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Volumn 8, Issue 10, 2009, Pages 2321-2338

Proteomics analysis of Lactobacillus casei Zhang, a new probiotic bacterium isolated from traditional home-made Koumiss in Inner Mongolia of China

Author keywords

[No Author keywords available]

Indexed keywords

LACTIC ACID; LACTOBACILLUS CASEI EXTRACT; PROBIOTIC AGENT;

EID: 71049166652     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M800483-MCP200     Document Type: Article
Times cited : (80)

References (66)
  • 1
    • 0346850959 scopus 로고    scopus 로고
    • Lactobacillus casei, dominant species in naturally fermented Sicilian green olives
    • Randazzo, C. L., Restuccia, C., Romano, A. D., and Caggia, C. (2004) Lactobacillus casei, dominant species in naturally fermented Sicilian green olives. Int. J. Food Microbiol. 90, 9-14
    • (2004) Int. J. Food Microbiol. , vol.90 , pp. 9-14
    • Randazzo, C.L.1    Restuccia, C.2    Romano, A.D.3    Caggia, C.4
  • 3
    • 8344268491 scopus 로고    scopus 로고
    • Numbers and strains of lactobacilli in some probiotic products
    • Coeuret, V., Gueguen, M., and Vernoux, J. P. (2004) Numbers and strains of lactobacilli in some probiotic products. Int. J. Food Microbiol. 97, 147-156
    • (2004) Int. J. Food Microbiol. , vol.97 , pp. 147-156
    • Coeuret, V.1    Gueguen, M.2    Vernoux, J.P.3
  • 4
    • 67650491767 scopus 로고    scopus 로고
    • Isolation and preliminary probiotic selection of Lactobacilli from koumiss in Inner Mongolia
    • Wu, R., Wang, L., Wang, J., Li, H., Menghe, B., Wu, J., Guo, M., and Zhang, H. (2009) Isolation and preliminary probiotic selection of Lactobacilli from koumiss in Inner Mongolia. J. Basic Microbiol. 49, 318-326
    • (2009) J. Basic Microbiol. , vol.49 , pp. 318-326
    • Wu, R.1    Wang, L.2    Wang, J.3    Li, H.4    Menghe, B.5    Wu, J.6    Guo, M.7    Zhang, H.8
  • 5
    • 57649174864 scopus 로고    scopus 로고
    • Immunological evaluation of Lactobacillus casei Zhang: A newly isolated strain from koumiss in Inner Mongolia, China
    • Ya, T., Zhang, Q., Chu, F., Merritt, J., Bilige, M., Sun, T., Du, R., and Zhang, H. (2008) (2006) Immunological evaluation of Lactobacillus casei Zhang: a newly isolated strain from koumiss in Inner Mongolia, China. BMC Immunol. 9, 68
    • (2006) BMC Immunol. , vol.9 , pp. 68
    • Ya, T.1    Zhang, Q.2    Chu, F.3    Merritt, J.4    Bilige, M.5    Sun, T.6    Du, R.7    Zhang, H.8
  • 6
    • 62949124912 scopus 로고    scopus 로고
    • Effect of oral administration of L. casei Zhang on T-lymphocyte subclass, serum IgG and intestinal mucous SIgA of mouse
    • Zhang, H., Zhang, Q., Menghe, B., and Amuer, J. (2006) Effect of oral administration of L. casei Zhang on T-lymphocyte subclass, serum IgG and intestinal mucous SIgA of mouse. China Dairy Ind. 34, 4-8
    • (2006) China Dairy Ind. , vol.34 , pp. 4-8
    • Zhang, H.1    Zhang, Q.2    Menghe, B.3    Amuer, J.4
  • 7
    • 71049173032 scopus 로고    scopus 로고
    • The antagonism of Lactobacillus casei Zhang to pathogenic Escherichia coli in mice and the influence on the microbial population in gut
    • Zhang, H., Zhang, Q., Ren, G., and Bao, Q. (2007) The antagonism of Lactobacillus casei Zhang to pathogenic Escherichia coli in mice and the influence on the microbial population in gut. Microbiol. China 5, 63-68
    • (2007) Microbiol. China , vol.5 , pp. 63-68
    • Zhang, H.1    Zhang, Q.2    Ren, G.3    Bao, Q.4
  • 8
    • 0035296650 scopus 로고    scopus 로고
