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Volumn 114, Issue , 2015, Pages 247-262

A comprehensive proteomic analysis of totarol induced alterations in Bacillus subtilis by multipronged quantitative proteomics

Author keywords

B. subtilis; Dehydrogenases; Filamentation; ITRAQ; Proteomics; Totarol

Indexed keywords

DITERPENOID; OXIDOREDUCTASE; PROTEOME; TOTAROL; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; BACTERIAL PROTEIN; DITERPENE;

EID: 84917706936     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2014.10.025     Document Type: Article
Times cited : (17)

References (58)
  • 1
    • 0004271659 scopus 로고    scopus 로고
    • WHO global strategy for containment of antimicrobial resistance
    • World Health Organization, Geneva, Switzerland
    • World Health Organization WHO global strategy for containment of antimicrobial resistance. Report W.H.O./CDS/CSR/DRS/2001.2 2001, World Health Organization, Geneva, Switzerland.
    • (2001) Report W.H.O./CDS/CSR/DRS/2001.2
  • 2
    • 17844399025 scopus 로고    scopus 로고
    • Natural products to drugs: natural product derived compounds in clinical trials
    • Butler M.S. Natural products to drugs: natural product derived compounds in clinical trials. Nat Prod Rep 2005, 22:162-195.
    • (2005) Nat Prod Rep , vol.22 , pp. 162-195
    • Butler, M.S.1
  • 3
    • 77955891916 scopus 로고    scopus 로고
    • FtsZ inhibition: a promising approach for antistaphylococcal therapy
    • Singh P., Panda D. FtsZ inhibition: a promising approach for antistaphylococcal therapy. Drug News Perspect 2010, 23:295-304.
    • (2010) Drug News Perspect , vol.23 , pp. 295-304
    • Singh, P.1    Panda, D.2
  • 4
    • 0033946964 scopus 로고    scopus 로고
    • The synthesis and antibacterial activity of totarol derivatives. Part 2: modifications at C-12 and O-13
    • Evans G.B., Furneaux R.H. The synthesis and antibacterial activity of totarol derivatives. Part 2: modifications at C-12 and O-13. Bioorg Med Chem 2000, 8:1653-1662.
    • (2000) Bioorg Med Chem , vol.8 , pp. 1653-1662
    • Evans, G.B.1    Furneaux, R.H.2
  • 5
    • 0030836809 scopus 로고    scopus 로고
    • Antioxidative action of diterpenoids from Podocarpus nagi
    • Haraguchi H., Ishikawa H., Kubo I. Antioxidative action of diterpenoids from Podocarpus nagi. Planta Med 1997, 63:213-215.
    • (1997) Planta Med , vol.63 , pp. 213-215
    • Haraguchi, H.1    Ishikawa, H.2    Kubo, I.3
  • 7
    • 36849079896 scopus 로고    scopus 로고
    • The antifungal compound totarol of Thujopsis dolabrata var. hondai seeds selects for fungi on seedling root surfaces
    • Yamaji K., Mori S., Akiyama M., Kato A., Nakashima T. The antifungal compound totarol of Thujopsis dolabrata var. hondai seeds selects for fungi on seedling root surfaces. J Chem Ecol 2007, 33:2254-2265.
    • (2007) J Chem Ecol , vol.33 , pp. 2254-2265
    • Yamaji, K.1    Mori, S.2    Akiyama, M.3    Kato, A.4    Nakashima, T.5
  • 8
    • 0041333074 scopus 로고    scopus 로고
    • Synthesis of totarol amino alcohol derivatives and their antiplasmodial activity and cytotoxicity
    • Clarkson C., Musonda C.C., Chibale K., Campbell W.E., Smith P. Synthesis of totarol amino alcohol derivatives and their antiplasmodial activity and cytotoxicity. Bioorg Med Chem 2003, 11:4417-4422.
    • (2003) Bioorg Med Chem , vol.11 , pp. 4417-4422
    • Clarkson, C.1    Musonda, C.C.2    Chibale, K.3    Campbell, W.E.4    Smith, P.5
  • 9
    • 0034939302 scopus 로고    scopus 로고
    • Anti-tumor promoting diterpenes from the stem bark of Thuja standishii (Cupressaceae)
    • Iwamoto M., Ohtsu H., Tokuda H., Nishino H., Matsunaga S., Tanaka R. Anti-tumor promoting diterpenes from the stem bark of Thuja standishii (Cupressaceae). Bioorg Med Chem 2001, 9(7):1911-1921.
