikarainen, T. & Papageorgiou, A. C. (2010). Dps-like proteins: structural and functional insights into a versatile protein family. Cell Mol Life Sci 67, 341-351.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 341-351
    • Haikarainen, T.1    Papageorgiou, A.C.2
  • 21
    • 0842326209 scopus 로고    scopus 로고
    • The ferritin-like Dps protein is required for Salmonella enterica serovar Typhimurium oxidative stress resistance and virulence
    • Halsey, T. A., Vazquez-Torres, A., Gravdahl, D. J., Fang, F. C. & Libby, S. J. (2004). The ferritin-like Dps protein is required for Salmonella enterica serovar Typhimurium oxidative stress resistance and virulence. Infect Immun 72, 1155-1158.
    • (2004) Infect Immun , vol.72 , pp. 1155-1158
    • Halsey, T.A.1    Vazquez-Torres, A.2    Gravdahl, D.J.3    Fang, F.C.4    Libby, S.J.5
  • 22
    • 78751512475 scopus 로고    scopus 로고
    • Complete genome sequence of Bifidobacterium longum subsp. longum BBMN68, a new strain from healthy Chinese centenarian
    • other authors
    • Hao, Y., Huang, D., Guo, H., Xiao, M., An, H., Zhao, L., Zuo, F., Zhang, B., Hu, S. & other authors (2011). Complete genome sequence of Bifidobacterium longum subsp. longum BBMN68, a new strain from healthy Chinese centenarian. J Bacteriol 193, 787-788.
    • (2011) J Bacteriol , vol.193 , pp. 787-788
    • Hao, Y.1    Huang, D.2    Guo, H.3    Xiao, M.4    An, H.5    Zhao, L.6    Zuo, F.7    Zhang, B.8    Hu, S.9
  • 23
    • 33744752455 scopus 로고    scopus 로고
    • Human polynucleotide phosphorylase protein in response to oxidative stress
    • Hayakawa, H. & Sekiguchi, M. (2006). Human polynucleotide phosphorylase protein in response to oxidative stress. Biochemistry 45, 6749-6755.
    • (2006) Biochemistry , vol.45 , pp. 6749-6755
    • Hayakawa, H.1    Sekiguchi, M.2
  • 24
    • 77950610038 scopus 로고    scopus 로고
    • Upregulation of a non-heme iron-containing ferritin with dual ferroxidase and DNA-binding activities in Helicobacter pylori under acid stress
    • Huang, C. H., Lee, I. L., Yeh, I. J., Liao, J. H., Ni, C. L., Wu, S. H. & Chiou, S. H. (2010). Upregulation of a non-heme iron-containing ferritin with dual ferroxidase and DNA-binding activities in Helicobacter pylori under acid stress. J Biochem 147, 535-543.
    • (2010) J Biochem , vol.147 , pp. 535-543
    • Huang, C.H.1    Lee, I.L.2    Yeh, I.J.3    Liao, J.H.4    Ni, C.L.5    Wu, S.H.6    Chiou, S.H.7
  • 26
    • 33750051645 scopus 로고    scopus 로고
    • Response of the microaerophilic Bifidobacterium species, B. boum and B. thermophilum, to oxygen
    • Kawasaki, S., Mimura, T., Satoh, T., Takeda, K. & Niimura, Y. (2006). Response of the microaerophilic Bifidobacterium species, B. boum and B. thermophilum, to oxygen. Appl Environ Microbiol 72, 6854-6858.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 6854-6858
    • Kawasaki, S.1    Mimura, T.2    Satoh, T.3    Takeda, K.4    Niimura, Y.5
  • 27
    • 59949105355 scopus 로고    scopus 로고
    • 2-responsive NADH: Rubredoxin oxidoreductaseflavoprotein A2-desulfoferrodoxin operon enzymes, rubperoxin, and rubredoxin, in Clostridium acetobutylicum
    • 2-responsive NADH: rubredoxin oxidoreductaseflavoprotein A2-desulfoferrodoxin operon enzymes, rubperoxin, and rubredoxin, in Clostridium acetobutylicum. Appl Environ Microbiol 75, 1021-1029.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 1021-1029
    • Kawasaki, S.1    Sakai, Y.2    Takahashi, T.3    Suzuki, I.4    Niimura, Y.5
  • 29
    • 23944479421 scopus 로고    scopus 로고
    • Lessons from the genomes of bifidobacteria
    • Klijn, A., Mercenier, A. & Arigoni, F. (2005). Lessons from the genomes of bifidobacteria. FEMS Microbiol Rev 29, 491-509.