    • The effect of growth phase, cryoprotectants and freezing rates on the survival of selected micro-organisms during freezing and thawing
    • DOI 10.1556/AAlim.30.2001.1.10
    • Peter, G., and Reichart, O. (2001) The effect of growth phase, cryoprotectants and freeze-drying rates on the survival of selected micro-organisms during freeze-drying and thawing. Acta Aliment. 30, 89-97 (Pubitemid 34983671)
    • (2001) Acta Alimentaria , vol.30 , Issue.1 , pp. 89-97
    • Peter, G.1    Reichart, O.2
  • 9
    • 2542527675 scopus 로고    scopus 로고
    • Stationary-phase acid and heat treatments for improvement of the viability of probiotic lactobacilli and bifidobacteria
    • Saarela, M., Rantala, M., Hallamaa, K., Nohynek, L., Virkajärvi, I., and Mättö, J. (2004) Stationary-phase acid and heat treatments for improvement of the viability of probiotic lactobacilli and bifidobacteria. J. Appl. Microbiol. 96, 1205-1214
    • (2004) J. Appl. Microbiol. , vol.96 , pp. 1205-1214
    • Saarela, M.1    Rantala, M.2    Hallamaa, K.3    Nohynek, L.4    Virkajärvi, I.5    Mättö, J.6
  • 10
    • 0027509821 scopus 로고
    • Survival of hunger and stress: The role of rpoS in early stationary phase gene regulation in E. coli
    • DOI 10.1016/0092-8674(93)90655-A
    • Hengge-Aronis, R. (1993) Survival of hunger and stress: the role of rpoS in early stationary phase regulation in E. coli. Cell 72, 165-168 (Pubitemid 23044932)
    • (1993) Cell , vol.72 , Issue.2 , pp. 165-168
    • Hengge-Aronis, R.1
  • 11
    • 0001780156 scopus 로고
    • Metabolic regulation of sporulation and other stationary phase phenomena
    • Smith, I., Slepecky, R. A., and Setlow, P., eds American Society for Microbiology, Washington, DC
    • Sonestein, A. L. (1989) Metabolic regulation of sporulation and other stationary phase phenomena, in Regulation of Prokaryotic Development (Smith, I., Slepecky, R. A., and Setlow, P., eds) pp. 109-130, American Society for Microbiology, Washington, DC
    • (1989) Regulation of Prokaryotic Development , pp. 109-130
    • Sonestein, A.L.1
  • 12
    • 0026145882 scopus 로고
    • Adaptation by Streptococcus mutans to acid tolerance
    • Hamilton, I. R., and Buckley, N. D. (1991) Adaptation by Streptococcus mutans to acid tolerance. Oral Microbiol. Immunol. 6, 65-71
    • (1991) Oral Microbiol. Immunol. , vol.6 , pp. 65-71
    • Hamilton, I.R.1    Buckley, N.D.2
  • 13
    • 0032971127 scopus 로고    scopus 로고
    • Differentiation of Lactococcus lactis subspecies lactis and subspecies cremoris strains by their adaptive response to stresses
    • Kim, W. S., Ren, J., and Dunn, N. W. (1999) Differentiation of Lactococcus lactis subspecies lactis and subspecies cremoris strains by their adaptive response to stresses. FEMS Microbiol. Lett. 171, 57-65
    • (1999) FEMS Microbiol. Lett. , vol.171 , pp. 57-65
    • Kim, W.S.1    Ren, J.2    Dunn, N.W.3
  • 14
    • 0035104482 scopus 로고    scopus 로고
    • A low-pH-inducible, stationary-phase acid tolerance response in Lactobacillus acidophilus CRL. 639
    • Lorca, G. L., and Valdez, G. F. (2001) A low-pH-inducible, stationary-phase acid tolerance response in Lactobacillus acidophilus CRL. 639. Curr. Microbiol. 42, 21-25
    • (2001) Curr. Microbiol. , vol.42 , pp. 21-25
    • Lorca, G.L.1    Valdez, G.F.2
  • 15
    • 34347401001 scopus 로고    scopus 로고
    • Comparison of growth-phase-dependent cytosolic proteomes of two Lactobacillus plantarum strains used in food and feed fermentations
    • Koistinen, K. M., Plumed-Ferrer, C., Lehesranta, S. J., Kärenlampi, S. O., and von Wright, A. (2007) Comparison of growth-phase-dependent cytosolic proteomes of two Lactobacillus plantarum strains used in food and feed fermentations. FEMS Microbiol. Lett. 273, 12-21
