메뉴 건너뛰기




Volumn 13, Issue 6, 2014, Pages 2856-2866

Mass spectrometry-based proteomic approach in oenococcus oeni enological starter

Author keywords

bacteria; enzymes; MALDI; mass spectrometry; Oenoccoccus oeni; phosphorylation; point mutation; shotgun approach

Indexed keywords

ALCOHOL DEHYDROGENASE; CHAPERONIN; CYTOPLASM PROTEIN; MEMBRANE PROTEIN; METHIONINE; PHOSPHOPROTEIN; BACTERIAL PROTEIN; PROTEOME; TRYPSIN;

EID: 84902108685     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr4012798     Document Type: Article
Times cited : (40)

References (59)
  • 2
    • 52949117757 scopus 로고    scopus 로고
    • Genotyping by Amplified Fragment Length Polymorphism and malate metabolism performances of indigenous Oenococcus oeni strains isolated from Primitivo wine
    • Cappello, M. S.; Stefani, D.; Grieco, F.; Logrieco, A.; Zapparoli, G. Genotyping by Amplified Fragment Length Polymorphism and malate metabolism performances of indigenous Oenococcus oeni strains isolated from Primitivo wine Int. J. Food Microbiol. 2008, 127, 241-245
    • (2008) Int. J. Food Microbiol. , vol.127 , pp. 241-245
    • Cappello, M.S.1    Stefani, D.2    Grieco, F.3    Logrieco, A.4    Zapparoli, G.5
  • 3
    • 57049108787 scopus 로고    scopus 로고
    • Molecular identification and typing of lactic acid bacteria associated with the production of two artisanal raw milk cheeses
    • Van Hoorde, K.; Vandamme, P.; Huys, G. Molecular identification and typing of lactic acid bacteria associated with the production of two artisanal raw milk cheeses Dairy Sci. Technol. 2008, 88, 445-455
    • (2008) Dairy Sci. Technol. , vol.88 , pp. 445-455
    • Van Hoorde, K.1    Vandamme, P.2    Huys, G.3
  • 4
    • 28044461748 scopus 로고    scopus 로고
    • Combined cold, acid, ethanol shocks in Oenococcus oeni: Effects on membrane fluidity and cell viability
    • Chu-Ky, S.; Tourdot-Maréchal, R.; Marechal, P. A.; Guzzo, J. Combined cold, acid, ethanol shocks in Oenococcus oeni: Effects on membrane fluidity and cell viability Biochim. Biophys. Acta 2005, 1717, 118-124
    • (2005) Biochim. Biophys. Acta , vol.1717 , pp. 118-124
    • Chu-Ky, S.1    Tourdot-Maréchal, R.2    Marechal, P.A.3    Guzzo, J.4
  • 5
    • 23144445051 scopus 로고    scopus 로고
    • Oenococcus oeni and malolactic fermentation - Moving into the molecular arena
    • Bartowsky, E. J. Oenococcus oeni and malolactic fermentation-moving into the molecular arena Aust. J. Grape Wine Res. 2005, 11, 174-187
    • (2005) Aust. J. Grape Wine Res. , vol.11 , pp. 174-187
    • Bartowsky, E.J.1
  • 7
    • 78649699406 scopus 로고    scopus 로고
    • Molecular and biochemical diversity of Oenococcus oeni strains isolated during spontaneous malolactic fermentation of Malvasia Nera wine
    • Cappello, M. S.; Zapparoli, G.; Stefani, D.; Logrieco, A. Molecular and biochemical diversity of Oenococcus oeni strains isolated during spontaneous malolactic fermentation of Malvasia Nera wine Syst. Appl. Microbiol. 2010, 33, 461-467
    • (2010) Syst. Appl. Microbiol. , vol.33 , pp. 461-467
    • Cappello, M.S.1    Zapparoli, G.2    Stefani, D.3    Logrieco, A.4
  • 9
    • 70449868563 scopus 로고    scopus 로고
    • Proteomic analysis of Oenococcus oeni freeze-dried culture to assess the importance of cell acclimation to conduct malolactic fermentation in wine
