메뉴 건너뛰기




Volumn 79, Issue 1, 2015, Pages 81-100

Exploring the existence of lipid rafts in bacteria

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CARDIOLIPIN; CHOLESTEROL; MEVALONIC ACID; FLOTILLINS; MEMBRANE LIPID; MEMBRANE PROTEIN;

EID: 84925267126     PISSN: 10922172     EISSN: 10985557     Source Type: Journal    
DOI: 10.1128/MMBR.00036-14     Document Type: Review
Times cited : (157)

References (189)
  • 1
    • 79952672026 scopus 로고    scopus 로고
    • Signaling from the living plasma membrane
    • Grecco HE, Schmick M, Bastiaens PI. 2011. Signaling from the living plasma membrane. Cell 144: 897-909. http://dx.doi.org/10.1016/j.cell.2011.01.029.
    • (2011) Cell , vol.144 , pp. 897-909
    • Grecco, H.E.1    Schmick, M.2    Bastiaens, P.I.3
  • 2
    • 70349469585 scopus 로고    scopus 로고
    • Domains in biological membranes
    • Lindner R, Naim HY. 2009. Domains in biological membranes. Exp Cell Res 315: 2871-2878. http://dx.doi.org/10.1016/j.yexcr.2009.07.020.
    • (2009) Exp Cell Res , vol.315 , pp. 2871-2878
    • Lindner, R.1    Naim, H.Y.2
  • 4
    • 84865341927 scopus 로고    scopus 로고
    • Membranes: First steps to rafts?
    • Silvius JR. 2012. Membranes: First steps to rafts? Nat Chem Biol 8: 743-744. http://dx.doi.org/10.1038/nchembio.1045.
    • (2012) Nat Chem Biol , vol.8 , pp. 743-744
    • Silvius, J.R.1
  • 5
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer SJ, Nicolson GL. 1972. The fluid mosaic model of the structure of cell membranes. Science 175: 720-731. http://dx.doi.org/10.1126/science.175.4023.720.
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 6
    • 84865560483 scopus 로고    scopus 로고
    • Cell biology. Beyond oil and water-phase transitions in cells
    • Hyman AA, Simons K. 2012. Cell biology. Beyond oil and water-phase transitions in cells. Science 337: 1047-1049. http://dx.doi.org/10.1126/science.1223728.
    • (2012) Science , vol.337 , pp. 1047-1049
    • Hyman, A.A.1    Simons, K.2
  • 7
    • 28444437064 scopus 로고    scopus 로고
    • Membranes are more mosaic than fluid
    • Engelman DM. 2005. Membranes are more mosaic than fluid. Nature 438: 578-580. http://dx.doi.org/10.1038/nature04394.
    • (2005) Nature , vol.438 , pp. 578-580
    • Engelman, D.M.1
  • 8
    • 80855133525 scopus 로고    scopus 로고
    • Cell membranes: The lipid perspective
    • Coskun U, Simons K. 2011. Cell membranes: The lipid perspective. Structure 19: 1543-1548. http://dx.doi.org/10.1016/j.str.2011.10.010.
    • (2011) Structure , vol.19 , pp. 1543-1548
    • Coskun, U.1    Simons, K.2
  • 9
    • 0242693130 scopus 로고    scopus 로고
    • Bacterial membrane lipids: Where do we stand?
    • Cronan JE. 2003. Bacterial membrane lipids: Where do we stand? Annu Rev Microbiol 57: 203-224. http://dx.doi.org/10.1146/annurev.micro.57.030502.090851.
    • (2003) Annu Rev Microbiol , vol.57 , pp. 203-224
    • Cronan, J.E.1
  • 10
    • 38549173564 scopus 로고    scopus 로고
    • Membrane lipids: Where they are and how they behave
    • van Meer G, Voelker DR, Feigenson GW. 2008. Membrane lipids: Where they are and how they behave. Nat Rev Mol Cell Biol 9: 112-124. http://dx.doi.org/10.1038/nrm2330.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 112-124
    • Van Meer, G.1    Voelker, D.R.2    Feigenson, G.W.3
  • 11
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood D, Simons K. 2010. Lipid rafts as a membrane-organizing principle. Science 327: 46-50. http://dx.doi.org/10.1126/science.1174621.
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 12
    • 84860448210 scopus 로고    scopus 로고
    • Membrane organization and lipid rafts
    • Simons K, Sampaio JL. 2011. Membrane organization and lipid rafts. Cold Spring Harb Perspect Biol 3: A004697. http://dx.doi.org/10.1101/cshperspect.a004697.
    • (2011) Cold Spring Harb Perspect Biol , vol.3 , pp. a004697
    • Simons, K.1    Sampaio, J.L.2
  • 13
    • 84884490244 scopus 로고    scopus 로고
    • Plasma membrane organization and function: Moving past lipid rafts
    • Kraft ML. 2013. Plasma membrane organization and function: Moving past lipid rafts. Mol Biol Cell 24: 2765-2768. http://dx.doi.org/10.1091/mbc.E13-03-0165.
    • (2013) Mol Biol Cell , vol.24 , pp. 2765-2768
    • Kraft, M.L.1
  • 14
    • 77955081952 scopus 로고    scopus 로고
    • Understanding lipid rafts and other related membrane domains
    • Neumann AK, Itano MS, Jacobson K. 2010. Understanding lipid rafts and other related membrane domains. F1000 Biol Rep 2: 31. http://dx.doi.org/10.3410/B2-31.
    • (2010) F1000 Biol Rep , vol.2 , pp. 31
    • Neumann, A.K.1    Itano, M.S.2    Jacobson, K.3
  • 15
  • 16
    • 84861592141 scopus 로고    scopus 로고
    • Patchwork organization of the yeast plasma membrane into numerous coexisting domains
    • Spira F, Mueller NS, Beck G, von Olshausen P, Beig J, Wedlich-Soldner R. 2012. Patchwork organization of the yeast plasma membrane into numerous coexisting domains. Nat Cell Biol 14: 640-648. http://dx.doi.org/10.1038/ncb2487.
    • (2012) Nat Cell Biol , vol.14 , pp. 640-648
    • Spira, F.1    Mueller, N.S.2    Beck, G.3    Von Olshausen, P.4    Beig, J.5    Wedlich-Soldner, R.6
  • 17
    • 12344260000 scopus 로고    scopus 로고
    • Polarized sorting in epithelial cells: Raft clustering and the biogenesis of the apical membrane
    • Schuck S, Simons K. 2004. Polarized sorting in epithelial cells: Raft clustering and the biogenesis of the apical membrane. J Cell Sci 117: 5955-5964. http://dx.doi.org/10.1242/jcs.01596.
    • (2004) J Cell Sci , vol.117 , pp. 5955-5964
    • Schuck, S.1    Simons, K.2
  • 18
    • 0023788823 scopus 로고
    • Lipid sorting in epithelial cells
    • Simons K, van Meer G. 1988. Lipid sorting in epithelial cells. Biochemistry 27: 6197-6202. http://dx.doi.org/10.1021/bi00417a001.
    • (1988) Biochemistry , vol.27 , pp. 6197-6202
    • Simons, K.1    Van Meer, G.2
  • 19
    • 0023671841 scopus 로고
    • Lipid polarity and sorting in epithelial cells
    • van Meer G, Simons K. 1988. Lipid polarity and sorting in epithelial cells. J Cell Biochem 36: 51-58. http://dx.doi.org/10.1002/jcb.240360106.
    • (1988) J Cell Biochem , vol.36 , pp. 51-58
    • Van Meer, G.1    Simons, K.2
  • 20
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • Simons K, Toomre D. 2000. Lipid rafts and signal transduction. Nat Rev Mol Cell Biol 1: 31-39. http://dx.doi.org/10.1038/35036052.
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 22
    • 84875111340 scopus 로고    scopus 로고
    • The role of lipid domains in bacterial cell processes
    • Barak I, Muchova K. 2013. The role of lipid domains in bacterial cell processes. Int J Mol Sci 14: 4050-4065. http://dx.doi.org/10.3390/ijms14024050.
    • (2013) Int J Mol Sci , vol.14 , pp. 4050-4065
    • Barak, I.1    Muchova, K.2
  • 23
    • 43449093719 scopus 로고    scopus 로고
    • Lipid spirals in Bacillus subtilis and their role in cell division
    • Barak I, Muchova K, Wilkinson AJ, O'Toole PJ, Pavlendova N. 2008. Lipid spirals in Bacillus subtilis and their role in cell division. Mol Microbiol 68: 1315-1327. http://dx.doi.org/10.1111/j.1365-2958.2008.06236.x.
    • (2008) Mol Microbiol , vol.68 , pp. 1315-1327
    • Barak, I.1    Muchova, K.2    Wilkinson, A.J.3    O'Toole, P.J.4    Pavlendova, N.5
  • 24
    • 33747038638 scopus 로고    scopus 로고
    • Lipid domains in bacterial membranes
    • Matsumoto K, Kusaka J, Nishibori A, Hara H. 2006. Lipid domains in bacterial membranes. Mol Microbiol 61: 1110-1117. http://dx.doi.org/10.1111/j.1365-2958.2006.05317.x.
    • (2006) Mol Microbiol , vol.61 , pp. 1110-1117
    • Matsumoto, K.1    Kusaka, J.2    Nishibori, A.3    Hara, H.4
  • 25
    • 78649884855 scopus 로고    scopus 로고
    • Lipid domains in Bacillus subtilis anucleate cells
    • Muchova K, Jamroskovic J, Barak I. 2010. Lipid domains in Bacillus subtilis anucleate cells. Res Microbiol 161: 783-790. http://dx.doi.org/10.1016/j.resmic.2010.07.006.
    • (2010) Res Microbiol , vol.161 , pp. 783-790
    • Muchova, K.1    Jamroskovic, J.2    Barak, I.3
  • 26
    • 1342282997 scopus 로고    scopus 로고
    • Cardiolipin domains in Bacillus subtilis Marburg membranes
    • Kawai F, Shoda M, Harashima R, Sadaie Y, Hara H, Matsumoto K. 2004. Cardiolipin domains in Bacillus subtilis Marburg membranes. J Bacteriol 186: 1475-1483. http://dx.doi.org/10.1128/JB.186.5.1475-1483.2004.
    • (2004) J Bacteriol , vol.186 , pp. 1475-1483
    • Kawai, F.1    Shoda, M.2    Harashima, R.3    Sadaie, Y.4    Hara, H.5    Matsumoto, K.6
  • 27
    • 0033956407 scopus 로고    scopus 로고
    • Visualization of phospholipid domains in Escherichia coli by using the cardiolipin-specific fluorescent dye 10-N-nonyl acridine orange
    • Mileykovskaya E, Dowhan W. 2000. Visualization of phospholipid domains in Escherichia coli by using the cardiolipin-specific fluorescent dye 10-N-nonyl acridine orange. J Bacteriol 182: 1172-1175. http://dx.doi.org/10.1128/JB.182.4.1172-1175.2000.
