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Volumn 7, Issue , 2009, Pages 37-

2-DE analysis indicates that Acinetobacter baumannii displays a robust and versatile metabolism

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CYTOPLASM PROTEIN; HEAT SHOCK PROTEIN; MEMBRANE PROTEIN; PORIN;

EID: 70449464951     PISSN: None     EISSN: 14775956     Source Type: Journal    
DOI: 10.1186/1477-5956-7-37     Document Type: Article
Times cited : (27)

References (51)
  • 2
    • 33144460009 scopus 로고    scopus 로고
    • The epidemiology and control of Acinetobacter baumannii in health care facilities
    • Fournier P, Richet H. The epidemiology and control of Acinetobacter baumannii in health care facilities. Clin Infect Dis Dis 2006, 42:692-699.
    • (2006) Clin Infect Dis Dis , vol.42 , pp. 692-699
    • Fournier, P.1    Richet, H.2
  • 3
    • 43949088799 scopus 로고    scopus 로고
    • Acinetobacter baumannii infections in a surgical intensive care unit: predictors of multi-drug resistance
    • 10.1007/s00268-008-9571-3, 18408967
    • Katsaragakis S, Markogiannakis H, Toutouzas K, Drimousis P, Larentzakis A, Theodoraki E-M, Theodorou D. Acinetobacter baumannii infections in a surgical intensive care unit: predictors of multi-drug resistance. World J Surg 2008, 32:1194-1202. 10.1007/s00268-008-9571-3, 18408967.
    • (2008) World J Surg , vol.32 , pp. 1194-1202
    • Katsaragakis, S.1    Markogiannakis, H.2    Toutouzas, K.3    Drimousis, P.4    Larentzakis, A.5    Theodoraki, E.-.M.6    Theodorou, D.7
  • 4
    • 0033827703 scopus 로고    scopus 로고
    • Characterization of a nosocomial outbreak caused by a multiresistant Acinetobacter baumannii strain with a carbapenem-hydrolyzing enzyme: high-level carbapenem resistance in A. baumannii is not due solely to the presence of beta-lactamases
    • 87377, 10970374
    • Bou G, Cervero G, Dominguez MA, Quereda C, Martinez-Beltran J. Characterization of a nosocomial outbreak caused by a multiresistant Acinetobacter baumannii strain with a carbapenem-hydrolyzing enzyme: high-level carbapenem resistance in A. baumannii is not due solely to the presence of beta-lactamases. J Clin Microbiol 2000, 38:3299-3305. 87377, 10970374.
    • (2000) J Clin Microbiol , vol.38 , pp. 3299-3305
    • Bou, G.1    Cervero, G.2    Dominguez, M.A.3    Quereda, C.4    Martinez-Beltran, J.5
  • 5
    • 9444250412 scopus 로고    scopus 로고
    • Emerging resistance among bacterial pathogens in the intensive care unit - a European and North American Surveillance study (2000-2002)
    • 10.1186/1476-0711-3-14, 509280, 15283864
    • Jones M, Draghi D, Thornsberry C, Karlowsky J, Sahm D, Wenzel R. Emerging resistance among bacterial pathogens in the intensive care unit - a European and North American Surveillance study (2000-2002). Ann Clin Microbiol Antimicrob 2004, 3:14. 10.1186/1476-0711-3-14, 509280, 15283864.
    • (2004) Ann Clin Microbiol Antimicrob , vol.3 , pp. 14
    • Jones, M.1    Draghi, D.2    Thornsberry, C.3    Karlowsky, J.4    Sahm, D.5    Wenzel, R.6
  • 6
    • 34447556772 scopus 로고    scopus 로고
    • Porins, efflux pumps and multidrug resistance in Acinetobacter baumannii
    • 10.1093/jac/dkl509, 17324960
    • Vila J, Marti S, Sanchez-Cespedes J. Porins, efflux pumps and multidrug resistance in Acinetobacter baumannii. J Antimicrob Chemother 2007, 59:1210-1215. 10.1093/jac/dkl509, 17324960.