    • Cecconi, D.; Milli, A.; Rinalducci, S.; Zolla, L.; Zapparoli, G. Proteomic analysis of Oenococcus oeni freeze-dried culture to assess the importance of cell acclimation to conduct malolactic fermentation in wine Electrophoresis 2009, 30, 2988-2995
    • (2009) Electrophoresis , vol.30 , pp. 2988-2995
    • Cecconi, D.1    Milli, A.2    Rinalducci, S.3    Zolla, L.4    Zapparoli, G.5
  • 11
    • 2442673205 scopus 로고    scopus 로고
    • Effect of Adaptation to Ethanol on Cytoplasmic and Membrane Protein Profiles of Oenococcus oeni
    • Silveira, M. G.; Baumgärtner, M.; Rombouts, F. M.; Abee, T. Effect of Adaptation to Ethanol on Cytoplasmic and Membrane Protein Profiles of Oenococcus oeni Appl. Environ. Microbiol. 2004, 70, 2748-2755
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 2748-2755
    • Silveira, M.G.1    Baumgärtner, M.2    Rombouts, F.M.3    Abee, T.4
  • 12
    • 53449086322 scopus 로고    scopus 로고
    • Changes in membrane lipid composition in ethanol- and acid-adapted Oenococcus oeni cells: Characterization of the cfa gene by heterologous complementation
    • Grandvalet, C.; Assad-García, J. S.; Chu-Ky, S.; Tollot, M.; Guzzo, J.; Gresti, J.; Tourdot-Maréchal, R. Changes in membrane lipid composition in ethanol- and acid-adapted Oenococcus oeni cells: characterization of the cfa gene by heterologous complementation Microbiology 2008, 154, 2611-2619
    • (2008) Microbiology , vol.154 , pp. 2611-2619
    • Grandvalet, C.1    Assad-García, J.S.2    Chu-Ky, S.3    Tollot, M.4    Guzzo, J.5    Gresti, J.6    Tourdot-Maréchal, R.7
  • 14
    • 62249212696 scopus 로고    scopus 로고
    • A CTAB based method for the preparation of total protein extract of wine spoilage microrganisms for proteomic analysis
    • Polati, R.; Zapparoli, G.; Giudici, P.; Bossi, A. A CTAB based method for the preparation of total protein extract of wine spoilage microrganisms for proteomic analysis J. Chromatogr., B: Anal. Technol. Biomed. Life Sci. 2009, 877, 887-891
    • (2009) J. Chromatogr., B: Anal. Technol. Biomed. Life Sci. , vol.877 , pp. 887-891
    • Polati, R.1    Zapparoli, G.2    Giudici, P.3    Bossi, A.4
  • 15
    • 0030805824 scopus 로고    scopus 로고
    • Two-dimensional map of Haemophilus influenzae following protein enrichment by heparin chromatography
    • Fountoulakis, M.; Langen, H.; Evers, S.; Gray, C. P.; Takàcs, B. Two-dimensional map of Haemophilus influenzae following protein enrichment by heparin chromatography Electrophoresis 1997, 18, 1193-1202
    • (1997) Electrophoresis , vol.18 , pp. 1193-1202
    • Fountoulakis, M.1    Langen, H.2    Evers, S.3    Gray, C.P.4    Takàcs, B.5
  • 17
    • 84884908061 scopus 로고    scopus 로고
    • Evaluation of dialdehydic anti-inflammatory active principles in extra-virgin olive oil by reactive paper spray mass spectrometry
    • Mazzotti, F.; Di Donna, L.; Taverna, D.; Nardi, M.; Aiello, D.; Napoli, A.; Sindona, G. Evaluation of dialdehydic anti-inflammatory active principles in extra-virgin olive oil by reactive paper spray mass spectrometry Int. J. Mass Spectrom. 2013, 352, 87-91
    • (2013) Int. J. Mass Spectrom. , vol.352 , pp. 87-91
    • Mazzotti, F.1    Di Donna, L.2    Taverna, D.3    Nardi, M.4    Aiello, D.5    Napoli, A.6    Sindona, G.7
