메뉴 건너뛰기




Volumn , Issue , 2011, Pages 603-625

Proteomics for the Analysis of Environmental Stress Responses in Prokaryotes

Author keywords

Metaproteomics, proteomics for analysis of environmental stress responses in prokaryotes; Proteomics application to analysis of stress response in microorganisms, stress responses; Top down proteomics analysis information about molecular weight of intact protein, fragmentation ladders

Indexed keywords


EID: 84886157855     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9781118010518.ch66     Document Type: Chapter
Times cited : (1)

References (231)
  • 1
    • 0032810422 scopus 로고    scopus 로고
    • Microbial stress response in minimal processing Int
    • Abee T, Wouters JA. 1999. Microbial stress response in minimal processing Int. J. Food Microbiol. 50:65-91.
    • (1999) J. Food Microbiol. , vol.50 , pp. 65-91
    • Abee, T.1    Wouters, J.A.2
  • 2
    • 53249147141 scopus 로고    scopus 로고
    • Not just for Eukarya anymore: Protein glycosylation in Bacteria and Archaea
    • Abu-Qarn M, Eichler J, Sharon N. 2008. Not just for Eukarya anymore: Protein glycosylation in Bacteria and Archaea. Curr. Opin Struct. Biol. 18:544-550.
    • (2008) Curr. Opin Struct. Biol. , vol.18 , pp. 544-550
    • Abu-Qarn, M.1    Eichler, J.2    Sharon, N.3
  • 4
    • 0032489015 scopus 로고    scopus 로고
    • The cells as a collection of protein machines: Preparing the next generation of molecular biologists
    • Alberts B. 1998. The cells as a collection of protein machines: Preparing the next generation of molecular biologists. Cell 92:291-294.
    • (1998) Cell , vol.92 , pp. 291-294
    • Alberts, B.1
  • 5
    • 33645721632 scopus 로고    scopus 로고
    • Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins
    • Anderson L, Hunter CL. 2006. Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins. Mol. Cell Proteom. 5:573-588.
    • (2006) Mol. Cell Proteom. , vol.5 , pp. 573-588
    • Anderson, L.1    Hunter, C.L.2
  • 6
    • 0033895238 scopus 로고    scopus 로고
    • Phosphate starvationinducible proteins of Bacillus subtilis: Proteomics and transcriptional analysis
    • Antelmann H, Scharf C, Hecker M. 2000. Phosphate starvationinducible proteins of Bacillus subtilis: Proteomics and transcriptional analysis. J. Bacteriol. 182:4478-4490.
    • (2000) J. Bacteriol. , vol.182 , pp. 4478-4490
    • Antelmann, H.1    Scharf, C.2    Hecker, M.3
  • 7
    • 35948969847 scopus 로고    scopus 로고
    • Stenotrophomonas maltophilia SeITE02, a new bacterial strain suitable for bioremediation of selenite-contaminated environmental matrices
    • Antonioli P, Lampis S, Chesini I. 2007. Stenotrophomonas maltophilia SeITE02, a new bacterial strain suitable for bioremediation of selenite-contaminated environmental matrices. Appl. Environ. Microbiol. 73:6854-6863.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 6854-6863
    • Antonioli, P.1    Lampis, S.2    Chesini, I.3
  • 9
    • 30744451442 scopus 로고    scopus 로고
    • In- gel stable-isotope labeling (ISIL): A strategy for mass spectrometry-based relative quantification
    • Asara JM, Zhang X, Zheng B, Christofk HH, Wu N, Cantley LC. 2006. In-gel stable-isotope labeling (ISIL): A strategy for mass spectrometry-based relative quantification. J. Proteome Res 5:155-163.
    • (2006) J. Proteome Res , vol.5 , pp. 155-163
    • Asara, J.M.1    Zhang, X.2    Zheng, B.3    Christofk, H.H.4    Wu, N.5    Cantley, L.C.6
  • 10
    • 23844471958 scopus 로고    scopus 로고
    • Molecular insight into extreme copper resistance in the extremophilic archaeon "Ferroplasma acidarmanus" Fer1
    • Baker-Austin C, Dopson M, Wexler M. 2005. Molecular insight into extreme copper resistance in the extremophilic archaeon "Ferroplasma acidarmanus" Fer1. Microbiology 151:2637-2646.
    • (2005) Microbiology , vol.151 , pp. 2637-2646
    • Baker-Austin, C.1    Dopson, M.2    Wexler, M.3
  • 11
    • 34248327854 scopus 로고    scopus 로고
    • Extreme arsenic resistance by the acidophilic archaeon "Ferroplasma acidarmanus" Fer1
    • Baker-Austin C, Dopson M, Wexler M. 2007. Extreme arsenic resistance by the acidophilic archaeon "Ferroplasma acidarmanus" Fer1 Extremophiles 11:425-434.
    • (2007) Extremophiles , vol.11 , pp. 425-434
    • Baker-Austin, C.1    Dopson, M.2    Wexler, M.3
  • 12
    • 33645215770 scopus 로고    scopus 로고
    • Signal transduction in bacterial chemotaxis
    • Baker MD, Wolanin PM, Stock JB. 2006. Signal transduction in bacterial chemotaxis. BioEssays 28:9-22.
    • (2006) BioEssays , vol.28 , pp. 9-22
    • Baker, M.D.1    Wolanin, P.M.2    Stock, J.B.3
  • 14
    • 33846908531 scopus 로고    scopus 로고
    • Proteomic profiling of cellular stresses in Bacillus subtilis reveals cellular networks and assists in elucidating antibiotic mechanisms of action
    • Bandow JE, Hecker M. 2007. Proteomic profiling of cellular stresses in Bacillus subtilis reveals cellular networks and assists in elucidating antibiotic mechanisms of action. Prog. Drug Res. 64:81-101.
    • (2007) Prog. Drug Res. , vol.64 , pp. 81-101
    • Bandow, J.E.1    Hecker, M.2
  • 17
    • 0028895181 scopus 로고
    • High pressure influences on gene and protein expression
    • Bartlett DH, Kato C, Horikoshi K. 1995. High pressure influences on gene and protein expression. Res. Microbiol. 146:697-706.
    • (1995) Res. Microbiol. , vol.146 , pp. 697-706
    • Bartlett, D.H.1    Kato, C.2    Horikoshi, K.3
  • 18
    • 0036185884 scopus 로고    scopus 로고
    • Involvement of superoxide dismutases in the response of Escherichia coli to selenium oxides
    • Bebien M, Lagniel G, Garin J. 2002. Involvement of superoxide dismutases in the response of Escherichia coli to selenium oxides. J Bacteriol. 184:1556-1564.
    • (2002) J Bacteriol , vol.184 , pp. 1556-1564
    • Bebien, M.1    Lagniel, G.2    Garin, J.3
  • 19
    • 0023405116 scopus 로고
    • Membrane ATPases and acid tolerance of Actinomyces viscosus and Lactobacillus casei
    • Bender GR, Marquis RE. 1987. Membrane ATPases and acid tolerance of Actinomyces viscosus and Lactobacillus casei. Appl. Environ Microbiol. 53:2124-2128.
    • (1987) Appl. Environ Microbiol. , vol.53 , pp. 2124-2128
    • Bender, G.R.1    Marquis, R.E.2
  • 21
    • 0037317457 scopus 로고    scopus 로고
    • Bacillus subtilis during feast and famine: Visualization of the overall regulation of protein synthesis during glucose starvation by proteome analysis
    • Bernhardt J, Weibezahn J, Scharf C, Hecker M. 2003. Bacillus subtilis during feast and famine: Visualization of the overall regulation of protein synthesis during glucose starvation by proteome analysis. Genome Res. 13:224-237.
    • (2003) Genome Res , vol.13 , pp. 224-237
    • Bernhardt, J.1    Weibezahn, J.2    Scharf, C.3    Hecker, M.4
  • 22
    • 22144475854 scopus 로고    scopus 로고
    • Environmental stress, adaptation and evolution: An overview
    • Bijlsma R, Loeschcke V. 2005. Environmental stress, adaptation and evolution: An overview. J. Evol. Biol. 18:744-749.
    • (2005) J. Evol. Biol. , vol.18 , pp. 744-749
    • Bijlsma, R.1    Loeschcke, V.2
  • 23
    • 0032784646 scopus 로고    scopus 로고
    • Proteomics: Quantitative and physical mapping of cellular proteins
    • Blackstock WP, Weir MP. 1999. Proteomics: Quantitative and physical mapping of cellular proteins. Trends Biotechnol. 17:121-127.
    • (1999) Trends Biotechnol , vol.17 , pp. 121-127
    • Blackstock, W.P.1    Weir, M.P.2
  • 24
    • 4444371652 scopus 로고    scopus 로고
    • Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics
    • Blagoev B, Ong SE, Kratchmarova I, Mann M. 2004. Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics. Nat. Biotechnol. 22:1139-1145.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1139-1145
    • Blagoev, B.1    Ong, S.E.2    Kratchmarova, I.3    Mann, M.4
  • 25
    • 0038444555 scopus 로고    scopus 로고
    • Chill induction of the SigB-dependent general stress response in Bacillus subtilis and its contribution to lowtemperature adaptation
    • Brigulla M, Hoffmann T, Krisp A, Voelker A, Bremer E, Voelker U. 2003. Chill induction of the SigB-dependent general stress response in Bacillus subtilis and its contribution to lowtemperature adaptation. J. Bacteriol. 185:4305-4314.
    • (2003) J. Bacteriol. , vol.185 , pp. 4305-4314
    • Brigulla, M.1    Hoffmann, T.2    Krisp, A.3    Voelker, A.4    Bremer, E.5    Voelker, U.6
  • 26
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B, Horwich AL. 1998. The Hsp70 and Hsp60 chaperone machines. Cell 92:351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 27
    • 41149086763 scopus 로고    scopus 로고
    • Automated proteomics of Escherichia coli via topdown electron-transfer dissociation mass spectrometry
    • Bunger MK, Cargile BJ, Ngunjiri A, Bundy JL, Stephenson JLJ. 2008. Automated proteomics of Escherichia coli via topdown electron-transfer dissociation mass spectrometry. Anal. Chem 80:1459-1467.
    • (2008) Anal. Chem , vol.80 , pp. 1459-1467
    • Bunger, M.K.1    Cargile, B.J.2    Ngunjiri, A.3    Bundy, J.L.4    Stephenson, J.L.J.5
  • 28
    • 0034152767 scopus 로고    scopus 로고
    • Oxidative stress in bacteria and protein damage by reactive oxygen species
    • Cabiscol E, Tamarit J, Ros J. 2000. Oxidative stress in bacteria and protein damage by reactive oxygen species. Int. Microbiol. 3:3-8.
    • (2000) Int. Microbiol. , vol.3 , pp. 3-8
    • Cabiscol, E.1    Tamarit, J.2    Ros, J.3
  • 29
    • 0036171359 scopus 로고    scopus 로고
    • De novo peptide sequencing and quantitative profiling of complex protein mixtures using mass-coded abundance tagging
    • Cagney G, Emili A. 2002. De novo peptide sequencing and quantitative profiling of complex protein mixtures using mass-coded abundance tagging. Nat. Biotechnol. 20:163-170.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 163-170
    • Cagney, G.1    Emili, A.2
  • 30
    • 0032496137 scopus 로고    scopus 로고
    • Chaperone properties of bacterial elongation factor EF-Tu
    • Caldas TD, El Yaagoubi A, 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
  • 32
    • 67349214353 scopus 로고    scopus 로고
    • Proteomic analyses of the response of cyanobacteria to different stress conditions
    • Castielli O, De la Cerda B, Navarro JA, Hervas M, De la Rosa MA. 2009. Proteomic analyses of the response of cyanobacteria to different stress conditions. FEBS Lett. 583:1753-1758.