    • (2007) J Antimicrob Chemother , vol.59 , pp. 1210-1215
    • Vila, J.1    Marti, S.2    Sanchez-Cespedes, J.3
  • 9
    • 33947145569 scopus 로고    scopus 로고
    • New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis
    • 10.1101/gad.1510307, 1820901, 17344419
    • Smith MG, Gianoulis TA, Pukatzki S, Mekalanos JJ, Ornston LN, Gerstein M, Snyder M. New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis. Genes Dev 2007, 21:601-614. 10.1101/gad.1510307, 1820901, 17344419.
    • (2007) Genes Dev , vol.21 , pp. 601-614
    • Smith, M.G.1    Gianoulis, T.A.2    Pukatzki, S.3    Mekalanos, J.J.4    Ornston, L.N.5    Gerstein, M.6    Snyder, M.7
  • 10
    • 63849104493 scopus 로고    scopus 로고
    • Environmental proteomics: a paradigm shift in characterizing microbial activities at the molecular level
    • 10.1128/MMBR.00028-08, 19258533
    • Keller M, Hettich R. Environmental proteomics: a paradigm shift in characterizing microbial activities at the molecular level. Microbiol Mol Biol Rev 2009, 73:62-70. 10.1128/MMBR.00028-08, 19258533.
    • (2009) Microbiol Mol Biol Rev , vol.73 , pp. 62-70
    • Keller, M.1    Hettich, R.2
  • 11
    • 34548452940 scopus 로고    scopus 로고
    • Whole proteome analysis of post-translational modifications: applications of mass-spectrometry for proteogenomic annotation
    • 10.1101/gr.6427907, 1950905, 17690205
    • Gupta N, Tanner S, Jaitly N, Adkins JN, Lipton M, Edwards R, Romine M, Osterman A, Bafna V, Smith RD, Pevzner PA. Whole proteome analysis of post-translational modifications: applications of mass-spectrometry for proteogenomic annotation. Genome Res 2007, 17:1362-1377. 10.1101/gr.6427907, 1950905, 17690205.
    • (2007) Genome Res , vol.17 , pp. 1362-1377
    • Gupta, N.1    Tanner, S.2    Jaitly, N.3    Adkins, J.N.4    Lipton, M.5    Edwards, R.6    Romine, M.7    Osterman, A.8    Bafna, V.9    Smith, R.D.10    Pevzner, P.A.11
  • 12
    • 17144410529 scopus 로고    scopus 로고
    • Bacterial proteomics and its role in antibacterial drug discovery
    • Brötz-Oesterhelt H, Bandow JE, Labischinski H. Bacterial proteomics and its role in antibacterial drug discovery. Mass Spectrom 2005, 24:549-565.
    • (2005) Mass Spectrom , vol.24 , pp. 549-565
    • Brötz-Oesterhelt, H.1    Bandow, J.E.2    Labischinski, H.3
  • 13
    • 33845467685 scopus 로고    scopus 로고
    • Proteomic analysis of a fraction enriched in cell envelope proteins of Acinetobacter baumannii
    • 10.1002/pmic.200500323, 16544276
    • Martí S, Sánchez-Céspedes J, Oliveira E, Bellido D, Giralt E, Vila J. Proteomic analysis of a fraction enriched in cell envelope proteins of Acinetobacter baumannii. Proteomics 2006, 6:S82-S87. 10.1002/pmic.200500323, 16544276.
    • (2006) Proteomics , vol.6
    • Martí, S.1    Sánchez-Céspedes, J.2    Oliveira, E.3    Bellido, D.4    Giralt, E.5    Vila, J.6
  • 14
    • 33845450679 scopus 로고    scopus 로고
    • Global comparison of the membrane subproteomes between a multidrug-resistant Acinetobacter baumannii strain and a reference strain
    • 10.1021/pr060372s, 17137340
    • Siroy A, Cosette P, Seyer D, Lemaitre-Guillier C, Vallenet D, Van Dorsselaer A, Boyer-Mariotte S, Jouenne T, De E. Global comparison of the membrane subproteomes between a multidrug-resistant Acinetobacter baumannii strain and a reference strain. J Proteome Res 2006, 5:3385-3398. 10.1021/pr060372s, 17137340.