    • (2001) Bioorg Med Chem , vol.9 , Issue.7 , pp. 1911-1921
    • Iwamoto, M.1    Ohtsu, H.2    Tokuda, H.3    Nishino, H.4    Matsunaga, S.5    Tanaka, R.6
  • 10
    • 0026663089 scopus 로고
    • Antibacterial activity of totarol and its potentiation
    • Kubo I., Muroi H., Himejima M. Antibacterial activity of totarol and its potentiation. J Nat Prod 1992, 55:1436-1440.
    • (1992) J Nat Prod , vol.55 , pp. 1436-1440
    • Kubo, I.1    Muroi, H.2    Himejima, M.3
  • 11
    • 0029946709 scopus 로고    scopus 로고
    • Mode of antibacterial action of totarol, a diterpene from Podocarpus nagi
    • Haraguchi H., Oike S., Muroi H., Kubo I. Mode of antibacterial action of totarol, a diterpene from Podocarpus nagi. Planta Med 1996, 62:122-125.
    • (1996) Planta Med , vol.62 , pp. 122-125
    • Haraguchi, H.1    Oike, S.2    Muroi, H.3    Kubo, I.4
  • 12
    • 0033920245 scopus 로고    scopus 로고
    • The synthesis and antibacterial activity of totarol derivatives. Part 3: modification of ring-B
    • Evans G.B., Furneaux R.H., Gainsford G.J., Murphy M.P. The synthesis and antibacterial activity of totarol derivatives. Part 3: modification of ring-B. Bioorg Med Chem 2000, 8:1663-1675.
    • (2000) Bioorg Med Chem , vol.8 , pp. 1663-1675
    • Evans, G.B.1    Furneaux, R.H.2    Gainsford, G.J.3    Murphy, M.P.4
  • 13
    • 23944461262 scopus 로고    scopus 로고
    • Plants as a source of bacterial resistance modulators and anti-infective agents
    • Gibbons S. Plants as a source of bacterial resistance modulators and anti-infective agents. Phytochem Rev 2005, 4:63-78.
    • (2005) Phytochem Rev , vol.4 , pp. 63-78
    • Gibbons, S.1
  • 15
    • 0035795111 scopus 로고    scopus 로고
    • Effects of (+)-totarol, a diterpenoid antibacterial agent, on phospholipid model membranes
    • Micol V., Mateo C.R., Shapiro S., Aranda F.J., Villalaín J. Effects of (+)-totarol, a diterpenoid antibacterial agent, on phospholipid model membranes. Biochim Biophys Acta 2001, 1511:281-290.
    • (2001) Biochim Biophys Acta , vol.1511 , pp. 281-290
    • Micol, V.1    Mateo, C.R.2    Shapiro, S.3    Aranda, F.J.4    Villalaín, J.5
  • 16
    • 34147136107 scopus 로고    scopus 로고
    • Totarol inhibits bacterial cytokinesis by perturbing the assembly dynamics of FtsZ
    • Jaiswal R., Beuria T.K., Mohan R., Mahajan S.K., Panda D. Totarol inhibits bacterial cytokinesis by perturbing the assembly dynamics of FtsZ. Biochemistry 2007, 46:4211-4220.
    • (2007) Biochemistry , vol.46 , pp. 4211-4220
    • Jaiswal, R.1    Beuria, T.K.2    Mohan, R.3    Mahajan, S.K.4    Panda, D.5
  • 17
    • 33645088173 scopus 로고    scopus 로고
    • Salt stress adaptation of Bacillus subtilis: a physiological proteomics approach
    • Höper D., Bernhardt J., Hecker M. Salt stress adaptation of Bacillus subtilis: a physiological proteomics approach. Proteomics 2006, 6:1550-1562.
    • (2006) Proteomics , vol.6 , pp. 1550-1562
    • Höper, D.1    Bernhardt, J.2    Hecker, M.3
  • 18
    • 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. Physiological proteomics and stress/starvation responses in Bacillus subtilis and Staphylococcus aureus. Res Microbiol 2009, 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
  • 19
    • 37549068524 scopus 로고    scopus 로고
    • Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis
    • Gerth U., Kock H., Kusters I., Michalik S., Switzer R.L., Hecker M. Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 2008, 190:321-331.
