메뉴 건너뛰기




Volumn 171, Issue 6, 2017, Pages 1354-1367.e20

Membrane Microdomain Disassembly Inhibits MRSA Antibiotic Resistance

Author keywords

[No Author keywords available]

Indexed keywords

OXACILLIN; PENICILLIN DERIVATIVE; ZARAGOZIC ACID A; BACTERIAL PROTEIN; CAROTENOID; FLOTILLINS; MECA PROTEIN, STAPHYLOCOCCUS AUREUS; MEMBRANE PROTEIN; PENICILLIN BINDING PROTEIN; STAPHYLOXANTHIN; XANTHOPHYLL;

EID: 85035041754     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2017.10.012     Document Type: Article
Times cited : (170)

References (67)
  • 1
    • 8744309111 scopus 로고    scopus 로고
    • New vector for efficient allelic replacement in naturally nontransformable, low-GC-content, gram-positive bacteria
    • Arnaud, M., Chastanet, A., Débarbouillé M., New vector for efficient allelic replacement in naturally nontransformable, low-GC-content, gram-positive bacteria. Appl. Environ. Microbiol. 70 (2004), 6887–6891.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 6887-6891
    • Arnaud, M.1    Chastanet, A.2    Débarbouillé, M.3
  • 2
    • 0010455189 scopus 로고
    • Ampicillin inactivation and sensitivity of coliform bacilli
    • Ayliffe, G.A., Ampicillin inactivation and sensitivity of coliform bacilli. J. Gen. Microbiol. 30 (1963), 339–348.
    • (1963) J. Gen. Microbiol. , vol.30 , pp. 339-348
    • Ayliffe, G.A.1
  • 3
    • 84879030282 scopus 로고    scopus 로고
    • Flotillins functionally organize the bacterial membrane
    • Bach, J.N., Bramkamp, M., Flotillins functionally organize the bacterial membrane. Mol. Microbiol. 88 (2013), 1205–1217.
    • (2013) Mol. Microbiol. , vol.88 , pp. 1205-1217
    • Bach, J.N.1    Bramkamp, M.2
  • 4
    • 84922196301 scopus 로고    scopus 로고
    • Dissecting the molecular properties of prokaryotic flotillins
    • Bach, J.N., Bramkamp, M., Dissecting the molecular properties of prokaryotic flotillins. PLoS ONE, 10, 2015, e0116750.
    • (2015) PLoS ONE , vol.10 , pp. e0116750
    • Bach, J.N.1    Bramkamp, M.2
  • 6
    • 0031010267 scopus 로고    scopus 로고
    • Flotillin and epidermal surface antigen define a new family of caveolae-associated integral membrane proteins
    • Bickel, P.E., Scherer, P.E., Schnitzer, J.E., Oh, P., Lisanti, M.P., Lodish, H.F., Flotillin and epidermal surface antigen define a new family of caveolae-associated integral membrane proteins. J. Biol. Chem. 272 (1997), 13793–13802.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13793-13802
    • Bickel, P.E.1    Scherer, P.E.2    Schnitzer, J.E.3    Oh, P.4    Lisanti, M.P.5    Lodish, H.F.6
  • 7
    • 84925267126 scopus 로고    scopus 로고
    • Exploring the existence of lipid rafts in bacteria
    • Bramkamp, M., Lopez, D., Exploring the existence of lipid rafts in bacteria. Microbiol. Mol. Biol. Rev. 79 (2015), 81–100.
    • (2015) Microbiol. Mol. Biol. Rev. , vol.79 , pp. 81-100
    • Bramkamp, M.1    Lopez, D.2
  • 8
    • 43549086881 scopus 로고    scopus 로고
    • Isolation and use of rafts. In Curr Protoc Immunol
    • John Wiley & Sons
    • Brown, D.A., Isolation and use of rafts. In Curr Protoc Immunol. 2002, John Wiley & Sons.
    • (2002)
    • Brown, D.A.1
  • 9
    • 79956342165 scopus 로고    scopus 로고
    • Loss of the SPHF homologue Slr1768 leads to a catastrophic failure in the maintenance of thylakoid membranes in Synechocystis sp. PCC 6803
    • Bryan, S.J., Burroughs, N.J., Evered, C., Sacharz, J., Nenninger, A., Mullineaux, C.W., Spence, E.M., Loss of the SPHF homologue Slr1768 leads to a catastrophic failure in the maintenance of thylakoid membranes in Synechocystis sp. PCC 6803. PLoS ONE, 6, 2011, e19625.