  • 18
    • 79954592907 scopus 로고    scopus 로고
    • High-Throughput Assay of Oleopentanedialdheydes in Extra Virgin Olive Oil by the UHPLC-ESI-MS/MS and Isotope Dilution Methods
    • Di Donna, L.; Benabdelkamel, H.; Mazzotti, F.; Napoli, A.; Nardi, M.; Sindona, G. High-Throughput Assay of Oleopentanedialdheydes in Extra Virgin Olive Oil by the UHPLC-ESI-MS/MS and Isotope Dilution Methods Anal. Chem. 2011, 83 (6) 1990-1995
    • (2011) Anal. Chem. , vol.83 , Issue.6 , pp. 1990-1995
    • Di Donna, L.1    Benabdelkamel, H.2    Mazzotti, F.3    Napoli, A.4    Nardi, M.5    Sindona, G.6
  • 19
    • 33846841174 scopus 로고    scopus 로고
    • Secondary metabolism of olive secoiridoids. New microcomponents detected in drupes by electrospray ionization and high-resolution tandem mass spectrometry
    • Di Donna, L.; Mazzotti, F.; Napoli, A.; Salerno, R.; Sajjad, A.; Sindona, G. Secondary metabolism of olive secoiridoids. New microcomponents detected in drupes by electrospray ionization and high-resolution tandem mass spectrometry Rapid Mass Commun. Mass Spectrom. 2007, 21 (3) 273-278
    • (2007) Rapid Mass Commun. Mass Spectrom. , vol.21 , Issue.3 , pp. 273-278
    • Di Donna, L.1    Mazzotti, F.2    Napoli, A.3    Salerno, R.4    Sajjad, A.5    Sindona, G.6
  • 20
    • 84865788792 scopus 로고    scopus 로고
    • Assay of tyrosol and hydroxytyrosol in olive oil by tandem mass spectrometry and isotope dilution method
    • Mazzotti, F.; Benabdelkamel, H.; Di Donna, L.; Maiuolo, L.; Napoli, A.; Sindona, G. Assay of tyrosol and hydroxytyrosol in olive oil by tandem mass spectrometry and isotope dilution method Food Chem. 2012, 135 (3) 1006-1010
    • (2012) Food Chem. , vol.135 , Issue.3 , pp. 1006-1010
    • Mazzotti, F.1    Benabdelkamel, H.2    Di Donna, L.3    Maiuolo, L.4    Napoli, A.5    Sindona, G.6
  • 22
    • 84884677748 scopus 로고    scopus 로고
    • Binding ability of glutathione towards alkyltin(IV) compounds in aqueous solution
    • Cardiano, P.; Falcone, G.; Foti, C.; Giuffrè, O.; Napoli, A. Binding ability of glutathione towards alkyltin(IV) compounds in aqueous solution J. Inorg. Biochem. 2013, 129, 84-93
    • (2013) J. Inorg. Biochem. , vol.129 , pp. 84-93
    • Cardiano, P.1    Falcone, G.2    Foti, C.3    Giuffrè, O.4    Napoli, A.5
  • 24
    • 84887452241 scopus 로고    scopus 로고
    • Multisite phosphorylation of c-Jun at threonine 91/93/95 triggers the onset of c-Jun pro-apoptotic activity in cerebellar granule neurons
    • Reddy, C. E.; Albanito, L.; De Marco, P.; Aiello, D.; Napoli, A.; Musti, A. M. Multisite phosphorylation of c-Jun at threonine 91/93/95 triggers the onset of c-Jun pro-apoptotic activity in cerebellar granule neurons Cell. Death Dis. 2013, 4, e852
    • (2013) Cell. Death Dis. , vol.4 , pp. 852
    • Reddy, C.E.1    Albanito, L.2    De Marco, P.3    Aiello, D.4    Napoli, A.5    Musti, A.M.6
  • 25
    • 51649115314 scopus 로고    scopus 로고
    • Vegetable proteomics: The detection of Ole e 1 isoallergens by peptide matching of MALDI MS/MS spectra of underivatized and dansylated glycopeptides
    • Napoli, A.; Aiello, D.; Di Donna, L.; Moschidis, P.; Sindona, G. Vegetable proteomics: the detection of Ole e 1 isoallergens by peptide matching of MALDI MS/MS spectra of underivatized and dansylated glycopeptides J. Proteome Res. 2008, 7, 2723-2732