    • (2000) J Bacteriol , vol.182 , pp. 1172-1175
    • Mileykovskaya, E.1    Dowhan, W.2
  • 28
    • 70349523247 scopus 로고    scopus 로고
    • Cardiolipin membrane domains in prokaryotes and eukaryotes
    • Mileykovskaya E, Dowhan W. 2009. Cardiolipin membrane domains in prokaryotes and eukaryotes. Biochim Biophys Acta 1788: 2084-2091. http://dx.doi.org/10.1016/j.bbamem.2009.04.003.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 2084-2091
    • Mileykovskaya, E.1    Dowhan, W.2
  • 29
    • 33846603187 scopus 로고    scopus 로고
    • Anionic lipids enriched at the ExPortal of Streptococcus pyogenes
    • Rosch JW, Hsu FF, Caparon MG. 2007. Anionic lipids enriched at the ExPortal of Streptococcus pyogenes. J Bacteriol 189: 801-806. http://dx.doi.org/10.1128/JB.01549-06.
    • (2007) J Bacteriol , vol.189 , pp. 801-806
    • Rosch, J.W.1    Hsu, F.F.2    Caparon, M.G.3
  • 31
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E. 1997. Functional rafts in cell membranes. Nature 387: 569-572. http://dx.doi.org/10.1038/42408.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 32
    • 23844462163 scopus 로고    scopus 로고
    • Flotillins and the PHB domain protein family: Rafts, worms and anaesthetics
    • Morrow IC, Parton RG. 2005. Flotillins and the PHB domain protein family: Rafts, worms and anaesthetics. Traffic 6: 725-740. http://dx.doi.org/10.1111/j.1600-0854.2005.00318.x.
    • (2005) Traffic , vol.6 , pp. 725-740
    • Morrow, I.C.1    Parton, R.G.2
  • 33
    • 34547726345 scopus 로고    scopus 로고
    • Dissecting the molecular function of reggie/flotillin proteins
    • Babuke T, Tikkanen R. 2007. Dissecting the molecular function of reggie/flotillin proteins. Eur J Cell Biol 86: 525-532. http://dx.doi.org/10.1016/j.ejcb.2007.03.003.
    • (2007) Eur J Cell Biol , vol.86 , pp. 525-532
    • Babuke, T.1    Tikkanen, R.2
  • 34
    • 84856866968 scopus 로고    scopus 로고
    • The roles of flotillin microdomains-endocytosis and beyond
    • Otto GP, Nichols BJ. 2011. The roles of flotillin microdomains-endocytosis and beyond. J Cell Sci 124: 3933-3940. http://dx.doi.org/10.1242/jcs.092015.
    • (2011) J Cell Sci , vol.124 , pp. 3933-3940
    • Otto, G.P.1    Nichols, B.J.2
  • 35
    • 79851479445 scopus 로고    scopus 로고
    • Reggie/flotillin and the targeted delivery of cargo
    • Stuermer CA. 2011. Reggie/flotillin and the targeted delivery of cargo. J Neurochem 116: 708-713. http://dx.doi.org/10.1111/j.1471-4159.2010.07007.x.
    • (2011) J Neurochem , vol.116 , pp. 708-713
    • Stuermer, C.A.1
  • 36
    • 80054827742 scopus 로고    scopus 로고
    • Research advances on flotillins
    • Zhao F, Zhang J, Liu YS, Li L, He YL. 2011. Research advances on flotillins. Virol J 8: 479. http://dx.doi.org/10.1186/1743-422X-8-479.
    • (2011) Virol J , vol.8 , pp. 479
    • Zhao, F.1    Zhang, J.2    Liu, Y.S.3    Li, L.4    He, Y.L.5
  • 37
    • 33847706096 scopus 로고    scopus 로고
    • Lipid rafts in health and disease
    • Michel V, Bakovic M. 2007. Lipid rafts in health and disease. Biol Cell 99: 129-140. http://dx.doi.org/10.1042/BC20060051.
    • (2007) Biol Cell , vol.99 , pp. 129-140
    • Michel, V.1    Bakovic, M.2
  • 38
    • 7944221332 scopus 로고    scopus 로고
    • Receptor clustering and signal processing in E. Coli chemotaxis
    • Sourjik V. 2004. Receptor clustering and signal processing in E. Coli chemotaxis. Trends Microbiol 12: 569-576. http://dx.doi.org/10.1016/j.tim.2004.10.003.
    • (2004) Trends Microbiol , vol.12 , pp. 569-576
    • Sourjik, V.1
  • 39
    • 0032492852 scopus 로고    scopus 로고
    • Receptor clustering as a cellular mechanism to control sensitivity
    • Bray D, Levin MD, Morton-Firth CJ. 1998. Receptor clustering as a cellular mechanism to control sensitivity. Nature 393: 85-88. http://dx.doi.org/10.1038/30018.
    • (1998) Nature , vol.393 , pp. 85-88
    • Bray, D.1    Levin, M.D.2    Morton-Firth, C.J.3
  • 40
    • 77956292192 scopus 로고    scopus 로고
    • Functional microdomains in bacterial membranes
    • Lopez D, Kolter R. 2010. Functional microdomains in bacterial membranes. Genes Dev 24: 1893-1902. http://dx.doi.org/10.1101/gad.1945010.
    • (2010) Genes Dev , vol.24 , pp. 1893-1902
    • Lopez, D.1    Kolter, R.2
  • 41
    • 0001590871 scopus 로고    scopus 로고
    • The SPFH domain: Implicated in regulating targeted protein turnover in stomatins and other membrane-Associated proteins
    • Tavernarakis N, Driscoll M, Kyrpides NC. 1999. The SPFH domain: Implicated in regulating targeted protein turnover in stomatins and other membrane-Associated proteins. Trends Biochem Sci 24: 425-427. http://dx.doi.org/10.1016/S0968-0004(99)01467-X.
    • (1999) Trends Biochem Sci , vol.24 , pp. 425-427
    • Tavernarakis, N.1    Driscoll, M.2    Kyrpides, N.C.3
  • 42
    • 79955770162 scopus 로고    scopus 로고
    • Scaffold proteins: Hubs for controlling the flow of cellular information
    • Good MC, Zalatan JG, Lim WA. 2011. Scaffold proteins: Hubs for controlling the flow of cellular information. Science 332: 680-686. http://dx.doi.org/10.1126/science.1198701.
    • (2011) Science , vol.332 , pp. 680-686
    • Good, M.C.1    Zalatan, J.G.2    Lim, W.A.3
  • 43
    • 27144543784 scopus 로고    scopus 로고
    • Scaffolding microdomains and beyond: The function of reggie/flotillin proteins
    • Langhorst MF, Reuter A, Stuermer CA. 2005. Scaffolding microdomains and beyond: The function of reggie/flotillin proteins. Cell Mol Life Sci 62: 2228-2240. http://dx.doi.org/10.1007/s00018-005-5166-4.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 2228-2240
    • Langhorst, M.F.1    Reuter, A.2    Stuermer, C.A.3
  • 44
    • 58549115547 scopus 로고    scopus 로고
    • Structurally diverse natural products that cause potassium leakage trigger multicellularity in Bacillus subtilis
    • Lopez D, Fischbach MA, Chu F, Losick R, Kolter R. 2009. Structurally diverse natural products that cause potassium leakage trigger multicellularity in Bacillus subtilis. Proc Natl Acad Sci U S A 106: 280-285. http://dx.doi.org/10.1073/pnas.0810940106.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 280-285
    • Lopez, D.1    Fischbach, M.A.2    Chu, F.3    Losick, R.4    Kolter, R.5
  • 45
    • 0028942309 scopus 로고
    • Different roles for KinA, KinB, and KinC in the initiation of sporulation in Bacillus subtilis
    • LeDeaux JR, Yu N, Grossman AD. 1995. Different roles for KinA, KinB, and KinC in the initiation of sporulation in Bacillus subtilis. J Bacteriol 177: 861-863.
    • (1995) J Bacteriol , vol.177 , pp. 861-863
    • LeDeaux, J.R.1    Yu, N.2    Grossman, A.D.3
  • 47
    • 43549086881 scopus 로고    scopus 로고
    • Isolation and use of rafts
    • Unit 11.10
    • Brown DA. 2002. Isolation and use of rafts. Curr Protoc Immunol Chapter 11: Unit 11.10. http://dx.doi.org/10.1002/0471142735.im1110s51.
    • (2002) Curr Protoc Immunol Chapter , vol.11
    • Brown, D.A.1
  • 48
    • 38949119499 scopus 로고    scopus 로고
    • Nondetergent isolation of rafts
    • Shah MB, Sehgal PB. 2007. Nondetergent isolation of rafts. Methods Mol Biol 398: 21-28. http://dx.doi.org/10.1007/978-1-59745-513-8-3.
    • (2007) Methods Mol Biol , vol.398 , pp. 21-28
    • Shah, M.B.1    Sehgal, P.B.2
  • 49
    • 67650708496 scopus 로고    scopus 로고
    • Characterization and subcellular localization of a bacterial flotillin homologue
    • Donovan C, Bramkamp M. 2009. Characterization and subcellular localization of a bacterial flotillin homologue. Microbiology 155: 1786-1799. http://dx.doi.org/10.1099/mic.0.025312-0.
    • (2009) Microbiology , vol.155 , pp. 1786-1799
    • Donovan, C.1    Bramkamp, M.2
  • 50
    • 21044433322 scopus 로고    scopus 로고
    • An alkali-inducible flotillin-like protein from Bacillus halodurans C-125
    • Zhang HM, Li Z, Tsudome M, Ito S, Takami H, Horikoshi K. 2005. An alkali-inducible flotillin-like protein from Bacillus halodurans C-125. Protein J 24: 125-131. http://dx.doi.org/10.1007/s10930-004-1519-3.
    • (2005) Protein J , vol.24 , pp. 125-131
    • Zhang, H.M.1    Li, Z.2    Tsudome, M.3    Ito, S.4    Takami, H.5    Horikoshi, K.6
  • 51
    • 84866321770 scopus 로고    scopus 로고
    • Synthetic motility and cell shape defects for deletions of flotillin/reggie paralogs in Bacillus subtilis and interplay with NfeD proteins
    • Dempwolff F, Moller HM, Graumann PL. 2012. Synthetic motility and cell shape defects for deletions of flotillin/reggie paralogs in Bacillus subtilis and interplay with NfeD proteins. J Bacteriol 194: 4652-4661. http://dx.doi.org/10.1128/JB.00910-12.
    • (2012) J Bacteriol , vol.194 , pp. 4652-4661
    • Dempwolff, F.1    Moller, H.M.2    Graumann, P.L.3
  • 53
    • 0017043554 scopus 로고
    • Competitive inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase by ML-236A and ML-236B fungal metabolites, having hypocholesterolemic activity
    • Endo A, Kuroda M, Tanzawa K. 1976. Competitive inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase by ML-236A and ML-236B fungal metabolites, having hypocholesterolemic activity. FEBS Lett 72: 323-326. http://dx.doi.org/10.1016/0014-5793(76)80996-9.
    • (1976) FEBS Lett , vol.72 , pp. 323-326
    • Endo, A.1    Kuroda, M.2    Tanzawa, K.3
  • 54
    • 25444443095 scopus 로고    scopus 로고
    • Structure and biosynthesis of staphyloxanthin from Staphylococcus aureus
    • Pelz A, Wieland KP, Putzbach K, Hentschel P, Albert K, Gotz F. 2005. Structure and biosynthesis of staphyloxanthin from Staphylococcus aureus. J Biol Chem 280: 32493-32498. http://dx.doi.org/10.1074/jbc.M505070200.