    • (2011) PLoS ONE , vol.6 , pp. e19625
    • Bryan, S.J.1    Burroughs, N.J.2    Evered, C.3    Sacharz, J.4    Nenninger, A.5    Mullineaux, C.W.6    Spence, E.M.7
  • 11
    • 67650708496 scopus 로고    scopus 로고
    • Characterization and subcellular localization of a bacterial flotillin homologue
    • Donovan, C., Bramkamp, M., Characterization and subcellular localization of a bacterial flotillin homologue. Microbiology 155 (2009), 1786–1799.
    • (2009) Microbiology , vol.155 , pp. 1786-1799
    • Donovan, C.1    Bramkamp, M.2
  • 13
    • 84911490656 scopus 로고    scopus 로고
    • Structural and functional analysis of Bacillus subtilis YisP reveals a role of its product in biofilm production
    • Feng, X., Hu, Y., Zheng, Y., Zhu, W., Li, K., Huang, C.H., Ko, T.P., Ren, F., Chan, H.C., Nega, M., et al. Structural and functional analysis of Bacillus subtilis YisP reveals a role of its product in biofilm production. Chem. Biol. 21 (2014), 1557–1563.
    • (2014) Chem. Biol. , vol.21 , pp. 1557-1563
    • Feng, X.1    Hu, Y.2    Zheng, Y.3    Zhu, W.4    Li, K.5    Huang, C.H.6    Ko, T.P.7    Ren, F.8    Chan, H.C.9    Nega, M.10
  • 14
    • 84928320829 scopus 로고    scopus 로고
    • Penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus
    • Fishovitz, J., Hermoso, J.A., Chang, M., Mobashery, S., Penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus. IUBMB Life 66 (2014), 572–577.
    • (2014) IUBMB Life , vol.66 , pp. 572-577
    • Fishovitz, J.1    Hermoso, J.A.2    Chang, M.3    Mobashery, S.4
  • 16
    • 84934931337 scopus 로고    scopus 로고
    • Chemical probes reveal an extraseptal mode of cross-linking in Staphylococcus aureus
    • Gautam, S., Kim, T., Spiegel, D.A., Chemical probes reveal an extraseptal mode of cross-linking in Staphylococcus aureus. J. Am. Chem. Soc. 137 (2015), 7441–7447.
    • (2015) J. Am. Chem. Soc. , vol.137 , pp. 7441-7447
    • Gautam, S.1    Kim, T.2    Spiegel, D.A.3
  • 17
    • 84871442933 scopus 로고    scopus 로고
    • Effects of statins and cholesterol on memory functions in mice
    • Ghodke, R.M., Tour, N., Devi, K., Effects of statins and cholesterol on memory functions in mice. Metab. Brain Dis. 27 (2012), 443–451.
    • (2012) Metab. Brain Dis. , vol.27 , pp. 443-451
    • Ghodke, R.M.1    Tour, N.2    Devi, K.3
  • 18
    • 79955770162 scopus 로고    scopus 로고
    • Scaffold proteins: hubs for controlling the flow of cellular information
    • Good, M.C., Zalatan, J.G., Lim, W.A., Scaffold proteins: hubs for controlling the flow of cellular information. Science 332 (2011), 680–686.
    • (2011) Science , vol.332 , pp. 680-686
    • Good, M.C.1    Zalatan, J.G.2    Lim, W.A.3
  • 19
    • 0004028486 scopus 로고
    • Stains and cytochemical methods
    • Plenun Press New York, London
    • Hayat, M.A., Stains and cytochemical methods. 1993, Plenun Press, New York, London.
    • (1993)
    • Hayat, M.A.1
  • 20
    • 84897896914 scopus 로고    scopus 로고
    • Impact of Campylobacter jejuni cj0268c knockout mutation on intestinal colonization, translocation, and induction of immunopathology in gnotobiotic IL-10 deficient mice
    • Heimesaat, M.M., Lugert, R., Fischer, A., Alutis, M., Kühl, A.A., Zautner, A.E., Tareen, A.M., Göbel, U.B., Bereswill, S., Impact of Campylobacter jejuni cj0268c knockout mutation on intestinal colonization, translocation, and induction of immunopathology in gnotobiotic IL-10 deficient mice. PLoS ONE, 9, 2014, e90148.