    • (2008) J. Proteome Res. , vol.7 , pp. 2723-2732
    • Napoli, A.1    Aiello, D.2    Di Donna, L.3    Moschidis, P.4    Sindona, G.5
  • 27
    • 24944537884 scopus 로고    scopus 로고
    • Characterization of enterobacteria using MALDI-TOF mass spectrometry
    • Pribil, P.; Fenselau, C. Characterization of enterobacteria using MALDI-TOF mass spectrometry Anal. Chem. 2005, 77 (18) 6092-6095
    • (2005) Anal. Chem. , vol.77 , Issue.18 , pp. 6092-6095
    • Pribil, P.1    Fenselau, C.2
  • 28
    • 0142040605 scopus 로고    scopus 로고
    • Characterization of Bacillus spore species and their mixtures using post-source decay with a curved-field reflectron
    • Warscheid, B.; Fenselau, C. Characterization of Bacillus spore species and their mixtures using post-source decay with a curved-field reflectron Anal. Chem. 2003, 75, 5618-5627
    • (2003) Anal. Chem. , vol.75 , pp. 5618-5627
    • Warscheid, B.1    Fenselau, C.2
  • 29
    • 0142135686 scopus 로고    scopus 로고
    • MALDI analysis of Bacilli in spore mixtures by applying a quadrupole ion trap time-of-flight tandem mass spectrometer
    • Warscheid, B.; Jackson, K.; Sutton, C.; Fenselau, C. MALDI analysis of Bacilli in spore mixtures by applying a quadrupole ion trap time-of-flight tandem mass spectrometer Anal. Chem. 2003, 75, 5608-5617
    • (2003) Anal. Chem. , vol.75 , pp. 5608-5617
    • Warscheid, B.1    Jackson, K.2    Sutton, C.3    Fenselau, C.4
  • 30
    • 18344393456 scopus 로고    scopus 로고
    • Rapid characterization of Bacillus spores targeting species-unique peptides produced with an atmospheric pressure matrix-assisted laser desorption/ionization source
    • Pribil, P. A.; Patton, E.; Black, G.; Doroshenko, V.; Fenselau, C. Rapid characterization of Bacillus spores targeting species-unique peptides produced with an atmospheric pressure matrix-assisted laser desorption/ionization source J. Mass Spectrom. 2005, 40, 464-474
    • (2005) J. Mass Spectrom. , vol.40 , pp. 464-474
    • Pribil, P.A.1    Patton, E.2    Black, G.3    Doroshenko, V.4    Fenselau, C.5
  • 31
    • 84898868272 scopus 로고    scopus 로고
    • Structural Characterisation of Malonyl Flavonols in Leek (Allium porrum L.) Using High-performance Liquid Chromatography and Mass Spectrometry
    • Di Donna, L.; Mazzotti, F.; Taverna, D.; Napoli, A.; Sindona, G. Structural Characterisation of Malonyl Flavonols in Leek (Allium porrum L.) Using High-performance Liquid Chromatography and Mass Spectrometry Phytochem. Anal. 2014, 25 (3) 207-212
    • (2014) Phytochem. Anal. , vol.25 , Issue.3 , pp. 207-212
    • Di Donna, L.1    Mazzotti, F.2    Taverna, D.3    Napoli, A.4    Sindona, G.5
  • 32
    • 34848889259 scopus 로고    scopus 로고
    • The Paragon Algorithm, a Next Generation Search Engine That Uses Sequence Temperature Values and Feature Probabilities to Identify Peptides from Tandem Mass Spectra
    • Shilov, I. V.; Seymour, S. L.; Patel, A. A.; Loboda, A.; Tang, W. H.; Keating, S. P.; Hunter, C. L.; Nuwaysir, L. M.; Schaeffer, D. A. The Paragon Algorithm, a Next Generation Search Engine That Uses Sequence Temperature Values and Feature Probabilities to Identify Peptides from Tandem Mass Spectra Mol. Cell. Proteomics 2007, 6 (9) 1638-1655