    • (2009) FEBS Lett , vol.583 , pp. 1753-1758
    • Castielli, O.1    De la Cerda, B.2    Navarro, J.A.3    Hervas, M.4    De la Rosa, M.A.5
  • 33
    • 33749615256 scopus 로고    scopus 로고
    • Mass spectrometry: Bottom-up or top-down ?
    • Chait BT. 2006. Mass spectrometry: Bottom-up or top-down ? Science 314:65-66.
    • (2006) Science , vol.314 , pp. 65-66
    • Chait, B.T.1
  • 34
    • 0037040607 scopus 로고    scopus 로고
    • Global internal standard technology for comparative proteomics
    • Chakraborty A, Regnier FE. 2002. Global internal standard technology for comparative proteomics. J. Chromatogr. A 949:173-184.
    • (2002) J. Chromatogr. A , vol.949 , pp. 173-184
    • Chakraborty, A.1    Regnier, F.E.2
  • 35
    • 66949152206 scopus 로고    scopus 로고
    • Proteomic analysis of the response to the plant growth-promoting bacterium Pseudomonas putida UW4 to nickel stress
    • Cheng Z, Wei Y-YC, Sung WWL, Glick BR, McConkey BJ. 2009 Proteomic analysis of the response to the plant growth-promoting bacterium Pseudomonas putida UW4 to nickel stress. Proteome Sci. 7:1-8.
    • (2009) Proteome Sci , vol.7 , pp. 1-8
    • Cheng, Z.1    Wei, Y.-Y.C.2    Sung, W.W.L.3    Glick, B.R.4    McConkey, B.J.5
  • 36
    • 33644748620 scopus 로고    scopus 로고
    • Global analysis of heat shock response in Desulfovibrio vulgaris Hildenborough
    • Chhabra SR, He Q, Huang KH, Gaucher SP, Alm EJ, et al. 2006 Global analysis of heat shock response in Desulfovibrio vulgaris Hildenborough. J. Bacteriol. 188:1817-1828.
    • (2006) J. Bacteriol. , vol.188 , pp. 1817-1828
    • Chhabra, S.R.1    He, Q.2    Huang, K.H.3    Gaucher, S.P.4    Alm, E.J.5
  • 38
    • 0034739891 scopus 로고    scopus 로고
    • Proteome analysis of light-induced proteins in Synechocystis sp. PCC 6803 Identification of proteins separated by 2D-PAGE using N-terminal sequencing and MALDITOF MS
    • Choi JS, Kim DS, Lee J, Kim SJ, Kim SI, Kim YH, Hong J, Yoo JS, Suh KH, Park YM. 2000. Proteome analysis of light-induced proteins in Synechocystis sp. PCC 6803: Identification of proteins separated by 2D-PAGE using N-terminal sequencing and MALDITOF MS. Mol. Cells 10:705-711.
    • (2000) Mol. Cells , vol.10 , pp. 705-711
    • Choi, J.S.1    Kim, D.S.2    Lee, J.3    Kim, S.J.4    Kim, S.I.5    Kim, Y.H.6    Hong, J.7    Yoo, J.S.8    Suh, K.H.9    Park, Y.M.10
  • 39
    • 33847123483 scopus 로고    scopus 로고
    • Translational and transcriptional analysis of Sulfolobus solfataricus P2 to provide insights into alcohol and ketone utilisation
    • Chong PK, Burja AM, Radianingtyas H, Fazeli A, Wright PC. 2007. Translational and transcriptional analysis of Sulfolobus solfataricus P2 to provide insights into alcohol and ketone utilisation Proteomics 7:424-435.
    • (2007) Proteomics , vol.7 , pp. 424-435
    • Chong, P.K.1    Burja, A.M.2    Radianingtyas, H.3    Fazeli, A.4    Wright, P.C.5
  • 40
    • 0041358793 scopus 로고    scopus 로고
    • OLAV: Towards high-throughput tandem mass spectrometry data identification
    • Colinge J, Masselot A, Giron M, Dessingy T, Magnin J. 2003 OLAV: Towards high-throughput tandem mass spectrometry data identification. Proteomics 3:1454-1463.
    • (2003) Proteomics , vol.3 , pp. 1454-1463
    • Colinge, J.1    Masselot, A.2    Giron, M.3    Dessingy, T.4    Magnin, J.5
  • 41
    • 34548481968 scopus 로고    scopus 로고
    • Labeling of Bifidobacterium longum cells with 13C-substituted leucine for quantitative proteomic analyses
    • Coute Y, Hernandez C, Appel RD, Sanchez JC, Margolles A. 2007. Labeling of Bifidobacterium longum cells with 13C-substituted leucine for quantitative proteomic analyses. Appl. Environ. Microbiol 73:5653-5656.
    • (2007) Appl. Environ. Microbiol , vol.73 , pp. 5653-5656
    • Coute, Y.1    Hernandez, C.2    Appel, R.D.3    Sanchez, J.C.4    Margolles, A.5
  • 42
    • 33645715370 scopus 로고    scopus 로고
    • Multiple reaction monitoring as a method for identifying protein posttranslational modifications
    • Cox DM, Zhong F, Du M, Duchoslav E, Sakuma T, McDermott JC. 2005. Multiple reaction monitoring as a method for identifying protein posttranslational modifications. J. Biomol. Tech. 16:83-90.
    • (2005) J. Biomol. Tech. , vol.16 , pp. 83-90
    • Cox, D.M.1    Zhong, F.2    Du, M.3    Duchoslav, E.4    Sakuma, T.5    McDermott, J.C.6
  • 43
    • 0141955057 scopus 로고    scopus 로고
    • A method for reducing the time required to match protein sequences with tandem mass spectra
    • Craig R, Beavis RC. 2003. A method for reducing the time required to match protein sequences with tandem mass spectra. Rapid Commun Mass Spectrom. 17:2310-2316.
    • (2003) Rapid Commun Mass Spectrom , vol.17 , pp. 2310-2316
    • Craig, R.1    Beavis, R.C.2
  • 44
    • 3142702204 scopus 로고    scopus 로고
    • TANDEM: Matching proteins with tandem mass spectra
    • Craig R, Beavis RC. 2004. TANDEM: Matching proteins with tandem mass spectra. Bioinformatics 20:1466-1467.
    • (2004) Bioinformatics , vol.20 , pp. 1466-1467
    • Craig, R.1    Beavis, R.C.2
  • 45
    • 37249014081 scopus 로고    scopus 로고
    • The biological impact of mass-spectrometry-based proteomics
    • Cravatt BF, Simon GM, Yates J. 2007. The biological impact of mass-spectrometry-based proteomics. Nature 450:991-1000.
    • (2007) Nature , vol.450 , pp. 991-1000
    • Cravatt, B.F.1    Simon, G.M.2    Yates, J.3
  • 47
    • 0036951961 scopus 로고    scopus 로고
    • Arginine catabolism by sourdough lactic acid bacteria: purification and characterization of the arginine deiminase pathway enzymes from Lactobacillus sanfranciscensis CB1
    • De Angelis M, Mariotti L, Rossi J, Servili M, Fox PF, Rollan G, Gobbetti M. 2002. Arginine catabolism by sourdough lactic acid bacteria: purification and characterization of the arginine deiminase pathway enzymes from Lactobacillus sanfranciscensis CB1. Appl Environ. Microbiol. 68:6193-6201.
    • (2002) Appl Environ. Microbiol. , vol.68 , pp. 6193-6201
    • De Angelis, M.1    Mariotti, L.2    Rossi, J.3    Servili, M.4    Fox, P.F.5    Rollan, G.6    Gobbetti, M.7
  • 49
    • 17444383113 scopus 로고    scopus 로고
    • Search for cancer markers from endometrial tissues using differentially labeled tags iTRAQ and cICAT with multidimensional liquid chromatography and tandem mass spectrometry J
    • de Souza L, Diehl G, Rodrigues MJ, Guo J, Romaschin AD, Colgan TJ, Siu KW. 2005. Search for cancer markers from endometrial tissues using differentially labeled tags iTRAQ and cICAT with multidimensional liquid chromatography and tandem mass spectrometry J. Proteome Res. 4:377-386.
    • (2005) Proteome Res , vol.4 , pp. 377-386
    • de Souza, L.1    Diehl, G.2    Rodrigues, M.J.3    Guo, J.4    Romaschin, A.D.5    Colgan, T.J.6    Siu, K.W.7
  • 50
    • 13844271208 scopus 로고    scopus 로고
    • Protein identification using 2D-LCMS/MS
    • Delahunty C, Yates JR. 2005. Protein identification using 2D-LCMS/MS. Methods 35:248-255.
    • (2005) Methods , vol.35 , pp. 248-255
    • Delahunty, C.1    Yates, J.R.2
  • 51
    • 0034876617 scopus 로고    scopus 로고
    • Securing genome stability by orchestrating DNA repair: Removal of radiation-induced clustered lesions in DNA
    • Dianov GL, O'Neill P, Goodhead DT. 2001. Securing genome stability by orchestrating DNA repair: Removal of radiation-induced clustered lesions in DNA. BioEssays 23:745-749.
    • (2001) BioEssays , vol.23 , pp. 745-749
    • Dianov, G.L.1    O'Neill, P.2    Goodhead, D.T.3
  • 52
    • 33750622611 scopus 로고    scopus 로고
    • Challenges and opportunities in proteomics data analysis
    • Domon B, Aebersold R. 2006a. Challenges and opportunities in proteomics data analysis. Mol. Cell. Proteom. 5:1921-1926.
    • (2006) Mol. Cell. Proteom. , vol.5 , pp. 1921-1926
    • Domon, B.1    Aebersold, R.2
  • 53
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • Domon B, Aebersold R. 2006b. Mass spectrometry and protein analysis Science 312:212-217.
    • (2006) Science , vol.312 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 54
    • 0030884713 scopus 로고    scopus 로고
    • Emerging tandem-massspectrometry techniques for the rapid identification of proteins
    • Dongre AR, Eng JK, Yates JR. 1997. Emerging tandem-massspectrometry techniques for the rapid identification of proteins. Trends Biotechnol. 15:418-425.
    • (1997) Trends Biotechnol , vol.15 , pp. 418-425
    • Dongre, A.R.1    Eng, J.K.2    Yates, J.R.3
  • 55
    • 0028172999 scopus 로고
    • The oxidative stress response in Bacillus subtilis
    • Dowds BC. 1994. The oxidative stress response in Bacillus subtilis FEMS Microbiol. 124:155-264.
    • (1994) FEMS Microbiol , vol.124 , pp. 155-264
    • Dowds, B.C.1
  • 56
    • 0035987521 scopus 로고    scopus 로고
    • High pressure effects stepwise altered protein expression in Lactobacillus sanfranciscensis
    • Drews O, Weiss W, Reil G, Parlar H, Wait R, Goerg A. 2002. High pressure effects stepwise altered protein expression in Lactobacillus sanfranciscensis. Proteomics 2:765-774.