    • (2007) FEMS Microbiol. Lett. , vol.273 , pp. 12-21
    • Koistinen, K.M.1    Plumed-Ferrer, C.2    Lehesranta, S.J.3    Kärenlampi, S.O.4    Von Wright, A.5
  • 16
    • 33845993904 scopus 로고    scopus 로고
    • Proteomic analysis of log to stationary growth phase Lactobacillus plantarum cells and a 2-DE database
    • DOI 10.1002/pmic.200600361
    • Cohen, D. P., Renes, J., Bouwman, F. G., Zoetendal, E. G., Mariman, E., de Vos, W. M., and Vaughan, E. E. (2006) Proteomic analysis of log to stationary growth phase Lactobacillus plantarum cells and a 2-DE database. Proteomics 6, 6485-6493 (Pubitemid 46048387)
    • (2006) Proteomics , vol.6 , Issue.24 , pp. 6485-6493
    • Cohen, D.P.A.1    Renes, J.2    Bouwman, F.G.3    Zoetendal, E.G.4    Mariman, E.5    De Vos, W.M.6    Vaughan, E.E.7
  • 17
    • 33845779367 scopus 로고    scopus 로고
    • The phosphotransferase system of Lactobacillus casei: Regulation of carbon metabolism and connection to cold shock response
    • Monedero, V., Mazé, A., Boël, G., Zuñiga, M., Beaufils, S., Hartke, A., and Deutscher, J. (2007) The phosphotransferase system of Lactobacillus casei: regulation of carbon metabolism and connection to cold shock response. J. Mol. Microbiol. Biotechnol. 12, 20-32
    • (2007) J. Mol. Microbiol. Biotechnol. , vol.12 , pp. 20-32
    • Monedero, V.1    Mazé, A.2    Boël, G.3    Zuñiga, M.4    Beaufils, S.5    Hartke, A.6    Deutscher, J.7
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0037344041 scopus 로고    scopus 로고
    • Proteomic analysis of Lactococcus lactis, a lactic acid bacterium
    • DOI 10.1002/pmic.200390047
    • Guillot, A., Gitton, C., Anglade, P., and Mistou, M. Y. (2003) Proteomic analysis of Lactococcus lactis, a lactic acid bacterium. Proteomics 3, 337-354 (Pubitemid 36343690)
    • (2003) Proteomics , vol.3 , Issue.3 , pp. 337-354
    • Guillot, A.1    Gitton, C.2    Anglade, P.3    Mistou, M.-Y.4
  • 21
    • 0034837018 scopus 로고    scopus 로고
    • A comprehensive two-dimensional map of cytosolic proteins of Bacillus subtilis
    • DOI 10.1002/1522-2683(200108)22:14<2908::AID-ELPS2908>3.0.CO;2-M
    • Büttner, K., Bernhardt, J., Scharf, C., Schmid, R., Mäder, U., Eymann, C., Antelmann, H., Völker, A., Völker, U., and Hecker, M. (2001) A comprehensive two-dimensional map of cytosolic proteins of Bacillus subtilis. Electrophoresis 22, 2908-2935 (Pubitemid 32861410)
    • (2001) Electrophoresis , vol.22 , Issue.14 , pp. 2908-2935
    • Guo, X.1    Ying, W.2    Wan, J.3    Hu, Z.4    Qian, X.5    Zhang, H.6    He, F.7
  • 22
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 22DDCT method
    • Livak, K. J., and Schmittgen, T. D. (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 22DDCT method. Methods 25, 402-408
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 23
    • 0033815045 scopus 로고    scopus 로고
    • Folate levels in cultures of lactic acid bacteria
    • Lin, M. Y., and Young, C. M. (2000) Folate levels in cultures of lactic acid bacteria. Int. Dairy J. 10, 409-413
    • (2000) Int. Dairy J. , vol.10 , pp. 409-413
    • Lin, M.Y.1    Young, C.M.2
  • 25
    • 2442568591 scopus 로고    scopus 로고
    • Setting up standards and a reference map for the alkaline proteome of the Gram-positive bacterium Lactococcus lactis
    • DOI 10.1002/pmic.200300720