    • (2007) Mol. Cell. Proteomics , vol.6 , Issue.9 , pp. 1638-1655
    • Shilov, I.V.1    Seymour, S.L.2    Patel, A.A.3    Loboda, A.4    Tang, W.H.5    Keating, S.P.6    Hunter, C.L.7    Nuwaysir, L.M.8    Schaeffer, D.A.9
  • 33
    • 2442568591 scopus 로고    scopus 로고
    • Setting up standards and a reference map for the alkaline proteome of the Gram-positive bacterium Lactococcus lactis
    • Drews, O.; Reil, G.; Parlar, H.; Gorg, A. Setting up standards and a reference map for the alkaline proteome of the Gram-positive bacterium Lactococcus lactis Proteomics 2004, 4, 1293-1304
    • (2004) Proteomics , vol.4 , pp. 1293-1304
    • Drews, O.1    Reil, G.2    Parlar, H.3    Gorg, A.4
  • 34
    • 1142287342 scopus 로고    scopus 로고
    • Ion-pair assisted recovery of matrix-assisted laser desorption/ionization mass spectral signals from SDS-containing peptide-protein mixtures
    • Rajnarayanan, R. V.; Wang, K. Ion-pair assisted recovery of matrix-assisted laser desorption/ionization mass spectral signals from SDS-containing peptide-protein mixtures J. Mass Spectrom. 2004, 39, 79-85
    • (2004) J. Mass Spectrom. , vol.39 , pp. 79-85
    • Rajnarayanan, R.V.1    Wang, K.2
  • 35
    • 33646715948 scopus 로고    scopus 로고
    • Profiling of Hydrophilic Proteins from Olea europaea Olive Pollen by MALDI TOF Mass Spectrometry
    • Napoli, A.; Aiello, D.; Di Donna, L.; Sajjad, A.; Perri, E.; Sindona, G. Profiling of Hydrophilic Proteins from Olea europaea Olive Pollen by MALDI TOF Mass Spectrometry Anal. Chem. 2006, 78 (10) 3434-3443
    • (2006) Anal. Chem. , vol.78 , Issue.10 , pp. 3434-3443
    • Napoli, A.1    Aiello, D.2    Di Donna, L.3    Sajjad, A.4    Perri, E.5    Sindona, G.6
  • 36
    • 34547779366 scopus 로고    scopus 로고
    • Exploitation of Endogenous Protease Activity in Raw Mastitic Milk by MALDI TOF/TOF
    • Napoli, A.; Aiello, D.; Di Donna, L.; Prendushi, H.; Sindona, G. Exploitation of Endogenous Protease Activity in Raw Mastitic Milk by MALDI TOF/TOF Anal. Chem. 2007, 79 (15) 5941-5948
    • (2007) Anal. Chem. , vol.79 , Issue.15 , pp. 5941-5948
    • Napoli, A.1    Aiello, D.2    Di Donna, L.3    Prendushi, H.4    Sindona, G.5
  • 38
    • 1642547007 scopus 로고    scopus 로고
    • Release of glycosidically bound flavour compounds of Chardonnay by Oenococcus oeni during malolactic fermentation
    • D'Incecco, N.; Bartowsky, E.; Kassara, S.; Lante, A.; Spettoli, P.; Henschke, P. Release of glycosidically bound flavour compounds of Chardonnay by Oenococcus oeni during malolactic fermentation Food Microbiol. 2004, 21, 257-265
    • (2004) Food Microbiol. , vol.21 , pp. 257-265
    • D'Incecco, N.1    Bartowsky, E.2    Kassara, S.3    Lante, A.4    Spettoli, P.5    Henschke, P.6
  • 39
    • 49449101678 scopus 로고    scopus 로고
    • Comparative Genomics of Enzymes in Flavor-Forming Pathways from Amino Acids in Lactic Acid Bacteria
    • Liu, M.; Nauta, A.; Francke, C.; Siezen, R. J. Comparative Genomics of Enzymes in Flavor-Forming Pathways from Amino Acids in Lactic Acid Bacteria Appl. Environ. Microbiol. 2008, 74 (15) 4590-4600
    • (2008) Appl. Environ. Microbiol. , vol.74 , Issue.15 , pp. 4590-4600
    • Liu, M.1    Nauta, A.2    Francke, C.3    Siezen, R.J.4
  • 40
    • 84885369980 scopus 로고    scopus 로고