    • (2006) J Proteome Res , vol.5 , pp. 3385-3398
    • Siroy, A.1    Cosette, P.2    Seyer, D.3    Lemaitre-Guillier, C.4    Vallenet, D.5    Van Dorsselaer, A.6    Boyer-Mariotte, S.7    Jouenne, T.8    De, E.9
  • 15
    • 68249144375 scopus 로고    scopus 로고
    • Proteome analysis of outer membrane vesicles from clinical Acinetobacter baumannii isolate
    • Kwon S-O, Gho YS, Lee JC, Kim SI. Proteome analysis of outer membrane vesicles from clinical Acinetobacter baumannii isolate. FEMS Microbiol Lett 2009, 297:159-156.
    • (2009) FEMS Microbiol Lett , vol.297 , pp. 159-1156
    • Kwon, S.-.O.1    Gho, Y.S.2    Lee, J.C.3    Kim, S.I.4
  • 17
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • 10.1016/0003-2697(76)90527-3, 942051
    • Bradford M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254. 10.1016/0003-2697(76)90527-3, 942051.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 18
    • 0032603137 scopus 로고    scopus 로고
    • Quantifying protein in 2-D PAGE solubilisation buffers
    • Ramagli L. Quantifying protein in 2-D PAGE solubilisation buffers. Methods Mol Biol 1999, 112:99-103.
    • (1999) Methods Mol Biol , vol.112 , pp. 99-103
    • Ramagli, L.1
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of head proteins of bacteriophage T4
    • 10.1038/227680a0, 5432063
    • Laemmli UK. Cleavage of structural proteins during the assembly of head proteins of bacteriophage T4. Nature 1970, 227:680-685. 10.1038/227680a0, 5432063.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • Blum H, Beier H, Gross H. Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 1987, 8:93-99.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.3
  • 21
    • 0034690931 scopus 로고    scopus 로고
    • Use of mass spectrometry to study signalling pathways
    • 10.1126/stke.2000.37.pl1, 11752594
    • Pandey A, Andersen J, Mann M. Use of mass spectrometry to study signalling pathways. Sci STKE 2000, 2000:PL1. 10.1126/stke.2000.37.pl1, 11752594.
    • (2000) Sci STKE , vol.2000
    • Pandey, A.1    Andersen, J.2    Mann, M.3
  • 22
    • 0032535467 scopus 로고    scopus 로고
    • Modification of cysteine residues by alkylation. A tool in peptide mapping and protein identification
    • 10.1021/ac9806005, 9868912
    • Sechi S, Chait BT. Modification of cysteine residues by alkylation. A tool in peptide mapping and protein identification. Anal Chem 1998, 70:5150-5158. 10.1021/ac9806005, 9868912.
    • (1998) Anal Chem , vol.70 , pp. 5150-5158
    • Sechi, S.1    Chait, B.T.2
  • 23
    • 34249826612 scopus 로고    scopus 로고
    • Combined cup loading, bis(2-hydroxyethyl) disulfide, and protein precipitation protocols to improve the alkaline proteome of Lactobacillus hilgardii
    • 10.1002/elps.200600496, 17492720
    • Lamberti C, Pessione E, Giuffrida MG, Mazzoli R, Barello C, Conti A, Giunta C. Combined cup loading, bis(2-hydroxyethyl) disulfide, and protein precipitation protocols to improve the alkaline proteome of Lactobacillus hilgardii. Electrophoresis 2007, 28:1633-1638. 10.1002/elps.200600496, 17492720.
    • (2007) Electrophoresis , vol.28 , pp. 1633-1638
    • Lamberti, C.1    Pessione, E.2    Giuffrida, M.G.3    Mazzoli, R.4    Barello, C.5    Conti, A.6    Giunta, C.7
  • 24
    • 33846990172 scopus 로고    scopus 로고
    • Characterization of beta-ketoadipate pathway from multi-drug resistance bacterium, Acinetobacter baumannii DU202 by proteomic approach
    • Park S-H, Kim J-W, Yun S-H, Leem S-H, Kahng H-Y, Kim SI. Characterization of beta-ketoadipate pathway from multi-drug resistance bacterium, Acinetobacter baumannii DU202 by proteomic approach. J Microbiol 2006, 44:632-640.