    • (2005) FEMS Microbiol Rev , vol.29 , pp. 491-509
    • Klijn, A.1    Mercenier, A.2    Arigoni, F.3
  • 30
    • 44849097452 scopus 로고    scopus 로고
    • The hyperthermophilic anaerobe Thermotoga Maritima is able to cope with limited amount of oxygen: Insights into its defence strategies
    • Le Fourn, C., Fardeau, M. L., Ollivier, B., Lojou, E. & Dolla, A. (2008). The hyperthermophilic anaerobe Thermotoga Maritima is able to cope with limited amount of oxygen: insights into its defence strategies. Environ Microbiol 10, 1877-1887.
    • (2008) Environ Microbiol , vol.10 , pp. 1877-1887
    • le Fourn, C.1    Fardeau, M.L.2    Ollivier, B.3    Lojou, E.4    Dolla, A.5
  • 31
    • 14044257165 scopus 로고    scopus 로고
    • Protein thiol modifications visualized in vivo
    • Leichert, L. I. & Jakob, U. (2004). Protein thiol modifications visualized in vivo. PLoS Biol 2, e333.
    • (2004) PLoS Biol , vol.2
    • Leichert, L.I.1    Jakob, U.2
  • 32
    • 0027006036 scopus 로고
    • A specific stain for the detection of nonheme iron proteins in polyacrylamide gels
    • Leong, L. M., Tan, B. H. & Ho, K. K. (1992). A specific stain for the detection of nonheme iron proteins in polyacrylamide gels. Anal Biochem 207, 317-320.
    • (1992) Anal Biochem , vol.207 , pp. 317-320
    • Leong, L.M.1    Tan, B.H.2    Ho, K.K.3
  • 33
    • 33846407246 scopus 로고    scopus 로고
    • The anaerobe Desulfovibrio desulfuricans ATCC 27774 grows at nearly atmospheric oxygen levels
    • Lobo, S. A., Melo, A. M., Carita, J. N., Teixeira, M. & Saraiva, L. M. (2007). The anaerobe Desulfovibrio desulfuricans ATCC 27774 grows at nearly atmospheric oxygen levels. FEBS Lett 581, 433-436.
    • (2007) FEBS Lett , vol.581 , pp. 433-436
    • Lobo, S.A.1    Melo, A.M.2    Carita, J.N.3    Teixeira, M.4    Saraiva, L.M.5
  • 34
    • 59849097794 scopus 로고    scopus 로고
    • New insights into the role of Fur proteins: FurB (All2473) from Anabaena protects DNA and increases cell survival under oxidative stress
    • López-Gomollón, S., Sevilla, E., Bes, M. T., Peleato, M. L. & Fillat, M. F. (2009). New insights into the role of Fur proteins: FurB (All2473) from Anabaena protects DNA and increases cell survival under oxidative stress. Biochem J 418, 201-207.
    • (2009) Biochem J , vol.418 , pp. 201-207
    • López-Gomollón, S.1    Sevilla, E.2    Bes, M.T.3    Peleato, M.L.4    Fillat, M.F.5
  • 35
    • 77956258367 scopus 로고    scopus 로고
    • Mycobacterial MazG is a novel NTP pyrophosphohydrolase involved in oxidative stress response
    • Lu, L. D., Sun, Q., Fan, X. Y., Zhong, Y., Yao, Y. F. & Zhao, G. P. (2010). Mycobacterial MazG is a novel NTP pyrophosphohydrolase involved in oxidative stress response. J Biol Chem 285, 28076-28085.
    • (2010) J Biol Chem , vol.285 , pp. 28076-28085
    • Lu, L.D.1    Sun, Q.2    Fan, X.Y.3    Zhong, Y.4    Yao, Y.F.5    Zhao, G.P.6
  • 36
    • 0026513966 scopus 로고
    • MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis
    • Maki, H. & Sekiguchi, M. (1992). MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis. Nature 355, 273-275.