    • Structural and biochemical characterization of a NAD(+)-dependent alcohol dehydrogenase from Oenococcus oeni as a new model molecule for industrial biotechnology applications
    • Elleuche, S.; Fodor, K.; Klippel, B.; von der Heyde, A.; Wilmanns, M.; Antranikian, G. Structural and biochemical characterization of a NAD(+)-dependent alcohol dehydrogenase from Oenococcus oeni as a new model molecule for industrial biotechnology applications Appl. Microbio.l Biotechnol. 2013, 97 (20) 8963-8975
    • (2013) Appl. Microbio.l Biotechnol. , vol.97 , Issue.20 , pp. 8963-8975
    • Elleuche, S.1    Fodor, K.2    Klippel, B.3    Von Der Heyde, A.4    Wilmanns, M.5    Antranikian, G.6
  • 41
    • 58549113141 scopus 로고    scopus 로고
    • Purification of an alcohol dehydrogenase involved in the conversion of methional to methionol in Oenococcus oeni IOEB 8406
    • Vallet, A.; Santarelli, X.; Lonvaud-Funel, A.; de Revel, G.; Cabanne, C. Purification of an alcohol dehydrogenase involved in the conversion of methional to methionol in Oenococcus oeni IOEB 8406 Appl. Microbiol. Biotechnol. 2009, 82, 87-94
    • (2009) Appl. Microbiol. Biotechnol. , vol.82 , pp. 87-94
    • Vallet, A.1    Santarelli, X.2    Lonvaud-Funel, A.3    De Revel, G.4    Cabanne, C.5
  • 42
    • 84899693272 scopus 로고    scopus 로고
    • Bacterial group III alcohol dehydrogenases - Function, evolution and biotechnological applications
    • Elleuche, S.; Antranikian, G. Bacterial group III alcohol dehydrogenases-function, evolution and biotechnological applications OA Alcohol 2013, 1 (1) 2-6
    • (2013) OA Alcohol , vol.1 , Issue.1 , pp. 2-6
    • Elleuche, S.1    Antranikian, G.2
  • 43
    • 60849122826 scopus 로고    scopus 로고
    • 1,3-Propanediol Dehydrogenase from Klebsiella pneumoniae: Decameric Quaternary Structure and Possible Subunit Cooperativity
    • Marçal, D.; Toste Rêgo, A.; Carrondo, M. A.; Enguita, F. J. 1,3-Propanediol Dehydrogenase from Klebsiella pneumoniae: Decameric Quaternary Structure and Possible Subunit Cooperativity J. Bacteriol. 2009, 191 (4) 1143-1151
    • (2009) J. Bacteriol. , vol.191 , Issue.4 , pp. 1143-1151
    • Marçal, D.1    Toste Rêgo, A.2    Carrondo, M.A.3    Enguita, F.J.4
  • 44
    • 78049427906 scopus 로고    scopus 로고
    • β-Glucoside metabolism in Oenococcus oeni: Cloning and characterisation of the phospho-β-glucosidase bglD
    • Capaldo, A.; Walker, M. E.; Ford, C. M.; Jiranek, V. β-Glucoside metabolism in Oenococcus oeni: Cloning and characterisation of the phospho-β-glucosidase bglD Food Chem. 2011, 125, 476-482
    • (2011) Food Chem. , vol.125 , pp. 476-482
    • Capaldo, A.1    Walker, M.E.2    Ford, C.M.3    Jiranek, V.4
  • 45
    • 0028280120 scopus 로고
    • Growth and energetics of Leuconostoc oenos during cometabolism of glucose with citrate or fructose
    • Salou, P.; Loubiere, P.; Pareilleux, A. Growth and energetics of Leuconostoc oenos during cometabolism of glucose with citrate or fructose Appl. Environ. Microbiol. 1994, 60, 1459-1466
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 1459-1466
    • Salou, P.1    Loubiere, P.2    Pareilleux, A.3
  • 46
    • 78149470645 scopus 로고    scopus 로고
    • Multigenic expression analysis as an approach to understanding the behaviour of Oenococcus oeni in wine-like conditions