    • (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    Gotz, F.6
  • 56
    • 84863230621 scopus 로고    scopus 로고
    • Glutamate dehydrogenase affects resistance to cell wall antibiotics in Bacillus subtilis
    • Lee YH, Kingston AW, Helmann JD. 2012. Glutamate dehydrogenase affects resistance to cell wall antibiotics in Bacillus subtilis. J Bacteriol 194: 993-1001. http://dx.doi.org/10.1128/JB.06547-11.
    • (2012) J Bacteriol , vol.194 , pp. 993-1001
    • Lee, Y.H.1    Kingston, A.W.2    Helmann, J.D.3
  • 57
    • 84865532003 scopus 로고    scopus 로고
    • Functional convergence of hopanoids and sterols in membrane ordering
    • Saenz JP, Sezgin E, Schwille P, Simons K. 2012. Functional convergence of hopanoids and sterols in membrane ordering. Proc Natl Acad Sci U S A 109: 14236-14240. http://dx.doi.org/10.1073/pnas.1212141109.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 14236-14240
    • Saenz, J.P.1    Sezgin, E.2    Schwille, P.3    Simons, K.4
  • 58
  • 59
    • 17244380947 scopus 로고    scopus 로고
    • Lipid rafts and membrane dynamics
    • Rajendran L, Simons K. 2005. Lipid rafts and membrane dynamics. J Cell Sci 118: 1099-1102. http://dx.doi.org/10.1242/jcs.01681.
    • (2005) J Cell Sci , vol.118 , pp. 1099-1102
    • Rajendran, L.1    Simons, K.2
  • 60
    • 77957167810 scopus 로고    scopus 로고
    • Revitalizing membrane rafts: New tools and insights
    • Simons K, Gerl MJ. 2010. Revitalizing membrane rafts: New tools and insights. Nat Rev Mol Cell Biol 11: 688-699. http://dx.doi.org/10.1038/nrm2977.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 688-699
    • Simons, K.1    Gerl, M.J.2
  • 61
    • 34548486955 scopus 로고    scopus 로고
    • The SPFH domaincontaining proteins: More than lipid raft markers
    • Browman DT, Hoegg MB, Robbins SM. 2007. The SPFH domaincontaining proteins: More than lipid raft markers. Trends Cell Biol 17: 394-402. http://dx.doi.org/10.1016/j.tcb.2007.06.005.
    • (2007) Trends Cell Biol , vol.17 , pp. 394-402
    • Browman, D.T.1    Hoegg, M.B.2    Robbins, S.M.3
  • 62
    • 84875958424 scopus 로고    scopus 로고
    • Bacterial lipids: Metabolism and membrane homeostasis
    • Parsons JB, Rock CO. 2013. Bacterial lipids: Metabolism and membrane homeostasis. Prog Lipid Res 52: 249-276. http://dx.doi.org/10.1016/j.plipres.2013.02.002.
    • (2013) Prog Lipid Res , vol.52 , pp. 249-276
    • Parsons, J.B.1    Rock, C.O.2
  • 65
    • 77958089989 scopus 로고    scopus 로고
    • Cholesterol lipids of Borrelia burgdorferi form lipid rafts and are required for the bactericidal activity of a complement-independent antibody
    • LaRocca TJ, Crowley JT, Cusack BJ, Pathak P, Benach J, London E, Garcia-Monco JC, Benach JL. 2010. Cholesterol lipids of Borrelia burgdorferi form lipid rafts and are required for the bactericidal activity of a complement-independent antibody. Cell Host Microbe 8: 331-342. http://dx.doi.org/10.1016/j.chom.2010.09.001.
    • (2010) Cell Host Microbe , vol.8 , pp. 331-342
    • LaRocca, T.J.1    Crowley, J.T.2    Cusack, B.J.3    Pathak, P.4    Benach, J.5    London, E.6    Garcia-Monco, J.C.7    Benach, J.L.8
  • 66
    • 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 TJ, Pathak P, Chiantia S, Toledo A, Silvius JR, Benach JL, London E. 2013. Proving lipid rafts exist: Membrane domains in the prokaryote Borrelia burgdorferi have the same properties as eukaryotic lipid rafts. PLoS Pathog 9: E1003353. http://dx.doi.org/10.1371/journal.ppat.1003353.
    • (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
  • 67
    • 44349145919 scopus 로고    scopus 로고
    • A polycyclic terpenoid that alleviates oxidative stress
    • Bosak T, Losick RM, Pearson A. 2008. A polycyclic terpenoid that alleviates oxidative stress. Proc Natl Acad Sci USA105: 6725-6729. http://dx.doi.org/10.1073/pnas.0800199105.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 6725-6729
    • Bosak, T.1    Losick, R.M.2    Pearson, A.3
  • 68
    • 0023515798 scopus 로고
    • Prokaryotic hopanoids and other polyterpenoid sterol surrogates
    • Ourisson G, Rohmer M, Poralla K. 1987. Prokaryotic hopanoids and other polyterpenoid sterol surrogates. Annu Rev Microbiol 41: 301-333. http://dx.doi.org/10.1146/annurev.mi.41.100187.001505.
    • (1987) Annu Rev Microbiol , vol.41 , pp. 301-333
    • Ourisson, G.1    Rohmer, M.2    Poralla, K.3
  • 69
    • 0343775629 scopus 로고    scopus 로고
    • Bacterial triterpenoids of the hopane series as biomarkers for the chemotaxonomy of Burkholderia, Pseudomonas and Ralstonia spp
    • Cvejic JH, Putra SR, El-Beltagy A, Hattori R, Hattori T, Rohmer M. 2000. Bacterial triterpenoids of the hopane series as biomarkers for the chemotaxonomy of Burkholderia, Pseudomonas and Ralstonia spp. FEMS Microbiol Lett 183: 295-299. http://dx.doi.org/10.1111/j.1574-6968.20 00.tb08974.x.
    • (2000) FEMS Microbiol Lett , vol.183 , pp. 295-299
    • Cvejic, J.H.1    Putra, S.R.2    El-Beltagy, A.3    Hattori, R.4    Hattori, T.5    Rohmer, M.6
  • 70
    • 0034849420 scopus 로고    scopus 로고
    • Hopanoid lipids in Frankia: Identification of squalene-hopene cyclase gene sequences
    • Dobritsa SV, Potter D, Gookin TE, Berry AM. 2001. Hopanoid lipids in Frankia: Identification of squalene-hopene cyclase gene sequences. Can J Microbiol 47: 535-540. http://dx.doi.org/10.1139/w01-045.
    • (2001) Can J Microbiol , vol.47 , pp. 535-540
    • Dobritsa, S.V.1    Potter, D.2    Gookin, T.E.3    Berry, A.M.4
  • 71
    • 70449556446 scopus 로고    scopus 로고
    • 2-Methylhopanoids are maximally produced in akinetes of Nostoc punctiforme: Geobiological implications
    • Doughty DM, Hunter RC, Summons RE, Newman DK. 2009. 2-Methylhopanoids are maximally produced in akinetes of Nostoc punctiforme: Geobiological implications. Geobiology 7: 524-532. http://dx.doi.org/10.1111/j.1472-4669.2009.00217.x.
    • (2009) Geobiology , vol.7 , pp. 524-532
    • Doughty, D.M.1    Hunter, R.C.2    Summons, R.E.3    Newman, D.K.4
  • 72
    • 12844254527 scopus 로고    scopus 로고
    • Occurrence of hopanoid lipids in anaerobic Geobacter species
    • Hartner T, Straub KL, Kannenberg E. 2005. Occurrence of hopanoid lipids in anaerobic Geobacter species. FEMS Microbiol Lett 243: 59-64. http://dx.doi.org/10.1016/j.femsle.2004.11.039.
    • (2005) FEMS Microbiol Lett , vol.243 , pp. 59-64
    • Hartner, T.1    Straub, K.L.2    Kannenberg, E.3
  • 73
    • 65349189508 scopus 로고    scopus 로고
    • Diversity of hopanoids and squalene-hopene cyclases across a tropical land-sea gradient
    • Pearson A, Leavitt WD, Saenz JP, Summons RE, Tam MC, Close HG. 2009. Diversity of hopanoids and squalene-hopene cyclases across a tropical land-sea gradient. Environ Microbiol 11: 1208-1223. http://dx.doi.org/10.1111/j.1462-2920.2008.01817.x.
    • (2009) Environ Microbiol , vol.11 , pp. 1208-1223
    • Pearson, A.1    Leavitt, W.D.2    Saenz, J.P.3    Summons, R.E.4    Tam, M.C.5    Close, H.G.6
  • 74
    • 60749104423 scopus 로고    scopus 로고
    • Distribution of microbial terpenoid lipid cyclases in the global ocean metagenome
    • Pearson A, Rusch DB. 2009. Distribution of microbial terpenoid lipid cyclases in the global ocean metagenome. ISME J 3: 352-363. http://dx.doi.org/10.1038/ismej.2008.116.
    • (2009) ISME J , vol.3 , pp. 352-363
    • Pearson, A.1    Rusch, D.B.2
  • 75
    • 84855415181 scopus 로고    scopus 로고
    • Hopanoid production is required for low-pH tolerance, antimicrobial resistance, and motility in Burkholderia cenocepacia
    • Schmerk CL, Bernards MA, Valvano MA. 2011. Hopanoid production is required for low-pH tolerance, antimicrobial resistance, and motility in Burkholderia cenocepacia. J Bacteriol 193: 6712-6723. http://dx.doi.org/10.1128/JB.05979-11.
    • (2011) J Bacteriol , vol.193 , pp. 6712-6723
    • Schmerk, C.L.1    Bernards, M.A.2    Valvano, M.A.3
  • 76
    • 57449092073 scopus 로고    scopus 로고
    • Bacteriohopanepolyol signatures of bacterial populations in Western Canadian soils
    • Xu Y, Cooke MP, Talbot HM, Simpson MJ. 2009. Bacteriohopanepolyol signatures of bacterial populations in Western Canadian soils. OrgGeochem 40: 79-86. http://dx.doi.org/10.1016/j.orggeochem.2008.09.003.
    • (2009) OrgGeochem , vol.40 , pp. 79-86
    • Xu, Y.1    Cooke, M.P.2    Talbot, H.M.3    Simpson, M.J.4
  • 78
    • 79960094417 scopus 로고    scopus 로고
    • Squalene-hopene cyclases
    • Siedenburg G, Jendrossek D. 2011. Squalene-hopene cyclases. Appl Environ Microbiol 77: 3905-3915. http://dx.doi.org/10.1128/AEM.00 300-11.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 3905-3915
    • Siedenburg, G.1    Jendrossek, D.2
  • 79
    • 0020359514 scopus 로고
    • The influence of hopanoids on growth of Mycoplasma mycoides
    • Kannenberg E, Poralla K. 1982. The influence of hopanoids on growth of Mycoplasma mycoides. Arch Microbiol 133: 100-102. http://dx.doi.org/10.1007/BF00413519.