    • (2014) PLoS ONE , vol.9 , pp. e90148
    • Heimesaat, M.M.1    Lugert, R.2    Fischer, A.3    Alutis, M.4    Kühl, A.A.5    Zautner, A.E.6    Tareen, A.M.7    Göbel, U.B.8    Bereswill, S.9
  • 21
    • 84937252531 scopus 로고    scopus 로고
    • Presynaptic architecture of the larval zebrafish neuromuscular junction
    • Helmprobst, F., Frank, M., Stigloher, C., Presynaptic architecture of the larval zebrafish neuromuscular junction. J. Comp. Neurol. 523 (2015), 1984–1997.
    • (2015) J. Comp. Neurol. , vol.523 , pp. 1984-1997
    • Helmprobst, F.1    Frank, M.2    Stigloher, C.3
  • 22
    • 84896870282 scopus 로고    scopus 로고
    • Bioluminescence and 19F magnetic resonance imaging visualize the efficacy of lysostaphin alone and in combination with oxacillin against Staphylococcus aureus in murine thigh and catheter-associated infection models
    • Hertlein, T., Sturm, V., Lorenz, U., Sumathy, K., Jakob, P., Ohlsen, K., Bioluminescence and 19F magnetic resonance imaging visualize the efficacy of lysostaphin alone and in combination with oxacillin against Staphylococcus aureus in murine thigh and catheter-associated infection models. Antimicrob. Agents Chemother. 58 (2014), 1630–1638.
    • (2014) Antimicrob. Agents Chemother. , vol.58 , pp. 1630-1638
    • Hertlein, T.1    Sturm, V.2    Lorenz, U.3    Sumathy, K.4    Jakob, P.5    Ohlsen, K.6
  • 23
    • 84861889493 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis in bacterial pathogens
    • Heuston, S., Begley, M., Gahan, C.G., Hill, C., Isoprenoid biosynthesis in bacterial pathogens. Microbiology 158 (2012), 1389–1401.
    • (2012) Microbiology , vol.158 , pp. 1389-1401
    • Heuston, S.1    Begley, M.2    Gahan, C.G.3    Hill, C.4
  • 24
    • 84862570136 scopus 로고    scopus 로고
    • The posttranslocational chaperone lipoprotein PrsA is involved in both glycopeptide and oxacillin resistance in Staphylococcus aureus
    • Jousselin, A., Renzoni, A., Andrey, D.O., Monod, A., Lew, D.P., Kelley, W.L., The posttranslocational chaperone lipoprotein PrsA is involved in both glycopeptide and oxacillin resistance in Staphylococcus aureus. Antimicrob. Agents Chemother. 56 (2012), 3629–3640.
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 3629-3640
    • Jousselin, A.1    Renzoni, A.2    Andrey, D.O.3    Monod, A.4    Lew, D.P.5    Kelley, W.L.6
  • 25
    • 84960158574 scopus 로고    scopus 로고
    • The Staphylococcus aureus Chaperone PrsA Is a New Auxiliary Factor of Oxacillin Resistance Affecting Penicillin-Binding Protein 2A
    • Jousselin, A., Manzano, C., Biette, A., Reed, P., Pinho, M.G., Rosato, A.E., Kelley, W.L., Renzoni, A., The Staphylococcus aureus Chaperone PrsA Is a New Auxiliary Factor of Oxacillin Resistance Affecting Penicillin-Binding Protein 2A. Antimicrob. Agents Chemother. 60 (2015), 1656–1666.
    • (2015) Antimicrob. Agents Chemother. , vol.60 , pp. 1656-1666
    • Jousselin, A.1    Manzano, C.2    Biette, A.3    Reed, P.4    Pinho, M.G.5    Rosato, A.E.6    Kelley, W.L.7    Renzoni, A.8
  • 26
    • 85021331199 scopus 로고    scopus 로고
    • Attenuating Staphylococcus aureus Virulence by Targeting Flotillin Protein Scaffold Activity
    • Koch, G., Wermser, C., Acosta, I.C., Kricks, L., Stengel, S.T., Yepes, A., Lopez, D., Attenuating Staphylococcus aureus Virulence by Targeting Flotillin Protein Scaffold Activity. Cell Chem Biol 24 (2017), 845–857 e6.
