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Volumn 75, Issue 4, 2012, Pages 1357-1374

Effect of acid stress on protein expression and phosphorylation in Lactobacillus rhamnosus GG

Author keywords

2 D DIGE; Bacteria; Lactobacillus rhamnosus GG; Phosphorylation; Probiotic; Stress

Indexed keywords

BACTERIAL ANTIGEN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 84855901086     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2011.11.009     Document Type: Article
Times cited : (131)

References (70)
  • 3
    • 22244486448 scopus 로고    scopus 로고
    • Effects of Lactobacillus GG on genes expression pattern in small bowel mucosa
    • Di Caro S., Tao H., Grillo A., Elia C., Gasbarrini G., Sepulveda A.R., et al. Effects of Lactobacillus GG on genes expression pattern in small bowel mucosa. Dig Liver Dis 2005, 37:320-329.
    • (2005) Dig Liver Dis , vol.37 , pp. 320-329
    • Di Caro, S.1    Tao, H.2    Grillo, A.3    Elia, C.4    Gasbarrini, G.5    Sepulveda, A.R.6
  • 5
    • 33646394091 scopus 로고    scopus 로고
    • Soluble factors from Lactobacillus GG activate MAPKs and induce cytoprotective heat shock proteins in intestinal epithelial cells
    • Tao Y., Drabik K.A., Waypa T.S., Musch M.W., Alverdy J.C., Schneewind O., et al. Soluble factors from Lactobacillus GG activate MAPKs and induce cytoprotective heat shock proteins in intestinal epithelial cells. Am J Physiol Cell Physiol 2006, 290:C1018-C1030.
    • (2006) Am J Physiol Cell Physiol , vol.290
    • Tao, Y.1    Drabik, K.A.2    Waypa, T.S.3    Musch, M.W.4    Alverdy, J.C.5    Schneewind, O.6
  • 6
    • 33847021973 scopus 로고    scopus 로고
    • Soluble proteins produced by probiotic bacteria regulate intestinal epithelial cell survival and growth
    • Yan F., Cao H., Cover T.L., Whitehead R., Washington M.K., Polk D.B. Soluble proteins produced by probiotic bacteria regulate intestinal epithelial cell survival and growth. Gastroenterology 2007, 132:562-575.
    • (2007) Gastroenterology , vol.132 , pp. 562-575
    • Yan, F.1    Cao, H.2    Cover, T.L.3    Whitehead, R.4    Washington, M.K.5    Polk, D.B.6
  • 7
    • 78649247551 scopus 로고    scopus 로고
    • Impact of lipoteichoic acid modification on the performance of the probiotic Lactobacillus rhamnosus GG in experimental colitis
    • Claes I.J.J., Lebeer S., Shen C., Verhoeven T.L.A., Dilissen E., De Hertogh G., et al. Impact of lipoteichoic acid modification on the performance of the probiotic Lactobacillus rhamnosus GG in experimental colitis. Clin Exp Immunol 2010, 162:306-314.
    • (2010) Clin Exp Immunol , vol.162 , pp. 306-314
    • Claes, I.J.J.1    Lebeer, S.2    Shen, C.3    Verhoeven, T.L.A.4    Dilissen, E.5    De Hertogh, G.6
  • 8
    • 70350134948 scopus 로고    scopus 로고
    • Comparative genomic analysis of Lactobacillus rhamnosus GG reveals pili containing a human-mucus binding protein
    • Kankainen M., Paulin L., Tynkkynen S., von Ossowski I., Reunanen J., Partanen P., et al. Comparative genomic analysis of Lactobacillus rhamnosus GG reveals pili containing a human-mucus binding protein. Proc Natl Acad Sci USA 2009, 106:17193-17199.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 17193-17199
    • Kankainen, M.1    Paulin, L.2    Tynkkynen, S.3    von Ossowski, I.4    Reunanen, J.5    Partanen, P.6
  • 9
    • 79953219103 scopus 로고    scopus 로고
    • Proteomics and transcriptomics characterization of bile stress response in probiotic Lactobacillus rhamnosus GG
    • 002741.
    • Koskenniemi K., Laakso K., Koponen J., Kankainen M., Greco D., Auvinen P., et al. Proteomics and transcriptomics characterization of bile stress response in probiotic Lactobacillus rhamnosus GG. Mol Cell Proteomics 2011; 10: M110.002741.