    • (2006) J Microbiol , vol.44 , pp. 632-640
    • Park, S.-.H.1    Kim, J.-.W.2    Yun, S.-.H.3    Leem, S.-.H.4    Kahng, H.-.Y.5    Kim, S.I.6
  • 25
    • 0030660581 scopus 로고    scopus 로고
    • A genomic perspective on protein families
    • 10.1126/science.278.5338.631, 9381173
    • Tatusov RL, Koonin EV, Lipman DJ. A genomic perspective on protein families. Science 1997, 278:631-637. 10.1126/science.278.5338.631, 9381173.
    • (1997) Science , vol.278 , pp. 631-637
    • Tatusov, R.L.1    Koonin, E.V.2    Lipman, D.J.3
  • 26
    • 15844431346 scopus 로고    scopus 로고
    • PSORTb v.2.0: Expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis
    • 10.1093/bioinformatics/bti057, 15501914
    • Gardy JL, Laird MR, Chen F, Rey S, Walsh CJ, Ester M, Brinkman FS. PSORTb v.2.0: Expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis. Bioinformatics 2005, 21:617-623. 10.1093/bioinformatics/bti057, 15501914.
    • (2005) Bioinformatics , vol.21 , pp. 617-623
    • Gardy, J.L.1    Laird, M.R.2    Chen, F.3    Rey, S.4    Walsh, C.J.5    Ester, M.6    Brinkman, F.S.7
  • 27
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • 10.1128/MMBR.67.4.593-656.2003, 309051, 14665678
    • Nikaido H. Molecular basis of bacterial outer membrane permeability revisited. Microbiol Mol Biol Rev 2003, 67:593-656. 10.1128/MMBR.67.4.593-656.2003, 309051, 14665678.
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 28
    • 0029056666 scopus 로고
    • The OprB porin plays a central role in carbohydrate uptake in Pseudomonas aeruginosa
    • 176988, 7768797
    • Wylie JL, Worobec EA. The OprB porin plays a central role in carbohydrate uptake in Pseudomonas aeruginosa. J Bacteriol 1995, 177:3021-3026. 176988, 7768797.
    • (1995) J Bacteriol , vol.177 , pp. 3021-3026
    • Wylie, J.L.1    Worobec, E.A.2
  • 29
    • 0141669010 scopus 로고    scopus 로고
    • Molecular and structural characterization of the HMP-AB gene encoding a pore-forming protein from a clinical isolate of Acinetobacter baumannii
    • 10.1007/s00284-003-4050-4, 14669924
    • Gribun A, Nitzan Y, Pechatnikov I, Hershkovits G, Katcoff DJ. Molecular and structural characterization of the HMP-AB gene encoding a pore-forming protein from a clinical isolate of Acinetobacter baumannii. Curr Microbiol 2003, 47:434-443. 10.1007/s00284-003-4050-4, 14669924.
    • (2003) Curr Microbiol , vol.47 , pp. 434-443
    • Gribun, A.1    Nitzan, Y.2    Pechatnikov, I.3    Hershkovits, G.4    Katcoff, D.J.5
  • 30
    • 0032771326 scopus 로고    scopus 로고
    • Isolation and characterization of heat-modifiable proteins from the outer membrane of Porphyromonas asaccharolytica and Acinetobacter baumannii
    • 10.1006/anae.1998.0181, 16887661
    • Nitzan Y, Pechatnikov I, Bar-El D, Wexler H. Isolation and characterization of heat-modifiable proteins from the outer membrane of Porphyromonas asaccharolytica and Acinetobacter baumannii. Anaerobe 1999, 5:43-50. 10.1006/anae.1998.0181, 16887661.
    • (1999) Anaerobe , vol.5 , pp. 43-50
    • Nitzan, Y.1    Pechatnikov, I.2    Bar-El, D.3    Wexler, H.4
  • 31
    • 28844433971 scopus 로고    scopus 로고
    • Cloning and functional analysis of the gene encoding the 33- to 36-kilodalton outer membrane protein associated with carbapenem resistance in Acinetobacter baumannii
    • 10.1128/AAC.49.12.5172-5175.2005
    • del Mar Tomas M, Beceiro A, Perez A, Velasco D, Moure R, Villanueva R, Martinez-Beltran J, Bou G. Cloning and functional analysis of the gene encoding the 33- to 36-kilodalton outer membrane protein associated with carbapenem resistance in Acinetobacter baumannii. Antimicrob Agents 2005, 49:5172-5175. 10.1128/AAC.49.12.5172-5175.2005.