    • (1982) Arch Microbiol , vol.133 , pp. 100-102
    • Kannenberg, E.1    Poralla, K.2
  • 80
    • 0030948127 scopus 로고    scopus 로고
    • Modulation of lipoxygenase activity by bacterial hopanoids
    • Moreau RA, Agnew J, Hicks KB, Powell MJ. 1997. Modulation of lipoxygenase activity by bacterial hopanoids. J Nat Prod 60: 397-398. http://dx.doi.org/10.1021/np960611y.
    • (1997) J Nat Prod , vol.60 , pp. 397-398
    • Moreau, R.A.1    Agnew, J.2    Hicks, K.B.3    Powell, M.J.4
  • 81
    • 0034255872 scopus 로고    scopus 로고
    • Hopanoids are formed during transition from substrate to aerial hyphae in Streptomyces coelicolor A3(2)
    • Poralla K, Muth G, Hartner T. 2000. Hopanoids are formed during transition from substrate to aerial hyphae in Streptomyces coelicolor A3(2). FEMS Microbiol Lett 189: 93-95. http://dx.doi.org/10.1111/j.1574-6968.2000.tb09212.x.
    • (2000) FEMS Microbiol Lett , vol.189 , pp. 93-95
    • Poralla, K.1    Muth, G.2    Hartner, T.3
  • 82
    • 67749145240 scopus 로고    scopus 로고
    • Hopanoids are not essential for growth of Streptomyces scabies 87-22
    • Seipke RF, Loria R. 2009. Hopanoids are not essential for growth of Streptomyces scabies 87-22. J Bacteriol 191: 5216-5223. http://dx.doi.org/10.1128/JB.00390-09.
    • (2009) J Bacteriol , vol.191 , pp. 5216-5223
    • Seipke, R.F.1    Loria, R.2
  • 83
    • 81055130186 scopus 로고    scopus 로고
    • The RND-family transporter, HpnN, is required for hopanoid localization to the outer membrane of Rhodopseudomonas palustris TIE-1
    • Doughty DM, Coleman ML, Hunter RC, Sessions AL, Summons RE, Newman DK. 2011. The RND-family transporter, HpnN, is required for hopanoid localization to the outer membrane of Rhodopseudomonas palustris TIE-1. Proc Natl Acad Sci USA108: E1045-E1051. http://dx.doi.org/10.1073/pnas.1104209108.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. E1045-E1051
    • Doughty, D.M.1    Coleman, M.L.2    Hunter, R.C.3    Sessions, A.L.4    Summons, R.E.5    Newman, D.K.6
  • 84
    • 0021222921 scopus 로고
    • Bacterial triterpenoids
    • Taylor RF. 1984. Bacterial triterpenoids. Microbiol Rev 48: 181-198.
    • (1984) Microbiol Rev , vol.48 , pp. 181-198
    • Taylor, R.F.1
  • 85
    • 36949089636 scopus 로고
    • Function of carotenoids in photosynthetic bacteria
    • Dworkin M. 1959. Function of carotenoids in photosynthetic bacteria. Nature 184: 1891-1892. http://dx.doi.org/10.1038/1841891b0.
    • (1959) Nature , vol.184 , pp. 1891-1892
    • Dworkin, M.1
  • 86
    • 0032745777 scopus 로고    scopus 로고
    • Biological functions of carotenoids-diversity and evolution
    • Vershinin A. Biological functions of carotenoids-diversity and evolution. Biofactors 1999, 99-104. http://dx.doi.org/10.1002/biof.5520100203
    • (1999) Biofactors , vol.10 , pp. 99-104
    • Vershinin, A.1
  • 87
    • 85193650279 scopus 로고    scopus 로고
    • Organization of carotenoids in models of biological membranes: Current status of knowledge and research
    • Vershinin A. 1999. Biological functions of carotenoids-diversity and evolution. Biofactors 10: 99-104. http://dx.doi.org/10.1002/biof.5520100203. 87. Cvetkovic D, Fiedor L, Wisniewska-Becker A, Markovic D. 2013. Organization of carotenoids in models of biological membranes: Current status of knowledge and research. Curr Anal Chem 9: 1573-4110. http://dx.doi.org/10.2174/1573411011309010086.
    • (2013) Curr Anal Chem , vol.9 , pp. 1573-4110
    • Cvetkovic, D.1    Fiedor, L.2    Wisniewska-Becker, A.3    Markovic, D.4
  • 88
    • 84860425335 scopus 로고    scopus 로고
    • Can macular xanthophylls replace cholesterol in formation of the liquid-ordered phase in lipid-bilayer membranes?
    • Subczynski WK, Wisniewska-Becker A, Widomska J. 2012. Can macular xanthophylls replace cholesterol in formation of the liquid-ordered phase in lipid-bilayer membranes? Acta Biochim Pol 59: 109-114.
    • (2012) Acta Biochim Pol , vol.59 , pp. 109-114
    • Subczynski, W.K.1    Wisniewska-Becker, A.2    Widomska, J.3
  • 89
    • 0014824353 scopus 로고
    • Carotenoid formation by Staphylococcus aureus
    • Hammond RK, White DC. 1970. Carotenoid formation by Staphylococcus aureus. J Bacteriol 103: 191-198.
    • (1970) J Bacteriol , vol.103 , pp. 191-198
    • Hammond, R.K.1    White, D.C.2
  • 90
    • 33645080662 scopus 로고    scopus 로고
    • Carotenoids present in halotolerant Bacillus spore formers
    • Duc LH, Fraser PD, Tam NK, Cutting SM. 2006. Carotenoids present in halotolerant Bacillus spore formers. FEMS Microbiol Lett 255: 215-224. http://dx.doi.org/10.1111/j.1574-6968.2005.00091.x.
    • (2006) FEMS Microbiol Lett , vol.255 , pp. 215-224
    • Duc, L.H.1    Fraser, P.D.2    Tam, N.K.3    Cutting, S.M.4
  • 92
    • 44349097602 scopus 로고    scopus 로고
    • Cloning, solubilization, and characterization of squalene synthase from Thermosynechococcus elongatus BP-1
    • Lee S, Poulter CD. 2008. Cloning, solubilization, and characterization of squalene synthase from Thermosynechococcus elongatus BP-1. J Bacteriol 190: 3808-3816. http://dx.doi.org/10.1128/JB.01939-07.
    • (2008) J Bacteriol , vol.190 , pp. 3808-3816
    • Lee, S.1    Poulter, C.D.2
  • 94
    • 84872105939 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of YisP protein from Bacillus subtilis subsp. Subtilis strain 168
    • Hu Y, Jia S, Ren F, Huang CH, Ko TP, Mitchell DA, Guo RT, Zheng Y. 2013. Crystallization and preliminary X-ray diffraction analysis of YisP protein from Bacillus subtilis subsp. subtilis strain 168. Acta Crystallogr Sect F Struct Biol Cryst Commun 69: 77-79. http://dx.doi.org/10.1107/S1744309112049330.
    • (2013) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.69 , pp. 77-79
    • Hu, Y.1    Jia, S.2    Ren, F.3    Huang, C.H.4    Ko, T.P.5    Mitchell, D.A.6    Guo, R.T.7    Zheng, Y.8
  • 95
    • 51449112852 scopus 로고    scopus 로고
    • Cardiolipin synthesis for the assembly of bacterial and mitochondrial membranes
    • Schlame M. 2008. Cardiolipin synthesis for the assembly of bacterial and mitochondrial membranes. J Lipid Res 49: 1607-1620. http://dx.doi.org/10.1194/jlr.R700018-JLR200.
    • (2008) J Lipid Res , vol.49 , pp. 1607-1620
    • Schlame, M.1
  • 96
    • 17144431348 scopus 로고    scopus 로고
    • Cardiolipin in energy transducing membranes
    • Mileykovskaya E, Zhang M, Dowhan W. 2005. Cardiolipin in energy transducing membranes. Biochemistry Mosc. 70: 154-158. http://dx.doi.org/10.1007/s10541-005-0095-2.
    • (2005) Biochemistry Mosc). , vol.70 , pp. 154-158
    • Mileykovskaya, E.1    Zhang, M.2    Dowhan, W.3
  • 97
    • 34249989948 scopus 로고    scopus 로고
    • Subcellular localization of Escherichia coli osmosensory transporter ProP: Focus on cardiolipin membrane domains
    • Mileykovskaya E. 2007. Subcellular localization of Escherichia coli osmosensory transporter ProP: Focus on cardiolipin membrane domains. Mol Microbiol 64: 1419-1422. http://dx.doi.org/10.1111/j.1365-2958.2007.05766.x.
    • (2007) Mol Microbiol , vol.64 , pp. 1419-1422
    • Mileykovskaya, E.1
  • 99
    • 0035955450 scopus 로고    scopus 로고
    • Cardiolipin binds nonyl acridine orange by aggregating the dye at exposed hydrophobic domains on bilayer surfaces
    • Mileykovskaya E, Dowhan W, Birke RL, Zheng D, Lutterodt L, Haines TH. 2001. Cardiolipin binds nonyl acridine orange by aggregating the dye at exposed hydrophobic domains on bilayer surfaces. FEBS Lett 507: 187-190. http://dx.doi.org/10.1016/S0014-5793(01)02948-9.
    • (2001) FEBS Lett , vol.507 , pp. 187-190
    • Mileykovskaya, E.1    Dowhan, W.2    Birke, R.L.3    Zheng, D.4    Lutterodt, L.5    Haines, T.H.6
  • 100
    • 0031010267 scopus 로고    scopus 로고
    • Flotillin and epidermal surface antigen define a new family of caveolae-Associated integral membrane proteins
    • Bickel PE, Scherer PE, Schnitzer JE, Oh P, Lisanti MP, Lodish HF. 1997. Flotillin and epidermal surface antigen define a new family of caveolae-Associated integral membrane proteins. J Biol Chem 272: 13793-13802. http://dx.doi.org/10.1074/jbc.272.21.13793.
    • (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
  • 101
    • 0031795591 scopus 로고    scopus 로고
    • Identification of reggie-1 and reggie-2 as plasmamembrane-Associated proteins which cocluster with activated GPI-Anchored cell adhesion molecules in non-caveolar micropatches in neurons
    • Lang DM, Lommel S, Jung M, Ankerhold R, Petrausch B, Laessing U, Wiechers MF, Plattner H, Stuermer CA. 1998. Identification of reggie-1 and reggie-2 as plasmamembrane-Associated proteins which cocluster with activated GPI-Anchored cell adhesion molecules in non-caveolar micropatches in neurons. J Neurobiol 37: 502-523. http://dx.doi.org/10.1002/(SICI)1097-4695(199812)37: 4502:AID-NEU2-3.0.CO;2-S.
    • (1998) J Neurobiol , vol.37 , pp. 502-523
    • Lang, D.M.1    Lommel, S.2    Jung, M.3    Ankerhold, R.4    Petrausch, B.5    Laessing, U.6    Wiechers, M.F.7    Plattner, H.8    Stuermer, C.A.9
  • 102
    • 0037073697 scopus 로고    scopus 로고
    • Flotillin-1/reggie-2 traffics to surface raft domains via a novel Golgi-independent pathway. Identification of a novel membrane targeting domain and a role for palmitoylation
    • Morrow IC, Rea S, Martin S, Prior IA, Prohaska R, Hancock JF, James DE, Parton RG. 2002. Flotillin-1/reggie-2 traffics to surface raft domains via a novel Golgi-independent pathway. Identification of a novel membrane targeting domain and a role for palmitoylation. J Biol Chem 277: 48834-48841. http://dx.doi.org/10.1074/jbc.M209082200.