    • (2011) Mol Cell Proteomics. , vol.10
    • Koskenniemi, K.1    Laakso, K.2    Koponen, J.3    Kankainen, M.4    Greco, D.5    Auvinen, P.6
  • 10
    • 80054119261 scopus 로고    scopus 로고
    • Growth phase-associated changes in the proteome and transcriptome of Lactobacillus rhamnosus GG in industrial-type whey medium
    • Laakso K., Koskenniemi K., Koponen J., Kankainen M., Surakka A., Salusjärvi T., et al. Growth phase-associated changes in the proteome and transcriptome of Lactobacillus rhamnosus GG in industrial-type whey medium. Microb Biotechnol 2011, 4:746-766.
    • (2011) Microb Biotechnol , vol.4 , pp. 746-766
    • Laakso, K.1    Koskenniemi, K.2    Koponen, J.3    Kankainen, M.4    Surakka, A.5    Salusjärvi, T.6
  • 12
    • 0034048221 scopus 로고    scopus 로고
    • Dynamic changes of intracellular pH in individual lactic acid bacterium cells in response to a rapid drop in extracellular pH
    • Siegumfeldt H., Rechinger K.B., Jakobsen M. Dynamic changes of intracellular pH in individual lactic acid bacterium cells in response to a rapid drop in extracellular pH. Appl Environ Microbiol 2000, 66:2330-2335.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 2330-2335
    • Siegumfeldt, H.1    Rechinger, K.B.2    Jakobsen, M.3
  • 13
    • 21144483442 scopus 로고
    • PH homeostasis in lactic acid bacteria
    • Hutkins R.W., Nannen N.L. pH homeostasis in lactic acid bacteria. J Dairy Sci 1993, 76:2354-2365.
    • (1993) J Dairy Sci , vol.76 , pp. 2354-2365
    • Hutkins, R.W.1    Nannen, N.L.2
  • 14
    • 0942297972 scopus 로고    scopus 로고
    • Environmental stress responses in Lactobacillus: a review
    • De Angelis M., Gobbetti M. Environmental stress responses in Lactobacillus: a review. Proteomics 2004, 4:106-122.
    • (2004) Proteomics , vol.4 , pp. 106-122
    • De Angelis, M.1    Gobbetti, M.2
  • 15
    • 42549161072 scopus 로고    scopus 로고
    • The effect of low pH on protein expression by the probiotic bacterium Lactobacillus reuteri
    • Lee K., Lee H.-G., Pi K., Choi Y.-J. The effect of low pH on protein expression by the probiotic bacterium Lactobacillus reuteri. Proteomics 2008, 8:1624-1630.
    • (2008) Proteomics , vol.8 , pp. 1624-1630
    • Lee, K.1    Lee, H.-G.2    Pi, K.3    Choi, Y.-J.4
  • 16
    • 36348932799 scopus 로고    scopus 로고
    • Acid, bile, and heat tolerance of free and microencapsulated probiotic bacteria
    • Ding W.K., Shah N.P. Acid, bile, and heat tolerance of free and microencapsulated probiotic bacteria. J Food Sci 2007, 72:M446-M450.
    • (2007) J Food Sci , vol.72
    • Ding, W.K.1    Shah, N.P.2
  • 17
    • 34250872250 scopus 로고    scopus 로고
    • The early response to acid shock in Lactobacillus reuteri involves the ClpL chaperone and a putative cell wall-altering esterase
    • Wall T., Båth K., Britton R.A., Jonsson H., Versalovic J., Roos S. The early response to acid shock in Lactobacillus reuteri involves the ClpL chaperone and a putative cell wall-altering esterase. Appl Environ Microbiol 2007, 73:3924-3935.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 3924-3935
    • Wall, T.1    Båth, K.2    Britton, R.A.3    Jonsson, H.4    Versalovic, J.5    Roos, S.6
  • 18
    • 31344461921 scopus 로고    scopus 로고
    • A study of Streptococcus thermophilus proteome by integrated analytical procedures and differential expression investigations
    • Arena S., D'Ambrosio C., Renzone G., Rullo R., Ledda L., Vitale F., et al. A study of Streptococcus thermophilus proteome by integrated analytical procedures and differential expression investigations. Proteomics 2006, 6:181-192.