    • (1992) Nature , vol.355 , pp. 273-275
    • Maki, H.1    Sekiguchi, M.2
  • 37
    • 21244451548 scopus 로고    scopus 로고
    • Culture-dependent and culture-independent qualitative analysis of probiotic products claimed to contain bifidobacteria
    • Masco, L., Huys, G., De Brandt, E., Temmerman, R. & Swings, J. (2005). Culture-dependent and culture-independent qualitative analysis of probiotic products claimed to contain bifidobacteria. Int J Food Microbiol 102, 221-230.
    • (2005) Int J Food Microbiol , vol.102 , pp. 221-230
    • Masco, L.1    Huys, G.2    de Brandt, E.3    Temmerman, R.4    Swings, J.5
  • 38
    • 33748127928 scopus 로고    scopus 로고
    • Antimicrobial susceptibility of Bifidobacterium strains from humans, animals and probiotic products
    • Masco, L., Van Hoorde, K., De Brandt, E., Swings, J. & Huys, G. (2006). Antimicrobial susceptibility of Bifidobacterium strains from humans, animals and probiotic products. J Antimicrob Chemother 58, 85-94.
    • (2006) J Antimicrob Chemother , vol.58 , pp. 85-94
    • Masco, L.1    van Hoorde, K.2    de Brandt, E.3    Swings, J.4    Huys, G.5
  • 40
    • 0035947685 scopus 로고    scopus 로고
    • Expression analysis of the nrdHIEF operon from Escherichia coli. Conditions that trigger the transcript level in vivo
    • Monje-Casas, F., Jurado, J., Prieto-Alamo, M. J., Holmgren, A. & Pueyo, C. (2001). Expression analysis of the nrdHIEF operon from Escherichia coli. Conditions that trigger the transcript level in vivo. J Biol Chem 276, 18031-18037.
    • (2001) J Biol Chem , vol.276 , pp. 18031-18037
    • Monje-Casas, F.1    Jurado, J.2    Prieto-Alamo, M.J.3    Holmgren, A.4    Pueyo, C.5
  • 42
    • 3042662444 scopus 로고    scopus 로고
    • Dps protects cells against multiple stresses during stationary phase
    • Nair, S. & Finkel, S. E. (2004). Dps protects cells against multiple stresses during stationary phase. J Bacteriol 186, 4192-4198.
    • (2004) J Bacteriol , vol.186 , pp. 4192-4198
    • Nair, S.1    Finkel, S.E.2
  • 43
    • 34548845570 scopus 로고    scopus 로고
    • The active site cysteine of the proapoptotic protein glyceraldehyde-3-phosphate dehydrogenase is essential in oxidative stress-induced aggregation and cell death
    • Nakajima, H., Amano, W., Fujita, A., Fukuhara, A., Azuma, Y. T., Hata, F., Inui, T. & Takeuchi, T. (2007). The active site cysteine of the proapoptotic protein glyceraldehyde-3-phosphate dehydrogenase is essential in oxidative stress-induced aggregation and cell death. J Biol Chem 282, 26562-26574.
    • (2007) J Biol Chem , vol.282 , pp. 26562-26574
    • Nakajima, H.1    Amano, W.2    Fujita, A.3    Fukuhara, A.4    Azuma, Y.T.5    Hata, F.6    Inui, T.7    Takeuchi, T.8
  • 44
  • 45
    • 0032851571 scopus 로고    scopus 로고
    • Role of the alkyl hydroperoxide reductase (ahpCF) gene in oxidative stress defense of the obligate anaerobe Bacteroides fragilis
    • Rocha, E. R. & Smith, C. J. (1999). Role of the alkyl hydroperoxide reductase (ahpCF) gene in oxidative stress defense of the obligate anaerobe Bacteroides fragilis. J Bacteriol 181, 5701-5710.
    • (1999) J Bacteriol , vol.181 , pp. 5701-5710
    • Rocha, E.R.1    Smith, C.J.2
  • 47
    • 59149085483 scopus 로고    scopus 로고
    • RecFOR and RecOR as distinct RecA loading pathways
    • Sakai, A. & Cox, M. M. (2009). RecFOR and RecOR as distinct RecA loading pathways. J Biol Chem 284, 3264-3272.
    • (2009) J Biol Chem , vol.284 , pp. 3264-3272
    • Sakai, A.1    Cox, M.M.2
  • 51
    • 34547619421 scopus 로고    scopus 로고
    • Oxidative DNA damage defense systems in avoidance of stationaryphase mutagenesis in Pseudomonas putida
    • Saumaa, S., Tover, A., Tark, M., Tegova, R. & Kivisaar, M. (2007). Oxidative DNA damage defense systems in avoidance of stationaryphase mutagenesis in Pseudomonas putida. J Bacteriol 189, 5504-5514.