    • (2002) Proteomics , vol.2 , pp. 765-774
    • Drews, O.1    Weiss, W.2    Reil, G.3    Parlar, H.4    Wait, R.5    Goerg, A.6
  • 57
    • 0032531568 scopus 로고    scopus 로고
    • Coupling 2D SDS-PAGE with CNBr cleavage and MALDI-TOFMS: A strategy applied to the identification of proteins induced by a hypochlorous acid stress in Escherichia coli
    • Dukan S, Turlin E, Biville F. 1998. Coupling 2D SDS-PAGE with CNBr cleavage and MALDI-TOFMS: A strategy applied to the identification of proteins induced by a hypochlorous acid stress in Escherichia coli. Anal. Chem. 70:4433-4440.
    • (1998) Anal. Chem. , vol.70 , pp. 4433-4440
    • Dukan, S.1    Turlin, E.2    Biville, F.3
  • 59
    • 24944463449 scopus 로고    scopus 로고
    • Posttranslational protein modification in Archaea
    • Eichler J, Adams MW. 2005. Posttranslational protein modification in Archaea. Microbiol. Mol. Biol. Rev. 69:393-425.
    • (2005) Microbiol. Mol. Biol. Rev. , vol.69 , pp. 393-425
    • Eichler, J.1    Adams, M.W.2
  • 60
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng JK, McCormack AL, Yates JRI. 1994. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 5:976-989.
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.I.3
  • 61
    • 0035750172 scopus 로고    scopus 로고
    • Toxic metals and oxidative stress part I: Mechanisms involved in metal-induced oxidative damage
    • Ercal N, Gurer-Orhan H, Aykin-Burns N. 2001. Toxic metals and oxidative stress part I: Mechanisms involved in metal-induced oxidative damage. Curr. Top. Med. Chem. 1:529-539.
    • (2001) Curr. Top. Med. Chem. , vol.1 , pp. 529-539
    • Ercal, N.1    Gurer-Orhan, H.2    Aykin-Burns, N.3
  • 62
  • 63
    • 0029905620 scopus 로고    scopus 로고
    • Phosphatestarvation-inducible proteins in Bacillus subtilis: A two-dimensional gel electrophoresis study
    • Eymann C, Mach H, Harwood CR, Hecker M. 1996. Phosphatestarvation-inducible proteins in Bacillus subtilis: A two-dimensional gel electrophoresis study. Microbiology 142:3163-3170.
    • (1996) Microbiology , vol.142 , pp. 3163-3170
    • Eymann, C.1    Mach, H.2    Harwood, C.R.3    Hecker, M.4
  • 64
    • 57649220810 scopus 로고    scopus 로고
    • A proteome analysis of the cadmium and mercury response in Corynebacterium japonicum
    • Fanous A, Weiss W, Goerg A, Jacob F, Parlar H. 2008. A proteome analysis of the cadmium and mercury response in Corynebacterium japonicum. Proteomics 8:4976-4986.
    • (2008) Proteomics , vol.8 , pp. 4976-4986
    • Fanous, A.1    Weiss, W.2    Goerg, A.3    Jacob, F.4    Parlar, H.5
  • 66
    • 0026347284 scopus 로고
    • Inducible pH homeostasis and the acid tolerance response of Salmonella typhimurium
    • Foster JW, Hall HK. 1991. Inducible pH homeostasis and the acid tolerance response of Salmonella typhimurium. J. Bacteriol 173:5129-5135.
    • (1991) J. Bacteriol , vol.173 , pp. 5129-5135
    • Foster, J.W.1    Hall, H.K.2
  • 67
    • 0033797930 scopus 로고    scopus 로고
    • Proteomics of Synechocystis sp. strain PCC 6803 Identification of periplasmic protein in cells grown at low and high salt concentrations Eur
    • Fulda S, Huang F, Nilsson F, Hagemann M, Norling B. 2000 Proteomics of Synechocystis sp. strain PCC 6803. Identification of periplasmic protein in cells grown at low and high salt concentrations Eur. J. Biochem. 267:5900-5907.
    • (2000) J. Biochem. , vol.267 , pp. 5900-5907
    • Fulda, S.1    Huang, F.2    Nilsson, F.3    Hagemann, M.4    Norling, B.5
  • 68
    • 33646724888 scopus 로고    scopus 로고
    • Proteome analysis of salt stress response in the cyanobacterium Synechocystis sp. strain PCC 6803
    • Fulda S, Mikkat S, Huang F, Huckauf J, Marin K, Norling B, Hagemann M. 2006. Proteome analysis of salt stress response in the cyanobacterium Synechocystis sp. strain PCC 6803. Proteomics 6:2733-2745.
    • (2006) Proteomics , vol.6 , pp. 2733-2745
    • Fulda, S.1    Mikkat, S.2    Huang, F.3    Huckauf, J.4    Marin, K.5    Norling, B.6    Hagemann, M.7
  • 69
    • 0032447960 scopus 로고    scopus 로고
    • General stress transcription factor ?B and sporulation transcription factor ?H each contribute to survival of Bacillus subtilis under extreme growth conditions
    • Gaidenko TA, Price CW. 1998. General stress transcription factor ?B and sporulation transcription factor ?H each contribute to survival of Bacillus subtilis under extreme growth conditions. J. Bacteriol 180:3730-3733.
    • (1998) J. Bacteriol , vol.180 , pp. 3730-3733
    • Gaidenko, T.A.1    Price, C.W.2
  • 70
    • 20544442274 scopus 로고    scopus 로고
    • Comparison of protein and peptide prefractionation methods for the shotgun proteomic analysis of Synechocystis sp PCC 6803
    • Gan CS, Reardon KF, Wright PC. 2005. Comparison of protein and peptide prefractionation methods for the shotgun proteomic analysis of Synechocystis sp. PCC 6803. Proteomics 5:2468-2478.
    • (2005) Proteomics , vol.5 , pp. 2468-2478
    • Gan, C.S.1    Reardon, K.F.2    Wright, P.C.3
  • 71
    • 64949130793 scopus 로고    scopus 로고
    • Identification of the proteomic changes in Synechocystis sp PCC 6803 following prolonged UV-B irradiation
    • Gao Y, Xiong W, Li XB, Gao CF, Zhang YL, Li H, Wu QY. 2009. Identification of the proteomic changes in Synechocystis sp PCC 6803 following prolonged UV-B irradiation. J. Exp. Bot. 60:1141-1154.
    • (2009) J. Exp. Bot. , vol.60 , pp. 1141-1154
    • Gao, Y.1    Xiong, W.2    Li, X.B.3    Gao, C.F.4    Zhang, Y.L.5    Li, H.6    Wu, Q.Y.7
  • 73
    • 8744300809 scopus 로고    scopus 로고
    • Multiplexed fluorescence detection of phosphorylation, glycosylation, and total protein in the proteomic analysis of breast cancer refractoriness
    • Ge Y, Rajkumar L, Guzman RC, Nandi S, Patton WF, Agnew BJ. 2004. Multiplexed fluorescence detection of phosphorylation, glycosylation, and total protein in the proteomic analysis of breast cancer refractoriness. Proteomics 4:3464-3467.
    • (2004) Proteomics , vol.4 , pp. 3464-3467
    • Ge, Y.1    Rajkumar, L.2    Guzman, R.C.3    Nandi, S.4    Patton, W.F.5    Agnew, B.J.6
  • 76
    • 10644230916 scopus 로고    scopus 로고
    • Current two-dimensional electrophoresis technology for proteomics
    • Gorg A, Weiss W, Dunn MJ. 2004. Current two-dimensional electrophoresis technology for proteomics. Proteomics 4:3665-3685.
    • (2004) Proteomics , vol.4 , pp. 3665-3685
    • Gorg, A.1    Weiss, W.2    Dunn, M.J.3
  • 77
    • 0036198666 scopus 로고    scopus 로고
    • Two- dimensional electrophoresis study of Lactobacillus delbrueckii subsp. bulgaricus thermotolerance Appl
    • Gouesbet G, Jan G, Boyaval P. 2002. Two-dimensional electrophoresis study of Lactobacillus delbrueckii subsp. bulgaricus thermotolerance Appl. Environ. Microbiol. 68:1055-1063.
    • (2002) Environ. Microbiol. , vol.68 , pp. 1055-1063
    • Gouesbet, G.1    Jan, G.2    Boyaval, P.3
  • 78
    • 33645784124 scopus 로고    scopus 로고
    • Topdown proteomic analysis of the soluble sub-proteome of the obligate thermophile Geobacillus thermoleovorans T80: Insights into the cellular processes
    • Graham RLJ, Pollock CE, Ternan NG, McMullan G. 2006. Topdown proteomic analysis of the soluble sub-proteome of the obligate thermophile, Geobacillus thermoleovorans T80: Insights into the cellular processes. J. Proteome Res. 5:822-828.
    • (2006) J. Proteome Res. , vol.5 , pp. 822-828
    • Graham, R.L.J.1    Pollock, C.E.2    Ternan, N.G.3    McMullan, G.4
  • 81
    • 0033002716 scopus 로고    scopus 로고
    • Cold shock proteins CspB and CspC are major stationary-phase-induced proteins in Bacillus subtilis Arch
    • Graumann PL, Marahiel MA. 1999a. Cold shock proteins CspB and CspC are major stationary-phase-induced proteins in Bacillus subtilis Arch. Microbiol. 171:135-138.
    • (1999) Microbiol , vol.171 , pp. 135-138
    • Graumann, P.L.1    Marahiel, M.A.2
  • 83
    • 0022972149 scopus 로고
    • Starvation proteins in Escherichia coli: Kinetics of synthesis and role in starvation survival
    • Groat RG, Schultz JE, Zychlinsky E, Bockman A, Matin A. 1986 Starvation proteins in Escherichia coli: Kinetics of synthesis and role in starvation survival. J. Bacteriol. 168:486-493.
    • (1986) J. Bacteriol. , vol.168 , pp. 486-493
    • Groat, R.G.1    Schultz, J.E.2    Zychlinsky, E.3    Bockman, A.4    Matin, A.5
  • 87
    • 33749606981 scopus 로고    scopus 로고
    • Extending topdown mass spectrometry to proteins with masses greater than 200 kilodaltons
    • Han X, Jin M, Breuker K, McLafferty FW. 2006. Extending topdown mass spectrometry to proteins with masses greater than 200 kilodaltons. Science 314:109-112.
    • (2006) Science , vol.314 , pp. 109-112
    • Han, X.1    Jin, M.2    Breuker, K.3    McLafferty, F.W.4
  • 88
    • 0034012953 scopus 로고    scopus 로고
    • Biomedical applications of two-dimensional electrophoresis using immobilized pH gradients: Current status
    • Hanash SM. 2000. Biomedical applications of two-dimensional electrophoresis using immobilized pH gradients: Current status. Electrophoresis 21:1202-1209.
    • (2000) Electrophoresis , vol.21 , pp. 1202-1209
    • Hanash, S.M.1
  • 91
    • 0038621801 scopus 로고    scopus 로고
    • Reactive oxygen species and UV-B: Effect on cyanobacteria
    • He YY, Haeder D. 2002. Reactive oxygen species and UV-B: Effect on cyanobacteria. Photochem. Photobiol. Sci. 1:729-736.