    • (2006) Proteomics , vol.6 , pp. 181-192
    • Arena, S.1    D'Ambrosio, C.2    Renzone, G.3    Rullo, R.4    Ledda, L.5    Vitale, F.6
  • 19
    • 29544443526 scopus 로고    scopus 로고
    • Proteomic characterization of the acid tolerance response in Lactococcus lactis MG1363
    • Budin-Verneuil A., Pichereau V., Auffray Y., Ehrlich D.S., Maguin E. Proteomic characterization of the acid tolerance response in Lactococcus lactis MG1363. Proteomics 2005, 5:4794-4807.
    • (2005) Proteomics , vol.5 , pp. 4794-4807
    • Budin-Verneuil, A.1    Pichereau, V.2    Auffray, Y.3    Ehrlich, D.S.4    Maguin, E.5
  • 20
    • 0141646554 scopus 로고    scopus 로고
    • Identification of proteins induced at low pH in Lactococcus lactis
    • Frees D., Vogensen F.K., Ingmer H. Identification of proteins induced at low pH in Lactococcus lactis. Int J Food Microbiol 2003, 87:293-300.
    • (2003) Int J Food Microbiol , vol.87 , pp. 293-300
    • Frees, D.1    Vogensen, F.K.2    Ingmer, H.3
  • 21
    • 77951080079 scopus 로고    scopus 로고
    • Physiological and transcriptional response of Lactobacillus casei ATCC 334 to acid stress
    • Broadbent J.R., Larsen R.L., Deibel V., Steele J.L. Physiological and transcriptional response of Lactobacillus casei ATCC 334 to acid stress. J Bacteriol 2010, 192:2445-2458.
    • (2010) J Bacteriol , vol.192 , pp. 2445-2458
    • Broadbent, J.R.1    Larsen, R.L.2    Deibel, V.3    Steele, J.L.4
  • 23
    • 52049108947 scopus 로고    scopus 로고
    • Acid adaptation of Lactobacillus delbrueckii subsp. bulgaricus induces physiological responses at membrane and cytosolic levels that improves cryotolerance
    • Streit F., Delettre J., Corrieu G., Béal C. Acid adaptation of Lactobacillus delbrueckii subsp. bulgaricus induces physiological responses at membrane and cytosolic levels that improves cryotolerance. J Appl Microbiol 2008, 105:1071-1080.
    • (2008) J Appl Microbiol , vol.105 , pp. 1071-1080
    • Streit, F.1    Delettre, J.2    Corrieu, G.3    Béal, C.4
  • 24
    • 79957620420 scopus 로고    scopus 로고
    • Proteomic analysis of responses of a new probiotic bacterium Lactobacillus casei Zhang to low acid stress
    • Wu R., Zhang W., Sun T., Wu J., Yue X., Meng H., et al. Proteomic analysis of responses of a new probiotic bacterium Lactobacillus casei Zhang to low acid stress. Int J Food Microbiol 2011, 147:181-187.
    • (2011) Int J Food Microbiol , vol.147 , pp. 181-187
    • Wu, R.1    Zhang, W.2    Sun, T.3    Wu, J.4    Yue, X.5    Meng, H.6
  • 25
    • 77951685445 scopus 로고    scopus 로고
    • Effect of transient acid stress on the proteome of intestinal probiotic Lactobacillus reuteri
    • Lee K., Pi K. Effect of transient acid stress on the proteome of intestinal probiotic Lactobacillus reuteri. Biochemistry (Mosc) 2010, 75:460-465.
    • (2010) Biochemistry (Mosc) , vol.75 , pp. 460-465
    • Lee, K.1    Pi, K.2
  • 26
    • 79953736535 scopus 로고    scopus 로고
    • Proteomic analysis of differentially expressed proteins in Lactobacillus brevis NCL912 under acid stress
    • Huang G., Li C., Cao Y. Proteomic analysis of differentially expressed proteins in Lactobacillus brevis NCL912 under acid stress. FEMS Microbiol Lett 2011, 318:177-182.