    • (2008) J Bacteriol , vol.190 , pp. 321-331
    • Gerth, U.1    Kock, H.2    Kusters, I.3    Michalik, S.4    Switzer, R.L.5    Hecker, M.6
  • 20
    • 50049125078 scopus 로고    scopus 로고
    • Depletion of thiol-containing proteins in response to quinones in Bacillus subtilis
    • Liebeke M., Pöther D.C., van Duy N., Albrecht D., Becher D., Hochgräfe F., et al. Depletion of thiol-containing proteins in response to quinones in Bacillus subtilis. Mol Microbiol 2008, l69(6):1513-1529.
    • (2008) Mol Microbiol , vol.l69 , Issue.6 , pp. 1513-1529
    • Liebeke, M.1    Pöther, D.C.2    van Duy, N.3    Albrecht, D.4    Becher, D.5    Hochgräfe, F.6
  • 22
    • 75149171079 scopus 로고    scopus 로고
    • A comprehensive proteomics and transcriptomics analysis of Bacillus subtilis salt stress adaptation
    • Hahne H., Mäder U., Otto A., Bonn F., Steil L., Bremer E., et al. A comprehensive proteomics and transcriptomics analysis of Bacillus subtilis salt stress adaptation. J Bacteriol 2010, 192(3):870-882.
    • (2010) J Bacteriol , vol.192 , Issue.3 , pp. 870-882
    • Hahne, H.1    Mäder, U.2    Otto, A.3    Bonn, F.4    Steil, L.5    Bremer, E.6
  • 23
    • 79251551042 scopus 로고    scopus 로고
    • Systems-wide temporal proteomic profiling in glucose-starved Bacillus subtilis
    • Otto A., Bernhardt J., Meyer H., Schaffer M., Herbst F.A., Siebourg J., et al. Systems-wide temporal proteomic profiling in glucose-starved Bacillus subtilis. Nat Commun 2010, 1:137.
    • (2010) Nat Commun , vol.1 , pp. 137
    • Otto, A.1    Bernhardt, J.2    Meyer, H.3    Schaffer, M.4    Herbst, F.A.5    Siebourg, J.6
  • 24
    • 33746295997 scopus 로고    scopus 로고
    • Gel-free and gel-based proteomics in Bacillus subtilis: a comparative study. Mol Cell Proteomics
    • Wolff S, Otto A, Albrecht D, Zeng JS, Büttner K, Glückmann M, et al. Gel-free and gel-based proteomics in Bacillus subtilis: a comparative study. Mol Cell Proteomics 2005(7):1183-92.
    • (2005) , Issue.7 , pp. 1183-1192
    • Wolff, S.1    Otto, A.2    Albrecht, D.3    Zeng, J.S.4    Büttner, K.5    Glückmann, M.6
  • 25
    • 41749098049 scopus 로고    scopus 로고
    • Peptide inhibitor of cytokinesis during sporulation in Bacillus subtilis
    • Handler A.A., Lim J.E., Losick R. Peptide inhibitor of cytokinesis during sporulation in Bacillus subtilis. Mol Microbiol 2008, 68:588-599.
    • (2008) Mol Microbiol , vol.68 , pp. 588-599
    • Handler, A.A.1    Lim, J.E.2    Losick, R.3
  • 26
    • 84894035081 scopus 로고    scopus 로고
    • A simple protein extraction method for proteomic analysis of diverse samples
    • Reddy P.J., Rao A.A., Malhotra D., Sharma S., Kumar R., Jain R., et al. A simple protein extraction method for proteomic analysis of diverse samples. Curr Proteomics 2013, 10:298-311.
    • (2013) Curr Proteomics , vol.10 , pp. 298-311
    • Reddy, P.J.1    Rao, A.A.2    Malhotra, D.3    Sharma, S.4    Kumar, R.5    Jain, R.6
  • 27
    • 84892856706 scopus 로고    scopus 로고
    • Proteomic analysis of Streptomyces coelicolor in response to Ciprofloxacin challenge
    • Rao A.A., Patkari M., Reddy P.J., Srivastava R., Pendharkar N., Rapole S., et al. Proteomic analysis of Streptomyces coelicolor in response to Ciprofloxacin challenge. J Proteomics 2014, 97:222-234.
    • (2014) J Proteomics , vol.97 , pp. 222-234
    • Rao, A.A.1    Patkari, M.2    Reddy, P.J.3    Srivastava, R.4    Pendharkar, N.5    Rapole, S.6
  • 28
    • 84865019674 scopus 로고    scopus 로고
    • Proteomic investigation of falciparum and vivax malaria for identification of surrogate protein markers
    • Ray S., Renu D., Srivastava R., Gollapalli K., Taur S., Jhaveri T., et al. Proteomic investigation of falciparum and vivax malaria for identification of surrogate protein markers. PLoS One 2012, 7:e41751.