    • Drews, O., Reil, G., Parlar, H., and Görg, A. (2004) Setting up standards and a reference map for the alkaline proteome of the Gram-positive bacterium Lactococcus lactis. Proteomics 4, 1293-1304 (Pubitemid 38648017)
    • (2004) Proteomics , vol.4 , Issue.5 , pp. 1293-1304
    • Drews, O.1    Reil, G.2    Parlar, H.3    Gorg, A.4
  • 26
    • 0343569981 scopus 로고    scopus 로고
    • Reference map of soluble proteins from Streptococcus thermophilus by two-dimensional electrophoresis
    • DOI 10.1002/(SICI)1522-2683(20000301)21:5<949::AID-ELPS949>3.0. CO;2-5
    • Perrin, C., González-Márquez, H., Gaillard, J. L., Bracquart, P., and Guimont, C. (2000) Reference map of soluble proteins from Streptococcus thermophilus by two-dimensional electrophoresis. Electrophoresis 21, 949-955 (Pubitemid 30194074)
    • (2000) Electrophoresis , vol.21 , Issue.5 , pp. 949-955
    • Perrin, C.1    Gonzalez-Marquez, H.2    Gaillard, J.-L.3    Bracquart, P.4    Guimont, C.5
  • 27
    • 0033931002 scopus 로고    scopus 로고
    • Identification of stress-inducible proteins in Lactobacillus delbrueckii subsp. bulgaricus
    • DOI 10.1002/1522-2683(20000701)21:12<2557::AID-ELPS2557>3.0.CO;2-B
    • Lim, E. M., Ehrlich, S. D., and Maguin, E. (2000) Identification of stress-inducible proteins in Lactobacillus delbrueckii subsp. bulgaricus. Electrophoresis 21, 2557-2561 (Pubitemid 30484947)
    • (2000) Electrophoresis , vol.21 , Issue.12 , pp. 2557-2561
    • Lim, E.M.1    Ehrlich, S.D.2    Maguin, E.3
  • 28
    • 0033915213 scopus 로고    scopus 로고
    • Towards a proteomic map of Lactococcus lactis NCDO 763
    • DOI 10.1002/1522-2683(20000701)21:12<2546::AID-ELPS2546>3.0.CO;2-J
    • Anglade, P., Demey, E., Labas, V., Le Caer, J. P., and Chich, J. F. (2000) Towards a proteomic map of Lactococcus lactis NCDO 763. Electrophoresis 21, 2546-2549 (Pubitemid 30484945)
    • (2000) Electrophoresis , vol.21 , Issue.12 , pp. 2546-2549
    • Anglade, P.1    Demey, E.2    Labas, V.3    Caer, J.-P.L.4    Chich, J.-F.5
  • 29
    • 1842375705 scopus 로고    scopus 로고
    • A 16 kDa protein family overexpressed by Streptococcus thermophilus PB18 in acid environments
    • González-Márquez, H., Perrin, C., Bracquart, P., Guimont, C., and Linden, G. (1997) A 16 kDa protein family overexpressed by Streptococcus thermophilus PB18 in acid environments. Microbiology 143, 1587-1594 (Pubitemid 27230747)
    • (1997) Microbiology , vol.143 , Issue.5 , pp. 1587-1594
    • Gonzalez-Marquez, H.1    Perrin, C.2    Bracquart, P.3    Guimont, C.4    Linden, G.5
  • 30
    • 0033842191 scopus 로고    scopus 로고
    • "Early" protein synthesis of Lactobacillus delbrueckii ssp. bulgaricus in milk revealed by [35S]methionine labeling and two-dimensional gel electrophoresis
    • Rechinger, K. B., Siegumfeldt, H., Svendsen, I., and Jakobsen, M. (2000) "Early" protein synthesis of Lactobacillus delbrueckii ssp. bulgaricus in milk revealed by [35S]methionine labeling and two-dimensional gel electrophoresis. Electrophoresis 21, 2660-2669
    • (2000) Electrophoresis , vol.21 , pp. 2660-2669
    • Rechinger, K.B.1    Siegumfeldt, H.2    Svendsen, I.3    Jakobsen, M.4
  • 32
    • 23644445359 scopus 로고    scopus 로고
    • Proteomic analysis of global changes in protein expression during bile salt exposure of Bifidobacterium longum NCIMB 8809
    • DOI 10.1128/JB.187.16.5799-5808.2005
    • Sánchez, B., Champomier-Vergès, M. C., Anglade, P., Baraige, F., de Los Reyes-Gavilán, C. G., Margolles, A., and Zagorec, M. (2005) Proteomic analysis of global changes in protein expression during bile salt exposure of Bifidobacterium longum NCIMB 8809. J. Bacteriol. 187, 5799-5808 (Pubitemid 41134318)