    • (2002) J Biol Chem , vol.277 , pp. 48834-48841
    • Morrow, I.C.1    Rea, S.2    Martin, S.3    Prior, I.A.4    Prohaska, R.5    Hancock, J.F.6    James, D.E.7    Parton, R.G.8
  • 103
    • 0031054457 scopus 로고    scopus 로고
    • Reggie-1 and reggie-2, two cell surface proteins expressed by retinal ganglion cells during axon regeneration
    • Schulte T, Paschke KA, Laessing U, Lottspeich F, Stuermer CA. 1997. Reggie-1 and reggie-2, two cell surface proteins expressed by retinal ganglion cells during axon regeneration. Development 124: 577-587.
    • (1997) Development , vol.124 , pp. 577-587
    • Schulte, T.1    Paschke, K.A.2    Laessing, U.3    Lottspeich, F.4    Stuermer, C.A.5
  • 104
    • 15544380905 scopus 로고    scopus 로고
    • The 'lipid raft' microdomain proteins reggie-1 and reggie-2 flotillins. Are scaffolds for protein interaction and signalling
    • Stuermer CA, Plattner H. 2005. The 'lipid raft' microdomain proteins reggie-1 and reggie-2 flotillins. are scaffolds for protein interaction and signalling. Biochem Soc Symp 72: 109-118.
    • (2005) Biochem Soc Symp , vol.72 , pp. 109-118
    • Stuermer, C.A.1    Plattner, H.2
  • 105
    • 33846419488 scopus 로고    scopus 로고
    • Lipid raft microdomains and neurotransmitter signalling
    • Allen JA, Halverson-Tamboli RA, Rasenick MM. 2007. Lipid raft microdomains and neurotransmitter signalling. Nat Rev Neurosci 8: 128-140. http://dx.doi.org/10.1038/nrn2059.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 128-140
    • Allen, J.A.1    Halverson-Tamboli, R.A.2    Rasenick, M.M.3
  • 106
    • 72549086774 scopus 로고    scopus 로고
    • The reggie/flotillin connection to growth
    • Stuermer CA. 2010. The reggie/flotillin connection to growth. Trends Cell Biol 20: 6-13. http://dx.doi.org/10.1016/j.tcb.2009.10.003.
    • (2010) Trends Cell Biol , vol.20 , pp. 6-13
    • Stuermer, C.A.1
  • 107
    • 67349189783 scopus 로고    scopus 로고
    • Hetero-oligomerization of reggie-1/flotillin-2 and reggie-2/flotillin-1 is required for their endocytosis
    • Babuke T, Ruonala M, Meister M, Amaddii M, Genzler C, Esposito A, Tikkanen R. 2009. Hetero-oligomerization of reggie-1/flotillin-2 and reggie-2/flotillin-1 is required for their endocytosis. Cell Signal 21: 1287-1297. http://dx.doi.org/10.1016/j.cellsig.2009.03.012.
    • (2009) Cell Signal , vol.21 , pp. 1287-1297
    • Babuke, T.1    Ruonala, M.2    Meister, M.3    Amaddii, M.4    Genzler, C.5    Esposito, A.6    Tikkanen, R.7
  • 108
    • 84857128669 scopus 로고    scopus 로고
    • Functional aspects of membrane association of reggie/flotillin proteins
    • Banning A, Tomasovic A, Tikkanen R. 2011. Functional aspects of membrane association of reggie/flotillin proteins. Curr Protein Pept Sci 12: 725-735. http://dx.doi.org/10.2174/138920311798841708.
    • (2011) Curr Protein Pept Sci , vol.12 , pp. 725-735
    • Banning, A.1    Tomasovic, A.2    Tikkanen, R.3
  • 109
    • 84857746692 scopus 로고    scopus 로고
    • Flotillin-1/reggie-2 protein plays dual role in activation of receptor-Tyrosine kinase/mitogen-Activated protein kinase signaling
    • Amaddii M, Meister M, Banning A, Tomasovic A, Mooz J, Rajalingam K, Tikkanen R. 2012. Flotillin-1/reggie-2 protein plays dual role in activation of receptor-Tyrosine kinase/mitogen-Activated protein kinase signaling. J Biol Chem 287: 7265-7278. http://dx.doi.org/10.1074/jbc.M111.287599.
    • (2012) J Biol Chem , vol.287 , pp. 7265-7278
    • Amaddii, M.1    Meister, M.2    Banning, A.3    Tomasovic, A.4    Mooz, J.5    Rajalingam, K.6    Tikkanen, R.7
  • 110
    • 78650664669 scopus 로고    scopus 로고
    • Palmitoylation regulates raft affinity for the majority of integral raft proteins
    • Levental I, Lingwood D, Grzybek M, Coskun U, Simons K. 2010. Palmitoylation regulates raft affinity for the majority of integral raft proteins. Proc Natl Acad Sci U S A 107: 22050-22054. http://dx.doi.org/10.1073/pnas.1016184107.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 22050-22054
    • Levental, I.1    Lingwood, D.2    Grzybek, M.3    Coskun, U.4    Simons, K.5
  • 111
    • 1642271441 scopus 로고    scopus 로고
    • Membrane and raft association of reggie-1/flotillin-2: Role of myristoylation, palmitoylation and oligomerization and induction of filopodia by overexpression
    • Neumann-Giesen C, Falkenbach B, Beicht P, Claasen S, Luers G, Stuermer CA, Herzog V, Tikkanen R. 2004. Membrane and raft association of reggie-1/flotillin-2: Role of myristoylation, palmitoylation and oligomerization and induction of filopodia by overexpression. Biochem J 378: 509-518. http://dx.doi.org/10.1042/BJ20031100.
    • (2004) Biochem J , vol.378 , pp. 509-518
    • Neumann-Giesen, C.1    Falkenbach, B.2    Beicht, P.3    Claasen, S.4    Luers, G.5    Stuermer, C.A.6    Herzog, V.7    Tikkanen, R.8
  • 112
    • 32044464800 scopus 로고    scopus 로고
    • Ancient origin of reggie flotillin), reggie-like, and other lipid-raft proteins: Convergent evolution of the SPFH domain
    • Rivera-Milla E, Stuermer CA, Malaga-Trillo E. 2006. Ancient origin of reggie flotillin), reggie-like, and other lipid-raft proteins: Convergent evolution of the SPFH domain. Cell Mol Life Sci 63: 343-357. http://dx.doi.org/10.1007/s00018-005-5434-3.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 343-357
    • Rivera-Milla, E.1    Stuermer, C.A.2    Malaga-Trillo, E.3
  • 113
    • 0036307635 scopus 로고    scopus 로고
    • Defining the Bacillus subtilis sigma(W. Regulon: A comparative analysis of promoter consensus search, run-off transcription/macroarray analysis ROMA), and transcriptional profiling approaches
    • Cao M, Kobel PA, Morshedi MM, Wu MF, Paddon C, Helmann JD. 2002. Defining the Bacillus subtilis sigma(W. regulon: A comparative analysis of promoter consensus search, run-off transcription/macroarray analysis ROMA), and transcriptional profiling approaches. J Mol Biol 316: 443-457. http://dx.doi.org/10.1006/jmbi.2001.5372.
    • (2002) J Mol Biol , vol.316 , pp. 443-457
    • Cao, M.1    Kobel, P.A.2    Morshedi, M.M.3    Wu, M.F.4    Paddon, C.5    Helmann, J.D.6
  • 114
    • 0036146932 scopus 로고    scopus 로고
    • Evolution of duplicated reggie genes in zebrafish and goldfish
    • Malaga-Trillo E, Laessing U, Lang DM, Meyer A, Stuermer CA. 2002. Evolution of duplicated reggie genes in zebrafish and goldfish. J Mol Evol 54: 235-245. http://dx.doi.org/10.1007/s00239-001-0005-1.
    • (2002) J Mol Evol , vol.54 , pp. 235-245
    • Malaga-Trillo, E.1    Laessing, U.2    Lang, D.M.3    Meyer, A.4    Stuermer, C.A.5
  • 115
    • 0036081063 scopus 로고    scopus 로고
    • SubtiList: The reference database for the Bacillus subtilis genome
    • Moszer I, Jones LM, Moreira S, Fabry C, Danchin A. 2002. SubtiList: The reference database for the Bacillus subtilis genome. Nucleic Acids Res 30: 62-65. http://dx.doi.org/10.1093/nar/30.1.62.
    • (2002) Nucleic Acids Res , vol.30 , pp. 62-65
    • Moszer, I.1    Jones, L.M.2    Moreira, S.3    Fabry, C.4    Danchin, A.5
  • 116
    • 51749088334 scopus 로고    scopus 로고
    • Solution structure of the soluble domain of the NfeD protein YuaF from Bacillus subtilis
    • Walker CA, Hinderhofer M, Witte DJ, Boos W, Moller HM. 2008. Solution structure of the soluble domain of the NfeD protein YuaF from Bacillus subtilis. J Biomol NMR 42: 69-76. http://dx.doi.org/10.1007/s10858-008-9261-3.
    • (2008) J Biomol NMR , vol.42 , pp. 69-76
    • Walker, C.A.1    Hinderhofer, M.2    Witte, D.J.3    Boos, W.4    Moller, H.M.5
  • 118
    • 0034931152 scopus 로고    scopus 로고
    • Alkaline shock induces the Bacillus subtilis sigma(W. Regulon
    • Wiegert T, Homuth G, Versteeg S, Schumann W. 2001. Alkaline shock induces the Bacillus subtilis sigma(W. regulon. Mol Microbiol 41: 59-71. http://dx.doi.org/10.1046/j.1365-2958.2001.02489.x.
    • (2001) Mol Microbiol , vol.41 , pp. 59-71
    • Wiegert, T.1    Homuth, G.2    Versteeg, S.3    Schumann, W.4
  • 119
    • 84891613679 scopus 로고    scopus 로고
    • Overproduction of flotillin influences cell differentiation and shape in Bacillus subtilis
    • Mielich-Suss B, Schneider J, Lopez D. 2013. Overproduction of flotillin influences cell differentiation and shape in Bacillus subtilis. mBio 4(6): E00719-13. http://dx.doi.org/10.1128/mBio.00719-13.
    • (2013) MBio , vol.4 , Issue.6 , pp. e00719-e00723
    • Mielich-Suss, B.1    Schneider, J.2    Lopez, D.3
  • 120
    • 84879030282 scopus 로고    scopus 로고
    • Flotillins functionally organize the bacterial membrane
    • Bach JN, Bramkamp M. 2013. Flotillins functionally organize the bacterial membrane. Mol Microbiol 88: 1205-1217. http://dx.doi.org/10.1111/mmi.12252.