    • (2012) PLoS One , vol.7 , pp. e41751
    • Ray, S.1    Renu, D.2    Srivastava, R.3    Gollapalli, K.4    Taur, S.5    Jhaveri, T.6
  • 29
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko A., Tomas H., Havlis J., Olsen J.V., Mann M. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat Protoc 2006, 1:2856-2860.
    • (2006) Nat Protoc , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 32
    • 84866973317 scopus 로고    scopus 로고
    • Proteins with altered levels in plasma from glioblastoma patients as revealed by iTRAQ-based quantitative proteomic analysis
    • Gautam P., Nair S.C., Gupta M.K., Sharma R., Polisetty R.V., Uppin M.S., et al. Proteins with altered levels in plasma from glioblastoma patients as revealed by iTRAQ-based quantitative proteomic analysis. PLoS One 2012, 7(9):e46153.
    • (2012) PLoS One , vol.7 , Issue.9 , pp. e46153
    • Gautam, P.1    Nair, S.C.2    Gupta, M.K.3    Sharma, R.4    Polisetty, R.V.5    Uppin, M.S.6
  • 33
    • 84874762979 scopus 로고    scopus 로고
    • The PRoteomics IDEntifications (PRIDE) database and associated tools: status in 2013
    • [Database issue]
    • Vizcaíno J.A., CÔté R.G., Csordas A., Dianes J.A., Fabregat A., Foster J.M., et al. The PRoteomics IDEntifications (PRIDE) database and associated tools: status in 2013. Nucleic Acids Res 2013, 41:D1063-D1069. [Database issue].
    • (2013) Nucleic Acids Res , vol.41 , pp. D1063-D1069
    • Vizcaíno, J.A.1    CÔté, R.G.2    Csordas, A.3    Dianes, J.A.4    Fabregat, A.5    Foster, J.M.6
  • 34
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID Bioinformatics Resources
    • Huang D.W., Sherman B.T., Lempicki R.A. Systematic and integrative analysis of large gene lists using DAVID Bioinformatics Resources. Nat Protoc 2009, 4:44-57.
    • (2009) Nat Protoc , vol.4 , pp. 44-57
    • Huang, D.W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 35
    • 58549112996 scopus 로고    scopus 로고
    • Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists
    • Huang D.W., Sherman B.T., Lempicki R.A. Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists. Nucleic Acids Res 2009, 37:1-13.
    • (2009) Nucleic Acids Res , vol.37 , pp. 1-13
    • Huang, D.W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 36
    • 79959986975 scopus 로고    scopus 로고
    • KOBAS 2.0: a web server for annotation and identification of enriched pathways and diseases
    • [Web Server issue]
    • Xie C., Mao X., Huang J., Ding Y., Wu J., Dong S., et al. KOBAS 2.0: a web server for annotation and identification of enriched pathways and diseases. Nucleic Acids Res 2011, 39:W316-W322. [Web Server issue].
    • (2011) Nucleic Acids Res , vol.39 , pp. W316-W322
    • Xie, C.1    Mao, X.2    Huang, J.3    Ding, Y.4    Wu, J.5    Dong, S.6
  • 37
    • 84876515907 scopus 로고    scopus 로고
    • STRING v9.1: protein-protein interaction networks, with increased coverage and integration
    • [Database issue]
    • Franceschini A., Szklarczyk D., Frankild S., Kuhn M., Simonovic M., Roth A., et al. STRING v9.1: protein-protein interaction networks, with increased coverage and integration. Nucleic Acids Res 2013, 41:D808-D815. [Database issue].
    • (2013) Nucleic Acids Res , vol.41 , pp. D808-D815
    • Franceschini, A.1    Szklarczyk, D.2    Frankild, S.3    Kuhn, M.4    Simonovic, M.5    Roth, A.6
  • 38
    • 0026642952 scopus 로고
    • Use of a fluorescent redox probe for direct visualization of actively respiring bacteria
    • Rodriguez G.G., Phipps D., Ishiguro K., Ridgway H.F. Use of a fluorescent redox probe for direct visualization of actively respiring bacteria. Appl Environ Microbiol 1992, 58(6):1801-1808.