    • (2005) Journal of Bacteriology , vol.187 , Issue.16 , pp. 5799-5808
    • Sanchez, B.1    Champomier-Verges, M.-C.2    Anglade, P.3    Baraige, F.4    De Los Reyes-Gavilan, C.G.5    Margolles, A.6    Zagorec, M.7
  • 33
    • 33645462173 scopus 로고    scopus 로고
    • Comparative proteome approach to characterize the high-pressure stress response of Lactobacillus sanfranciscensis DSM 20451T
    • Hörmann, S., Scheyhing, C., Behr, J., Pavlovic, M., Ehrmann, M., and Vogel, R. F. (2006) Comparative proteome approach to characterize the high-pressure stress response of Lactobacillus sanfranciscensis DSM 20451T. Proteomics 6, 1878-1885
    • (2006) Proteomics , vol.6 , pp. 1878-1885
    • Hörmann, S.1    Scheyhing, C.2    Behr, J.3    Pavlovic, M.4    Ehrmann, M.5    Vogel, R.F.6
  • 34
    • 0035430777 scopus 로고    scopus 로고
    • Altered protein expression of Streptococcus oralis cultured at low pH revealed by two-dimensional gel electrophoresis
    • Wilkins, J. C., Homer, K. A., and Beighton, D. (2001) Altered protein expression of Streptococcus oralis cultured at low pH revealed by two-dimensional gel electrophoresis. Appl. Environ. Microbiol. 67, 3396-3405
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 3396-3405
    • Wilkins, J.C.1    Homer, K.A.2    Beighton, D.3
  • 35
    • 0036195722 scopus 로고    scopus 로고
    • Alpha-crystallin-type heat shock proteins: Socializing minichaperones in the context of a multichaperone network
    • Narberhaus, F. (2002) Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network. Microbiol. Mol. Biol. Rev. 66, 64-93
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 64-93
    • Narberhaus, F.1
  • 36
    • 8144225912 scopus 로고    scopus 로고
    • Improved stress tolerance of GroESL-overproducing Lactococcus lactis and probiotic Lactobacillus paracasei NFBC 338
    • Desmond, C., Fitzgerald, G. F., Stanton, C., and Ross, R. P. (2004) Improved stress tolerance of GroESL-overproducing Lactococcus lactis and probiotic Lactobacillus paracasei NFBC 338. Appl. Environ. Microbiol. 70, 5929-5936
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 5929-5936
    • Desmond, C.1    Fitzgerald, G.F.2    Stanton, C.3    Ross, R.P.4
  • 37
    • 0032079487 scopus 로고    scopus 로고
    • The small heat shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network
    • Veinger, L., Diamant, S., Buchner, J., and Goloubinoff, P. (1998) The small heat shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network. J. Biol. Chem. 273, 11032-11037
    • (1998) J. Biol. Chem. , vol.273 , pp. 11032-11037
    • Veinger, L.1    Diamant, S.2    Buchner, J.3    Goloubinoff, P.4
  • 38
    • 0026343040 scopus 로고
    • Biological role and regulation of the universally conserved heat shock proteins
    • Ang, D., Liberek, K., Skowyra, D., Zylicz, M., and Georgopoulos, C. (1991) Biological role and regulation of the universally conserved heat shock proteins. J. Biol. Chem. 266, 24233-24236
    • (1991) J. Biol. Chem. , vol.266 , pp. 24233-24236
    • Ang, D.1    Liberek, K.2    Skowyra, D.3    Zylicz, M.4    Georgopoulos, C.5
  • 39
    • 0027323041 scopus 로고
    • Isolation and properties of a mutant of Escherichia coli with an insertional inactivation of the uspA gene, which encodes a universal stress protein
    • Nyström, T., and Neidhardt, F. C. (1993) Isolation and properties of a mutant of Escherichia coli with an insertional inactivation of the uspA gene, which encodes a universal stress protein. J. Bacteriol. 175, 3949-3956 (Pubitemid 23206887)