    • (2011) FEMS Microbiol Lett , vol.318 , pp. 177-182
    • Huang, G.1    Li, C.2    Cao, Y.3
  • 28
    • 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.C., Rouault A., Boyaval P., Jan G. Mass spectrometry proteomic analysis of stress adaptation reveals both common and distinct response pathways in Propionibacterium freudenreichii. Arch Microbiol 2004, 181:215-230.
    • (2004) Arch Microbiol , vol.181 , pp. 215-230
    • Leverrier, P.1    Vissers, J.P.C.2    Rouault, A.3    Boyaval, P.4    Jan, G.5
  • 29
    • 77954361611 scopus 로고    scopus 로고
    • More than just activity control: phosphorylation may control all aspects of a protein's properties
    • Stülke J. More than just activity control: phosphorylation may control all aspects of a protein's properties. Mol Microbiol 2010, 77:273-275.
    • (2010) Mol Microbiol , vol.77 , pp. 273-275
    • Stülke, J.1
  • 30
    • 77954368576 scopus 로고    scopus 로고
    • Bacillus subtilis BY-kinase PtkA controls enzyme activity and localisation of its protein substrates
    • Jers C., Pedersen M.M., Paspaliari D.K., Schütz W., Johnsson C., Soufi B., et al. Bacillus subtilis BY-kinase PtkA controls enzyme activity and localisation of its protein substrates. Mol Microbiol 2010, 77:287-299.
    • (2010) Mol Microbiol , vol.77 , pp. 287-299
    • Jers, C.1    Pedersen, M.M.2    Paspaliari, D.K.3    Schütz, W.4    Johnsson, C.5    Soufi, B.6
  • 33
    • 70449366364 scopus 로고    scopus 로고
    • Proteome analysis of Lactobacillus rhamnosus GG using 2-D DIGE and mass spectrometry shows differential protein production in laboratory and industrial-type growth media
    • Koskenniemi K., Koponen J., Kankainen M., Savijoki K., Tynkkynen S., de Vos W.M., et al. Proteome analysis of Lactobacillus rhamnosus GG using 2-D DIGE and mass spectrometry shows differential protein production in laboratory and industrial-type growth media. J Proteome Res 2009, 8:4993-5007.
    • (2009) J Proteome Res , vol.8 , pp. 4993-5007
    • Koskenniemi, K.1    Koponen, J.2    Kankainen, M.3    Savijoki, K.4    Tynkkynen, S.5    de Vos, W.M.6
  • 35
    • 0242333835 scopus 로고    scopus 로고
    • Normalization of cDNA microarray data
    • Smyth G.K., Speed T. Normalization of cDNA microarray data. Methods 2003, 31:265-273.
    • (2003) Methods , vol.31 , pp. 265-273
    • Smyth, G.K.1    Speed, T.2
  • 36
    • 0034948896 scopus 로고    scopus 로고
    • A Bayesian framework for the analysis of microarray expression data: regularized t-test and statistical inferences of gene changes
    • Baldi P., Long A.D. A Bayesian framework for the analysis of microarray expression data: regularized t-test and statistical inferences of gene changes. Bioinformatics 2001, 17:509-519.
    • (2001) Bioinformatics , vol.17 , pp. 509-519
    • Baldi, P.1    Long, A.D.2
  • 38
    • 27344435774 scopus 로고    scopus 로고
    • Gene set enrichment analysis: a knowledge-based approach for interpreting genome-wide expression profiles
    • Subramanian A., Tamayo P., Mootha V.K., Mukherjee S., Ebert B.L., Gillette M.A., et al. Gene set enrichment analysis: a knowledge-based approach for interpreting genome-wide expression profiles. Proc Natl Acad Sci USA 2005, 102:15545-15550.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15545-15550
    • Subramanian, A.1    Tamayo, P.2    Mootha, V.K.3    Mukherjee, S.4    Ebert, B.L.5    Gillette, M.A.6
  • 39
    • 33751014852 scopus 로고    scopus 로고
    • Identifying functional gene sets from hierarchically clustered expression data: map of abiotic stress regulated genes in Arabidopsis thaliana
    • Kankainen M., Brader G., Törönen P., Palva E.T., Holm L. Identifying functional gene sets from hierarchically clustered expression data: map of abiotic stress regulated genes in Arabidopsis thaliana. Nucleic Acids Res 2006, 34:e124.