    • (2017) Cell Chem Biol , vol.24 , pp. 845-857 e6
    • Koch, G.1    Wermser, C.2    Acosta, I.C.3    Kricks, L.4    Stengel, S.T.5    Yepes, A.6    Lopez, D.7
  • 27
    • 84884490244 scopus 로고    scopus 로고
    • Plasma membrane organization and function: moving past lipid rafts
    • Kraft, M.L., Plasma membrane organization and function: moving past lipid rafts. Mol. Biol. Cell 24 (2013), 2765–2768.
    • (2013) Mol. Biol. Cell , vol.24 , pp. 2765-2768
    • Kraft, M.L.1
  • 29
    • 0031659829 scopus 로고    scopus 로고
    • Deletion of the alternative sigma factor sigmaB in Staphylococcus aureus reveals its function as a global regulator of virulence genes
    • Kullik, I., Giachino, P., Fuchs, T., Deletion of the alternative sigma factor sigmaB in Staphylococcus aureus reveals its function as a global regulator of virulence genes. J. Bacteriol. 180 (1998), 4814–4820.
    • (1998) J. Bacteriol. , vol.180 , pp. 4814-4820
    • Kullik, I.1    Giachino, P.2    Fuchs, T.3
  • 30
    • 84878482841 scopus 로고    scopus 로고
    • Proving lipid rafts exist: membrane domains in the prokaryote Borrelia burgdorferi have the same properties as eukaryotic lipid rafts
    • LaRocca, T.J., Pathak, P., Chiantia, S., Toledo, A., Silvius, J.R., Benach, J.L., London, E., Proving lipid rafts exist: membrane domains in the prokaryote Borrelia burgdorferi have the same properties as eukaryotic lipid rafts. PLoS Pathog., 9, 2013, e1003353.
    • (2013) PLoS Pathog. , vol.9 , pp. e1003353
    • LaRocca, T.J.1    Pathak, P.2    Chiantia, S.3    Toledo, A.4    Silvius, J.R.5    Benach, J.L.6    London, E.7
  • 31
    • 14244254169 scopus 로고    scopus 로고
    • Role of penicillin-binding protein 2 (PBP2) in the antibiotic susceptibility and cell wall cross-linking of Staphylococcus aureus: evidence for the cooperative functioning of PBP2, PBP4, and PBP2A
    • Łeski, T.A., Tomasz, A., Role of penicillin-binding protein 2 (PBP2) in the antibiotic susceptibility and cell wall cross-linking of Staphylococcus aureus: evidence for the cooperative functioning of PBP2, PBP4, and PBP2A. J. Bacteriol. 187 (2005), 1815–1824.
    • (2005) J. Bacteriol. , vol.187 , pp. 1815-1824
    • Łeski, T.A.1    Tomasz, A.2
  • 32
    • 0035887840 scopus 로고    scopus 로고
    • The effect of statins on mortality in patients with bacteremia
    • Liappis, A.P., Kan, V.L., Rochester, C.G., Simon, G.L., The effect of statins on mortality in patients with bacteremia. Clin. Infect. Dis. 33 (2001), 1352–1357.
    • (2001) Clin. Infect. Dis. , vol.33 , pp. 1352-1357
    • Liappis, A.P.1    Kan, V.L.2    Rochester, C.G.3    Simon, G.L.4
  • 34
    • 77956292192 scopus 로고    scopus 로고
    • Functional microdomains in bacterial membranes
    • López, D., Kolter, R., Functional microdomains in bacterial membranes. Genes Dev. 24 (2010), 1893–1902.
    • (2010) Genes Dev. , vol.24 , pp. 1893-1902
    • López, D.1    Kolter, R.2
  • 35
    • 84922724046 scopus 로고    scopus 로고
    • In vivo attenuation and genetic evolution of a ST247-SCCmecI MRSA clone after 13 years of pathogenic bronchopulmonary colonization in a patient with cystic fibrosis: implications of the innate immune response
    • López-Collazo, E., Jurado, T., de Dios Caballero, J., Pérez-Vázquez, M., Vindel, A., Hernández-Jiménez, E., Tamames, J., Cubillos-Zapata, C., Manrique, M., Tobes, R., et al. In vivo attenuation and genetic evolution of a ST247-SCCmecI MRSA clone after 13 years of pathogenic bronchopulmonary colonization in a patient with cystic fibrosis: implications of the innate immune response. Mucosal Immunol. 8 (2015), 362–371.