    • (1993) Journal of Bacteriology , vol.175 , Issue.13 , pp. 3949-3956
    • Nystrom, T.1    Neidhardt, F.C.2
  • 40
    • 0030066140 scopus 로고    scopus 로고
    • Effects of overproducing the universal stress protein, UspA, in Escherichia coli K-12
    • Nyström, T., and Neidhardt, F. C. (1996) Effects of overproducing the universal stress protein, UspA, in Escherichia coli K-12. J. Bacteriol. 178, 927-930 (Pubitemid 26036673)
    • (1996) Journal of Bacteriology , vol.178 , Issue.3 , pp. 927-930
    • Nystrom, T.1    Neidhardt, F.C.2
  • 41
    • 0036192462 scopus 로고    scopus 로고
    • The universal stress protein paralogues of Escherichia coli are coordinately regulated and co-operate in the defense against DNA damage
    • Gustavsson, N., Diez, A., and Nyström, T. (2002) The universal stress protein paralogues of Escherichia coli are coordinately regulated and co-operate in the defense against DNA damage. Mol. Microbiol. 43, 107-117
    • (2002) Mol. Microbiol. , vol.43 , pp. 107-117
    • Gustavsson, N.1    Diez, A.2    Nyström, T.3
  • 42
    • 0038013951 scopus 로고    scopus 로고
    • The bacterial universal stress protein: Function and regulation
    • Kvint, K., Nachin, L., Diez, A., and Nyström, T. (2003) The bacterial universal stress protein: function and regulation. Curr. Opin. Microbiol. 6, 140-145
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 140-145
    • Kvint, K.1    Nachin, L.2    Diez, A.3    Nyström, T.4
  • 43
    • 24044479701 scopus 로고    scopus 로고
    • The glycolytic genes pfk and pyk from Lactobacillus casei are induced by sugars transported by the phosphoenolpyruvate:sugar phosphotransferase system and repressed by CcpA
    • Viana, R., Pérez-Martínez, G., Deutscher, J., and Monedero, V. (2005) The glycolytic genes pfk and pyk from Lactobacillus casei are induced by sugars transported by the phosphoenolpyruvate:sugar phosphotransferase system and repressed by CcpA. Arch. Microbiol. 183, 385-393
    • (2005) Arch. Microbiol. , vol.183 , pp. 385-393
    • Viana, R.1    Pérez-Martínez, G.2    Deutscher, J.3    Monedero, V.4
  • 44
    • 42549161072 scopus 로고    scopus 로고
    • The effect of low pH on protein expression by the probiotic bacterium Lactobacillus reuteri
    • DOI 10.1002/pmic.200700663
    • Lee, K., Lee, H. G., Pi, K., and Choi, Y. J. (2008) The effect of low pH on protein expression by he probiotic bacterium Lactobacillus reuteri. Proteomics 8, 1624-1630 (Pubitemid 351580208)
    • (2008) Proteomics , vol.8 , Issue.8 , pp. 1624-1630
    • Lee, K.1    Lee, H.-G.2    Pi, K.3    Choi, Y.-J.4
  • 45
    • 2942625671 scopus 로고    scopus 로고
    • Stress-responsive proteins are upregulated in Streptococcus mutants during acid tolerance
    • Len, A. C., Harty, D. W., and Jacques, N. A. (2004) Stress-responsive proteins are upregulated in Streptococcus mutants during acid tolerance. Microbiology 150, 1339-1351
    • (2004) Microbiology , vol.150 , pp. 1339-1351
    • Len, A.C.1    Harty, D.W.2    Jacques, N.A.3
  • 46
    • 1942440947 scopus 로고    scopus 로고
    • Effect of pyruvate kinase overproduction on glucose metabolism of Lactococcus lactis
    • Ramos, A., Neves, A. R, Ventura, R., Maycock, C., López, P., and Santos, H. (2004) Effect of pyruvate kinase overproduction on glucose metabolism of Lactococcus lactis. Microbiology 150, 1103-1111 (Pubitemid 38519330)
    • (2004) Microbiology , vol.150 , Issue.4 , pp. 1103-1111
    • Ramos, A.1    Neves, A.R.2    Ventura, R.3    Maycock, C.4    Lopez, P.5    Santos, H.6
  • 47
    • 1642576068 scopus 로고    scopus 로고