    • (2006) Nucleic Acids Res , vol.34
    • Kankainen, M.1    Brader, G.2    Törönen, P.3    Palva, E.T.4    Holm, L.5
  • 41
    • 0030898043 scopus 로고    scopus 로고
    • Identification of mouse liver proteins on two-dimensional electrophoresis gels by matrix-assisted laser desorption/ionization mass spectrometry of in situ enzymatic digests
    • O'Connell K.L., Stults J.T. Identification of mouse liver proteins on two-dimensional electrophoresis gels by matrix-assisted laser desorption/ionization mass spectrometry of in situ enzymatic digests. Electrophoresis 1997, 18:349-359.
    • (1997) Electrophoresis , vol.18 , pp. 349-359
    • O'Connell, K.L.1    Stults, J.T.2
  • 42
    • 33846942977 scopus 로고    scopus 로고
    • Clp ATPases and ClpP proteolytic complexes regulate vital biological processes in low GC, Gram-positive bacteria
    • Frees D., Savijoki K., Varmanen P., Ingmer H. Clp ATPases and ClpP proteolytic complexes regulate vital biological processes in low GC, Gram-positive bacteria. Mol Microbiol 2007, 63:1285-1295.
    • (2007) Mol Microbiol , vol.63 , pp. 1285-1295
    • Frees, D.1    Savijoki, K.2    Varmanen, P.3    Ingmer, H.4
  • 43
    • 0041387477 scopus 로고    scopus 로고
    • ClpE from Lactococcus lactis promotes repression of CtsR-dependent gene expression
    • Varmanen P., Vogensen F.K., Hammer K., Palva A., Ingmer H. ClpE from Lactococcus lactis promotes repression of CtsR-dependent gene expression. J Bacteriol 2003, 185:5117-5124.
    • (2003) J Bacteriol , vol.185 , pp. 5117-5124
    • Varmanen, P.1    Vogensen, F.K.2    Hammer, K.3    Palva, A.4    Ingmer, H.5
  • 46
    • 0141789637 scopus 로고    scopus 로고
    • Surviving the acid test: responses of gram-positive bacteria to low pH
    • Cotter P.D., Hill C. Surviving the acid test: responses of gram-positive bacteria to low pH. Microbiol Mol Biol Rev 2003, 67:429-453.
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 429-453
    • Cotter, P.D.1    Hill, C.2
  • 48
    • 33645999355 scopus 로고    scopus 로고
    • S-adenosylmethionine: jack of all trades and master of everything?
    • Loenen W.A.M. S-adenosylmethionine: jack of all trades and master of everything?. Biochem Soc Trans 2006, 34:330-333.
    • (2006) Biochem Soc Trans , vol.34 , pp. 330-333
    • Loenen, W.A.M.1
  • 49
    • 70349758461 scopus 로고    scopus 로고
    • AI-2 signalling is induced by acidic shock in probiotic strains of Lactobacillus spp
    • Moslehi-Jenabian S., Gori K., Jespersen L. AI-2 signalling is induced by acidic shock in probiotic strains of Lactobacillus spp. Int J Food Microbiol 2009, 135:295-302.
    • (2009) Int J Food Microbiol , vol.135 , pp. 295-302
    • Moslehi-Jenabian, S.1    Gori, K.2    Jespersen, L.3
  • 50
    • 35948957069 scopus 로고    scopus 로고
    • Impact of environmental and genetic factors on biofilm formation by the probiotic strain Lactobacillus rhamnosus GG
    • Lebeer S., Verhoeven T.L.A., Vélez M.P., Vanderleyden J., De Keersmaecker S.C.J. Impact of environmental and genetic factors on biofilm formation by the probiotic strain Lactobacillus rhamnosus GG. Appl Environ Microbiol 2007, 73:6768-6775.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 6768-6775
    • Lebeer, S.1    Verhoeven, T.L.A.2    Vélez, M.P.3    Vanderleyden, J.4    De Keersmaecker, S.C.J.5
  • 51
    • 33846632778 scopus 로고    scopus 로고
    • Functional analysis of luxS in the probiotic strain Lactobacillus rhamnosus GG reveals a central metabolic role important for growth and biofilm formation
    • Lebeer S., De Keersmaecker S.C.J., Verhoeven T.L.A., Fadda A.A., Marchal K., Vanderleyden J. Functional analysis of luxS in the probiotic strain Lactobacillus rhamnosus GG reveals a central metabolic role important for growth and biofilm formation. J Bacteriol 2007, 189:860-871.