    • (2013) Mol Microbiol , vol.88 , pp. 1205-1217
    • Bach, J.N.1    Bramkamp, M.2
  • 121
    • 84862221167 scopus 로고    scopus 로고
    • SMART 7: Recent updates to the protein domain annotation resource
    • Letunic I, Doerks T, Bork P. 2012. SMART 7: Recent updates to the protein domain annotation resource. Nucleic Acids Res 40: D302-D305. http://dx.doi.org/10.1093/nar/gkr931.
    • (2012) Nucleic Acids Res , vol.40 , pp. D302-D305
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 122
    • 72449165351 scopus 로고    scopus 로고
    • The NfeD protein family and its conserved gene neighbours throughout prokaryotes: Functional implications for stomatin-like proteins
    • Green JB, Lower RP, Young JP. 2009. The NfeD protein family and its conserved gene neighbours throughout prokaryotes: Functional implications for stomatin-like proteins. J Mol Evol 69: 657-667. http://dx.doi.org/10.1007/s00239-009-9304-8.
    • (2009) J Mol Evol , vol.69 , pp. 657-667
    • Green, J.B.1    Lower, R.P.2    Young, J.P.3
  • 123
    • 84886668835 scopus 로고    scopus 로고
    • Entry of Listeria monocytogenes in mammalian epithelial cells: An updated view
    • Pizarro-Cerda J, Kuhbacher A, Cossart P. 2012. Entry of Listeria monocytogenes in mammalian epithelial cells: An updated view. Cold Spring Harb Perspect Med 2: A010009. http://dx.doi.org/10.1101/cshperspect.a010009.
    • (2012) Cold Spring Harb Perspect Med , vol.2 , pp. a010009
    • Pizarro-Cerda, J.1    Kuhbacher, A.2    Cossart, P.3
  • 124
    • 77954586271 scopus 로고    scopus 로고
    • Community-Associated methicillinresistant Staphylococcus aureus: Epidemiology and clinical consequences of an emerging epidemic
    • David MZ, Daum RS. 2010. Community-Associated methicillinresistant Staphylococcus aureus: Epidemiology and clinical consequences of an emerging epidemic. Clin Microbiol Rev 23: 616-687. http://dx.doi.org/10.1128/CMR.00081-09.
    • (2010) Clin Microbiol Rev , vol.23 , pp. 616-687
    • David, M.Z.1    Daum, R.S.2
  • 125
    • 33645312378 scopus 로고    scopus 로고
    • The Escherichia coli plasma membrane contains two PHB prohibitin homology. Domain protein complexes of opposite orientations
    • Chiba S, Ito K, Akiyama Y. 2006. The Escherichia coli plasma membrane contains two PHB prohibitin homology. domain protein complexes of opposite orientations. Mol Microbiol 60: 448-457. http://dx.doi.org/10.1111/j.1365-2958.2006.05104.x.
    • (2006) Mol Microbiol , vol.60 , pp. 448-457
    • Chiba, S.1    Ito, K.2    Akiyama, Y.3
  • 128
    • 0036164090 scopus 로고    scopus 로고
    • Lipid-protein stoichiometries in a crystalline biological membrane: NMR quantitative analysis of the lipid extract of the purple membrane
    • Corcelli A, Lattanzio VM, Mascolo G, Papadia P, Fanizzi F. 2002. Lipid-protein stoichiometries in a crystalline biological membrane: NMR quantitative analysis of the lipid extract of the purple membrane. J Lipid Res 43: 132-140.
    • (2002) J Lipid Res , vol.43 , pp. 132-140
    • Corcelli, A.1    Lattanzio, V.M.2    Mascolo, G.3    Papadia, P.4    Fanizzi, F.5
  • 129
    • 84879521145 scopus 로고    scopus 로고
    • Role of squalene in the organization of monolayers derived from lipid extracts of Halobacterium salinarum
    • Gilmore SF, Yao AI, Tietel Z, Kind T, Facciotti MT, Parikh AN. 2013. Role of squalene in the organization of monolayers derived from lipid extracts of Halobacterium salinarum. Langmuir 29: 7922-7930. http://dx.doi.org/10.1021/la401412t.
    • (2013) Langmuir , vol.29 , pp. 7922-7930
    • Gilmore, S.F.1    Yao, A.I.2    Tietel, Z.3    Kind, T.4    Facciotti, M.T.5    Parikh, A.N.6
  • 130
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: Elusive or illusive?
    • Munro S. 2003. Lipid rafts: Elusive or illusive? Cell 115: 377-388. http://dx.doi.org/10.1016/S0092-8674(03)00882-1.
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 131
    • 33750130964 scopus 로고    scopus 로고
    • Lipid rafts: Now you see them, now you don't
    • Shaw AS. 2006. Lipid rafts: Now you see them, now you don't. Nat Immunol 7: 1139-1142. http://dx.doi.org/10.1038/ni1405.
    • (2006) Nat Immunol , vol.7 , pp. 1139-1142
    • Shaw, A.S.1
  • 133
    • 33645085864 scopus 로고    scopus 로고
    • A major protein component of the Bacillus subtilis biofilm matrix
    • Branda SS, Chu F, Kearns DB, Losick R, Kolter R. 2006. A major protein component of the Bacillus subtilis biofilm matrix. Mol Microbiol 59: 1229-1238. http://dx.doi.org/10.1111/j.1365-2958.2005.05020.x.
    • (2006) Mol Microbiol , vol.59 , pp. 1229-1238
    • Branda, S.S.1    Chu, F.2    Kearns, D.B.3    Losick, R.4    Kolter, R.5
  • 135
    • 33645056701 scopus 로고    scopus 로고
    • Targets of the master regulator of biofilm formation in Bacillus subtilis
    • Chu F, Kearns DB, Branda SS, Kolter R, Losick R. 2006. Targets of the master regulator of biofilm formation in Bacillus subtilis. Mol Microbiol 59: 1216-1228. http://dx.doi.org/10.1111/j.1365-2958.2005.05019.x.
    • (2006) Mol Microbiol , vol.59 , pp. 1216-1228
    • Chu, F.1    Kearns, D.B.2    Branda, S.S.3    Kolter, R.4    Losick, R.5
  • 137
    • 13444292348 scopus 로고    scopus 로고
    • A master regulator for biofilm formation by Bacillus subtilis
    • Kearns DB, Chu F, Branda SS, Kolter R, Losick R. 2005. A master regulator for biofilm formation by Bacillus subtilis. Mol Microbiol 55: 739-749. http://dx.doi.org/10.1111/j.1365-2958.2004.04440.x.
    • (2005) Mol Microbiol , vol.55 , pp. 739-749
    • Kearns, D.B.1    Chu, F.2    Branda, S.S.3    Kolter, R.4    Losick, R.5
  • 138
    • 76649143766 scopus 로고    scopus 로고
    • Amyloid fibers provide structural integrity to Bacillus subtilis biofilms
    • Romero D, Aguilar C, Losick R, Kolter R. 2010. Amyloid fibers provide structural integrity to Bacillus subtilis biofilms. Proc Natl Acad Sci U S A 107: 2230-2234. http://dx.doi.org/10.1073/pnas.0910560107.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 2230-2234
    • Romero, D.1    Aguilar, C.2    Losick, R.3    Kolter, R.4
  • 139
    • 79957460465 scopus 로고    scopus 로고
    • An accessory protein required for anchoring and assembly of amyloid fibres in B. Subtilis biofilms
    • Romero D, Vlamakis H, Losick R, Kolter R. 2011. An accessory protein required for anchoring and assembly of amyloid fibres in B. subtilis biofilms. Mol Microbiol 80: 1155-1168. http://dx.doi.org/10.1111/j.1365-2958.2011.07653.x.
    • (2011) Mol Microbiol , vol.80 , pp. 1155-1168
    • Romero, D.1    Vlamakis, H.2    Losick, R.3    Kolter, R.4
  • 140
    • 24944483644 scopus 로고    scopus 로고
    • Evidence that entry into sporulation in Bacillus subtilis is governed by a gradual increase in the level and activity of the master regulator Spo0A
    • Fujita M, Losick R. 2005. Evidence that entry into sporulation in Bacillus subtilis is governed by a gradual increase in the level and activity of the master regulator Spo0A. Genes Dev 19: 2236-2244. http://dx.doi.org/10.1101/gad.1335705.
    • (2005) Genes Dev , vol.19 , pp. 2236-2244
    • Fujita, M.1    Losick, R.2
  • 141
    • 8844286124 scopus 로고    scopus 로고
    • Sporulation of Bacillus subtilis
    • Piggot PJ, Hilbert DW. 2004. Sporulation of Bacillus subtilis. Curr Opin Microbiol 7: 579-586. http://dx.doi.org/10.1016/j.mib.2004.10.001.
    • (2004) Curr Opin Microbiol , vol.7 , pp. 579-586
    • Piggot, P.J.1    Hilbert, D.W.2
  • 142
    • 0035725498 scopus 로고    scopus 로고
    • The sporulation transcription factor Spo0A is required for biofilm development in Bacillus subtilis
    • Hamon MA, Lazazzera BA. 2001. The sporulation transcription factor Spo0A is required for biofilm development in Bacillus subtilis. Mol Microbiol 42: 1199-1209. http://dx.doi.org/10.1046/j.1365-2958.2001.02709.x.
    • (2001) Mol Microbiol , vol.42 , pp. 1199-1209
    • Hamon, M.A.1    Lazazzera, B.A.2
  • 143
    • 0029039416 scopus 로고
    • The major role of Spo0A in genetic competence is to downregulate abrB, an essential competence gene
    • Hahn J, Roggiani M, Dubnau D. 1995. The major role of Spo0A in genetic competence is to downregulate abrB, an essential competence gene. J Bacteriol 177: 3601-3605.
    • (1995) J Bacteriol , vol.177 , pp. 3601-3605
    • Hahn, J.1    Roggiani, M.2    Dubnau, D.3
  • 144
    • 0029565061 scopus 로고
    • Genetic networks controlling the initiation of sporulation and the development of genetic competence in Bacillus subtilis
    • Grossman AD. 1995. Genetic networks controlling the initiation of sporulation and the development of genetic competence in Bacillus subtilis. Annu Rev Genet 29: 477-508. http://dx.doi.org/10.1146/annurev.ge.29.120195.002401.
    • (1995) Annu Rev Genet , vol.29 , pp. 477-508
    • Grossman, A.D.1
  • 145
    • 0023272642 scopus 로고
    • Role of AbrB in Spo0A-And Spo0B-dependent utilization of a sporulation promoter in Bacillus subtilis
    • Zuber P, Losick R. 1987. Role of AbrB in Spo0A-And Spo0B-dependent utilization of a sporulation promoter in Bacillus subtilis. J Bacteriol 169: 2223-2230.
    • (1987) J Bacteriol , vol.169 , pp. 2223-2230
    • Zuber, P.1    Losick, R.2
  • 146
    • 0033711144 scopus 로고    scopus 로고
    • Multiple histidine kinases regulate entry into stationary phase and sporulation in Bacillus subtilis
    • Jiang M, Shao W, Perego M, Hoch JA. 2000. Multiple histidine kinases regulate entry into stationary phase and sporulation in Bacillus subtilis. Mol Microbiol 38: 535-542. http://dx.doi.org/10.1046/j.1365-2958.2000.02148.x.