    • (2015) Mucosal Immunol. , vol.8 , pp. 362-371
    • López-Collazo, E.1    Jurado, T.2    de Dios Caballero, J.3    Pérez-Vázquez, M.4    Vindel, A.5    Hernández-Jiménez, E.6    Tamames, J.7    Cubillos-Zapata, C.8    Manrique, M.9    Tobes, R.10
  • 37
    • 84949534046 scopus 로고    scopus 로고
    • Structural determinants of protein partitioning into ordered membrane domains and lipid rafts
    • Lorent, J.H., Levental, I., Structural determinants of protein partitioning into ordered membrane domains and lipid rafts. Chem. Phys. Lipids 192 (2015), 23–32.
    • (2015) Chem. Phys. Lipids , vol.192 , pp. 23-32
    • Lorent, J.H.1    Levental, I.2
  • 38
    • 84979010855 scopus 로고    scopus 로고
    • Filling the gap: adding super-resolution to array tomography for correlated ultrastructural and molecular identification of electrical synapses at the C. elegans connectome
    • Markert, S.M., Britz, S., Proppert, S., Lang, M., Witvliet, D., Mulcahy, B., Sauer, M., Zhen, M., Bessereau, J.L., Stigloher, C., Filling the gap: adding super-resolution to array tomography for correlated ultrastructural and molecular identification of electrical synapses at the C. elegans connectome. Neurophotonics, 3, 2016, 041802.
    • (2016) Neurophotonics , vol.3 , pp. 041802
    • Markert, S.M.1    Britz, S.2    Proppert, S.3    Lang, M.4    Witvliet, D.5    Mulcahy, B.6    Sauer, M.7    Zhen, M.8    Bessereau, J.L.9    Stigloher, C.10
  • 39
    • 0019852937 scopus 로고
    • Proposed pathway of triterpenoid carotenoid biosynthesis in Staphylococcus aureus: evidence from a study of mutants
    • Marshall, J.H., Wilmoth, G.J., Proposed pathway of triterpenoid carotenoid biosynthesis in Staphylococcus aureus: evidence from a study of mutants. J. Bacteriol. 147 (1981), 914–919.
    • (1981) J. Bacteriol. , vol.147 , pp. 914-919
    • Marshall, J.H.1    Wilmoth, G.J.2
  • 40
    • 84929660640 scopus 로고    scopus 로고
    • FtsZ Polymers Tethered to the Membrane by ZipA Are Susceptible to Spatial Regulation by Min Waves
    • Martos, A., Raso, A., Jiménez, M., Petrášek, Z., Rivas, G., Schwille, P., FtsZ Polymers Tethered to the Membrane by ZipA Are Susceptible to Spatial Regulation by Min Waves. Biophys. J. 108 (2015), 2371–2383.
    • (2015) Biophys. J. , vol.108 , pp. 2371-2383
    • Martos, A.1    Raso, A.2    Jiménez, M.3    Petrášek, Z.4    Rivas, G.5    Schwille, P.6
  • 41
    • 0242677610 scopus 로고    scopus 로고
    • Pulsed-field gel electrophoresis typing of oxacillin-resistant Staphylococcus aureus isolates from the United States: establishing a national database
    • McDougal, L.K., Steward, C.D., Killgore, G.E., Chaitram, J.M., McAllister, S.K., Tenover, F.C., Pulsed-field gel electrophoresis typing of oxacillin-resistant Staphylococcus aureus isolates from the United States: establishing a national database. J. Clin. Microbiol. 41 (2003), 5113–5120.
    • (2003) J. Clin. Microbiol. , vol.41 , pp. 5113-5120
    • McDougal, L.K.1    Steward, C.D.2    Killgore, G.E.3    Chaitram, J.M.4    McAllister, S.K.5    Tenover, F.C.6
  • 42
    • 85036523380 scopus 로고
    • Bacterial Ribosomes and Protein Synthesis
    • McQuillen, K., Bacterial Ribosomes and Protein Synthesis. J. Gen. Microbiol. 29 (1962), 53–57.
    • (1962) J. Gen. Microbiol. , vol.29 , pp. 53-57
    • McQuillen, K.1
  • 46
    • 0002443434 scopus 로고
    • A small particulate component of the cytoplasm
    • Palade, G.E., A small particulate component of the cytoplasm. J. Biophys. Biochem. Cytol. 1 (1955), 59–68.