    • The Three-dimensional structure of the N-acetylglucosamine-6-phosphate deacetylase, NagA, from Bacillus subtilis
    • Vincent, F., Yates, D., Garman, E., Davies, G. J., and Brannigan, J. A. (2004) The Three-dimensional structure of the N-acetylglucosamine-6-phosphate deacetylase, NagA, from Bacillus subtilis. J. Biol. Chem. 279, 2809-2816
    • (2004) J. Biol. Chem. , vol.279 , pp. 2809-2816
    • Vincent, F.1    Yates, D.2    Garman, E.3    Davies, G.J.4    Brannigan, J.A.5
  • 48
    • 0034799007 scopus 로고    scopus 로고
    • Sugar catabolism and its impact on the biosynthesis and engineering of exopolysaccharide production in lactic acid bacteria
    • Boelsa, I. C., van Kranenburg, R., Hugenholtz, J., Kleerebezem, M., and de Vos, W. M. (2001) Sugar catabolism and its impact on the biosynthesis and engineering of exopolysaccharide production in lactic acid bacteria. Int. Dairy J. 11, 723-732
    • (2001) Int. Dairy J. , vol.11 , pp. 723-732
    • Boelsa, I.C.1    Van Kranenburg, R.2    Hugenholtz, J.3    Kleerebezem, M.4    De Vos, W.M.5
  • 49
    • 33845946001 scopus 로고    scopus 로고
    • Regulates pyruvate catabolism by interacting with the pyruvate dehydrogenase E1 subunit and modulating pyruvate dehydrogenase activity
    • Soo, P. C., Horng, Y. T., Lai, M. J., Wei, J. R., Hsieh, S. C., Chang, Y. L., Tsai, Y. H., and Lai, H. C. (2007) Regulates pyruvate catabolism by interacting with the pyruvate dehydrogenase E1 subunit and modulating pyruvate dehydrogenase activity. J. Bacteriol. 189, 109-118
    • (2007) J. Bacteriol. , vol.189 , pp. 109-118
    • Soo, P.C.1    Horng, Y.T.2    Lai, M.J.3    Wei, J.R.4    Hsieh, S.C.5    Chang, Y.L.6    Tsai, Y.H.7    Lai, H.C.8
  • 50
    • 0032537589 scopus 로고    scopus 로고
    • The pyruvate dehydrogenase multi-enzyme complex from Gram-negative bacteria
    • de Kok, A., Hengeveld, A. F., Martin, A., and Westphal, A. H. (1998) The pyruvate dehydrogenase multi-enzyme complex from Gram-negative bacteria. Biochim. Biophys. Acta 1385, 353-366
    • (1998) Biochim. Biophys. Acta , vol.1385 , pp. 353-366
    • De Kok, A.1    Hengeveld, A.F.2    Martin, A.3    Westphal, A.H.4
  • 51
    • 0036829080 scopus 로고    scopus 로고
    • Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex
    • Stark, H., Rodnina, M. V., Wieden, H. J., Zemlin, F., Wintermeyer, W., and van Heel, M. (2002) Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex. Nat. Struct. Biol. 9, 849-854
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 849-854
    • Stark, H.1    Rodnina, M.V.2    Wieden, H.J.3    Zemlin, F.4    Wintermeyer, W.5    Van Heel, M.6
  • 52
    • 0032496137 scopus 로고    scopus 로고
    • Chaperone properties of bacterial elongation factor EF-Tu
    • Caldas, T. D., El Yaagoubi, A., and Richarme, G. (1998) Chaperone properties of bacterial elongation factor EF-Tu. J. Biol. Chem. 273, 11478-11482
    • (1998) J. Biol. Chem. , vol.273 , pp. 11478-11482
    • Caldas, T.D.1    El Yaagoubi, A.2    Richarme, G.3
  • 53
    • 1542373514 scopus 로고    scopus 로고
    • Mass spectrometry proteomic analysis of stress adaptation reveals both common and distinct response pathways in Propionibacterium freudenreichii
    • Leverrier, P., Vissers, J. P., Rouault, A., Boyaval, P., and Jan, G. (2004) Mass spectrometry proteomic analysis of stress adaptation reveals both common and distinct response pathways in Propionibacterium freudenreichii. Arch. Microbiol. 181, 215-230
    • (2004) Arch. Microbiol. , vol.181 , pp. 215-230
    • Leverrier, P.1    Vissers, J.P.2    Rouault, A.3    Boyaval, P.4    Jan, G.5