    • Olguín, N.; Bordons, A.; Reguant, C. Multigenic expression analysis as an approach to understanding the behaviour of Oenococcus oeni in wine-like conditions Int. J. Food Microbiol. 2010, 144, 88-95
    • (2010) Int. J. Food Microbiol. , vol.144 , pp. 88-95
    • Olguín, N.1    Bordons, A.2    Reguant, C.3
  • 50
    • 0032032195 scopus 로고    scopus 로고
    • Increase of sulfite tolerance in Oenococcus oeni by means of acidic adaptation
    • Guzzo, J.; Jobin, M. P.; Diviès, C. Increase of sulfite tolerance in Oenococcus oeni by means of acidic adaptation FEMS Microbiol. Lett. 1998, 160, 43-47
    • (1998) FEMS Microbiol. Lett. , vol.160 , pp. 43-47
    • Guzzo, J.1    Jobin, M.P.2    Diviès, C.3
  • 51
    • 28444455603 scopus 로고    scopus 로고
    • A new approach for selection of Oenococcus oeni strains in order to produce malolactic starters
    • Coucheney, F.; Desroche, N.; Bou, M.; Tourdot-Maréchal, R.; Dulau, L.; Guzzo, J. A new approach for selection of Oenococcus oeni strains in order to produce malolactic starters Int. J. Food Microbiol. 2005, 105 (3) 463-470
    • (2005) Int. J. Food Microbiol. , vol.105 , Issue.3 , pp. 463-470
    • Coucheney, F.1    Desroche, N.2    Bou, M.3    Tourdot-Maréchal, R.4    Dulau, L.5    Guzzo, J.6
  • 52
    • 23644453928 scopus 로고    scopus 로고
    • CtsR Is the Master Regulator of Stress Response Gene Expression in Oenococcus oeni
    • Grandvalet, C.; Coucheney, F.; Beltramo, C.; Guzzo, J. CtsR Is the Master Regulator of Stress Response Gene Expression in Oenococcus oeni J. Bacteriol. 2005, 187 (16) 5614-5623
    • (2005) J. Bacteriol. , vol.187 , Issue.16 , pp. 5614-5623
    • Grandvalet, C.1    Coucheney, F.2    Beltramo, C.3    Guzzo, J.4
  • 53
    • 0031923448 scopus 로고    scopus 로고
    • ClpX and ClpP are essential for the efficient acquisition of genes specifying type IA and IB restriction systems
    • Makovets, S.; Titheradge, A. J. B.; Murray, N. E. ClpX and ClpP are essential for the efficient acquisition of genes specifying type IA and IB restriction systems Mol. Microbiol. 1998, 28 (1) 25-35
    • (1998) Mol. Microbiol. , vol.28 , Issue.1 , pp. 25-35
    • Makovets, S.1    Titheradge, A.J.B.2    Murray, N.E.3
  • 54
    • 0029979976 scopus 로고    scopus 로고
    • Influence of Matrix Solution Conditions on the MALDI-MS Analysis of Peptides and Proteins
    • Cohen, S. L.; Chait, B. T. Influence of Matrix Solution Conditions on the MALDI-MS Analysis of Peptides and Proteins Anal. Chem. 1996, 68, 31-37
    • (1996) Anal. Chem. , vol.68 , pp. 31-37
    • Cohen, S.L.1    Chait, B.T.2
  • 56
    • 77950369259 scopus 로고    scopus 로고
    • Moonlighting proteins: An intriguing mode of multitasking
    • Huberts, D. H.; van der Klei, I. J. Moonlighting proteins: an intriguing mode of multitasking Biochim. Biophys. Acta 2010, 1803 (4) 520-525
    • (2010) Biochim. Biophys. Acta , vol.1803 , Issue.4 , pp. 520-525
    • Huberts, D.H.1    Van Der Klei, I.J.2
  • 57
    • 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
  • 58
    • 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
  • 59
    • 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.; Macek, B. 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    Macek, B.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.