    • (2002) Photochem. Photobiol. Sci. , vol.1 , pp. 729-736
    • He, Y.Y.1    Haeder, D.2
  • 92
    • 0034987011 scopus 로고    scopus 로고
    • General stress response of Bacillus subtilis and other bacteria
    • Hecker M, Voelker U. 2001. General stress response of Bacillus subtilis and other bacteria. Adv. Microb. Physiol. 44:35-91.
    • (2001) Adv. Microb. Physiol. , vol.44 , pp. 35-91
    • Hecker, M.1    Voelker, U.2
  • 93
    • 10644274361 scopus 로고    scopus 로고
    • Towards a comprehensive understanding of Bacillus subtilis cell physiology by physiological proteomics
    • Hecker M, Voelker U. 2004. Towards a comprehensive understanding of Bacillus subtilis cell physiology by physiological proteomics Proteomics 4:3727-3750.
    • (2004) Proteomics , vol.4 , pp. 3727-3750
    • Hecker, M.1    Voelker, U.2
  • 94
    • 0030034307 scopus 로고    scopus 로고
    • Heat-shock and general stress response in Bacillus subtilis
    • Hecker M, Schumann W, Voelker U. 1996. Heat-shock and general stress response in Bacillus subtilis. Mol. Microbiol. 19:417-428.
    • (1996) Mol. Microbiol. , vol.19 , pp. 417-428
    • Hecker, M.1    Schumann, W.2    Voelker, U.3
  • 95
    • 57649218829 scopus 로고    scopus 로고
    • Gelbased proteomics of gram-positive bacteria: A powerful tool to address physiological questions
    • Hecker M, Antelmann H, Buettner K, Bernhardt J. 2008. Gelbased proteomics of gram-positive bacteria: A powerful tool to address physiological questions. Proteomics 8:4958-4975.
    • (2008) Proteomics , vol.8 , pp. 4958-4975
    • Hecker, M.1    Antelmann, H.2    Buettner, K.3    Bernhardt, J.4
  • 96
    • 67349215276 scopus 로고    scopus 로고
    • Physiological proteomics and stress/starvation responses in Bacillus subtilis and Staphylococcus aureus
    • Hecker M, Reder A, Fuchs S, Pagels M, Engelmann S. 2009. Physiological proteomics and stress/starvation responses in Bacillus subtilis and Staphylococcus aureus. Res. Microbiol. 160:245-258.
    • (2009) Res. Microbiol. , vol.160 , pp. 245-258
    • Hecker, M.1    Reder, A.2    Fuchs, S.3    Pagels, M.4    Engelmann, S.5
  • 97
    • 61649111730 scopus 로고    scopus 로고
    • Analysis of the secretome of the soybean symbiont Bradyrhizobium japonicum J
    • Hempel J, Zehner S, Goettfert M, Patschkowski T. 2009. Analysis of the secretome of the soybean symbiont Bradyrhizobium japonicum J. Biotechnol. 140:51-58.
    • (2009) Biotechnol , vol.140 , pp. 51-58
    • Hempel, J.1    Zehner, S.2    Goettfert, M.3    Patschkowski, T.4
  • 98
    • 0026330981 scopus 로고
    • Trehalose synthesis genes are controlled by the putative sigma factor encoded by rpoS and are involved in stationary-phase thermotolerance in Escherichia coli
    • Hengge-Aronis R, Klein W, Lange R, Rimmele M, Boos W. 1991. Trehalose synthesis genes are controlled by the putative sigma factor encoded by rpoS and are involved in stationary-phase thermotolerance in Escherichia coli. J. Bacteriol. 173:7918-7924.
    • (1991) J. Bacteriol. , vol.173 , pp. 7918-7924
    • Hengge-Aronis, R.1    Klein, W.2    Lange, R.3    Rimmele, M.4    Boos, W.5
  • 99
    • 33645088173 scopus 로고    scopus 로고
    • Salt stress adaptation of Bacillus subtilis: A physiological proteomics approach
    • Hoeper D, Bernhardt J, Hecker M. 2006. Salt stress adaptation of Bacillus subtilis: A physiological proteomics approach. Proteomics 6:1550-1562.
    • (2006) Proteomics , vol.6 , pp. 1550-1562
    • Hoeper, D.1    Bernhardt, J.2    Hecker, M.3
  • 102
    • 32944467003 scopus 로고    scopus 로고
    • Proteomic screening of salt-stress-induced changes in plasma membranes of Synechocystis sp. strain PCC 6803
    • Huang F, Fulda S, Hagemann M, Norling B. 2006. Proteomic screening of salt-stress-induced changes in plasma membranes of Synechocystis sp. strain PCC 6803. Proteomics 6:910-920.
    • (2006) Proteomics , vol.6 , pp. 910-920
    • Huang, F.1    Fulda, S.2    Hagemann, M.3    Norling, B.4
  • 103
    • 0022310512 scopus 로고
    • Chemical changes induced in DNA by ionizing radiation
    • Hutchinson F. 1985. Chemical changes induced in DNA by ionizing radiation. Prog. Nucleic Acid Res. Mol. Biol. 32:115-154.
    • (1985) Prog. Nucleic Acid Res. Mol. Biol. , vol.32 , pp. 115-154
    • Hutchinson, F.1
  • 104
    • 22844436250 scopus 로고    scopus 로고
    • Quantitative mouse brain proteomics using culturederived isotope tags as internal standards
    • Ishihama YST, Tabata T, Miyamoto N, Sagane K, Nagasu T, Oda Y. 2005. Quantitative mouse brain proteomics using culturederived isotope tags as internal standards. Nat. Biotechnol 23:617-621.
    • (2005) Nat. Biotechnol , vol.23 , pp. 617-621
    • Ishihama, Y.S.T.1    Tabata, T.2    Miyamoto, N.3    Sagane, K.4    Nagasu, T.5    Oda, Y.6
  • 106
    • 0023761363 scopus 로고
    • Starvation-induced cross protection against heat or H2O2 challenge in Escherichia coli
    • Jenkins DE, Schultz JE, Matin A. 1988. Starvation-induced cross protection against heat or H2O2 challenge in Escherichia coli. J Bacteriol. 170:3910-3914.
    • (1988) J Bacteriol , vol.170 , pp. 3910-3914
    • Jenkins, D.E.1    Schultz, J.E.2    Matin, A.3
  • 107
    • 0025332515 scopus 로고
    • Starvation-induced cross protection against osmotic challenge in Escherichia coli
    • Jenkins DE, Chaisson SA, Matin A. 1990. Starvation-induced cross protection against osmotic challenge in Escherichia coli. J. Bacteriol 172:2779-2781.
    • (1990) J. Bacteriol , vol.172 , pp. 2779-2781
    • Jenkins, D.E.1    Chaisson, S.A.2    Matin, A.3
  • 108
    • 23844453654 scopus 로고    scopus 로고
    • Recent advancements in differential proteomics based on stable isotope coding
    • Julka S, Regnier FE. 2005. Recent advancements in differential proteomics based on stable isotope coding. Brief. Funct. Genom. Proteom 4:158-177.
    • (2005) Brief. Funct. Genom. Proteom , vol.4 , pp. 158-177
    • Julka, S.1    Regnier, F.E.2
  • 109
    • 0031129664 scopus 로고    scopus 로고
    • Protein identification by 2D-E gels by MALDI mass spectrometry
    • Jungblut P, Thiede B. 1997. Protein identification by 2D-E gels by MALDI mass spectrometry. Mass Spectrom. Rev. 16:145-162.
    • (1997) Mass Spectrom. Rev. , vol.16 , pp. 145-162
    • Jungblut, P.1    Thiede, B.2
  • 110
    • 52449116251 scopus 로고    scopus 로고
    • Molecular response of Campylobacter jejuni to cadmium stress
    • Kaakoush NO, Raftery M, Mendz GL. 2008. Molecular response of Campylobacter jejuni to cadmium stress. FEBS J. 275:5021-5033.
    • (2008) FEBS J , vol.275 , pp. 5021-5033
    • Kaakoush, N.O.1    Raftery, M.2    Mendz, G.L.3
  • 111
    • 23944451618 scopus 로고    scopus 로고
    • An evaluation, comparison, and accurate benchmarking of several publicly available MS/MS search algorithms: Sensitivity and specificity analysis
    • Kapp EA, Schuetz F, Connolly LM, Chakel JA, Meza JE, Miller, et al. 2005. An evaluation, comparison, and accurate benchmarking of several publicly available MS/MS search algorithms: Sensitivity and specificity analysis. Proteomics 5:3475-3490.
    • (2005) Proteomics , vol.5 , pp. 3475-3490
    • Kapp, E.A.1    Schuetz, F.2    Connolly, L.M.3    Chakel, J.A.4    Meza, J.E.5    Miller, X.6
  • 112
    • 34249995931 scopus 로고    scopus 로고
    • Quantitation of target proteins and posttranslational modifications in affinity-based proteomics approaches Expert Rev
    • Kiernan UA. 2007. Quantitation of target proteins and posttranslational modifications in affinity-based proteomics approaches Expert Rev. Proteom. 4:421-428.
    • (2007) Proteom , vol.4 , pp. 421-428
    • Kiernan, U.A.1
  • 113
    • 34648822321 scopus 로고    scopus 로고
    • A proteomics strategy for the analysis of bacterial biodegradation pathways
    • Kim SI, Choi JS, Kahng HY. 2007. A proteomics strategy for the analysis of bacterial biodegradation pathways. OMICS 11:280-294.
    • (2007) OMICS , vol.11 , pp. 280-294
    • Kim, S.I.1    Choi, J.S.2    Kahng, H.Y.3
  • 114
    • 13444260275 scopus 로고    scopus 로고
    • The absolute quantification strategy: A general procedure for the quantification of proteins and post-translational modifications
    • Kirkpatrick DS, Gerber SA, Gygi SP. 2005. The absolute quantification strategy: A general procedure for the quantification of proteins and post-translational modifications. Methods 35:265-273.
    • (2005) Methods , vol.35 , pp. 265-273
    • Kirkpatrick, D.S.1    Gerber, S.A.2    Gygi, S.P.3
  • 115
    • 0036426322 scopus 로고    scopus 로고
    • The cell membrane plays a crucial role in survival of bacteria and archaea in extreme environments
    • Konings WN, Albers S-V, Koning S, Driessen AJM. 2002. The cell membrane plays a crucial role in survival of bacteria and archaea in extreme environments. Antonie van Leeuwenhoek 81:61-72.
    • (2002) Antonie van Leeuwenhoek , vol.81 , pp. 61-72
    • Konings, W.N.1    Albers, S.-V.2    Koning, S.3    Driessen, A.J.M.4
  • 117
    • 33745711866 scopus 로고    scopus 로고
    • Proteomic characterization of acid stress response in Synechocystis sp
    • Kurian D, Phadwal K, Maeenpaeae P. 2006. Proteomic characterization of acid stress response in Synechocystis sp. PCC 6803 Proteomics 6:3614-3624.