    • (1992) Appl Environ Microbiol , vol.58 , Issue.6 , pp. 1801-1808
    • Rodriguez, G.G.1    Phipps, D.2    Ishiguro, K.3    Ridgway, H.F.4
  • 39
    • 0031890703 scopus 로고    scopus 로고
    • Lacticin 3147, a broad-spectrum bacteriocin which selectively dissipates the membrane potential
    • McAuliffe O., Ryan M.P., Ross R.P., Hill C., Breeuwer P., Abee T. Lacticin 3147, a broad-spectrum bacteriocin which selectively dissipates the membrane potential. Appl Environ Microbiol 1998, 64(2):439-445.
    • (1998) Appl Environ Microbiol , vol.64 , Issue.2 , pp. 439-445
    • McAuliffe, O.1    Ryan, M.P.2    Ross, R.P.3    Hill, C.4    Breeuwer, P.5    Abee, T.6
  • 40
    • 84880834788 scopus 로고    scopus 로고
    • A moonlighting enzyme links Escherichia coli cell size with central metabolism
    • Hill N.S., Buske P.J., Shi Y., Levin P.A. A moonlighting enzyme links Escherichia coli cell size with central metabolism. PLoS Genet 2013, 9(7):e1003663.
    • (2013) PLoS Genet , vol.9 , Issue.7 , pp. e1003663
    • Hill, N.S.1    Buske, P.J.2    Shi, Y.3    Levin, P.A.4
  • 41
    • 70350194739 scopus 로고    scopus 로고
    • Metabolism, cell growth and the bacterial cell cycle
    • Wang J.D., Levin P.A. Metabolism, cell growth and the bacterial cell cycle. Nat Rev Microbiol 2009, 7(11):822-827.
    • (2009) Nat Rev Microbiol , vol.7 , Issue.11 , pp. 822-827
    • Wang, J.D.1    Levin, P.A.2
  • 42
    • 0032924410 scopus 로고    scopus 로고
    • Metabolic alarms and cell division in Escherichia coli
    • Joseleau-Petit D., Vinella D., D'Ari R. Metabolic alarms and cell division in Escherichia coli. J Bacteriol 1999, 181(1):9-14.
    • (1999) J Bacteriol , vol.181 , Issue.1 , pp. 9-14
    • Joseleau-Petit, D.1    Vinella, D.2    D'Ari, R.3
  • 43
    • 0029989167 scopus 로고    scopus 로고
    • Regulators of aerobic and anaerobic respiration in Bacillus subtilis
    • Sun G., Sharkova E., Chesnut R., Birkey S., Duggan M.F., Sorokin A., et al. Regulators of aerobic and anaerobic respiration in Bacillus subtilis. J Bacteriol 1996, 178(5):1374-1385.
    • (1996) J Bacteriol , vol.178 , Issue.5 , pp. 1374-1385
    • Sun, G.1    Sharkova, E.2    Chesnut, R.3    Birkey, S.4    Duggan, M.F.5    Sorokin, A.6
  • 44
    • 0033972849 scopus 로고    scopus 로고
    • Changes in protein synthesis during the adaptation of Bacillus subtilis to anaerobic growth conditions
    • Marino M., Hoffmann T., Schmid R., Möbitz H., Jahn D. Changes in protein synthesis during the adaptation of Bacillus subtilis to anaerobic growth conditions. Microbiology 2000, 146(Pt 1):97-105.
    • (2000) Microbiology , vol.146 , Issue.Pt 1 , pp. 97-105
    • Marino, M.1    Hoffmann, T.2    Schmid, R.3    Möbitz, H.4    Jahn, D.5
  • 45
    • 0000343873 scopus 로고    scopus 로고
    • Fermentative metabolism of Bacillus subtilis: physiology and regulation of gene expression
    • Cruz Ramos H., Hoffmann T., Marino M., Nedjari H., Presecan-Siedel E., Dreesen O., et al. Fermentative metabolism of Bacillus subtilis: physiology and regulation of gene expression. J Bacteriol 2000, 182(11):3072-3080.
    • (2000) J Bacteriol , vol.182 , Issue.11 , pp. 3072-3080
    • Cruz Ramos, H.1    Hoffmann, T.2    Marino, M.3    Nedjari, H.4    Presecan-Siedel, E.5    Dreesen, O.6
  • 48
    • 77955449195 scopus 로고    scopus 로고
    • Membrane potential is important for bacterial cell division
    • Strahl H., Hamoen L.W. Membrane potential is important for bacterial cell division. Proc Natl Acad Sci U S A 2010, 107(27):12281-12286.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.27 , pp. 12281-12286
    • Strahl, H.1    Hamoen, L.W.2
  • 50
    • 0033913150 scopus 로고    scopus 로고
    • Motility and chemotaxis of filamentous cells of Escherichia coli
    • Maki N., Gestwicki J.E., Lake E.M., Kiessling L.L., Adler J. Motility and chemotaxis of filamentous cells of Escherichia coli. J Bacteriol 2000, 182:4337-4342.