    • (2007) J Bacteriol , vol.189 , pp. 5504-5514
    • Saumaa, S.1    Tover, A.2    Tark, M.3    Tegova, R.4    Kivisaar, M.5
  • 53
    • 0030072561 scopus 로고    scopus 로고
    • MutT-related error avoidance mechanism for DNA synthesis
    • Sekiguchi, M. (1996). MutT-related error avoidance mechanism for DNA synthesis. Genes Cells 1, 139-145.
    • (1996) Genes Cells , vol.1 , pp. 139-145
    • Sekiguchi, M.1
  • 54
    • 0034166933 scopus 로고    scopus 로고
    • Probiotic bacteria: Selective enumeration and survival in dairy foods
    • Shah, N. P. (2000). Probiotic bacteria: selective enumeration and survival in dairy foods. J Dairy Sci 83, 894-907.
    • (2000) J Dairy Sci , vol.83 , pp. 894-907
    • Shah, N.P.1
  • 55
    • 0027013345 scopus 로고
    • Relationship between oxygen sensitivity and oxygen metabolism of Bifidobacterium species
    • Shimamura, S., Abe, F., Ishibashi, N., Miyakawa, H., Yaeshima, T., Araya, T. & Tomita, M. (1992). Relationship between oxygen sensitivity and oxygen metabolism of Bifidobacterium species. J Dairy Sci 75, 3296-3306.
    • (1992) J Dairy Sci , vol.75 , pp. 3296-3306
    • Shimamura, S.1    Abe, F.2    Ishibashi, N.3    Miyakawa, H.4    Yaeshima, T.5    Araya, T.6    Tomita, M.7
  • 56
    • 1642388498 scopus 로고    scopus 로고
    • Metabolic and biochemical responses of probiotic bacteria to oxygen
    • Talwalkar, A. & Kailasapathy, K. (2003). Metabolic and biochemical responses of probiotic bacteria to oxygen. J Dairy Sci 86, 2537-2546.
    • (2003) J Dairy Sci , vol.86 , pp. 2537-2546
    • Talwalkar, A.1    Kailasapathy, K.2
  • 57
    • 1642414197 scopus 로고    scopus 로고
    • The role of oxygen in the viability of probiotic bacteria with reference to L. acidophilus and Bifidobacterium spp
    • Talwalkar, A. & Kailasapathy, K. (2004). The role of oxygen in the viability of probiotic bacteria with reference to L. acidophilus and Bifidobacterium spp. Curr Issues Intest Microbiol 5, 1-8.
    • (2004) Curr Issues Intest Microbiol , vol.5 , pp. 1-8
    • Talwalkar, A.1    Kailasapathy, K.2
  • 58
    • 0034048222 scopus 로고    scopus 로고
    • Bile salt hydrolase of Bifidobacterium longum-biochemical and genetic characterization
    • Tanaka, H., Hashiba, H., Kok, J. & Mierau, I. (2000). Bile salt hydrolase of Bifidobacterium longum-biochemical and genetic characterization. Appl Environ Microbiol 66, 2502-2512.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 2502-2512
    • Tanaka, H.1    Hashiba, H.2    Kok, J.3    Mierau, I.4
  • 60
    • 49749101196 scopus 로고    scopus 로고
    • Proteomic analysis of antioxidant strategies of Staphylococcus aureus: Diverse responses to different oxidants
    • Wolf, C., Hochgräfe, F., Kusch, H., Albrecht, D., Hecker, M. & Engelmann, S. (2008). Proteomic analysis of antioxidant strategies of Staphylococcus aureus: diverse responses to different oxidants. Proteomics 8, 3139-3153.
    • (2008) Proteomics , vol.8 , pp. 3139-3153
    • Wolf, C.1    Hochgräfe, F.2    Kusch, H.3    Albrecht, D.4    Hecker, M.5    Engelmann, S.6
  • 61
    • 64549145786 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase protects Escherichia coli against oxidative stress
    • Wu, J., Jiang, Z., Liu, M., Gong, X., Wu, S., Burns, C. M. & Li, Z. (2009). Polynucleotide phosphorylase protects Escherichia coli against oxidative stress. Biochemistry 48, 2012-2020.