    • (2006) PCC 6803 Proteomics , vol.6 , pp. 3614-3624
    • Kurian, D.1    Phadwal, K.2    Maeenpaeae, P.3
  • 118
    • 33947577004 scopus 로고    scopus 로고
    • Metaproteomic analysis of a bacterial community response to cadmium exposure
    • Lacerda CMR, Choe LH, Reardon KF. 2007. Metaproteomic analysis of a bacterial community response to cadmium exposure. J. Proteome Res. 6:1145-1152.
    • (2007) J. Proteome Res. , vol.6 , pp. 1145-1152
    • Lacerda, C.M.R.1    Choe, L.H.2    Reardon, K.F.3
  • 119
    • 0026020230 scopus 로고
    • Identification of a central regulator of stationary-phase gene expression in Escherichia coli
    • Lange R, Hengge-Aronis R. 1991. Identification of a central regulator of stationary-phase gene expression in Escherichia coli. Mol Microbiol. 5:49-59.
    • (1991) Mol Microbiol , vol.5 , pp. 49-59
    • Lange, R.1    Hengge-Aronis, R.2
  • 120
    • 43049090085 scopus 로고    scopus 로고
    • Targeted quantitative analysis of Streptococcus pyogenes virulence factors by multiple reaction monitoring
    • Lange V, Malmstroem JA, Didion J, King NL, Johansson BP, et al. 2008a. Targeted quantitative analysis of Streptococcus pyogenes virulence factors by multiple reaction monitoring. Mol. Cell. Proteom 7:1489-1500.
    • (2008) Mol. Cell. Proteom , vol.7 , pp. 1489-1500
    • Lange, V.1    Malmstroem, J.A.2    Didion, J.3    King, N.L.4    Johansson, B.P.5
  • 121
    • 54049090766 scopus 로고    scopus 로고
    • Selected reaction monitoring for quantitative proteomics: A tutorial
    • Lange V, Picotti P, Domon B, Aebersold R. 2008b. Selected reaction monitoring for quantitative proteomics: A tutorial. Mol. Syst. Biol. 4: 222.
    • (2008) Mol. Syst. Biol. , vol.4 , pp. 222
    • Lange, V.1    Picotti, P.2    Domon, B.3    Aebersold, R.4
  • 122
    • 0037334843 scopus 로고    scopus 로고
    • Global characterization of disulfide stress in Bacillus subtilis
    • Leichert LI, Scharf C, Hecker M. 2003. Global characterization of disulfide stress in Bacillus subtilis. J. Bacteriol. 185:1967-1975.
    • (2003) J. Bacteriol. , vol.185 , pp. 1967-1975
    • Leichert, L.I.1    Scharf, C.2    Hecker, M.3
  • 124
    • 33750594230 scopus 로고    scopus 로고
    • Chemistry meets proteomics: The use of chemical tagging reactions for MS-based proteomics
    • Leithner A, Lindner W. 2006. Chemistry meets proteomics: The use of chemical tagging reactions for MS-based proteomics. Proteomics 6:5418-5434.
    • (2006) Proteomics , vol.6 , pp. 5418-5434
    • Leithner, A.1    Lindner, W.2
  • 125
    • 18144420399 scopus 로고    scopus 로고
    • Insights into the oxidative stress response in Francisella tularensis LVS and its mutant DeltaiglC1+2 by proteomic analysis
    • Lenco J, Pavkova I, Hubalek M, Stulik J. 2005. Insights into the oxidative stress response in Francisella tularensis LVS and its mutant DeltaiglC1+2 by proteomic analysis. FEMS. Microbiol. Lett. 246:47-54.
    • (2005) FEMS. Microbiol. Lett. , vol.246 , pp. 47-54
    • Lenco, J.1    Pavkova, I.2    Hubalek, M.3    Stulik, J.4
  • 126
    • 0033931002 scopus 로고    scopus 로고
    • Identification of stressinducible proteins in Lactobacillus delbrueckii subsp
    • Lim EM, Ehrlich SD, Maguin E. 2000. Identification of stressinducible proteins in Lactobacillus delbrueckii subsp. bulgaricus Electrophoresis 21:2557-2561.
    • (2000) bulgaricus Electrophoresis , vol.21 , pp. 2557-2561
    • Lim, E.M.1    Ehrlich, S.D.2    Maguin, E.3
  • 128
    • 33750601225 scopus 로고    scopus 로고
    • Proteome informatics II: Bioinformatics for comparative proteomics
    • Lisacek F, Cohen-Boulakia S, Appel RD. 2006 Proteome informatics II: Bioinformatics for comparative proteomics. Proteomics 6:5445-5466.
    • (2006) Proteomics , vol.6 , pp. 5445-5466
    • Lisacek, F.1    Cohen-Boulakia, S.2    Appel, R.D.3
  • 129
    • 0035104482 scopus 로고    scopus 로고
    • A low-pH-inducible, stationaryphase acid tolerance response inLactobacillus acidophilus CRL 639 Curr
    • Lorca GL, Font de Valdez G. 2001. A low-pH-inducible, stationaryphase acid tolerance response inLactobacillus acidophilus CRL 639 Curr. Microbiol. 42:21-25.
    • (2001) Microbiol , vol.42 , pp. 21-25
    • Lorca, G.L.1    Font de Valdez, G.2
  • 130
    • 67349202042 scopus 로고    scopus 로고
    • Stress responses in Synechocystis: Regulated genes and regulatory systems
    • Norfolk, VA: Caister Academic Press, In Herrero A, Flores E, eds
    • Los DA, Suzuki I, Zinchenko VV, Murata N. 2008. Stress responses in Synechocystis: Regulated genes and regulatory systems. In Herrero A, Flores E, eds. The Cyanobacteria: Molecular Biology, Genomics and Evolution. Norfolk, VA: Caister Academic Press, pp 117-157.
    • (2008) The Cyanobacteria: Molecular Biology, Genomics and Evolution , pp. 117-157
    • Los, D.A.1    Suzuki, I.2    Zinchenko, V.V.3    Murata, N.4
  • 131
    • 0036731568 scopus 로고    scopus 로고
    • Effects of high pressure on the viability, morphology, lysis, and cell wall hydrolase activity of Lactococcus lactis subsp. cremoris
    • Malone AS, Shellhammer TH, Courtney PD. 2002. Effects of high pressure on the viability, morphology, lysis, and cell wall hydrolase activity of Lactococcus lactis subsp. cremoris. Appl. Environ. Microbiol. 68:4357-4363.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 4357-4363
    • Malone, A.S.1    Shellhammer, T.H.2    Courtney, P.D.3
  • 132
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • Mann M, Jensen ON. 2003. Proteomic analysis of post-translational modifications. Nat. Biotechnol. 21:255-261.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 133
    • 0028575316 scopus 로고
    • Error-tolerant identification of peptides in sequence databases by peptide sequence tags
    • Mann M, Wilm M. 1994. Error-tolerant identification of peptides in sequence databases by peptide sequence tags. Anal. Chem 66:4390-4399.
    • (1994) Anal. Chem , vol.66 , pp. 4390-4399
    • Mann, M.1    Wilm, M.2
  • 134
    • 2442514028 scopus 로고    scopus 로고
    • Effect of high concentration of Co (II) on Enterobacter liquefaciens strain C-1: A bacterium highly resistant to heavy metals with an unknown genome
    • Marrero J, Gonzalez LJ, Sanchez A, Ayala M, Paz-Lago D, Gonzalez W, Fallarero A, Castellanos-Serra L, Coto O. 2004. Effect of high concentration of Co (II) on Enterobacter liquefaciens strain C-1: A bacterium highly resistant to heavy metals with an unknown genome. Proteomics 4:1265-1279.
    • (2004) Proteomics , vol.4 , pp. 1265-1279
    • Marrero, J.1    Gonzalez, L.J.2    Sanchez, A.3    Ayala, M.4    Paz-Lago, D.5    Gonzalez, W.6    Fallarero, A.7    Castellanos-Serra, L.8    Coto, O.9
  • 135
    • 66149117914 scopus 로고    scopus 로고
    • Proteomic analysis by two-dimensional differential gel electrophoresis (2D DIGE) of a high-pressure effect in Bacillus cereus
    • Martinez-Gomariz M, Hernaez ML, Gutierrez D, Ximenez-Embun P, Prestamo G. 2009. Proteomic analysis by two-dimensional differential gel electrophoresis (2D DIGE) of a high-pressure effect in Bacillus cereus. J. Agric. Food Chem. 57:3543-3549.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 3543-3549
    • Martinez-Gomariz, M.1    Hernaez, M.L.2    Gutierrez, D.3    Ximenez-Embun, P.4    Prestamo, G.5
  • 137
    • 65349151292 scopus 로고    scopus 로고
    • Heat pretreatment alleviates UV-B toxicity in the cyanobacterium Anabaena doliolum: A proteomic analysis of cross tolerance
    • Mishra Y, Chaurasia N, Rai LC. 2009. Heat pretreatment alleviates UV-B toxicity in the cyanobacterium Anabaena doliolum: A proteomic analysis of cross tolerance. Photochem. Photobiol 85:824-833.
    • (2009) Photochem. Photobiol , vol.85 , pp. 824-833
    • Mishra, Y.1    Chaurasia, N.2    Rai, L.C.3
  • 138
    • 0036727268 scopus 로고    scopus 로고
    • In situ determination of the intracellular pH of Lactococcus lactis and Lactobacillus plantarum during pressure treatment
    • Molina-Guitierrez A, Stippl V, Delgado A, Gaenzle MG, Vogel RF. 2002. In situ determination of the intracellular pH of Lactococcus lactis and Lactobacillus plantarum during pressure treatment. Appl Environ. Microbiol. 68:4399-4406.
    • (2002) Appl Environ. Microbiol. , vol.68 , pp. 4399-4406
    • Molina-Guitierrez, A.1    Stippl, V.2    Delgado, A.3    Gaenzle, M.G.4    Vogel, R.F.5
  • 139
    • 1242318677 scopus 로고    scopus 로고
    • Transcriptome and proteome analysis of Bacillus subtilis gene expression in response to superoxide and peroxide stress
    • Mostertz J, Scharf C, Hecker M, Homuth G. 2004. Transcriptome and proteome analysis of Bacillus subtilis gene expression in response to superoxide and peroxide stress. Microbiology 150:497-512.
    • (2004) Microbiology , vol.150 , pp. 497-512
    • Mostertz, J.1    Scharf, C.2    Hecker, M.3    Homuth, G.4
  • 140
    • 38649095599 scopus 로고    scopus 로고
    • An assessment of software solutions for the analysis of mass spectrometry based quantitative proteomics data
    • Mueller LN, Brusniak M-Y, Mani DR, Aebersold R. 2008. An assessment of software solutions for the analysis of mass spectrometry based quantitative proteomics data. J. Proteome Res. 7:51-61.
    • (2008) J. Proteome Res. , vol.7 , pp. 51-61
    • Mueller, L.N.1    Brusniak, M.-Y.2    Mani, D.R.3    Aebersold, R.4
  • 141
    • 33744776637 scopus 로고    scopus 로고
    • Salt stress in Desulfovibrio vulgaris Hildenborough: An integrated genomics approach
    • Mukhopadhyay A, He Z, Alm EJ, Arkin AP, Baidoo EE, et al. 2006 Salt stress in Desulfovibrio vulgaris Hildenborough: An integrated genomics approach. J. Bacteriol. 188:4068-4078.