    • (2005) Antimicrob Agents , vol.49 , pp. 5172-5175
    • del Mar Tomas, M.1    Beceiro, A.2    Perez, A.3    Velasco, D.4    Moure, R.5    Villanueva, R.6    Martinez-Beltran, J.7    Bou, G.8
  • 32
    • 36549000278 scopus 로고    scopus 로고
    • CarO, an Acinetobacter baumannii outer membrane protein involved in carbapenem resistance, is essential for L-ornithine uptake
    • Mussi MA, Relling VM, Limansky AS, Viale AM. CarO, an Acinetobacter baumannii outer membrane protein involved in carbapenem resistance, is essential for L-ornithine uptake. FEBS Let 2007, 581:5573-5578.
    • (2007) FEBS Let , vol.581 , pp. 5573-5578
    • Mussi, M.A.1    Relling, V.M.2    Limansky, A.S.3    Viale, A.M.4
  • 33
    • 0021197124 scopus 로고
    • Branched-Chain Amino Acid Metabolism
    • 10.1146/annurev.nu.04.070184.002205, 6380539
    • Harper AE, Miller RH, Block KP. Branched-Chain Amino Acid Metabolism. Annual Review of Nutrition 1984, 4:409. 10.1146/annurev.nu.04.070184.002205, 6380539.
    • (1984) Annual Review of Nutrition , vol.4 , pp. 409
    • Harper, A.E.1    Miller, R.H.2    Block, K.P.3
  • 34
    • 0033565448 scopus 로고    scopus 로고
    • Crystal structure of phenylalanine-regulated 3-deoxy-D-arabino-heptulosonate-7-phophate synthase from Escherichia coli
    • 10.1016/S0969-2126(99)80109-9, 10425687
    • Shumilin I, Kretsinger R, Bauerle R. Crystal structure of phenylalanine-regulated 3-deoxy-D-arabino-heptulosonate-7-phophate synthase from Escherichia coli. Structure 1999, 7:865-875. 10.1016/S0969-2126(99)80109-9, 10425687.
    • (1999) Structure , vol.7 , pp. 865-875
    • Shumilin, I.1    Kretsinger, R.2    Bauerle, R.3
  • 35
    • 70449622561 scopus 로고    scopus 로고
    • Media containing aromatic compounds induce peculiar proteins in Acinetobacter radioresistens, as revealed by proteome analysis
    • Giuffrida MG, Pessione E, Mazzoli R, Dellavalle G, Barello C, Conti A, Giunta C. Media containing aromatic compounds induce peculiar proteins in Acinetobacter radioresistens, as revealed by proteome analysis. Proteomics 2001, 22:1705-1711.
    • (2001) Proteomics , vol.22 , pp. 1705-1711
    • Giuffrida, M.G.1    Pessione, E.2    Mazzoli, R.3    Dellavalle, G.4    Barello, C.5    Conti, A.6    Giunta, C.7
  • 36
    • 0038385433 scopus 로고    scopus 로고
    • Membrane proteome of Acinetobacter radioresistens S13 during aromatic exposure
    • 10.1002/pmic.200300425, 12833532
    • Pessione E, Giuffrida MG, Barello C, Mazzoli R, Fortunato D, Conti A, Giunta C. Membrane proteome of Acinetobacter radioresistens S13 during aromatic exposure. Proteomics 2003, 3:1070-1076. 10.1002/pmic.200300425, 12833532.
    • (2003) Proteomics , vol.3 , pp. 1070-1076
    • Pessione, E.1    Giuffrida, M.G.2    Barello, C.3    Mazzoli, R.4    Fortunato, D.5    Conti, A.6    Giunta, C.7
  • 37
    • 2342666128 scopus 로고    scopus 로고
    • Proteomic analysis of Acinetobacter lwoffii K24 by 2-D gel electrophoresis and electrospray ionization quadrupole-time of flight mass spectrometry
    • Kim E-A, Kim JY, Kim S-J, Park KR, Chung H-J, Leem S-H, Kim SI. Proteomic analysis of Acinetobacter lwoffii K24 by 2-D gel electrophoresis and electrospray ionization quadrupole-time of flight mass spectrometry. J Microbio Methods 2004, 57:337-349.