    • (2000) Mol Microbiol , vol.38 , pp. 535-542
    • Jiang, M.1    Shao, W.2    Perego, M.3    Hoch, J.A.4
  • 147
    • 84880016919 scopus 로고    scopus 로고
    • A combination of glycerol and manganese promotes biofilm formation in Bacillus subtilis via histidine kinase KinD signaling
    • Shemesh M, Chai Y. 2013. A combination of glycerol and manganese promotes biofilm formation in Bacillus subtilis via histidine kinase KinD signaling. J Bacteriol 195: 2747-2754. http://dx.doi.org/10.1128/JB.00028-13.
    • (2013) J Bacteriol , vol.195 , pp. 2747-2754
    • Shemesh, M.1    Chai, Y.2
  • 148
    • 75749151681 scopus 로고    scopus 로고
    • Extracellular signals that define distinct and coexisting cell fates in Bacillus subtilis
    • Lopez D, Kolter R. 2010. Extracellular signals that define distinct and coexisting cell fates in Bacillus subtilis. FEMS Microbiol Rev 34: 134-149. http://dx.doi.org/10.1111/j.1574-6976.2009.00199.x.
    • (2010) FEMS Microbiol Rev , vol.34 , pp. 134-149
    • Lopez, D.1    Kolter, R.2
  • 149
    • 79952198569 scopus 로고    scopus 로고
    • Potassium sensing histidine kinase in Bacillus subtilis
    • Lopez D, Gontang EA, Kolter R. 2010. Potassium sensing histidine kinase in Bacillus subtilis. Methods Enzymol 471: 229-251. http://dx.doi.org/10.1016/S0076-6879(10)71013-2.
    • (2010) Methods Enzymol , vol.471 , pp. 229-251
    • Lopez, D.1    Gontang, E.A.2    Kolter, R.3
  • 150
    • 0027476641 scopus 로고
    • Integration of multiple developmental signals in Bacillus subtilis through the Spo0A transcription factor
    • Ireton K, Rudner DZ, Siranosian KJ, Grossman AD. 1993. Integration of multiple developmental signals in Bacillus subtilis through the Spo0A transcription factor. Genes Dev 7: 283-294. http://dx.doi.org/10.1101/gad.7.2.283.
    • (1993) Genes Dev , vol.7 , pp. 283-294
    • Ireton, K.1    Rudner, D.Z.2    Siranosian, K.J.3    Grossman, A.D.4
  • 151
    • 57549105056 scopus 로고    scopus 로고
    • Generation of multiple cell types in Bacillus subtilis
    • Lopez D, Vlamakis H, Kolter R. 2009. Generation of multiple cell types in Bacillus subtilis. FEMS Microbiol Rev 33: 152-163. http://dx.doi.org/10.1111/j.1574-6976.2008.00148.x.
    • (2009) FEMS Microbiol Rev , vol.33 , pp. 152-163
    • Lopez, D.1    Vlamakis, H.2    Kolter, R.3
  • 152
    • 65649111204 scopus 로고    scopus 로고
    • The Spo0E phosphatase of Bacillus subtilis is a substrate of the FtsH metalloprotease
    • Le AT, Schumann W. 2009. The Spo0E phosphatase of Bacillus subtilis is a substrate of the FtsH metalloprotease. Microbiology 155: 1122-1132. http://dx.doi.org/10.1099/mic.0.024182-0.
    • (2009) Microbiology , vol.155 , pp. 1122-1132
    • Le, A.T.1    Schumann, W.2
  • 153
    • 0030978686 scopus 로고    scopus 로고
    • Characterization of the ftsH gene of Bacillus subtilis
    • Lysenko E, Ogura T, Cutting SM. 1997. Characterization of the ftsH gene of Bacillus subtilis. Microbiology 143: 971-978. http://dx.doi.org/10.1099/00221287-143-3-971.
    • (1997) Microbiology , vol.143 , pp. 971-978
    • Lysenko, E.1    Ogura, T.2    Cutting, S.M.3
  • 154
    • 0037310554 scopus 로고    scopus 로고
    • The absence of FtsH metalloprotease activity causes overexpression of the sigmaWcontrolled pbpE gene, resulting in filamentous growth of Bacillus subtilis
    • Zellmeier S, Zuber U, Schumann W, Wiegert T. 2003. The absence of FtsH metalloprotease activity causes overexpression of the sigmaWcontrolled pbpE gene, resulting in filamentous growth of Bacillus subtilis. J Bacteriol 185: 973-982. http://dx.doi.org/10.1128/JB.185.3.973-982.2003.
    • (2003) J Bacteriol , vol.185 , pp. 973-982
    • Zellmeier, S.1    Zuber, U.2    Schumann, W.3    Wiegert, T.4
  • 155
    • 25844525796 scopus 로고    scopus 로고
    • Cellular functions, mechanism of action, and regulation of FtsH protease
    • Ito K, Akiyama Y. 2005. Cellular functions, mechanism of action, and regulation of FtsH protease. Annu Rev Microbiol 59: 211-231. http://dx.doi.org/10.1146/annurev.micro.59.030804.121316.
    • (2005) Annu Rev Microbiol , vol.59 , pp. 211-231
    • Ito, K.1    Akiyama, Y.2
  • 156
    • 0029910627 scopus 로고    scopus 로고
    • A protease complex in the Escherichia coli plasma membrane: HflKC HflA. Forms a complex with FtsH HflB), regulating its proteolytic activity against SecY
    • Kihara A, Akiyama Y, Ito K. 1996. A protease complex in the Escherichia coli plasma membrane: HflKC HflA. forms a complex with FtsH HflB), regulating its proteolytic activity against SecY. EMBO J 15: 6122-6131.
    • (1996) EMBO J , vol.15 , pp. 6122-6131
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 157
    • 0030914642 scopus 로고    scopus 로고
    • Host regulation of lysogenic decision in bacteriophage lambda: Transmembrane modulation of FtsH HflB), the cII degrading protease, by HflKC HflA)
    • Kihara A, Akiyama Y, Ito K. 1997. Host regulation of lysogenic decision in bacteriophage lambda: Transmembrane modulation of FtsH HflB), the cII degrading protease, by HflKC HflA). Proc Natl Acad Sci U S A 94: 5544-5549. http://dx.doi.org/10.1073/pnas.94.11.5544.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 5544-5549
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 158
    • 0032954927 scopus 로고    scopus 로고
    • Prohibitins regulate membrane protein degradation by the m-AAA protease in mitochondria
    • Steglich G, Neupert W, Langer T. 1999. Prohibitins regulate membrane protein degradation by the m-AAA protease in mitochondria. Mol Cell Biol 19: 3435-3442.
    • (1999) Mol Cell Biol , vol.19 , pp. 3435-3442
    • Steglich, G.1    Neupert, W.2    Langer, T.3
  • 159
    • 0026344236 scopus 로고
    • SecA protein needs both acidic phospholipids and SecY/E protein for functional high-Affinity binding to the Escherichia coli plasma membrane
    • Hendrick JP, Wickner W. 1991. SecA protein needs both acidic phospholipids and SecY/E protein for functional high-Affinity binding to the Escherichia coli plasma membrane. J Biol Chem 266: 24596-24600.
    • (1991) J Biol Chem , vol.266 , pp. 24596-24600
    • Hendrick, J.P.1    Wickner, W.2
  • 160
    • 84858238365 scopus 로고    scopus 로고
    • Two copies of the SecY channel and acidic lipids are necessary to activate the SecA translocation ATPase
    • Dalal K, Chan CS, Sligar SG, Duong F. 2012. Two copies of the SecY channel and acidic lipids are necessary to activate the SecA translocation ATPase. Proc Natl Acad Sci U S A 109: 4104-4109. http://dx.doi.org/10.1073/pnas.1117783109.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 4104-4109
    • Dalal, K.1    Chan, C.S.2    Sligar, S.G.3    Duong, F.4
  • 161
    • 0026031219 scopus 로고
    • The oligopeptide transport system of Bacillus subtilis plays a role in the initiation of sporulation
    • Perego M, Higgins CF, Pearce SR, Gallagher MP, Hoch JA. 1991. The oligopeptide transport system of Bacillus subtilis plays a role in the initiation of sporulation. Mol Microbiol 5: 173-185. http://dx.doi.org/10.1111/j.1365-2958.1991.tb01838.x.
    • (1991) Mol Microbiol , vol.5 , pp. 173-185
    • Perego, M.1    Higgins, C.F.2    Pearce, S.R.3    Gallagher, M.P.4    Hoch, J.A.5
  • 162
    • 0034830834 scopus 로고    scopus 로고
    • The intracellular function of extracellular signaling peptides
    • Lazazzera BA. 2001. The intracellular function of extracellular signaling peptides. Peptides 22: 1519-1527. http://dx.doi.org/10.1016/S0196-9781(01)00488-0.
    • (2001) Peptides , vol.22 , pp. 1519-1527
    • Lazazzera, B.A.1
  • 163
    • 84884292152 scopus 로고    scopus 로고
    • Differentiated roles for MreB-Actin isologues and autolytic enzymes in Bacillus subtilis morphogenesis
    • Dominguez-Cuevas P, Porcelli I, Daniel RA, Errington J. 2013. Differentiated roles for MreB-Actin isologues and autolytic enzymes in Bacillus subtilis morphogenesis. Mol Microbiol 89: 1084-1098. http://dx.doi.org/10.1111/mmi.12335.
    • (2013) Mol Microbiol , vol.89 , pp. 1084-1098
    • Dominguez-Cuevas, P.1    Porcelli, I.2    Daniel, R.A.3    Errington, J.4
  • 164
    • 84884286838 scopus 로고    scopus 로고
    • FtsEX is required for CwlO peptidoglycan hydrolase activity during cell wall elongation in Bacillus subtilis
    • Meisner J, Montero Llopis P, Sham LT, Garner E, Bernhardt TG, Rudner DZ. 2013. FtsEX is required for CwlO peptidoglycan hydrolase activity during cell wall elongation in Bacillus subtilis. Mol Microbiol 89: 1069-1083. http://dx.doi.org/10.1111/mmi.12330.
    • (2013) Mol Microbiol , vol.89 , pp. 1069-1083
    • Meisner, J.1    Montero Llopis, P.2    Sham, L.T.3    Garner, E.4    Bernhardt, T.G.5    Rudner, D.Z.6
  • 166
    • 84890120354 scopus 로고    scopus 로고
    • Complex formation and processing of the minor transformation pilins of Bacillus subtilis
    • Mann JM, Carabetta VJ, Cristea IM, Dubnau D. 2013. Complex formation and processing of the minor transformation pilins of Bacillus subtilis. Mol Microbiol 90: 1201-1215. http://dx.doi.org/10.1111/mmi.12425.
    • (2013) Mol Microbiol , vol.90 , pp. 1201-1215
    • Mann, J.M.1    Carabetta, V.J.2    Cristea, I.M.3    Dubnau, D.4
  • 167
    • 41149130813 scopus 로고    scopus 로고
    • Statins for infection and sepsis: A systematic review of the clinical evidence
    • Falagas ME, Makris GC, Matthaiou DK, Rafailidis PI. 2008. Statins for infection and sepsis: A systematic review of the clinical evidence. J Antimicrob Chemother 61: 774-785. http://dx.doi.org/10.1093/jac/dkn019.