    • (2000) J Bacteriol , vol.182 , pp. 4337-4342
    • Maki, N.1    Gestwicki, J.E.2    Lake, E.M.3    Kiessling, L.L.4    Adler, J.5
  • 51
    • 69949095254 scopus 로고    scopus 로고
    • Role of the sigmaD-dependent autolysins in Bacillus subtilis population heterogeneity
    • Chen R., Guttenplan S.B., Blair K.M., Kearns D.B. Role of the sigmaD-dependent autolysins in Bacillus subtilis population heterogeneity. J Bacteriol 2009, 191:5775-5784.
    • (2009) J Bacteriol , vol.191 , pp. 5775-5784
    • Chen, R.1    Guttenplan, S.B.2    Blair, K.M.3    Kearns, D.B.4
  • 53
    • 84872239404 scopus 로고    scopus 로고
    • Immediate and heterogeneous response of the LiaFSR two-component system of Bacillus subtilis to the peptide antibiotic bacitracin
    • Kesel S., Mader A., Höfler C., Mascher T., Leisner M. Immediate and heterogeneous response of the LiaFSR two-component system of Bacillus subtilis to the peptide antibiotic bacitracin. PLoS One 2013, 8:e53457.
    • (2013) PLoS One , vol.8 , pp. e53457
    • Kesel, S.1    Mader, A.2    Höfler, C.3    Mascher, T.4    Leisner, M.5
  • 54
    • 84868028806 scopus 로고    scopus 로고
    • Proteomic response of Bacillus subtilis to lantibiotics reflects differences in interaction with the cytoplasmic membrane
    • Wenzel M., Kohl B., Münch D., Raatschen N., Albada H.B., Hamoen L., et al. Proteomic response of Bacillus subtilis to lantibiotics reflects differences in interaction with the cytoplasmic membrane. Antimicrob Agents Chemother 2012, 56:5749-5757.
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 5749-5757
    • Wenzel, M.1    Kohl, B.2    Münch, D.3    Raatschen, N.4    Albada, H.B.5    Hamoen, L.6
  • 55
    • 22744447508 scopus 로고    scopus 로고
    • Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli
    • Kerner M.J., Naylor D.J., Ishihama Y., Maier T., Chang H.C., Stines A.P., et al. Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. Cell 2005, 122(2):209-220.
    • (2005) Cell , vol.122 , Issue.2 , pp. 209-220
    • Kerner, M.J.1    Naylor, D.J.2    Ishihama, Y.3    Maier, T.4    Chang, H.C.5    Stines, A.P.6
  • 56
    • 4444343627 scopus 로고    scopus 로고
    • FtsZ-dependent localization of GroEL protein at possible division sites
    • Ogino H., Wachi M., Ishii A., Iwai N., Nishida T., Yamada S., et al. FtsZ-dependent localization of GroEL protein at possible division sites. Genes Cells 2004, 9:765-771.
    • (2004) Genes Cells , vol.9 , pp. 765-771
    • Ogino, H.1    Wachi, M.2    Ishii, A.3    Iwai, N.4    Nishida, T.5    Yamada, S.6
  • 57
    • 0025003789 scopus 로고
    • Trigger factor depletion or overproduction causes defective cell division but does not block protein export
    • Guthrie B., Wickner W. Trigger factor depletion or overproduction causes defective cell division but does not block protein export. J Bacteriol 1990, 172(10):5555-5562.
    • (1990) J Bacteriol , vol.172 , Issue.10 , pp. 5555-5562
    • Guthrie, B.1    Wickner, W.2
  • 58
    • 27444437940 scopus 로고    scopus 로고
    • A deficiency in S-adenosylmethionine synthetase interrupts assembly of the septal ring in Escherichia coli K-12
    • Wang S., Arends S.J., Weiss D.S., Newman E.B. A deficiency in S-adenosylmethionine synthetase interrupts assembly of the septal ring in Escherichia coli K-12. Mol Microbiol 2005, 58:791-799.
    • (2005) Mol Microbiol , vol.58 , pp. 791-799
    • Wang, S.1    Arends, S.J.2    Weiss, D.S.3    Newman, E.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.