    • (2004) J Microbio Methods , vol.57 , pp. 337-349
    • Kim, E.-.A.1    Kim, J.Y.2    Kim, S.-.J.3    Park, K.R.4    Chung, H.-.J.5    Leem, S.-.H.6    Kim, S.I.7
  • 38
    • 34648822321 scopus 로고    scopus 로고
    • A proteomics strategy for the analysis of bacterial biodegradation pathways
    • 10.1089/omi.2007.0019, 17883339
    • Kim SI, Choi J-S, Kahng H-Y. A proteomics strategy for the analysis of bacterial biodegradation pathways. OMICS 2007, 11:280-294. 10.1089/omi.2007.0019, 17883339.
    • (2007) OMICS , vol.11 , pp. 280-294
    • Kim, S.I.1    Choi, J.-.S.2    Kahng, H.-.Y.3
  • 39
    • 0030743733 scopus 로고    scopus 로고
    • Structure/function analysis of the PII signal transduction protein of Escherichia coli: genetic separation of interactions with protein receptors
    • 179259, 9209053
    • Jiang P, Zucker P, Atkinson MR, Kamberov ES, Tirasophon W, Chandran P, Schefke BR, Ninfa AJ. Structure/function analysis of the PII signal transduction protein of Escherichia coli: genetic separation of interactions with protein receptors. J Bacteriol 1997, 179:4342-4353. 179259, 9209053.
    • (1997) J Bacteriol , vol.179 , pp. 4342-4353
    • Jiang, P.1    Zucker, P.2    Atkinson, M.R.3    Kamberov, E.S.4    Tirasophon, W.5    Chandran, P.6    Schefke, B.R.7    Ninfa, A.J.8
  • 41
    • 0343122782 scopus 로고
    • Pathways for biosynthesis of a bacterial capsular polysaccharide II.: Carbohydrate metabolism and terminal oxidation mechanisms of a capsule-producing Coccus
    • 279077, 13775653
    • Taylor WH, Juni E. Pathways for biosynthesis of a bacterial capsular polysaccharide II.: Carbohydrate metabolism and terminal oxidation mechanisms of a capsule-producing Coccus. J Bacteriol 1961, 81:694-703. 279077, 13775653.
    • (1961) J Bacteriol , vol.81 , pp. 694-703
    • Taylor, W.H.1    Juni, E.2
  • 43
    • 44349164550 scopus 로고    scopus 로고
    • Dissection of the regulatory mechanism of a heat-shock responsive promoter in Haloarchaea
    • 10.1093/nar/gkn152, 2396416, 18390887
    • Lu Q, Han J, Zhou L, Coker JA, DasSarma P, DasSarma S, Xiang H. Dissection of the regulatory mechanism of a heat-shock responsive promoter in Haloarchaea. Nucleic Acids Res 2008, 36:3031-3042. 10.1093/nar/gkn152, 2396416, 18390887.
    • (2008) Nucleic Acids Res , vol.36 , pp. 3031-3042
    • Lu, Q.1    Han, J.2    Zhou, L.3    Coker, J.A.4    DasSarma, P.5    DasSarma, S.6    Xiang, H.7
  • 44
    • 0021810896 scopus 로고
    • Heat shock response of Neurospora crassa: protein synthesis and induced thermotolerance
    • 215887, 3158641
    • Plesofsky-Vig N, Brambl R. Heat shock response of Neurospora crassa: protein synthesis and induced thermotolerance. J Bacteriol 1985, 162:1083-1091. 215887, 3158641.
    • (1985) J Bacteriol , vol.162 , pp. 1083-1091
    • Plesofsky-Vig, N.1    Brambl, R.2
  • 45
    • 0025633154 scopus 로고
    • Role of Escherichia coli heat shock proteins DnaK and HtpG (C62.5) in response to nutritional deprivation
    • 210841, 2254278
    • Spence J, Cegielska A, Georgopoulos C. Role of Escherichia coli heat shock proteins DnaK and HtpG (C62.5) in response to nutritional deprivation. J Bacteriol 1990, 172:7157-7166. 210841, 2254278.