    • (1955) J. Biophys. Biochem. Cytol. , vol.1 , pp. 59-68
    • Palade, G.E.1
  • 47
    • 84894226758 scopus 로고    scopus 로고
    • Statin therapy reduces the mycobacterium tuberculosis burden in human macrophages and in mice by enhancing autophagy and phagosome maturation
    • Parihar, S.P., Guler, R., Khutlang, R., Lang, D.M., Hurdayal, R., Mhlanga, M.M., Suzuki, H., Marais, A.D., Brombacher, F., Statin therapy reduces the mycobacterium tuberculosis burden in human macrophages and in mice by enhancing autophagy and phagosome maturation. J. Infect. Dis. 209 (2014), 754–763.
    • (2014) J. Infect. Dis. , vol.209 , pp. 754-763
    • Parihar, S.P.1    Guler, R.2    Khutlang, R.3    Lang, D.M.4    Hurdayal, R.5    Mhlanga, M.M.6    Suzuki, H.7    Marais, A.D.8    Brombacher, F.9
  • 48
    • 84930722588 scopus 로고    scopus 로고
    • Mechanisms of Methicillin Resistance in Staphylococcus aureus
    • Peacock, S.J., Paterson, G.K., Mechanisms of Methicillin Resistance in Staphylococcus aureus. Annu. Rev. Biochem. 84 (2015), 577–601.
    • (2015) Annu. Rev. Biochem. , vol.84 , pp. 577-601
    • Peacock, S.J.1    Paterson, G.K.2
  • 49
    • 25444443095 scopus 로고    scopus 로고
    • Structure and biosynthesis of staphyloxanthin from Staphylococcus aureus
    • Pelz, A., Wieland, K.P., Putzbach, K., Hentschel, P., Albert, K., Götz, F., Structure and biosynthesis of staphyloxanthin from Staphylococcus aureus. J. Biol. Chem. 280 (2005), 32493–32498.
    • (2005) J. Biol. Chem. , vol.280 , pp. 32493-32498
    • Pelz, A.1    Wieland, K.P.2    Putzbach, K.3    Hentschel, P.4    Albert, K.5    Götz, F.6
  • 50
    • 0035845487 scopus 로고    scopus 로고
    • An acquired and a native penicillin-binding protein cooperate in building the cell wall of drug-resistant staphylococci
    • Pinho, M.G., de Lencastre, H., Tomasz, A., An acquired and a native penicillin-binding protein cooperate in building the cell wall of drug-resistant staphylococci. Proc. Natl. Acad. Sci. USA 98 (2001), 10886–10891.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10886-10891
    • Pinho, M.G.1    de Lencastre, H.2    Tomasz, A.3
  • 51
    • 0034748911 scopus 로고    scopus 로고
    • Complementation of the essential peptidoglycan transpeptidase function of penicillin-binding protein 2 (PBP2) by the drug resistance protein PBP2A in Staphylococcus aureus
    • Pinho, M.G., Filipe, S.R., de Lencastre, H., Tomasz, A., Complementation of the essential peptidoglycan transpeptidase function of penicillin-binding protein 2 (PBP2) by the drug resistance protein PBP2A in Staphylococcus aureus. J. Bacteriol. 183 (2001), 6525–6531.
    • (2001) J. Bacteriol. , vol.183 , pp. 6525-6531
    • Pinho, M.G.1    Filipe, S.R.2    de Lencastre, H.3    Tomasz, A.4
  • 52
    • 0025118707 scopus 로고
    • Organization of glycosphingolipids in phosphatidylcholine bilayers: use of antibody molecules and Fab fragments as morphologic markers
    • Rock, P., Allietta, M., Young, W.W. Jr., Thompson, T.E., Tillack, T.W., Organization of glycosphingolipids in phosphatidylcholine bilayers: use of antibody molecules and Fab fragments as morphologic markers. Biochemistry 29 (1990), 8484–8490.