    • (2007) J Bacteriol , vol.189 , pp. 860-871
    • Lebeer, S.1    De Keersmaecker, S.C.J.2    Verhoeven, T.L.A.3    Fadda, A.A.4    Marchal, K.5    Vanderleyden, J.6
  • 52
    • 0036249521 scopus 로고    scopus 로고
    • Analysis of Streptococcus mutans proteins modulated by culture under acidic conditions
    • Wilkins J.C., Homer K.A., Beighton D. Analysis of Streptococcus mutans proteins modulated by culture under acidic conditions. Appl Environ Microbiol 2002, 68:2382-2390.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 2382-2390
    • Wilkins, J.C.1    Homer, K.A.2    Beighton, D.3
  • 53
    • 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., Beighton D. Altered protein expression of Streptococcus oralis cultured at low pH revealed by two-dimensional gel electrophoresis. Appl Environ Microbiol 2001, 67:3396-3405.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 3396-3405
    • Wilkins, J.C.1    Homer, K.A.2    Beighton, D.3
  • 55
    • 33645688327 scopus 로고    scopus 로고
    • Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes
    • Lévine A., Vannier F., Absalon C., Kuhn L., Jackson P., Scrivener E., et al. Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes. Proteomics 2006, 6:2157-2173.
    • (2006) Proteomics , vol.6 , pp. 2157-2173
    • Lévine, A.1    Vannier, F.2    Absalon, C.3    Kuhn, L.4    Jackson, P.5    Scrivener, E.6
  • 56
    • 0029931616 scopus 로고    scopus 로고
    • Phosphorylation of GroEL, DnaK and other proteins from Thiobacillus ferrooxidans grown under different conditions
    • Seeger M., Osorio G., Jerez C.A. Phosphorylation of GroEL, DnaK and other proteins from Thiobacillus ferrooxidans grown under different conditions. FEMS Microbiol Lett 1996, 138:129-134.
    • (1996) FEMS Microbiol Lett , vol.138 , pp. 129-134
    • Seeger, M.1    Osorio, G.2    Jerez, C.A.3
  • 57
    • 0032497336 scopus 로고    scopus 로고
    • Phosphorylation of Mycobacterium leprae heat-shock 70 protein at threonine 175 alters its substrate binding characteristics
    • Peake P., Winter N., Britton W. Phosphorylation of Mycobacterium leprae heat-shock 70 protein at threonine 175 alters its substrate binding characteristics. Biochim Biophys Acta 1998, 1387:387-394.
    • (1998) Biochim Biophys Acta , vol.1387 , pp. 387-394
    • Peake, P.1    Winter, N.2    Britton, W.3
  • 58
    • 0026519887 scopus 로고
    • Heat shock in Escherichia coli alters the protein-binding properties of the chaperonin groEL by inducing its phosphorylation
    • Sherman M.Y., Goldberg A.L. Heat shock in Escherichia coli alters the protein-binding properties of the chaperonin groEL by inducing its phosphorylation. Nature 1992, 357:167-169.
    • (1992) Nature , vol.357 , pp. 167-169
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 59
    • 0027220168 scopus 로고
    • Heat shock of Escherichia coli increases binding of dnaK (the hsp70 homolog) to polypeptides by promoting its phosphorylation
    • Sherman M.Y., Goldberg A.L. Heat shock of Escherichia coli increases binding of dnaK (the hsp70 homolog) to polypeptides by promoting its phosphorylation. Proc Natl Acad Sci USA 1993, 90:8648-8652.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8648-8652
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 60
    • 0031947980 scopus 로고    scopus 로고
    • Post-translational modification of proteins by reversible phosphorylation in prokaryotes
    • Cozzone A.J. Post-translational modification of proteins by reversible phosphorylation in prokaryotes. Biochimie 1998, 80:43-48.