    • (1990) J Bacteriol , vol.172 , pp. 7157-7166
    • Spence, J.1    Cegielska, A.2    Georgopoulos, C.3
  • 46
    • 0024722223 scopus 로고
    • Comparative analysis of proteins induced by heat shock, salinity, and osmotic stress in the nitrogen-fixing cyanobacterium Anabaena Csp. strain L-31
    • 210338, 2504700
    • Bhagwat AA, Apte SK. Comparative analysis of proteins induced by heat shock, salinity, and osmotic stress in the nitrogen-fixing cyanobacterium Anabaena Csp. strain L-31. J Bacteriol 1989, 171:5187-5189. 210338, 2504700.
    • (1989) J Bacteriol , vol.171 , pp. 5187-5189
    • Bhagwat, A.A.1    Apte, S.K.2
  • 47
    • 63049093296 scopus 로고    scopus 로고
    • The cost of resistance to colistin in Acinetobacter baumannii: a proteomic perspective
    • 10.1002/pmic.200800434, 19253303
    • Fernández-Reyes M, Rodríguez-Falcón M, Chiva C, Pachón J, Andreu D, Rivas L. The cost of resistance to colistin in Acinetobacter baumannii: a proteomic perspective. Proteomics 2009, 9:1632-45. 10.1002/pmic.200800434, 19253303.
    • (2009) Proteomics , vol.9 , pp. 1632-1645
    • Fernández-Reyes, M.1    Rodríguez-Falcón, M.2    Chiva, C.3    Pachón, J.4    Andreu, D.5    Rivas, L.6
  • 48
    • 0028225734 scopus 로고
    • Expression and role of the universal stress protein, UspA, of Eschrichia coli during growth arrest
    • 10.1111/j.1365-2958.1994.tb00334.x, 8152377
    • Nystrom T, Neidhardt FC. Expression and role of the universal stress protein, UspA, of Eschrichia coli during growth arrest. Mol Microbiol 1994, 11:537-544. 10.1111/j.1365-2958.1994.tb00334.x, 8152377.
    • (1994) Mol Microbiol , vol.11 , pp. 537-544
    • Nystrom, T.1    Neidhardt, F.C.2
  • 49
    • 22744445608 scopus 로고    scopus 로고
    • Outer membrane protein 38 of Acinetobacter baumannii localizes to the mitochondria and induces apoptosis of epithelial cells
    • 10.1111/j.1462-5822.2005.00538.x, 16008580
    • Choi CH, Lee EY, Lee YC, Park TI, Kim HJ, Hyun SH, Kim SA, Lee S-K, Lee JC. Outer membrane protein 38 of Acinetobacter baumannii localizes to the mitochondria and induces apoptosis of epithelial cells. Cell Microbiol 2005, 7:1127-1138. 10.1111/j.1462-5822.2005.00538.x, 16008580.
    • (2005) Cell Microbiol , vol.7 , pp. 1127-1138
    • Choi, C.H.1    Lee, E.Y.2    Lee, Y.C.3    Park, T.I.4    Kim, H.J.5    Hyun, S.H.6    Kim, S.A.7    Lee, S.-.K.8    Lee, J.C.9
  • 50
    • 15244360776 scopus 로고    scopus 로고
    • Proposed guidelines for a unified nomenclature and phylogenetic analysis of type III Hop effector proteins in the plant pathogen Pseudomonas syringae
    • 10.1094/MPMI-18-0275, 15828679
    • Lindeberg M, Stavrinides J, Chang JH, Alfano JR, Collmer A, Dangl JL, Greenberg JT, Mansfield JW, Guttman DS. Proposed guidelines for a unified nomenclature and phylogenetic analysis of type III Hop effector proteins in the plant pathogen Pseudomonas syringae. Mol Plant Microbe Interact 2005, 18:275-282. 10.1094/MPMI-18-0275, 15828679.
    • (2005) Mol Plant Microbe Interact , vol.18 , pp. 275-282
    • Lindeberg, M.1    Stavrinides, J.2    Chang, J.H.3    Alfano, J.R.4    Collmer, A.5    Dangl, J.L.6    Greenberg, J.T.7    Mansfield, J.W.8    Guttman, D.S.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.