    • (2006) J. Bacteriol. , vol.188 , pp. 4068-4078
    • Mukhopadhyay, A.1    He, Z.2    Alm, E.J.3    Arkin, A.P.4    Baidoo, E.E.5
  • 143
    • 28544433960 scopus 로고    scopus 로고
    • MASPIC: Intensity-based tandem mass spectrometry scoring scheme that improves peptide identification at high confidence
    • Narasimhan C, Tabb DL, Verberkmoes NC, Thompson MR, Hettich RL, Uberbacher EC. 2005. MASPIC: Intensity-based tandem mass spectrometry scoring scheme that improves peptide identification at high confidence. Anal. Chem. 77:7581-7593.
    • (2005) Anal. Chem. , vol.77 , pp. 7581-7593
    • Narasimhan, C.1    Tabb, D.L.2    Verberkmoes, N.C.3    Thompson, M.R.4    Hettich, R.L.5    Uberbacher, E.C.6
  • 144
    • 35348860923 scopus 로고    scopus 로고
    • Proteomics for the analysis of environmental stress responses in organisms
    • Nesatyy VJ, Suter MJ-F. 2007. Proteomics for the analysis of environmental stress responses in organisms. Environ. Sci. Technol 41:6891-6900.
    • (2007) Environ. Sci. Technol , vol.41 , pp. 6891-6900
    • Nesatyy, V.J.1    Suter, M.-F.2
  • 145
    • 57249108230 scopus 로고    scopus 로고
    • Analysis of environmental stress response on the proteome level
    • Nesatyy VJ, Suter MJ-F. 2008. Analysis of environmental stress response on the proteome level. Mass Spectrom. Rev. 27:556-574.
    • (2008) Mass Spectrom. Rev. , vol.27 , pp. 556-574
    • Nesatyy, V.J.1    Suter, M.-F.2
  • 146
    • 10044290651 scopus 로고    scopus 로고
    • Cold adaptation in the antarctic archaeon Methanococcoides burtonii involves membrane lipid unsaturation
    • Nichols DS, Miller MR, Davies NW, Goodchild A, Raftery M, Cavicchioli R. 2004. Cold adaptation in the antarctic archaeon Methanococcoides burtonii involves membrane lipid unsaturation. J Bacteriol. 186:8508-8515.
    • (2004) J Bacteriol , vol.186 , pp. 8508-8515
    • Nichols, D.S.1    Miller, M.R.2    Davies, N.W.3    Goodchild, A.4    Raftery, M.5    Cavicchioli, R.6
  • 147
    • 0033709566 scopus 로고    scopus 로고
    • Safety valves for photosynthesis
    • Niyogi KK. 2000. Safety valves for photosynthesis. Curr. Opin. Plant Biol. 3:455-460.
    • (2000) Curr. Opin. Plant Biol. , vol.3 , pp. 455-460
    • Niyogi, K.K.1
  • 148
    • 18844464043 scopus 로고    scopus 로고
    • Global analysis of the Ralstonia metallidurans proteome: Prelude for the large-scale study of heavy metal response
    • Noeel-Georis I, Vallaeys T, Chauvaux R, Monchy S, Falmagne P, Mergeay M, Wattiez R. 2004. Global analysis of the Ralstonia metallidurans proteome: Prelude for the large-scale study of heavy metal response. Proteomics 4:151-179.
    • (2004) Proteomics , vol.4 , pp. 151-179
    • Noeel-Georis, I.1    Vallaeys, T.2    Chauvaux, R.3    Monchy, S.4    Falmagne, P.5    Mergeay, M.6    Wattiez, R.7
  • 149
    • 0026557123 scopus 로고
    • Survival, stress resistance, and alterations in protein expression in the marine Vibrio sp strain S14 during starvation for different individual nutrients
    • Nystroem T, Olsson RM, Kjelleberg S. 1992. Survival, stress resistance, and alterations in protein expression in the marine Vibrio sp strain S14 during starvation for different individual nutrients. Appl Environ. Microbiol. 58:55-65.
    • (1992) Appl Environ. Microbiol. , vol.58 , pp. 55-65
    • Nystroem, T.1    Olsson, R.M.2    Kjelleberg, S.3
  • 150
    • 0035067251 scopus 로고    scopus 로고
    • Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome
    • Oda Y, Nagasu T, Chait BT. 2001. Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome. Nat Biotechnol. 19:379-382.
    • (2001) Nat Biotechnol , vol.19 , pp. 379-382
    • Oda, Y.1    Nagasu, T.2    Chait, B.T.3
  • 151
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, is a simple and accurate approach to expression proteomics
    • Ong S-E, Blagoev B, Kratchmarova I, Bach Kristensen D, Steen H, Pandey A, Mann M. 2002. Stable isotope labeling by amino acids in cell culture, SILAC, is a simple and accurate approach to expression proteomics. Mol. Cell. Proteom. 1:376-386.
    • (2002) Mol. Cell. Proteom. , vol.1 , pp. 376-386
    • Ong, S.-E.1    Blagoev, B.2    Kratchmarova, I.3    Bach Kristensen, D.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 152
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong SE, Mann M. 2005. Mass spectrometry-based proteomics turns quantitative. Nat. Chem. Biol. 1:252-262.
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 153
    • 0033013288 scopus 로고    scopus 로고
    • Relationship between acid tolerance, cytoplasmic pH, and ATP and H+-ATPase levels in chemostat cultures of Lactococcus lactis
    • O'Sullivan E, Condon S. 1999. Relationship between acid tolerance, cytoplasmic pH, and ATP and H+-ATPase levels in chemostat cultures of Lactococcus lactis. Appl. Environ. Microbiol. 65:2287-2293.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 2287-2293
    • O'Sullivan, E.1    Condon, S.2
  • 154
    • 0033929213 scopus 로고    scopus 로고
    • Relationship between membrane damage and cell death in pressure-treated Escherichia coli cells: Differences between exponential- and stationary-phase cells and variation among strains
    • Pagan R, Mackey B. 2000. Relationship between membrane damage and cell death in pressure-treated Escherichia coli cells: Differences between exponential- and stationary-phase cells and variation among strains. Appl. Environ. Microbiol. 66:2829-2834.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 2829-2834
    • Pagan, R.1    Mackey, B.2
  • 155
    • 33750600611 scopus 로고    scopus 로고
    • Proteome informatics I: Bioinformatics tools for processing experimental data
    • Palagi PM, Hernandez P, Walther D, Appel RD. 2006. Proteome informatics I: Bioinformatics tools for processing experimental data Proteomics 6:5435-5444.
    • (2006) Proteomics , vol.6 , pp. 5435-5444
    • Palagi, P.M.1    Hernandez, P.2    Walther, D.3    Appel, R.D.4
  • 156
    • 44049105535 scopus 로고    scopus 로고
    • Experimental and computational approaches to quantitative proteomics: Status quo and outlook
    • Panchaud A, Affolter M, Moreillon P, Kussmann M. 2008 Experimental and computational approaches to quantitative proteomics: Status quo and outlook. J. Proteom. 71:19-33.
    • (2008) J. Proteom. , vol.71 , pp. 19-33
    • Panchaud, A.1    Affolter, M.2    Moreillon, P.3    Kussmann, M.4
  • 157
    • 33947578259 scopus 로고    scopus 로고
    • A quantitative proteomic analysis of light adaptation in a globally significant marine cyanobacterium Prochlorococcus marinus MED4
    • Pandhal J, Wright PC, Biggs CA. 2007. A quantitative proteomic analysis of light adaptation in a globally significant marine cyanobacterium Prochlorococcus marinus MED4. J. Proteome Res 6:996-1005.
    • (2007) J. Proteome Res , vol.6 , pp. 996-1005
    • Pandhal, J.1    Wright, P.C.2    Biggs, C.A.3
  • 158
    • 61849116800 scopus 로고    scopus 로고
    • Comparative proteomics study of salt tolerance between a nonsequenced extremely halotolerant Cyanobacterium and its mildly halotolerant relative using in vivo metabolic labeling and in vitro isobaric labeling
    • Pandhal J, Ow SY, Wright PC, Biggs CA. 2009. Comparative proteomics study of salt tolerance between a nonsequenced extremely halotolerant Cyanobacterium and its mildly halotolerant relative using in vivo metabolic labeling and in vitro isobaric labeling. J. Proteome Res. 8:818-828.
    • (2009) J. Proteome Res. , vol.8 , pp. 818-828
    • Pandhal, J.1    Ow, S.Y.2    Wright, P.C.3    Biggs, C.A.4
  • 159
    • 33751110612 scopus 로고    scopus 로고
    • Proteomic identification of a two-component regulatory system in Pseudoalteromonas haloplanktis TAC125
    • Papa R, Glagla S, Danchin A, Schweder T, Marino G, Duilio A. 2006. Proteomic identification of a two-component regulatory system in Pseudoalteromonas haloplanktis TAC125. Extremophiles 10:483-491.
    • (2006) Extremophiles , vol.10 , pp. 483-491
    • Papa, R.1    Glagla, S.2    Danchin, A.3    Schweder, T.4    Marino, G.5    Duilio, A.6
  • 160
    • 12944269065 scopus 로고
    • Rapid identification of proteins by peptide-mass fingerprinting
    • Pappin DJC, Hojrup P, Bleasby AJ. 1993. Rapid identification of proteins by peptide-mass fingerprinting. Curr. Biol. 3:327-332.
    • (1993) Curr. Biol. , vol.3 , pp. 327-332
    • Pappin, D.J.C.1    Hojrup, P.2    Bleasby, A.J.3
  • 161
    • 50949106204 scopus 로고    scopus 로고
    • Candidate stress genes of Nitrosomonas europaea for monitoring inhibition of nitrification by heavy metals Appl
    • Park S, Ely RL. 2008. Candidate stress genes of Nitrosomonas europaea for monitoring inhibition of nitrification by heavy metals Appl. Environ. Microbiol. 74:5475-5482.
    • (2008) Environ. Microbiol. , vol.74 , pp. 5475-5482
    • Park, S.1    Ely, R.L.2
  • 162
    • 0018129628 scopus 로고
    • Effect of growth temperature on membrane fatty acid composition and susceptibility to cold shock of Bacillus amyloliquefaciens
    • Paton JC, McMurchie EJ, May BK, Elliott WH. 1978. Effect of growth temperature on membrane fatty acid composition and susceptibility to cold shock of Bacillus amyloliquefaciens. J. Bacteriol 135:754-759.
    • (1978) J. Bacteriol , vol.135 , pp. 754-759
    • Paton, J.C.1    McMurchie, E.J.2    May, B.K.3    Elliott, W.H.4
  • 164
    • 0033434080 scopus 로고    scopus 로고
    • Probabilitybased protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJ, Creasy DM, Cottrell JS. 1999. Probabilitybased protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20:3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 165
    • 0032728896 scopus 로고    scopus 로고
    • Expression of a new cold shock protein of 21 5kDa and of the major cold shock protein by Streptococcus thermophilus after cold shock
    • Perrin C, Guimont c, Bracquart P, Gaillard JL. 1999. Expression of a new cold shock protein of 21.5kDa and of the major cold shock protein by Streptococcus thermophilus after cold shock. Curr Microbiol. 39:342-347.