    • (1990) Biochemistry , vol.29 , pp. 8484-8490
    • Rock, P.1    Allietta, M.2    Young, W.W.3    Thompson, T.E.4    Tillack, T.W.5
  • 53
    • 84855747348 scopus 로고    scopus 로고
    • Streptomycin-induced expression in Bacillus subtilis of YtnP, a lactonase-homologous protein that inhibits development and streptomycin production in Streptomyces griseus
    • Schneider, J., Yepes, A., Garcia-Betancur, J.C., Westedt, I., Mielich, B., López, D., Streptomycin-induced expression in Bacillus subtilis of YtnP, a lactonase-homologous protein that inhibits development and streptomycin production in Streptomyces griseus. Appl. Environ. Microbiol. 78 (2012), 599–603.
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 599-603
    • Schneider, J.1    Yepes, A.2    Garcia-Betancur, J.C.3    Westedt, I.4    Mielich, B.5    López, D.6
  • 56
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., Ikonen, E., Functional rafts in cell membranes. Nature 387 (1997), 569–572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 57
  • 58
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer, S.J., Nicolson, G.L., The fluid mosaic model of the structure of cell membranes. Science 175 (1972), 720–731.
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 61
    • 0021979912 scopus 로고
    • Organization of glycosphingolipids in bilayers and plasma membranes of mammalian cells
    • Thompson, T.E., Tillack, T.W., Organization of glycosphingolipids in bilayers and plasma membranes of mammalian cells. Annu. Rev. Biophys. Biophys. Chem. 14 (1985), 361–386.
    • (1985) Annu. Rev. Biophys. Biophys. Chem. , vol.14 , pp. 361-386
    • Thompson, T.E.1    Tillack, T.W.2
  • 62
    • 0019310655 scopus 로고
    • Interactions of uranyl ions with lipid bilayer membranes
    • Ting-Beall, H.P., Interactions of uranyl ions with lipid bilayer membranes. J. Microsc. 118 (1980), 221–227.
    • (1980) J. Microsc. , vol.118 , pp. 221-227
    • Ting-Beall, H.P.1
  • 63
    • 84899937720 scopus 로고    scopus 로고
    • Effect of statin therapy on mortality from infection and sepsis: a meta-analysis of randomized and observational studies
    • Wan, Y.D., Sun, T.W., Kan, Q.C., Guan, F.X., Zhang, S.G., Effect of statin therapy on mortality from infection and sepsis: a meta-analysis of randomized and observational studies. Crit. Care, 18, 2014, R71.
    • (2014) Crit. Care , vol.18 , pp. R71
    • Wan, Y.D.1    Sun, T.W.2    Kan, Q.C.3    Guan, F.X.4    Zhang, S.G.5
  • 64
    • 0027971410 scopus 로고
    • Genetic and biochemical analyses of the biosynthesis of the yellow carotenoid 4,4′-diaponeurosporene of Staphylococcus aureus
    • Wieland, B., Feil, C., Gloria-Maercker, E., Thumm, G., Lechner, M., Bravo, J.M., Poralla, K., Götz, F., Genetic and biochemical analyses of the biosynthesis of the yellow carotenoid 4,4′-diaponeurosporene of Staphylococcus aureus. J. Bacteriol. 176 (1994), 7719–7726.
    • (1994) J. Bacteriol. , vol.176 , pp. 7719-7726
    • Wieland, B.1    Feil, C.2    Gloria-Maercker, E.3    Thumm, G.4    Lechner, M.5    Bravo, J.M.6    Poralla, K.7    Götz, F.8
  • 66
    • 84902158114 scopus 로고    scopus 로고
    • Reconstruction of mreB expression in Staphylococcus aureus via a collection of new integrative plasmids
    • Yepes, A., Koch, G., Waldvogel, A., Garcia-Betancur, J.C., Lopez, D., Reconstruction of mreB expression in Staphylococcus aureus via a collection of new integrative plasmids. Appl. Environ. Microbiol. 80 (2014), 3868–3878.
    • (2014) Appl. Environ. Microbiol. , vol.80 , pp. 3868-3878
    • Yepes, A.1    Koch, G.2    Waldvogel, A.3    Garcia-Betancur, J.C.4    Lopez, D.5
  • 67
    • 39149104344 scopus 로고    scopus 로고
    • Penicillin-binding proteins and beta-lactam resistance
    • Zapun, A., Contreras-Martel, C., Vernet, T., Penicillin-binding proteins and beta-lactam resistance. FEMS Microbiol. Rev. 32 (2008), 361–385.
    • (2008) FEMS Microbiol. Rev. , vol.32 , pp. 361-385
    • Zapun, A.1    Contreras-Martel, C.2    Vernet, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.