    • (2008) J Antimicrob Chemother , vol.61 , pp. 774-785
    • Falagas, M.E.1    Makris, G.C.2    Matthaiou, D.K.3    Rafailidis, P.I.4
  • 168
    • 65449182012 scopus 로고    scopus 로고
    • Statins for sepsis: A critical and updated review
    • Kopterides P, Falagas ME. 2009. Statins for sepsis: A critical and updated review. Clin Microbiol Infect 15: 325-334. http://dx.doi.org/10.1111/j.1469-0691.2009.02750.x.
    • (2009) Clin Microbiol Infect , vol.15 , pp. 325-334
    • Kopterides, P.1    Falagas, M.E.2
  • 169
    • 0035887840 scopus 로고    scopus 로고
    • The effect of statins on mortality in patients with bacteremia
    • Liappis AP, Kan VL, Rochester CG, Simon GL. 2001. The effect of statins on mortality in patients with bacteremia. Clin Infect Dis 33: 1352-1357. http://dx.doi.org/10.1086/323334.
    • (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
  • 170
    • 63449117005 scopus 로고    scopus 로고
    • The mevalonate pathway of Staphylococcus aureus
    • Balibar CJ, Shen X, Tao J. 2009. The mevalonate pathway of Staphylococcus aureus. J Bacteriol 191: 851-861. http://dx.doi.org/10.1128/JB.01357-08.
    • (2009) J Bacteriol , vol.191 , pp. 851-861
    • Balibar, C.J.1    Shen, X.2    Tao, J.3
  • 172
    • 0032544054 scopus 로고    scopus 로고
    • A 1-deoxy-Dxylulose 5-phosphate reductoisomerase catalyzing the formation of 2-Cmethyl-D-erythritol 4-phosphate in an alternative nonmevalonate pathway for terpenoid biosynthesis
    • Takahashi S, Kuzuyama T, Watanabe H, Seto H. 1998. A 1-deoxy-Dxylulose 5-phosphate reductoisomerase catalyzing the formation of 2-Cmethyl-D-erythritol 4-phosphate in an alternative nonmevalonate pathway for terpenoid biosynthesis. Proc Natl Acad Sci U S A 95: 9879-9884. http://dx.doi.org/10.1073/pnas.95.17.9879.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 9879-9884
    • Takahashi, S.1    Kuzuyama, T.2    Watanabe, H.3    Seto, H.4
  • 173
    • 34547609909 scopus 로고    scopus 로고
    • The non-mevalonate pathway of isoprenoid precursor biosynthesis
    • Hunter WN. 2007. The non-mevalonate pathway of isoprenoid precursor biosynthesis. J Biol Chem 282: 21573-21577. http://dx.doi.org/10.1074/jbc.R700005200.
    • (2007) J Biol Chem , vol.282 , pp. 21573-21577
    • Hunter, W.N.1
  • 174
    • 84895174793 scopus 로고    scopus 로고
    • Probing the subcellular localization of hopanoid lipids in bacteria using NanoSIMS
    • Doughty DM, Dieterle M, Sessions AL, Fischer WW, Newman DK. 2014. Probing the subcellular localization of hopanoid lipids in bacteria using NanoSIMS. PLoS One 9: E84455. http://dx.doi.org/10.1371/journal.pone.0084455.
    • (2014) PLoS One , vol.9 , pp. e84455
    • Doughty, D.M.1    Dieterle, M.2    Sessions, A.L.3    Fischer, W.W.4    Newman, D.K.5
  • 175
    • 84890531231 scopus 로고    scopus 로고
    • Exploring bacterial cell biology with single-molecule tracking and super-resolution imaging
    • Gahlmann A, Moerner WE. 2014. Exploring bacterial cell biology with single-molecule tracking and super-resolution imaging. Nat Rev Microbiol 12: 9-22. http://dx.doi.org/10.1038/nrmicro3154.
    • (2014) Nat Rev Microbiol , vol.12 , pp. 9-22
    • Gahlmann, A.1    Moerner, W.E.2
  • 176
    • 84901056407 scopus 로고    scopus 로고
    • Imaging lipid domains in cell membranes: The advent of super-resolution fluorescence microscopy
    • Owen DM, Gaus K. 2013. Imaging lipid domains in cell membranes: The advent of super-resolution fluorescence microscopy. Front Plant Sci 4: 503. http://dx.doi.org/10.3389/fpls.2013.00503.
    • (2013) Front Plant Sci , vol.4 , pp. 503
    • Owen, D.M.1    Gaus, K.2
  • 177
    • 77954995399 scopus 로고    scopus 로고
    • A guide to superresolution fluorescence microscopy
    • Schermelleh L, Heintzmann R, Leonhardt H. 2010. A guide to superresolution fluorescence microscopy. J Cell Biol 190: 165-175. http://dx.doi.org/10.1083/jcb.201002018.
    • (2010) J Cell Biol , vol.190 , pp. 165-175
    • Schermelleh, L.1    Heintzmann, R.2    Leonhardt, H.3
  • 179
    • 33748579946 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of the membrane skeleton at the plasma membrane interface by electron tomography
    • Morone N, Fujiwara T, Murase K, Kasai RS, Ike H, Yuasa S, Usukura J, Kusumi A. 2006. Three-dimensional reconstruction of the membrane skeleton at the plasma membrane interface by electron tomography. J Cell Biol 174: 851-862. http://dx.doi.org/10.1083/jcb.200606007.
    • (2006) J Cell Biol , vol.174 , pp. 851-862
    • Morone, N.1    Fujiwara, T.2    Murase, K.3    Kasai, R.S.4    Ike, H.5    Yuasa, S.6    Usukura, J.7    Kusumi, A.8
  • 180
    • 43149102677 scopus 로고    scopus 로고
    • High-resolution 3D quantitative analysis of caveolar ultrastructure and caveola-cytoskeleton interactions
    • Richter T, Floetenmeyer M, Ferguson C, Galea J, Goh J, Lindsay MR, Morgan GP, Marsh BJ, Parton RG. 2008. High-resolution 3D quantitative analysis of caveolar ultrastructure and caveola-cytoskeleton interactions. Traffic 9: 893-909. http://dx.doi.org/10.1111/j.1600-0854.2008.00733.x.
    • (2008) Traffic , vol.9 , pp. 893-909
    • Richter, T.1    Floetenmeyer, M.2    Ferguson, C.3    Galea, J.4    Goh, J.5    Lindsay, M.R.6    Morgan, G.P.7    Marsh, B.J.8    Parton, R.G.9
  • 182
    • 84878297375 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of bacteria with a complex endomembrane system
    • Santarella-Mellwig R, Pruggnaller S, Roos N, Mattaj IW, Devos DP. 2013. Three-dimensional reconstruction of bacteria with a complex endomembrane system. PLoS Biol 11: E1001565. http://dx.doi.org/10.1371/journal.pbio.1001565.
    • (2013) PLoS Biol , vol.11 , pp. e1001565
    • Santarella-Mellwig, R.1    Pruggnaller, S.2    Roos, N.3    Mattaj, I.W.4    Devos, D.P.5
  • 183
    • 79955504165 scopus 로고    scopus 로고
    • A genetically encoded tag for correlated light and electron microscopy of intact cells, tissues, and organisms
    • Shu X, Lev-Ram V, Deerinck TJ, Qi Y, Ramko EB, Davidson MW, Jin Y, Ellisman MH, Tsien RY. 2011. A genetically encoded tag for correlated light and electron microscopy of intact cells, tissues, and organisms. PLoS Biol 9: E1001041. http://dx.doi.org/10.1371/journal.pbio.1001041.
    • (2011) PLoS Biol , vol.9 , pp. e1001041
    • Shu, X.1    Lev-Ram, V.2    Deerinck, T.J.3    Qi, Y.4    Ramko, E.B.5    Davidson, M.W.6    Jin, Y.7    Ellisman, M.H.8    Tsien, R.Y.9
  • 184
    • 78649763791 scopus 로고    scopus 로고
    • Laurdan and di-4-ANEPPDHQ do not respond to membrane-inserted peptides and are good probes for lipid packing
    • Dinic J, Biverstahl H, Maler L, Parmryd I. 2011. Laurdan and di-4-ANEPPDHQ do not respond to membrane-inserted peptides and are good probes for lipid packing. Biochim Biophys Acta 1808: 298-306. http://dx.doi.org/10.1016/j.bbamem.2010.10.002.
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 298-306
    • Dinic, J.1    Biverstahl, H.2    Maler, L.3    Parmryd, I.4
  • 185
    • 33645299024 scopus 로고    scopus 로고
    • Visualizing membrane microdomains by Laurdan 2-photon microscopy
    • Gaus K, Zech T, Harder T. 2006. Visualizing membrane microdomains by Laurdan 2-photon microscopy. Mol Membr Biol 23: 41-48. http://dx.doi.org/10.1080/09687860500466857.
    • (2006) Mol Membr Biol , vol.23 , pp. 41-48
    • Gaus, K.1    Zech, T.2    Harder, T.3
  • 186
    • 78650587104 scopus 로고    scopus 로고
    • Widefield microscopy for live imaging of lipid domains and membrane dynamics
    • Wheeler G, Tyler KM. 2011. Widefield microscopy for live imaging of lipid domains and membrane dynamics. Biochim Biophys Acta 1808: 634-641. http://dx.doi.org/10.1016/j.bbamem.2010.11.017.
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 634-641
    • Wheeler, G.1    Tyler, K.M.2
  • 187
    • 84896797385 scopus 로고    scopus 로고
    • The actin homologue MreB organizes the bacterial cell membrane
    • Strahl H, Burmann F, Hamoen LW. 2014. The actin homologue MreB organizes the bacterial cell membrane. Nat Commun 5: 3442. http://dx.doi.org/10.1038/ncomms4442.
    • (2014) Nat Commun , vol.5 , pp. 3442
    • Strahl, H.1    Burmann, F.2    Hamoen, L.W.3
  • 188
    • 0141642121 scopus 로고    scopus 로고
    • Sphingomyelin phosphatidylcholine cholesterol phase diagram: Boundaries and composition of lipid rafts
    • de Almeida RF, Fedorov A, Prieto M. 2003. Sphingomyelin phosphatidylcholine cholesterol phase diagram: Boundaries and composition of lipid rafts. Biophys J 85: 2406-2416. http://dx.doi.org/10.1016/S0006-3495(03)74664-5.
    • (2003) Biophys J , vol.85 , pp. 2406-2416
    • De Almeida, R.F.1    Fedorov, A.2    Prieto, M.3
  • 189
    • 0030950269 scopus 로고    scopus 로고
    • Two-photon fluorescence microscopy of laurdan generalized polarization domains in model and natural membranes
    • Parasassi T, Gratton E, Yu WM, Wilson P, Levi M. 1997. Two-photon fluorescence microscopy of laurdan generalized polarization domains in model and natural membranes. Biophys J 72: 2413-2429. http://dx.doi.org/10.1016/S0006-3495(97)78887-8.
    • (1997) Biophys J , vol.72 , pp. 2413-2429
    • Parasassi, T.1    Gratton, E.2    Yu, W.M.3    Wilson, P.4    Levi, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.