    • (2009) Biochemistry , vol.48 , pp. 2012-2020
    • Wu, J.1    Jiang, Z.2    Liu, M.3    Gong, X.4    Wu, S.5    Burns, C.M.6    Li, Z.7
  • 62
    • 69949177490 scopus 로고    scopus 로고
    • Oral administration of live Bifidobacterium substrains isolated from centenarians enhances intestinal function in mice
    • Yang, H., Liu, A., Zhang, M., Ibrahim, S. A., Pang, Z., Leng, X. & Ren, F. (2009a). Oral administration of live Bifidobacterium substrains isolated from centenarians enhances intestinal function in mice. Curr Microbiol 59, 439-445.
    • (2009) Curr Microbiol , vol.59 , pp. 439-445
    • Yang, H.1    Liu, A.2    Zhang, M.3    Ibrahim, S.A.4    Pang, Z.5    Leng, X.6    Ren, F.7
  • 63
    • 65349157701 scopus 로고    scopus 로고
    • Oral administration of live Bifidobacterium substrains isolated from healthy centenarians enhanced immune function in BALB/c mice
    • Yang, H. Y., Liu, S. L., Ibrahim, S. A., Zhao, L., Jiang, J. L., Sun, W. F. & Ren, F. Z. (2009b). Oral administration of live Bifidobacterium substrains isolated from healthy centenarians enhanced immune function in BALB/c mice. Nutr Res 29, 281-289.
    • (2009) Nutr Res , vol.29 , pp. 281-289
    • Yang, H.Y.1    Liu, S.L.2    Ibrahim, S.A.3    Zhao, L.4    Jiang, J.L.5    Sun, W.F.6    Ren, F.Z.7
  • 64
    • 0036431442 scopus 로고    scopus 로고
    • Ribosome-associated factor Y adopts a fold resembling a doublestranded RNA binding domain scaffold
    • Ye, K., Serganov, A., Hu, W., Garber, M. & Patel, D. J. (2002). Ribosome-associated factor Y adopts a fold resembling a doublestranded RNA binding domain scaffold. Eur J Biochem 269, 5182-5191.
    • (2002) Eur J Biochem , vol.269 , pp. 5182-5191
    • Ye, K.1    Serganov, A.2    Hu, W.3    Garber, M.4    Patel, D.J.5
  • 65
    • 49449096728 scopus 로고    scopus 로고
    • Grape berry plasma membrane proteome analysis and its differential expression during ripening
    • Zhang, J., Ma, H., Feng, J., Zeng, L., Wang, Z. & Chen, S. (2008). Grape berry plasma membrane proteome analysis and its differential expression during ripening. J Exp Bot 59, 2979-2990.
    • (2008) J Exp Bot , vol.59 , pp. 2979-2990
    • Zhang, J.1    Ma, H.2    Feng, J.3    Zeng, L.4    Wang, Z.5    Chen, S.6
  • 66
    • 67349154762 scopus 로고    scopus 로고
    • Stress response proteins' differential expression in embryogenic and non-embryogenic callus of Vitis vinifera L. cv. Cabernet Sauvignon-a proteomic approach
    • Zhang, J., Ma, H., Chen, S., Ji, M., Perl, A., Kovacs, L. & Chen, S. (2009). Stress response proteins' differential expression in embryogenic and non-embryogenic callus of Vitis vinifera L. cv. Cabernet Sauvignon-a proteomic approach. Plant Sci 177, 103-113.
    • (2009) Plant Sci , vol.177 , pp. 103-113
    • Zhang, J.1    Ma, H.2    Chen, S.3    Ji, M.4    Perl, A.5    Kovacs, L.6    Chen, S.7
  • 67
    • 0037008743 scopus 로고    scopus 로고
    • Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritin-like DNA-binding protein of Escherichia coli
    • Zhao, G., Ceci, P., Ilari, A., Giangiacomo, L., Laue, T. M., Chiancone, E. & Chasteen, N. D. (2002). Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritin-like DNA-binding protein of Escherichia coli. J Biol Chem 277, 27689-27696.
    • (2002) J Biol Chem , vol.277 , pp. 27689-27696
    • Zhao, G.1    Ceci, P.2    Ilari, A.3    Giangiacomo, L.4    Laue, T.M.5    Chiancone, E.6    Chasteen, N.D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.