  • 56
    • 0032821236 scopus 로고    scopus 로고
    • Subunit interactions in ABC transporters: Towards a functional architecture
    • Jones, P. M., and George, A. M. (1999) Subunit interactions in ABC transporters: towards a functional architecture. FEMS Microbiol. Lett. 179, 187-202
    • (1999) FEMS Microbiol. Lett. , vol.179 , pp. 187-202
    • Jones, P.M.1    George, A.M.2
  • 58
    • 0035675837 scopus 로고    scopus 로고
    • Regulation of gene expression by cell-to-cell communication: Acyl-homoserine lactone quorum sensing
    • Fuqua, C., Parsek, M. R., and Greenberg, E. P. (2001) Regulation of gene expression by cell-to-cell communication: acyl-homoserine lactone quorum sensing. Annu. Rev. Genet. 35, 439-468
    • (2001) Annu. Rev. Genet. , vol.35 , pp. 439-468
    • Fuqua, C.1    Parsek, M.R.2    Greenberg, E.P.3
  • 59
    • 1942507978 scopus 로고    scopus 로고
    • LuxS-mediated signaling in Streptococcus mutans is involved in regulation of acid and oxidative stress tolerance and biofilm formation
    • Wen, Z. T., and Burne, R. A. (2004) LuxS-mediated signaling in Streptococcus mutans is involved in regulation of acid and oxidative stress tolerance and biofilm formation. J. Bacteriol. 186, 2682-2691
    • (2004) J. Bacteriol. , vol.186 , pp. 2682-2691
    • Wen, Z.T.1    Burne, R.A.2
  • 63
    • 23844540693 scopus 로고    scopus 로고
    • An esterase gene from Lactobacillus casei cotranscribed with genes encoding a phosphoenolpyruvate:sugar phosphotransferase system and regulated by a LevR-like activator and sigma54 factor
    • Yebra, M. J., Viana, R., Monedero, V., Deutscher, J., and Pérez-Martínez, G. (2004) An esterase gene from Lactobacillus casei cotranscribed with genes encoding a phosphoenolpyruvate:sugar phosphotransferase system and regulated by a LevR-like activator and sigma54 factor. J. Mol. Microbiol. Biotechnol. 8, 117-128
    • (2004) J. Mol. Microbiol. Biotechnol. , vol.8 , pp. 117-128
    • Yebra, M.J.1    Viana, R.2    Monedero, V.3    Deutscher, J.4    Pérez-Martínez, G.5
  • 64
    • 0025328743 scopus 로고
    • Cold shock induces a major ribosomal-associated protein that unwinds double-stranded RNA in Escherichia coli
    • VanBogelen, R. A., and Neidhardt, F. C. (1990) Cold shock induces a major ribosomal-associated protein that unwinds double-stranded RNA in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 87, 5589-5593
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 5589-5593
    • VanBogelen, R.A.1    Neidhardt, F.C.2
  • 65
    • 0036174975 scopus 로고    scopus 로고
    • RRNA promoter activity in the fast-growing bacterium Vibrio natriegens
    • Aiyar, S. E., Gaal, T., and Gourse, R. L. (2002) rRNA promoter activity in the fast-growing bacterium Vibrio natriegens. J. Bacteriol. 184, 1349-1358 (Pubitemid 34157557)
    • (2002) Journal of Bacteriology , vol.184 , Issue.5 , pp. 1349-1358
    • Aiyar, S.E.1    Gaal, T.2    Gourse, R.L.3
  • 66
    • 0034978593 scopus 로고    scopus 로고
    • Pleiotropic transcriptional repressor CodY senses the intracellular pool of branched-chain amino acids in Lactococcus lactis
    • Guédon, E., Serrer, P., Ehrlich, S. D., Renault, P., and Delorme, C. (2001) Pleiotropic transcriptional repressor CodY senses the intracellular pool of branched-chain amino acids in Lactococcus lactis. Mol. Microbiol. 40, 1227-1239
    • (2001) Mol. Microbiol. , vol.40 , pp. 1227-1239
    • Guédon, E.1    Serrer, P.2    Ehrlich, S.D.3    Renault, P.4    Delorme, C.5


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