    • (1998) Biochimie , vol.80 , pp. 43-48
    • Cozzone, A.J.1
  • 61
    • 34247325212 scopus 로고    scopus 로고
    • The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis
    • Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., et al. The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol Cell Proteomics 2007, 6:697-707.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 697-707
    • Macek, B.1    Mijakovic, I.2    Olsen, J.V.3    Gnad, F.4    Kumar, C.5    Jensen, P.R.6
  • 62
    • 52649125713 scopus 로고    scopus 로고
    • The Ser/Thr/Tyr phosphoproteome of Lactococcus lactis IL1403 reveals multiply phosphorylated proteins
    • Soufi B., Gnad F., Jensen P.R., Petranovic D., Mann M., Mijakovic I., et al. The Ser/Thr/Tyr phosphoproteome of Lactococcus lactis IL1403 reveals multiply phosphorylated proteins. Proteomics 2008, 8:3486-3493.
    • (2008) Proteomics , vol.8 , pp. 3486-3493
    • Soufi, B.1    Gnad, F.2    Jensen, P.R.3    Petranovic, D.4    Mann, M.5    Mijakovic, I.6
  • 63
    • 0037344041 scopus 로고    scopus 로고
    • Proteomic analysis of Lactococcus lactis, a lactic acid bacterium
    • Guillot A., Gitton C., Anglade P., Mistou M.Y. Proteomic analysis of Lactococcus lactis, a lactic acid bacterium. Proteomics 2003, 3:337-354.
    • (2003) Proteomics , vol.3 , pp. 337-354
    • Guillot, A.1    Gitton, C.2    Anglade, P.3    Mistou, M.Y.4
  • 64
    • 51149113074 scopus 로고    scopus 로고
    • Phosphoproteomics in bacteria: towards a systemic understanding of bacterial phosphorylation networks
    • Jers C., Soufi B., Grangeasse C., Deutscher J., Mijakovic I. Phosphoproteomics in bacteria: towards a systemic understanding of bacterial phosphorylation networks. Expert Rev Proteomics 2008, 5:619-627.
    • (2008) Expert Rev Proteomics , vol.5 , pp. 619-627
    • Jers, C.1    Soufi, B.2    Grangeasse, C.3    Deutscher, J.4    Mijakovic, I.5
  • 65
    • 77950369259 scopus 로고    scopus 로고
    • Moonlighting proteins: an intriguing mode of multitasking
    • Huberts D.H.E.W., van der Klei I.J. Moonlighting proteins: an intriguing mode of multitasking. Biochim Biophys Acta 2010, 1803:520-525.
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 520-525
    • Huberts, D.H.E.W.1    van der Klei, I.J.2
  • 66
    • 0026682564 scopus 로고
    • A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity
    • Pancholi V., Fischetti V.A. A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity. J Exp Med 1992, 176:415-426.
    • (1992) J Exp Med , vol.176 , pp. 415-426
    • Pancholi, V.1    Fischetti, V.A.2
  • 69
    • 1842431723 scopus 로고    scopus 로고
    • Cell surface-associated elongation factor Tu mediates the attachment of Lactobacillus johnsonii NCC533 (La1) to human intestinal cells and mucins
    • Granato D., Bergonzelli G.E., Pridmore R.D., Marvin L., Rouvet M., Corthésy-Theulaz I.E. Cell surface-associated elongation factor Tu mediates the attachment of Lactobacillus johnsonii NCC533 (La1) to human intestinal cells and mucins. Infect Immun 2004, 72:2160-2169.
    • (2004) Infect Immun , vol.72 , pp. 2160-2169
    • Granato, D.1    Bergonzelli, G.E.2    Pridmore, R.D.3    Marvin, L.4    Rouvet, M.5    Corthésy-Theulaz, I.E.6
  • 70
    • 26844454554 scopus 로고    scopus 로고
    • Correlation of probiotic Lactobacillus salivarius growth phase with its cell wall-associated proteome
    • Kelly P., Maguire P.B., Bennett M., Fitzgerald D.J., Edwards R.J., Thiede B., et al. Correlation of probiotic Lactobacillus salivarius growth phase with its cell wall-associated proteome. FEMS Microbiol Lett 2005, 252:153-159.
    • (2005) FEMS Microbiol Lett , vol.252 , pp. 153-159
    • Kelly, P.1    Maguire, P.B.2    Bennett, M.3    Fitzgerald, D.J.4    Edwards, R.J.5    Thiede, B.6


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