    • (1999) Curr Microbiol , vol.39 , pp. 342-347
    • Perrin, C.1    Guimont, C.2    Bracquart, P.3    Gaillard, J.L.4
  • 167
    • 0030935908 scopus 로고    scopus 로고
    • Hsp30, the integral plasma membrane heat shock protein of Saccharomyces cerevisiae, is a stress-inducible regulator of plasma membrane H+-ATPase
    • Piper PW, Ortiz-Calderon C, Holyoak C, Coote P, Cole M. 1997. Hsp30, the integral plasma membrane heat shock protein of Saccharomyces cerevisiae, is a stress-inducible regulator of plasma membrane H+-ATPase. Cell Stress Chaperones 2:12-24.
    • (1997) Cell Stress Chaperones , vol.2 , pp. 12-24
    • Piper, P.W.1    Ortiz-Calderon, C.2    Holyoak, C.3    Coote, P.4    Cole, M.5
  • 169
    • 33847179916 scopus 로고    scopus 로고
    • Multiplexed absolute quantification for proteomics using concatenated signature peptides encoded by QconCAT genes
    • Pratt JM, Simpson DM, Doherty MK, Rivers J, Gaskell SJ, Beynon RJ. 2006. Multiplexed absolute quantification for proteomics using concatenated signature peptides encoded by QconCAT genes Nat. Protoc. 1:1029-1043.
    • (2006) Nat Protoc , vol.1 , pp. 1029-1043
    • Pratt, J.M.1    Simpson, D.M.2    Doherty, M.K.3    Rivers, J.4    Gaskell, S.J.5    Beynon, R.J.6
  • 171
    • 0030442663 scopus 로고    scopus 로고
    • Alteration in photosynthetic characteristics of Anabaena doliolum following exposure to UV-B and Pb
    • Rai LC, Tyagi B, Mallick N. 1996. Alteration in photosynthetic characteristics of Anabaena doliolum following exposure to UV-B and Pb. Photochem. Photobiol. 64:658-663.
    • (1996) Photochem. Photobiol. , vol.64 , pp. 658-663
    • Rai, L.C.1    Tyagi, B.2    Mallick, N.3
  • 174
    • 3042737683 scopus 로고    scopus 로고
    • Improving reproducibility and sensitivity in identifying human proteins by shotgun proteomics
    • Resing KA, Meyer-Arendt K, Mendoza AM, Aveline-Wolf LD, et al. 2004. Improving reproducibility and sensitivity in identifying human proteins by shotgun proteomics. Anal. Chem. 76:3556-3568.
    • (2004) Anal. Chem. , vol.76 , pp. 3556-3568
    • Resing, K.A.1    Meyer-Arendt, K.2    Mendoza, A.M.3    Aveline-Wolf, L.D.4
  • 175
    • 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
  • 176
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantification in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross PL, Huang YLN, Marchese JN, Pappin DJC. 2004. Multiplexed protein quantification in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol. Cell. Proteomics 3:1154-1169.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 1154-1169
    • Ross, P.L.1    Huang, Y.L.N.2    Marchese, J.N.3    Pappin, D.J.C.4
  • 177
    • 33846604134 scopus 로고    scopus 로고
    • A topdown/bottom-up study of the ribosomal proteins of Caulobacter crescentus J
    • Running WE, Ravipaty S, Karty JA, Reilly JP. 2007. A topdown/bottom-up study of the ribosomal proteins of Caulobacter crescentus J. Proteome Res. 6:337-347.
    • (2007) Proteome Res , vol.6 , pp. 337-347
    • Running, W.E.1    Ravipaty, S.2    Karty, J.A.3    Reilly, J.P.4
  • 178
    • 0035831256 scopus 로고    scopus 로고
    • Osmolytes protect mitochondrial F0F1-ATPase complex against pressure inactivation Biochim
    • Saad-Nehme J, Silva JL, Meyer-Fernandes J. 2001. Osmolytes protect mitochondrial F0F1-ATPase complex against pressure inactivation Biochim. Biophys. Acta 1546:164-170.
    • (2001) Biophys. Acta , vol.1546 , pp. 164-170
    • Saad-Nehme, J.1    Silva, J.L.2    Meyer-Fernandes, J.3
  • 182
    • 0024075420 scopus 로고
    • Differential regulation by cyclic AMP of starvation protein synthesis in Escherichia coli
    • Schultz JE, Latter GI, Matin A. 1988. Differential regulation by cyclic AMP of starvation protein synthesis in Escherichia coli. J Bacteriol. 170:3903-3909.
    • (1988) J Bacteriol , vol.170 , pp. 3903-3909
    • Schultz, J.E.1    Latter, G.I.2    Matin, A.3
  • 183
    • 0033650048 scopus 로고    scopus 로고
    • The chemistry of protein sequence analysis
    • Shively JE. 2000. The chemistry of protein sequence analysis. EXS 88:99-117.
    • (2000) EXS , vol.88 , pp. 99-117
    • Shively, J.E.1
  • 184
    • 33750584707 scopus 로고    scopus 로고
    • Proteomics and metabolomics: The molecular make-up of toxic aromatic pollutant bioremediation
    • Singh OV. 2006. Proteomics and metabolomics: The molecular make-up of toxic aromatic pollutant bioremediation. Proteomics 6:5481-5492.
    • (2006) Proteomics , vol.6 , pp. 5481-5492
    • Singh, O.V.1
  • 186
    • 32944474675 scopus 로고    scopus 로고
    • Proteomic analysis of the heat shock response in Synechocystis PCC6803 and a thermally tolerant knockout strain lacking the histidine kinase 34 gene
    • Slabas AR, Suzuki I, Murata N, Simon WJ, Hall JJ. 2006. Proteomic analysis of the heat shock response in Synechocystis PCC6803 and a thermally tolerant knockout strain lacking the histidine kinase 34 gene. Proteomics 6:845-864.
    • (2006) Proteomics , vol.6 , pp. 845-864
    • Slabas, A.R.1    Suzuki, I.2    Murata, N.3    Simon, W.J.4    Hall, J.J.5
  • 187
    • 33846638822 scopus 로고    scopus 로고
    • Relative quantification of proteins across the species boundary through the use of shared peptides
    • Snijders AP, de Koning B, Wright PC. 2007. Relative quantification of proteins across the species boundary through the use of shared peptides. J. Proteome Res. 6:97-104.
    • (2007) J. Proteome Res. , vol.6 , pp. 97-104
    • Snijders, A.P.1    de Koning, B.2    Wright, P.C.3
  • 188
    • 54349095175 scopus 로고    scopus 로고
    • Genes and environment-Striking the fine balance between sophisticated biomonitoring and true functional environmental genomics
    • Steinberg CE, Stuerzenbaum SR, Menzel R. 2008. Genes and environment-Striking the fine balance between sophisticated biomonitoring and true functional environmental genomics. Sci. Total Environ. 400:142-161.
    • (2008) Sci. Total Environ. , vol.400 , pp. 142-161
    • Steinberg, C.E.1    Stuerzenbaum, S.R.2    Menzel, R.3
  • 189
    • 53149123972 scopus 로고    scopus 로고
    • Emerging high-throughput approaches to analyze bioremediation of sites contaminated with hazardous and/or recalcitrant waters
    • Stenuit B, Eyers L, Schuler L, Agathos SN, George I. 2008 Emerging high-throughput approaches to analyze bioremediation of sites contaminated with hazardous and/or recalcitrant waters. Biotechnol Adv. 26:561-575.
    • (2008) Biotechnol Adv , vol.26 , pp. 561-575
    • Stenuit, B.1    Eyers, L.2    Schuler, L.3    Agathos, S.N.4    George, I.5
  • 191
    • 33646265040 scopus 로고    scopus 로고
    • The heat shock response of Synechocystis sp PCC 6803 analysed by transcriptomics and proteomics
    • Suzuki I, Simon WJ, Slabas AR. 2006. The heat shock response of Synechocystis sp. PCC 6803 analysed by transcriptomics and proteomics J. Exp. Bot. 57:1573-1578.
    • (2006) J. Exp. Bot. , vol.57 , pp. 1573-1578
    • Suzuki, I.1    Simon, W.J.2    Slabas, A.R.3
  • 194
    • 33748358169 scopus 로고    scopus 로고
    • Proteome signatures for stress and starvation in Bacillus subtilis as revealed by a 2-D gel image color coding approach
    • Tam LT, Antelmann H, Eymann C, Albrecht D, Bernhardt J, Hecker M. 2006. Proteome signatures for stress and starvation in Bacillus subtilis as revealed by a 2-D gel image color coding approach. Proteomics 6:4565-4585.
    • (2006) Proteomics , vol.6 , pp. 4565-4585
    • Tam, L.T.1    Antelmann, H.2    Eymann, C.3    Albrecht, D.4    Bernhardt, J.5    Hecker, M.6
  • 195
    • 0030755723 scopus 로고    scopus 로고
    • Identification of sites of injury in Lactobacillus bulgaricus during heat stress J
    • Teixeira P, Castro H, Mohacsi-Farkas C, Kirby R. 1997. Identification of sites of injury in Lactobacillus bulgaricus during heat stress J. Appl. Microbiol. 83:219-226.
    • (1997) Appl. Microbiol. , vol.83 , pp. 219-226
    • Teixeira, P.1    Castro, H.2    Mohacsi-Farkas, C.3    Kirby, R.4
  • 197
    • 12444345515 scopus 로고    scopus 로고
    • Tandem mass tags: A novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS
    • Thompson A, Schaefer J, Kuhn K, Kienle S, Schwarz J, Schmidt G, Neumann T, Hamon C. 2003. Tandem mass tags: A novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS. Anal. Chem. 75:1895-1904.
    • (2003) Anal. Chem. , vol.75 , pp. 1895-1904
    • Thompson, A.1    Schaefer, J.2    Kuhn, K.3    Kienle, S.4    Schwarz, J.5    Schmidt, G.6    Neumann, T.7    Hamon, C.8
  • 198
    • 0023490019 scopus 로고
    • Developments in protein microsequencing
    • Tsugita A. 1987. Developments in protein microsequencing. Adv. Biophys 23:81-113.
    • (1987) Adv. Biophys , vol.23 , pp. 81-113
    • Tsugita, A.1
  • 199
    • 0032899676 scopus 로고    scopus 로고
    • Induction and enhancement of stress proteins in a trichloroethylene-degrading methanotrophic bacterium
    • Uchiyama H, Shinohara Y, Tomioka N, Kusakabe I. 1999. Induction and enhancement of stress proteins in a trichloroethylene-degrading methanotrophic bacterium, Methylocystis sp. M. FEMS MIcrobiol Lett. 170:125-130.
    • (1999) Methylocystis sp. M. FEMS MIcrobiol Lett. , vol.170 , pp. 125-130
    • Uchiyama, H.1    Shinohara, Y.2    Tomioka, N.3    Kusakabe, I.4
  • 200
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: a single gel method for detecting changes in protein extracts
    • Unlue M, Morgan ME, Minden JS. 1997. Difference gel electrophoresis: a single gel method for detecting changes in protein extracts. Electrophoresis 18:2071-2077.
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlue, M.1    Morgan, M.E.2    Minden, J.S.3
  • 201
    • 1242328741 scopus 로고    scopus 로고
    • Fluorescent two-dimensional difference gel electrophoresis unveils the potential of gel-based proteomics Curr
    • van den Bergh G, Arckens L. 2004. Fluorescent two-dimensional difference gel electrophoresis unveils the potential of gel-based proteomics Curr. Opin. Biotechnol. 15:38-43.
    • (2004) Opin. Biotechnol. , vol.15 , pp. 38-43
    • van den Bergh, G.1    Arckens, L.2
  • 202
    • 0025328743 scopus 로고
    • Ribosomes as sensors of heat and cold shock in Escherichia coli
    • VanBogelen RA, Neidhardt FC. 1990. Ribosomes as sensors of heat and cold shock in Escherichia coli. Proc. Natl. Acad. Sci. USA 87:5589-5593.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5589-5593
    • VanBogelen, R.A.1    Neidhardt, F.C.2
  • 203
    • 22744450094 scopus 로고    scopus 로고
    • From genomics via proteomics to cellular physiology of the Gram-positive model organism Bacillus subtilis Cell
    • Voelker U, Hecker M. 2005. From genomics via proteomics to cellular physiology of the Gram-positive model organism Bacillus subtilis Cell. Microbiol. 7:1077-1085.
    • (2005) Microbiol , vol.7 , pp. 1077-1085
    • Voelker, U.1    Hecker, M.2
  • 205
    • 35448967750 scopus 로고    scopus 로고
    • Top- down quantitation and characterization of SILAC-labeled proteins
    • Waanders LF, Hanke S, Mann M. 2007. Top-down quantitation and characterization of SILAC-labeled proteins. J. Am. Soc. Mass Spectrom 18:2058-2064.
    • (2007) J. Am. Soc. Mass Spectrom , vol.18 , pp. 2058-2064
    • Waanders, L.F.1    Hanke, S.2    Mann, M.3
  • 207
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology Nat
    • Washburn MP, Wolters D, Yates JR. 2001. Large-scale analysis of the yeast proteome by multidimensional protein identification technology Nat. Biotechnol. 19:242-247.
    • (2001) Biotechnol , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 208
    • 1942455710 scopus 로고    scopus 로고
    • Oxidative stress triggers thiol oxidation in the glyceraldehyde-3-phosphate dehydrogenase of Staphylococcus aureus
    • Weber H, Engelmann S, Becher D, Hecker M. 2004. Oxidative stress triggers thiol oxidation in the glyceraldehyde-3-phosphate dehydrogenase of Staphylococcus aureus. Mol. Microbiol. 52:133-140.
    • (2004) Mol. Microbiol. , vol.52 , pp. 133-140
    • Weber, H.1    Engelmann, S.2    Becher, D.3    Hecker, M.4
  • 209
    • 0036081377 scopus 로고    scopus 로고
    • CSDBase: An interactive database for cold shock domain-containing proteins and the bacterial cold shock response
    • Weber MHW, Fricke I, Doll N, Marahiel MA. 2002. CSDBase: An interactive database for cold shock domain-containing proteins and the bacterial cold shock response. Nucleic Acids Res. 30: 375-378.
    • (2002) Nucleic Acids Res , vol.30 , pp. 375-378
    • Weber, M.H.W.1    Fricke, I.2    Doll, N.3    Marahiel, M.A.4
  • 210
    • 0027370350 scopus 로고
    • Stress response of Escherichia coli to elevated hydrostatic pressure
    • Welch TJ, Farewell A, Neidhardt FC, Bartlett DH. 1993. Stress response of Escherichia coli to elevated hydrostatic pressure. J. Bacteriol. 175:7170-7177.
    • (1993) J. Bacteriol. , vol.175 , pp. 7170-7177
    • Welch, T.J.1    Farewell, A.2    Neidhardt, F.C.3    Bartlett, D.H.4
  • 212
    • 0030028208 scopus 로고    scopus 로고
    • Current challenges and future applications for protein maps and post-translational vector maps in proteome projects
    • Wilkins MR, Sanchez J-C, Williams KL, Hochstrasse DF. 1996 Current challenges and future applications for protein maps and post-translational vector maps in proteome projects. Electrophoresis 17:830-838.
    • (1996) Electrophoresis , vol.17 , pp. 830-838
    • Wilkins, M.R.1    Sanchez, J.-C.2    Williams, K.L.3    Hochstrasse, D.F.4
  • 213
    • 0026648953 scopus 로고
    • Characterization of cspB, a Bacillus subtilis inducible cold shock gene affecting cell viability at low temperatures
    • Willimsky G, Bang H, Fischer G, Marahiel MA. 1992. Characterization of cspB, a Bacillus subtilis inducible cold shock gene affecting cell viability at low temperatures. J. Bacteriol. 174:6326-6335.
    • (1992) J. Bacteriol. , vol.174 , pp. 6326-6335
    • Willimsky, G.1    Bang, H.2    Fischer, G.3    Marahiel, M.A.4
  • 214
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from polyacrlyamide gels by nano-electrospray mass spectrometry
    • Wilm M, Shevchenko A, Houthaeve T, Breit S, Schweigerer L, Fotsis T, Mann M. 1996. Femtomole sequencing of proteins from polyacrlyamide gels by nano-electrospray mass spectrometry. Nature 379:466-469.
    • (1996) Nature , vol.379 , pp. 466-469
    • Wilm, M.1    Shevchenko, A.2    Houthaeve, T.3    Breit, S.4    Schweigerer, L.5    Fotsis, T.6    Mann, M.7
  • 215
    • 4344646435 scopus 로고    scopus 로고
    • The application of two-dimensional polyacrylamide gel electrophoresis and downstream analyses to a mixed community of prokaryotic microorganisms
    • Wilmes P, Bond PL. 2004. The application of two-dimensional polyacrylamide gel electrophoresis and downstream analyses to a mixed community of prokaryotic microorganisms. Environ. Microbiol. 6:911-920.
    • (2004) Environ. Microbiol. , vol.6 , pp. 911-920
    • Wilmes, P.1    Bond, P.L.2
  • 216
    • 34250722602 scopus 로고    scopus 로고
    • Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks
    • Wolf-Yadlin A, Hautaniemi S, Lauffenburger DA, White FM. 2007. Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks. Proc. Natl. Acad. Sci. USA 104:5860-5865.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 5860-5865
    • Wolf-Yadlin, A.1    Hautaniemi, S.2    Lauffenburger, D.A.3    White, F.M.4
  • 217
    • 49749101196 scopus 로고    scopus 로고
    • Proteomic analysis of antioxidant strategies of Staphylococcus aureus: Diverse responses to different oxidants
    • Wolf C, Hochgraefe 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    Hochgraefe, F.2    Kusch, H.3    Albrecht, D.4    Hecker, M.5    Engelmann, S.6
  • 219
    • 42049094894 scopus 로고    scopus 로고
    • Computational methods for the comparative quantification of proteins in label-free LCn-MS experiments
    • Wong JW, Sullivan MJ, Cagney G. 2008. Computational methods for the comparative quantification of proteins in label-free LCn-MS experiments. Brief Bioinform. 9:156-165.
    • (2008) Brief Bioinform , vol.9 , pp. 156-165
    • Wong, J.W.1    Sullivan, M.J.2    Cagney, G.3
  • 220
    • 0031890795 scopus 로고    scopus 로고
    • Effects of high pressure on inactivation kinetics and events related to proton efflux in Lactobacillus plantarum
    • Wouters PC, Glaasker E, Smelt JP. 1998. Effects of high pressure on inactivation kinetics and events related to proton efflux in Lactobacillus plantarum. Appl. Environ. Microbiol. 64:509-514.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 509-514
    • Wouters, P.C.1    Glaasker, E.2    Smelt, J.P.3
  • 221
    • 0032696567 scopus 로고    scopus 로고
    • Analysis of the role of 7kDa cold-shock proteins of Lactococcus lactis MG1363 in cryoprotection
    • Wouters JA, Jeynov B, Rombouts FM, de Vos WM, Kuipers OP, Abee T. 1999a. Analysis of the role of 7kDa cold-shock proteins of Lactococcus lactis MG1363 in cryoprotection. Microbiology 145:3185-3194.
    • (1999) Microbiology , vol.145 , pp. 3185-3194
    • Wouters, J.A.1    Jeynov, B.2    Rombouts, F.M.3    de Vos, W.M.4    Kuipers, O.P.5    Abee, T.6
  • 224
    • 33746571946 scopus 로고    scopus 로고
    • Two- dimensional difference gel electrophoresis
    • Wu TL. 2006. Two-dimensional difference gel electrophoresis. Methods Mol. Biol. 328:71-95.
    • (2006) Methods Mol. Biol. , vol.328 , pp. 71-95
    • Wu, T.L.1
  • 225
    • 73249128251 scopus 로고    scopus 로고
    • Top- down identification of protein biomarkers in bacteria with unsequenced genomes
    • Wynne C, Fenselau C, Demirev PA, Edwards N. 2009. Top-down identification of protein biomarkers in bacteria with unsequenced genomes. Anal. Chem. 81:9633-9642.
    • (2009) Anal. Chem. , vol.81 , pp. 9633-9642
    • Wynne, C.1    Fenselau, C.2    Demirev, P.A.3    Edwards, N.4
  • 227
    • 47249144784 scopus 로고    scopus 로고
    • Extracellular proteome changes of Deinococcus radiodurans under gamma-irradiation stress conditions
    • Ying N, Zheng Z, Xu H, Tian B, Hua Y. 2008. Extracellular proteome changes of Deinococcus radiodurans under gamma-irradiation stress conditions. Protein Pept. Lett. 15:595-599.
    • (2008) Protein Pept. Lett. , vol.15 , pp. 595-599
    • Ying, N.1    Zheng, Z.2    Xu, H.3    Tian, B.4    Hua, Y.5
  • 229
    • 13244258359 scopus 로고    scopus 로고
    • Proteomic analysis of Deinococcus radiodurans recovering from gamma-irradiation
    • Zhang C, Wei J, Zheng Z. 2005. Proteomic analysis of Deinococcus radiodurans recovering from gamma-irradiation. Proteomics 5:138-143.
    • (2005) Proteomics , vol.5 , pp. 138-143
    • Zhang, C.1    Wei, J.2    Zheng, Z.3
  • 230
    • 67049095501 scopus 로고    scopus 로고
    • Proteomic analysis of plasma membranes of cyanobacterium Synechocystis sp. strain PCC 6803 in response to high pH stress
    • Zhang L-F, Yang H-M, Cui S-X, Hu J, Wang J, Kuang T-Y, Norling B, Huang F. 2009. Proteomic analysis of plasma membranes of cyanobacterium Synechocystis sp. strain PCC 6803 in response to high pH stress. J. Proteome Res. 8:2892-2902.
    • (2009) J. Proteome Res. , vol.8 , pp. 2892-2902
    • Zhang, L.-F.1    Yang, H.-M.2    Cui, S.-X.3    Hu, J.4    Wang, J.5    Kuang, T.-Y.6    Norling, B.7    Huang, F.8
  • 231
    • 70350247861 scopus 로고    scopus 로고
    • Modification-specific proteomics: Strategies for characterization of post-translational modifications using enrichment techniques
    • Zhao Y, Jensen ON. 2009. Modification-specific proteomics: Strategies for characterization of post-translational modifications using enrichment techniques. Proteomics 9:4632-4641.
    • (2009) Proteomics , vol.9 , pp. 4632-4641
    • Zhao, Y.1    Jensen, O.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.